Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O74423
|
ENT1_SCHPO
|
MKAAVRSVKNFSKGYTDTQIKVRNATTNDSWGPSGTAMAEIAELTYDQNEMLEVMDIIDRRLNDKGKNWRHVFKSLSLLEYCLHNGSENVVRWAKDNIYIITTLREFVYVDDNGHDQGQNVRTKAKEITSLLEDEHALKEARGDSRERDRDRDRTRSSRFDDDDDDRAPYEESRLSRAPSRASRYDDDDRDHRSRRRSRSRRPGRSRSRRRSRRPSPSAEHNSAEENDPELQRVIEESKRQAEEDAKRRNMANDSEAELQKAIQLSKEEDEARQRHQREREQQEQAFMGNQQNAYQPVDFFGNPVQPQPTGFLQQQPTGFIRPQNTGFVQPQYTGFVQPQHTGFVQPQATGFMQPQRTGFVQPQATGFVQPQATGFVQPQATGFMQPQRTGFVQPQATGFMQPQRTGFVQPQATGFMQPQRTGFVQPQATGFIQPQRTGFVQPQQNGFFNPQPTGYMQPQRTGMMQPQRTGFSQPFESNNPFPVMQPQRTGFGQTPNAPMMAPNHTGYVHPQPTGLQRQTTGYTGNNNPYSRPLQSQSTGILQQQQQQSAPRLEPTKTGSNNPFAQFSNLPSQSTAPATKPMKPVRTGDDRFSNIAQAISTGNPMGTDSFGNIGLTRVPTQHTGSKFTNSAGQTIQAQATGNTHNPFQSQQATGYYKQPMQQQQNMQQPYYNQQNYNYQNQQPMQGMQQQSMQPQVGSLIDL
| null | null |
actin cortical patch assembly [GO:0000147]; actin cytoskeleton organization [GO:0030036]; actin filament organization [GO:0007015]; endocytosis [GO:0006897]
|
actin cortical patch [GO:0030479]; clathrin vesicle coat [GO:0030125]; endosome [GO:0005768]; plasma membrane [GO:0005886]
|
clathrin binding [GO:0030276]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phospholipid binding [GO:0005543]
|
PF08226;PF01417;
|
1.25.40.90;
|
Epsin family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15659877}. Membrane {ECO:0000255|PROSITE-ProRule:PRU00243, ECO:0000269|PubMed:15659877}; Peripheral membrane protein {ECO:0000269|PubMed:15659877}. Note=Localizes in a punctate pattern. Colocalizes with F-actin.
| null | null | null | null | null |
FUNCTION: Binds to membranes enriched in phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Required for endocytosis and localization of actin. {ECO:0000269|PubMed:15659877}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74424
|
NU211_SCHPO
|
MHDSSWTEADILGVCSFLDIPKTKIDPLLQVDAFTSILIPLISKSKDYESIKNDRIVTEVNYEQQLRNSEKKLLQSNERYDLLEDERKLLENELSQIKEYLREKSSSYDTVLHDCSSLKSVNEALKQAQDQNLKQTAQLQNLLSDKEKEVEKKITIIKDLKDALASSTHQVLELQHTQQEKASLQTNYEFELQKLTQKNSILENNNTWLSRELQGVNDKLLSLHQEASLEKSQLSSQLSDAVLEKDALQRKVSSLSQQFTESNLRYQNIVAELSEMRKQYEFSQVSFEKEISSQKQISELWMEKCEDCSLRLKELQNSNGELEKLLEAAQSSFEEQLESHKEAEASLKSQINFLEKEVSSLESQLKLANERLRHYDEIEISDMSELKYSNLLNNSMKGFKGQSSVSDLYSERLYYKQKYEQTCQEVERLQRSYNHVMEEANLQHPLVKEQFKRFAHMQREIVAMSEQYQKSLEDCQKAKSRYEQLETLFKDKCTENKHYEQETKDLARQVQVLLHELDLCENGIVLGVDSRKKINSYVEKSLTEDETDTDQIISSRLVVFRNIRELQQQNQNLLSAVHELADRMEKDEKPDLDGAEIQEETLIKANETIDQLTKMLEEVSDQLRYSLKERDFFRSLVQENEKLLDMAPATPNSKLNTNLIEQTSYQRSLIRLEQLTNELESLKSISRNKEKKFEEAISSLQLEKSNIQLQLTSLTSERSLALEKLNDLEKSLVLSERSKDELDESYKSLQEQLASKKIEVQNVSSQLSICNSQLEQSNHIVDNLKSENLLLTSVKDKLKADLSNLESKLSSLQQDNFHMKAQIESSNQEYTATVDSMNSRILELSNDLRVANSKLSECSDDVRRLTLQNSFDLREHQTLVLQLQSNITELKQDITLQRTVRNQLEIQTTELKERLKFMEERQENLQSKLIAANKDTTQNPDNVEVEAISIELERTKEKLRMAELEKSNIQQKYLASEKTLEMMNETHEQFKHLVESEISTREEKITSLRSELLDLNKRVEVLKEEKESSSKELAKQLEDAVREKDSALSFKKDYEKIRSDADRVITSLKEDIEKERSLMKECHSNYESEIVSHGRTTQKLRDLRTEFDEVNTKYLKLKANFEQQHSGLSGAEKDWNIQRKAMEDEISSLKDYILGLENQNKLLHSQFDSLSQQITVLQQNSSENLNISANLEAVQDNDLRELVSYLRHEKEIMDNKYELTILDNRGLNQQVKSLQSTVDSLQLELNRLQSLPVSNDQTDTPIISGSQEVQLLYESNSVLRKDNDAKLGKIQELEKEVEKLNASLNPLQTEINELKAEIGAKTASLNLMKEYNSRWKLRFQSVLNKYERVDPTQLEELKKNCEALEKEKQELETKLQETAKETDTFKQQVNSLNEEVENLKKEVEQANTKNTRLAAAWNEKCENLKKSSLTRFAHLKQELTNKNKELTSKNAENEAMQKEIESLKDSNHQLQESASSDAEQITKEQFEQLKSEKERTEKELADSKNELEHLQSEAVDADGKTEISNLEKEIHELRSDKEGLVQQVQNLSAELAALREHSPTQGSLENADEIARLRSQLESTKQYYEKEKETEILAARSELVAEKEKTKEELENQLNEKSQRIKELEEQAQKNSSENTHDNIDDMIKQQVEEKLKENSANFDVKLKKVVAETEFRSKAKISVYEKKTRDLQNKITQLEETIENLNKQLSNPEKTDESTSSVTETKPVTSKPTASKADVGQNATEASSAKREPSGKSLSARLQGTGKQKGVQRPAVSRPVPMKPDSGKLSITGASKRIATSKNAAQNAKELSSTAKSGSLKRQRDDANKGGSSSNQKKAK
| null | null |
mRNA export from nucleus [GO:0006406]; protein import into nucleus [GO:0006606]; regulation of mitotic spindle assembly [GO:1901673]
|
cytoplasm [GO:0005737]; nuclear periphery [GO:0034399]; nuclear pore [GO:0005643]; nuclear pore nuclear basket [GO:0044615]; nucleolar peripheral inclusion body [GO:0140602]; nucleus [GO:0005634]
|
structural constituent of nuclear pore [GO:0017056]
|
PF07926;
|
1.10.287.1490;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:15116432}. Note=Nuclear rim. {ECO:0000269|PubMed:15116432}.
| null | null | null | null | null |
FUNCTION: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. {ECO:0000269|PubMed:15116432}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74429
|
VIP1_SCHPO
|
MIQNASHLTSIDTESSTRTASPVSSIVTPTKRNVVGICAMDAKARSKPCRNILNRIIAEGEFEAIVFGDNMILDEAVENWPACDYLICFYSSGFPLKKAEKYVELRKPFCVNDVVFQELLWDRRLVLNILDAIRVSTPQRLICSRDGGPKINKVLEEKLRRKFGIEITEVPTPEVKMLDEDTLSVDGKIIKKPYVEKPVYGEDHNIYIYFPKSVGGGGRKLFRKVANKSSDYDPDLCAPRTEGSFIYEEFMNVDNAEDVKVYTVGPHYSHAETRKSPVVDGIVRRNPHGKEIRFITNLSEEEKNMASKISIAFEQPVCGFDLLRVSGQSYVIDVNGWSFVKDNNDYYDNAARILKQMFHVAERHRRNRVPSVQEVLNPPPRESEAWRLKSLVGVLRHADRTPKQKFKFSFTSDPFVKLLQGHTEEVILRNEQLNSVLAATNLATELKCEDINKLKQLRLALETKKDLPGTKVQLKPAYSPEGKLLKLQLIIKWGGEFTHSARYQSKDLGEQFHKDLYIMNRDCLKDVEIYTSSERRVSASAEIFAMAFLEQETIPSDLLKVRKDLLDDSNAAKDTMDKVKKHLKSLLRVGDTARKEFTWPENMPKPCEVMQQVVQLMKYHRAVMRENFIILGPEVEQVQSRWCCNENPALFRERWEKLFSEFCDSEKADPSKVSELYDTLKYDALHNRQFLERIFTPYQYLKLPQSPSLIAKEPPQRTDSNGNLVGMTGANTNHTERPLEKLYELYDLAKVLFDFVSPQEYGIEPKEKLEIGLLTSVPLLRQIIHDIKEARDSDHASTRMYFTKESHIYTLLNCILESGLPMKLPRNQIPELDYLTQICFELFERTNPSGNKEFSVRITLSPGCYAQCPLDMNLDAKHCISVSPRRSLTRHLDLQQFITKTEDLCNSVHLPKRFIPVNIN
|
2.7.4.24
| null |
inositol metabolic process [GO:0006020]; inositol phosphate biosynthetic process [GO:0032958]; inositol phosphate catabolic process [GO:0071545]; inositol phosphate metabolic process [GO:0043647]; intracellular phosphate ion homeostasis [GO:0030643]; mitotic spindle assembly [GO:0090307]; phosphorylation [GO:0016310]; regulation of bipolar cell growth [GO:0051516]; regulation of microtubule cytoskeleton organization [GO:0070507]; regulation of mitotic spindle elongation (spindle phase three) [GO:0110162]; signaling [GO:0023052]
|
cytoskeleton [GO:0005856]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
2 iron, 2 sulfur cluster binding [GO:0051537]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; diphosphoinositol-pentakisphosphate kinase activity [GO:0033857]; inositol heptakisphosphate kinase activity [GO:0000829]; inositol hexakisphosphate 1-kinase activity [GO:0052723]; inositol hexakisphosphate 3-kinase activity [GO:0052724]; inositol hexakisphosphate 5-kinase activity [GO:0000832]; inositol hexakisphosphate kinase activity [GO:0000828]; inositol-1,3,4,5,6-pentakisphosphate kinase activity [GO:0000827]; inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 1-diphosphatase activity [GO:0052846]; inositol-1-diphosphate-2,3,4,5,6-pentakisphosphate diphosphatase activity [GO:0052843]
|
PF00328;PF18086;PF08443;
|
3.40.50.11950;3.30.470.20;3.40.50.1240;
|
Histidine acid phosphatase family, VIP1 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10388810, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:10388810}.
|
CATALYTIC ACTIVITY: Reaction=1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:37459, ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:74946, ChEBI:CHEBI:456216; EC=2.7.4.24; Evidence={ECO:0000250|UniProtKB:Q06685}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37460; Evidence={ECO:0000250|UniProtKB:Q06685}; CATALYTIC ACTIVITY: Reaction=5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP + H(+) = 1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate + ADP; Xref=Rhea:RHEA:10276, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58628, ChEBI:CHEBI:77983, ChEBI:CHEBI:456216; EC=2.7.4.24; Evidence={ECO:0000250|UniProtKB:Q06685}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10277; Evidence={ECO:0000250|UniProtKB:Q06685};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=58.18 uM for inositol hexakisphosphate {ECO:0000269|PubMed:25254656}; Vmax=450.5 nmol/min/ug enzyme {ECO:0000269|PubMed:25254656};
| null | null | null |
FUNCTION: Bifunctional inositol kinase that acts in concert with the IP6K kinases to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. Phosphorylates inositol hexakisphosphate (InsP6) at position 1 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates PP-InsP5 at position 1, produced by IP6Ks from InsP6, to produce (PP)2-InsP4 (By similarity). Required for maintaining cellular integrity, normal growth and interactions with the ARP complex (PubMed:10388810). Acts as a regulator of the PHO80-PHO85 cyclin/cyclin-dependent kinase (CDK) complex, thereby regulating signaling of phosphate availability (By similarity). Required for the function of the cortical actin cytoskeleton, possibly by participating in correct F-actin localization and ensuring polarized growth (PubMed:10388810). Regulates polarized growth and modulates interphase microtubule cytoskeleton. Regulates microtubule dynamics without the requirement of microtubule plus-end tracking protein Mal3. Required for growth zone selection (PubMed:25254656). {ECO:0000250|UniProtKB:O43314, ECO:0000250|UniProtKB:Q06685, ECO:0000269|PubMed:10388810, ECO:0000269|PubMed:25254656}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74435
|
CDC31_SCHPO
|
MFANARAKRRSRASSPTPARLGGYAPLRVEITEEQRQDINEAFKLFDSDKDNAIDYHELRAAMRALGFNAEKSEVLKILRDFDKTGKGYLQMEDFVRVMTEKIVERDPLEEIKRAFELFDDDETGKISLRNLRRVAKELNENIDDQELEAMIEEFDLDQDGEINEQEFIAIMMDEA
| null | null |
cell division [GO:0051301]; mitotic spindle pole body duplication [GO:1903087]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein localization to meiotic spindle pole body [GO:1902441]; spindle pole body duplication [GO:0030474]
|
cytosol [GO:0005829]; half bridge of mitotic spindle pole body [GO:0061496]; half bridge of spindle pole body [GO:0005825]; meiotic spindle pole body [GO:0035974]; mitotic spindle pole body [GO:0044732]; nucleus [GO:0005634]
|
calcium ion binding [GO:0005509]; microtubule binding [GO:0008017]
|
PF13499;
|
1.10.238.10;
|
Centrin family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12857865}. Note=Associates with the half-bridge structure of the SPB.
| null | null | null | null | null |
FUNCTION: Required for the proper coordination between exit from mitosis and the initiation of septation. Has a role in bipolar spindle formation during spindle pole body (SPB) duplication. Required for the localization of sad1 to the SPB (PubMed:12857865). {ECO:0000269|PubMed:12857865}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74441
|
CTL1_SCHPO
|
MFSDYASRFLAQSRFSSVDQRNFKYPTSRSNLQSVSIDRNSSIDSHETDLSAGSSSLHGLNSLIDSGSIHWQLREQEQSNSHISRNENELFSKENSIYNGNFSENLGVQPNPQTISHESVNEEYTELPYDAHLPSEQKVPDRKWGLTFGFLTLALFTYSFLMVWRTNPNIPPATSPYAAIQKAFPLFHKDAIICMMLSVIWLFCLVAIPRFLYFLLASVPLTMFAFAVYLLKASRIHLETSIQPKLMLLTGIILLVAPILLSYYVWRRRIHFETSFNIIRLACRVIADIPQITLIFISFLFSFYVLIFIWVRLFARLFLRGSTLVGSVWVLPRSSWVLASFYSLHFLWLCTFFHALQCAIISSIVSQWFFYRDTKSSATKTNLVSHFFYHVVSNQYGLCAFSSFLVVITKVPLHFLPTWLRHVSRIVYYMFSKTSASYVTSPLTLAYASIYSVPYMNASKALYQIEQLNRVGLRRRSYYFSKYTLLAARSLLAIGVGVTSWNYSIHENGVFYGYIVGLLGGFLAWLIIGAIEGGLSMIVDALLICSIIDISSCQGDPNGSHCFEAWQLFESNGY
| null | null |
macroautophagy [GO:0016236]; protein transport [GO:0015031]; transmembrane transport [GO:0055085]
|
endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; phagophore assembly site [GO:0000407]; phagophore assembly site membrane [GO:0034045]; plasma membrane [GO:0005886]
|
choline transmembrane transporter activity [GO:0015220]; transmembrane transporter activity [GO:0022857]
|
PF04515;
| null |
CTL (choline transporter-like) family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Preautophagosomal structure membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Required for the normal organization of the preautophagosomal structure (PAS) and for the correct subcellular location of atg9. {ECO:0000269|PubMed:23950735}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74456
|
PEF1_SCHPO
|
MNYQRLEKLGEGTYAHVYKGQNRVTGEIVALKVIRIDADEGTPSTAIREISLMKELRHPNIMSLSDVLQTENKLMLVFEYMEKDLKKYMDTYGNQGALPPSQVKNFTQQLLKGISFCHENRVLHRDLKPQNLLINSRGELKLADFGLARSIGIPVNTFSNEVVTLWYRAPDVLLGSRVYSTSIDIWSVGCIMAEMATGRPLFAGSNNEDQLLKIFRLLGTPTEQSWPGISLLPEYKPTFPIYKAQDLAYLFPTFDPLGLDLLRRMLRLQPELRTTGQDALQHAWFLTA
|
2.7.11.22
| null |
negative regulation of mitotic cohesin loading [GO:1905412]; phosphorylation [GO:0016310]; signal transduction [GO:0007165]; synaptic vesicle transport [GO:0048489]; traversing start control point of mitotic cell cycle [GO:0007089]; vesicle-mediated transport [GO:0016192]
|
ascospore-type prospore [GO:0042764]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein serine kinase activity [GO:0106310]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22;
| null | null | null | null | null |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74465
|
HRR1_SCHPO
|
MEQVQDEIWKLSTLDAWEMVNKNTEVVFDEIPEPETLSEMKRHPLYSNIFNADNNTTSFTEQIETSETSKTQDSEGNKVDKNLKENKSIRRKRSIDNDYELSNVKRNDITSGKNREFENEHHPASDTSSWRELPSIPTLEELTSKSVELPSNNIYGGYKSFEDYLSIHYRLLREDAVSPLRESVLRYKVNPNYITGSSLAVYDHVRIDGYTISSSVIAAKLSFSVRAKKKIKWATSRRLISGSLVLLSNDDFQTFRIGTVCARPLSGLNKHPHEIDVKFEDISISLDPREEYVMIEATSGYWEAYKHVLRSLQRLSASTFPMKDYLVHCKSNQETAKHIQNNPRIRINSILKNNSQKIVNALEPFGPGEYILDSSQLKAYQSMLTKRLSIIQGPPGTGKSFVTLKAIETLLENTHSHVLPILVACQTNHAVDQILIRLLHQGASVMRLGSRTKDPEIAAVTIFQKAKHTKHSFKAAYNEIRHKKQRLIKQITNIMHNFNLEFVTLSYLHSKGIITTSQLESLRNNTEWISSVAENGEKTEEELISIWLGDAKVELITPSEITDGFEEELQIDPEKLEEIQKEAEDSGALMEEELRGKFINLRCKYLFSKLTTLHEKEIDTLLTIPNIWDIPEYSRGIIYCRWLESAYAAAEKELNRLYRFYLKVDRERIGFSNKRAAILLRGANVIGMTTTGLNKYRDILERINPKICFIEEAADVLEGPIIPAVFPSLEQLVLIGDHKQLRPGCSTYALRQDPFNLSISMFERLVENDMEYTRLTMQRRMHPQIRRLVSSVYEDLSDYEITKYWPSIPGMGEIRRFFLTHSRIEDNDGFASKINLFEAQMLVQFAVYLINNGVEPQKITCLTFYAAQKDLIERLLSESLNREKHFIKVATVDGYQGEENDVVLLSLVRNNDRTEVGFLSSPHRVCVSLSRARRGLFIFGNAQLVAESNPLWWDAINTLMNDETIQGLGDHLPLFTKDGTIYVNDPVELLDVNMRLTRK
|
3.6.4.13
| null |
chromosome segregation [GO:0007059]; regulatory ncRNA-mediated heterochromatin formation [GO:0031048]; siRNA-mediated pericentric heterochromatin formation [GO:0140727]
|
cytosol [GO:0005829]; nuclear RNA-directed RNA polymerase complex [GO:0031380]; nucleus [GO:0005634]; RNA-directed RNA polymerase complex [GO:0031379]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]
|
PF13086;PF13087;
|
3.40.50.300;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
| null | null | null | null |
FUNCTION: Has a role in the RNA interference (RNAi) pathway which is important for heterochromatin formation and accurate chromosome segregation. A member of the RNA-directed RNA polymerase complex (RDRC) which is involved in the generation of small interfering RNAs (siRNAs) and mediate their association with the RNA-induced transcriptional silencing (RITS) complex. RITS acts as a priming complex for dsRNA synthesis at the site of non-coding centromeric RNA. {ECO:0000269|PubMed:15607976}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74469
|
YQC7_SCHPO
|
MDPEYSELFERLNKQLDNVEDVLKPLKDAESIFELAEGKSELEQAKLYITMSYAINSTLYSFYKLNGIDASERPVMQELQRVKNYISKIQQAEKNVNPKTEAVNTSNAAISSSSSNRPKVAKDAATRIIKHHT
| null | null |
exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000467]; maturation of 5.8S rRNA [GO:0000460]; nonfunctional rRNA decay [GO:0070651]; nuclear mRNA surveillance [GO:0071028]; nuclear polyadenylation-dependent mRNA catabolic process [GO:0071042]; nuclear polyadenylation-dependent rRNA catabolic process [GO:0071035]; nuclear polyadenylation-dependent tRNA catabolic process [GO:0071038]; regulation of gene expression [GO:0010468]; sno(s)RNA processing [GO:0043144]; snRNA processing [GO:0016180]
|
cytosol [GO:0005829]; exosome (RNase complex) [GO:0000178]; nuclear exosome (RNase complex) [GO:0000176]; nucleolus [GO:0005730]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; RNA binding [GO:0003723]
|
PF04000;
| null |
C1D family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Required for exosome-dependent processing of pre-rRNA and small nucleolar RNA (snRNA) precursors. Involved in processing of 35S pre-rRNA at the A0, A1 and A2 sites (By similarity). {ECO:0000250}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74473
|
CDC11_SCHPO
|
MEQLWLEHDLSEEWIPQPQEQGSDNSSEPPTTSNVNNTQSTGRGSSGTSTEHGTFKKGRNDAPDVPQWKQVNAKNPVARDIFARLDLENMFEESSKQSPPSKSPTKNPSKKSSNNSSRRSSSSVGKLSNVSNMQSSPSKDPFVSQDYEKESISSSQFSKKYSEGSLKSQQSNTRSNSVHEKQNTDHASNASSSSSVVSSPSLKPNNTSPLKLFQGASDPFTREHLNQLTQDVKSNSFENGEKQFSLPEPRRPQKPMRTTERKASLNTKDLYQEVEEVMARLRGRMPNSGRESTIFLPRKLSGLREEEEQDEISVEVSQEDSSNAFPSLSDQLHLKSLQSMKRVTSIFNDNDDSFPSASSSPQRQAYMTDKMPLREIDVGSSQSSSKTARLNSSPKSTLKTSSVKTRRSHSAQSSRKVSDYPNMVVITPADLPEGIDTTQGSMEFDRIHNRWRRKGHDSDLGFDFETDEDASLSHPERTILFKAASTRHQANNDPNNLEKQQPHSFPLRKQNVAQSEFPKHSLRDNSENAPQILSSFHDLSLQNESFDEMFNGRYENGSPIPFISSGSGLKSKADKDAEYSFSVSRQSIIQILSDVEPYEPFWKRIIQLDISRRHLDSLIGLSELCPSIEELTLEGNEIAYLTGCPVTIRDLNAVENRLSSLTSFSNLLNLQYLDISYNQLEDLTGLSSLIHLRELKVDSNHLWSLDGIQHLDGLLKLSACNNRIKELSFTNSNLHRLEELLLGNNEIEEIEEISSLQNLMVLQLDNNKLTNLKASQPMIHLRILRISNNAIHQLEVDQFPHLRTLYMDLNRFNRPPDIRRLKRLVNFSFRTQDPEASNFVIQPSLDIRNLYLSNNTFVTLDCKHMFLGVRYLELANVQLKEVPKYIATSMPNLRVLDLSHNYISDIESLKPLQMIHRLYLVGNRIKKMRNLCDILANLKQLNVLDLRMNPLNFNIYPVIDDSIYELSAASKYQQSINQKGHHRKEDPQKQWQEKELAFSSTLSEAWRTRRKMYAEAILLACPHLEWLDGSDVSQSSRAAFTKSSN
| null | null |
positive regulation of mitotic division septum assembly [GO:0140281]; regulation of mitotic cytokinesis [GO:1902412]; septation initiation signaling [GO:0031028]
|
cytoplasm [GO:0005737]; mitotic spindle pole body [GO:0044732]; outer plaque of mitotic spindle pole body [GO:0061499]; protein-containing complex [GO:0032991]
|
signaling adaptor activity [GO:0035591]
|
PF13855;
|
3.80.10.10;
| null |
PTM: Phosphorylated by cdc7 and cdk1. Hyperphosphorylated during anaphase. Dephosphorylated by par1. {ECO:0000269|PubMed:11676915, ECO:0000269|PubMed:12546793, ECO:0000269|PubMed:15062098, ECO:0000269|PubMed:18257517}.
|
SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Note=Localizes at the spindle pole body and the barrier septum.
| null | null | null | null | null |
FUNCTION: Essential for the onset of septum formation. Involved in the organization of astral microtubules during mitosis. Acts as a bridge between sid4 and the other SIN proteins mediating their association with the spindle pole body (SPB). The sid4-cdc11 complex organizes a signaling hub on the SPB which coordinates cell and nuclear division. {ECO:0000269|PubMed:11676915, ECO:0000269|PubMed:15062098}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74475
|
FKS4_SCHPO
|
MSGNNENVSGITGHDAVSDDQYAYDSEVYDDQNAYQRQPADAYSNEEFLDQADYDSMYGEGYNGYDYPTGVTESYGDEYTPVDTASSGINQYSTEKGKFTRPSDEYESEYSDYNAQPSDANNFYNLRGDGRYNAYDPSSDSLANVYNSVPYGSSPYDFSNSSFVGNSGSGTPLDGDSGSFYADSANLTNREPYPAWTPENELPLTKEEIEDIFIDLTNKLGFQRDSMRNMYDFFMCLLDSRASRMTPDQALLTLHADYIGSDIANYKKWYFASQMDREDAVGLANVGIYGGKVTSIKEKGKFFSRNKKAPKVVKPPRKSRFKRKKKKEQPEEAEDEYIDVNTDDSLESAEYRWRSHMRSMTQFERAQQIALWLLLWGEANNVRFMPEVIAFLFKCAYDYIISPEAQNVTEPVPEGYYLDNIVSPLYQYMHDQQFEIINGKYVRRERPHDQLIGYDDINQLFWHAEGIARLIFEDGTRLIDIPASERFHRLPEVQWNRAFYKTYYESRSWFHLITNFNRIWVIHFGMFWYFTAFNSPTLYTKPFHQRDGPKPTGASQWAAVACTSVVSCIIMAAASLCEYLFVPRRFPGSKPIWKRLCIIVLIAIINLIPIVYIFGFSSKHQQRSGRRIAVGVVAFLMSIATYVYFSLVPLQSTFGKLSVKDSRKYLANKYFTSNFAPLKFDNQALSVIIWVCVFTCKFAESYFFLTLSIRDPIIVLSTMRPYLCSIYWAGSRLCFVQPRIILGIMYFTDLILFFLDTYLWYIIFNTIFSVLRSFVLGISILTPWRNIFSRMPQRIYGKILATNDMEIKYKPKILISQIWNAIVISMYREHLLSIDHVQRLLYHQVPAEEGRRTLRTPTFFVSQDDNIVHTTFFPANSEAERRLSFFAQSLATPIPEPVPVDNMPTFTVLIPHYAEKILLSLREIIREEDQLSRVTLLEYLKQLHPVEWDCFVKDTKILVEENAPYENDSVSEKEGTYKSKVDDLPFYCIGFKSAMPEYTLRTRIWASLRSQTLYRTISGFMNYSRAIKLLYRVENPEIVQMFGGNTDRLERELDRMARRKFKLVVSMQRYAKFTKEEYENAEFLLRAYPDLQIAYLDEDPPEEEGAEPQLFAALIDGHSEIMENERRRPKYRIRLSGNPILGDGKSDNQNMSLPFYRGEYIQLIDANQDNYLEECLKIRSVLAEFEEMETDNVNPYSESARERNKHPVAILGAREYIFSENIGILGDVAAGKEQTFGTLFSRTLAQIGGKLHYGHPDFLNGIFMTTRGGVSKAQKGLHVNEDIYAGMNAMLRGGRIKHCEYFQCGKGRDLGFGSILNFNTKVGTGMGEQMLSREYYYLGTQLQLDRFLSFYFAHPGFHLNNMFIMLSVQLFMVVLINLGAIYHVVTVCYYNGNQKLSYDTSIVPRGCYQLGPVLSWLKRCVISIFIVFWISFIPLTVHELIERGVWRATKRFFKQIGSFSPLFEVFTCQVYSQAITSDLAYGGARYIGTGRGFATARLPFSILYSRFAVPSIYIGARFLMMLLFGTMTVWVAHLIYWWVSIMALCVAPFLFNPHQFDWNDFFVDYREFIRWLSRGNSRSHANSWIGYCRLTRTRITGYKRRVLGQPSDKISMDTPRAKFTNVFFSDVLIPALLAAGAIIPYFFINSQPGNPMFITDPNNPSPYVHDTKTGTNPILRLVIISLIPIAAGFGMSGFFGGMACCLGPAFGLCCKKFPSIFAAIAHTIQIFIFIAIFEVCWFLDGWSLPKTVLAFCAVTAIHRFIFKILTLLCLSREVKQDSANISWWSGKWYGKGYGYHAFTLPAREFVCKAIELNLFATDFFLGHLLLFFMLPVICIPYIDRWHSVLLFWLRPSRQIRPPIFSTKQNRLRKRIVRRYSALYFSILVIFLILIIVPLAAGAEIRQGLTASEAVAKGAVGWNQTNSSIGSGIIQPRDTNYTANYSFWYDRYHFEFNTTY
|
2.4.1.34
| null |
(1->3)-beta-D-glucan biosynthetic process [GO:0006075]; fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process [GO:0071970]; fungal-type cell wall polysaccharide biosynthetic process [GO:0051278]; secondary cell septum biogenesis [GO:1990344]
|
1,3-beta-D-glucan synthase complex [GO:0000148]; cell cortex of growing cell tip [GO:1902716]; cell division site [GO:0032153]; cell tip [GO:0051286]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; division septum [GO:0000935]; Golgi apparatus [GO:0005794]; mating projection tip [GO:0043332]; mitotic actomyosin contractile ring [GO:0110085]; new growing cell tip [GO:0035841]; plasma membrane [GO:0005886]; plasma membrane of cell tip [GO:0031520]; primary cell septum [GO:0000936]; site of polarized growth [GO:0030427]; spore wall [GO:0031160]
|
1,3-beta-D-glucan synthase activity [GO:0003843]; branched 1,3-beta-D-glucan synthase activity [GO:0140752]
|
PF14288;PF02364;
| null |
Glycosyltransferase 48 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15615781}; Multi-pass membrane protein {ECO:0000255}. Cell septum {ECO:0000269|PubMed:15615781}. Spore wall {ECO:0000269|PubMed:15615781}. Note=Localizes to regions of active cell wall synthesis in an F-actin dependent manner. Following nuclear division and formation of the contractile ring, relocalizes from the cell ends to the assembling division septum. During sexual development, localizes to the mating projection, the contact region at the cell-cell fusion site, and to the forming spore walls. {ECO:0000269|PubMed:15615781}.
|
CATALYTIC ACTIVITY: Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378, ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34; Evidence={ECO:0000305|PubMed:15615781};
| null | null | null | null |
FUNCTION: Alternate catalytic subunit of the 1,3-beta-glucan synthase (GS) complex. Synthesizes 1,3-beta-glucan, a major structural component of the yeast cell wall (By similarity). Required for maintaining cell integrity during cytokinesis and polarized growth (PubMed:15615781). {ECO:0000250|UniProtKB:P38631, ECO:0000269|PubMed:15615781}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74476
|
IMB3_SCHPO
|
MSSGFPPEVLSPLLNLVQGLSSPDNTVRNDAEKSLSSDWISQRADLLLNGLAILAYQSEDPAVRSFCLVLCRRISFRTLPGDSELEVFSSISNESKQSLQSQLLACFVKESVPTVRNKLCDTIAEIARSIYDCQGEWPELINVIFNAVNSPDESFRESVFRTITSLPRLLSGQDSAVTPLFTTGLADPSIRVRISAARAYSAVILESKQSTRDQVIPLLPSLMNILPPLQQDRDSDNLADCLMAITEIAEVFPKLFKPIFESVIAFGLGIIKDKELDNSARQAALELLVCFSEGAPAMCRKSSDYTDQLVLQCLLLMTDVAGDPEDEAEELQEWLNTDDLDQDESDANHVVAEQAMDRLSRKLGGKTILPPSFTWLPRLIPSQKWSERHAALMAISSIAEGAEKLMKKELSRVLDMVLPLLADPHPRVRWAACNAVGQMSTDFAPDMQVKYPSRILEALVPVLESPESRVQAHAAAAMVNFSEEADNKVLEPYLDDILQRLLTLLQSPKRYVQEQAVTTIATVADAAAKKFEKYFDAIMPLLFNVLQQADGKEFRTLRGKTMECATLIALAVGKQRFLPVSQELIQILGNIQMGITDSDDPQASYLISAWGRICRVLGSDFVPFLSSVMPPLLVAATSKPDFTIIDDEVDESKYSEQDGWEFIPVHGQQVGIRTSTLEDKCTATEMLVCYAAELKADFDPYVNEVLTSVVLPGLKFFFHDGVRSACCKCIPQLLNARILASNRDPAKVNELWEPILRKLLDHIQNEPSVEMLADYFECFYQSLEISGLNLSPSSMEALVAAVDLQLKGFISRVQQREEEAKNGDIDIEEDEDMILAVENDQNLLNEINKTFSVVLKIHKTAFCPFWERLLPYMDGFLSGNDTVAKQWALCMMDDLIEFTGPDSWNYKDHFLPYLAEGIQSSEPEIRQAASYGIGVAAQHGGELYAEICSSALPALFKMLELPDARDEEQIYATENICVAICKICRFCSQRVQDLDKVVTYWINTLPVTHDEDDAPYAYTFLAELMEQNHVAVASQMPTIITILAETFASGVLRGRTLTRLMEASKVYLARFPADQVNSVIATLSVDNQRALSAHF
| null | null |
protein import into nucleus [GO:0006606]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nuclear periphery [GO:0034399]; nucleus [GO:0005634]
|
nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139]
|
PF13513;PF18808;PF18816;PF18829;
|
1.25.10.10;
|
Importin beta family, Importin beta-3 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:12399381, ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:12399381, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:12399381, ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Involved in the nuclear import of cdc25 and mcs1. {ECO:0000269|PubMed:12399381}.; FUNCTION: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Involved in the nuclear import of cdc25 and mcs1 (PubMed:12399381). Mediates docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to repeat-containing nucleoporins. The complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, GTP-Ran binding leads to release of the cargo. The importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). {ECO:0000250|UniProtKB:P32337, ECO:0000269|PubMed:12399381}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74499
|
LSM7_SCHPO
|
MSSLQKRPGPGNSSQPTERPRKESILDLSRYQDQRIQATFTGGRQITGILKGFDQLMNLVLDDVEEQLRNPEDGKLTGAIRKLGLVVVRGTTLVLIAPMDGSEEIPNPFVQAE
| null | null |
mRNA cis splicing, via spliceosome [GO:0045292]; nuclear-transcribed mRNA catabolic process [GO:0000956]; rRNA processing [GO:0006364]; telomerase holoenzyme complex assembly [GO:1905323]; tRNA processing [GO:0008033]
|
catalytic step 2 spliceosome [GO:0071013]; cytosol [GO:0005829]; Lsm1-7-Pat1 complex [GO:1990726]; Lsm2-8 complex [GO:0120115]; nucleus [GO:0005634]; spliceosomal tri-snRNP complex [GO:0097526]; telomerase holoenzyme complex [GO:0005697]; U2 snRNP [GO:0005686]; U2-type prespliceosome [GO:0071004]; U4/U6 x U5 tri-snRNP complex [GO:0046540]; U5 snRNP [GO:0005682]; U6 snRNP [GO:0005688]
|
poly(U) RNA binding [GO:0008266]; U2 snRNA binding [GO:0030620]
|
PF01423;
|
2.30.30.100;
|
SnRNP Sm proteins family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner. Probable component of the spliceosome.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74511
|
EKC1_SCHPO
|
MFWRLGQGFGFQSSSAIEAILDKPEDEINLKELLEENGVLDECKSHNPKLLEYLCKPEVLSQLIDYILEVDETEIPSADGGYEEPEHTRLSYIASEILSSDVWSICEACVENKTLMVKLWSFLDSEGPLNPLQASYFAKVNEHFLDKKTEETVAFIQSIDNFVEKILRHAETSAIMDLLLKFISMDRCNTAIGIADWLYSQGLIQSLLRLLSPYVDPDVQFTVADVIKAIIAISANSNEPGVIGPNSLSRELVSRQTITTLTDYMTDSKAPHSATSLINGVSIVIELIRKNNSDYDVTPVLQMPLDTHPPTTRDPIYLGTMLRLFAEKIPVFQKILLKPSTESDLMPTSFGKIKPLGFERFRICELYAELLHCSNMSLLSDPNGEAMVMQRDHLRDYLFRHNSCARDLVMSDEDDDDSTFSDKNSKDFKETEDMNGAEDMHGRAPQITKDNLNLTTTDSPMSEAEPVSEEEYKDVMETAKALHHGDDDAASDTSYEPLPESVIEDAKKLPVIGDFLKIEFIQNNVIPTILDHFFDYPWNNFLHNVVYDVVQQVLNAPMDKDQNYALAVDMFKQGKITEKIVYGQELNDKKVAKPSGFRAGYMGHLTIIADEVVKFVEHYSSTFDQELLNLINDEKWQNFVNKTLVETRNRDNQLLGGLEPSMVGYLEDMDEGEMLDANNLPEMQFALEQELESNSSDDDVVEVHRELSHNSSSNDEDDGNDEDPLSREMSRRLSFESANDSDQDNRDHFAQYMSQQISDNNANQFSSSDEDDDDDDEVVEWVSRGNENKYPRSNFFINGSDREDFSDSEEEDGNDSSDDDRGFAEEEYSDGLVLNHGK
| null | null |
cell cycle [GO:0007049]; cell division [GO:0051301]; negative regulation of protein localization to kinetochore [GO:1905341]; signaling [GO:0023052]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein serine/threonine phosphatase complex [GO:0008287]
|
protein phosphatase activator activity [GO:0072542]; protein phosphatase binding [GO:0019903]; protein phosphatase regulator activity [GO:0019888]
|
PF04499;
| null |
SAPS family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12773390}. Note=Associated with chromatin.
| null | null | null | null | null |
FUNCTION: Has a role in chromosome segregation. May provide a dynamic connection between kinetochore microtubules and kinetochore chromatin. {ECO:0000269|PubMed:12773390}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74518
|
CID12_SCHPO
|
MGKVLLELHSVPWNEEGLSDNARLYSFLEFVSPKIEELKYRKLLLEKLQTHIREVVLDAELQVYGSMYIGTTLSISDVDVSLKSPRVGELEKRRVTMVLRKYLDADADFHSSARVPRINLVDVSGIGVDLTFGNDKACRTAELQKAYNEEHPIFGRLLMLLKHWLFERDLENVHHGGIASCALSYMLIGWLEMRFHKKGIDSEVQPIRALLQKFFYFWGVEWTYELFVLRPLTGQIVPKLQKGWLNEVQPNLLSIEDPIDRNNDIGKQSFQISMIKAAFVASANELLSDKTWFSTFAITEDEMFLCKQFENVINTKRSLVEGYDSDTESDELQAGG
|
2.7.7.19
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
|
chromosome segregation [GO:0007059]; regulatory ncRNA-mediated heterochromatin formation [GO:0031048]; RNA 3'-end processing [GO:0031123]; siRNA-mediated pericentric heterochromatin formation [GO:0140727]
|
cytosol [GO:0005829]; nuclear RNA-directed RNA polymerase complex [GO:0031380]; nucleolus [GO:0005730]; nucleus [GO:0005634]; RNA-directed RNA polymerase complex [GO:0031379]; TRAMP complex [GO:0031499]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; poly(A) RNA polymerase activity [GO:1990817]
|
PF03828;
|
1.10.1410.10;3.30.460.10;
|
DNA polymerase type-B-like family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:15607976, ECO:0000269|PubMed:16823372}.
|
CATALYTIC ACTIVITY: Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, ChEBI:CHEBI:173115; EC=2.7.7.19;
| null | null | null | null |
FUNCTION: Has a role in the RNA interference (RNAi) pathway which is important for heterochromatin formation and accurate chromosome segregation. A member of the RNA-directed RNA polymerase complex (RDRC) which is involved in the generation of small interfering RNAs (siRNAs) and mediate their association with the RNA-induced transcriptional silencing (RITS) complex. RITS acts as a priming complex for dsRNA synthesis at the site of non-coding centromeric RNA. {ECO:0000269|PubMed:15607976}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74536
|
SNF1_SCHPO
|
MQPQEVDLMENSTMRNGARVLPPEAISKRHIGPYIIRETLGEGSFGKVKLATHYKTQQKVALKFISRQLLKKSDMHMRVEREISYLKLLRHPHIIKLYDVITTPTDIVMVIEYAGGELFDYIVEKKRMTEDEGRRFFQQIICAIEYCHRHKIVHRDLKPENLLLDDNLNVKIADFGLSNIMTDGNFLKTSCGSPNYAAPEVINGKLYAGPEVDVWSCGIVLYVMLVGRLPFDDEFIPNLFKKVNSCVYVMPDFLSPGAQSLIRRMIVADPMQRITIQEIRRDPWFNVNLPDYLRPMEEVQGSYADSRIVSKLGEAMGFSEDYIVEALRSDENNEVKEAYNLLHENQVIQEKSHLSKSKRVDSFLSVSPPAFSEYTSELQKKSKQELIDPTLEGPRWTVSDPPTYAKQTIDSNICVLVPTAEKNKLEMRTLADAASAVDTSQSTRKKSRRNKWHFGVRCRGDAPEILLAVYRALQRAGAQFTVPKPVNGKYRSDMYTIKSRWEIPHCKREGKNTYAYIELQLYEVMPGCFMLDVKSNGYKDIYSHPERTADHGMDDLKSSFPFLDLCAMLVCKLFSA
|
2.7.11.1
| null |
CAMKK-AMPK signaling cascade [GO:0061762]; induction of conjugation with cellular fusion [GO:0010514]; negative regulation of cytoplasmic translation [GO:2000766]; negative regulation of TORC1 signaling [GO:1904262]; phosphorylation [GO:0016310]; positive regulation of ascus development [GO:0075319]; positive regulation of cell cycle switching, mitotic to meiotic cell cycle [GO:0140648]; positive regulation of transcription by RNA polymerase II [GO:0045944]; SREBP signaling pathway [GO:0032933]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitotic spindle pole body [GO:0044732]; nucleotide-activated protein kinase complex [GO:0031588]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF16579;PF00069;PF08587;
|
1.10.8.10;3.30.310.80;1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, SNF1 subfamily
|
PTM: Phosphorylation at Thr-189 by ssp1 is required for nuclear entry in nutritionally stressed cells (PubMed:22375066). {ECO:0000269|PubMed:22375066}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22375066}. Nucleus {ECO:0000269|PubMed:22140232, ECO:0000269|PubMed:22375066}. Note=Nuclear translocation occurs under nitrogen and glucose starvation conditions and depends on Thr-189 phosphorylation by ssp1 (PubMed:22375066). {ECO:0000269|PubMed:22375066}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P06782}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P06782};
| null | null | null | null |
FUNCTION: Serine/threonine protein kinase essential for release from glucose repression via the phosphorylation of scr1 upon glucose deprivation (PubMed:22140232). Catalytic subunit of the AMP-activated protein kinase complex also known as the SNF1 kinase complex (Snf1c), a central regulator of cellular energy homeostasis, which, in response to a fall in intracellular ATP levels, activates energy-producing pathways and inhibits energy-consuming processes (PubMed:22375066). The complex phosphorylates histone H3 to form H3S10ph, which promotes H3K14ac formation, leading to transcriptional activation through TBP recruitment to the promoters (By similarity). Regulates proper cell cycle exit and sexual differentiation (PubMed:22375066). Regulates also ste11 levels under nitrogen deprivation (PubMed:22375066). {ECO:0000250|UniProtKB:P06782, ECO:0000269|PubMed:22140232, ECO:0000269|PubMed:22375066}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74539
|
MAK3_SCHPO
|
MYSQHELRNKVSLALSSLLRYTFELTPFFELYEADFAYALYAGFELATNRKVVGKFSFQNVHLENEYNILTEIAKDERASKFSPTPIEFTSFPHIDLSACIAYDFGHGAELSTSYAYFRENPAEFVRFCIAICKCIEYLHSKGMVHGEIRLDSFIPISSYDNVYMLTVGSGASYFHNCLQAHNWRKYSEDSESMSRILFISPEQTGRTSYSVGYRTDIYSLGVLFFHYLSDCSPYTGSFVQRIRSILTEPLPDISKSCPKLPHLIFKIIEKMTRKNPDERYTSCSGIVNDLEACLDDIDKGLILNDHVLEKTGRTSLFYLPCSIYGREHEIKLIRKILRNSPRAINHQDKKDLETFNPYYLNAIESESSSQSLSLSQRASEVMPLVILITGCEGIGESSLIQTICDRREGYMAITKFEVSQSIVYSAIVSAVAEFIRQILAEDQLLLNNFFEELKNKLESDLYLLDSVFDLVPEIRSLLQQFSTSSGNTRKTSLLGSNHSSYSDKLGSPTILSTSFSLARPYPEPALVSPSTERPPRSSFSAALMTLLNIIASFKKVTMVIENIHLADESSLIILQKIVYSDLPLTLMITCDKENDHVINRFRLANDRIHEIELKPLSFNAVNSYVQATLHRTDDGLARFSSYVYHISKGVPLLVRNVLLSIYENKIIYFDWKKNRWEVNYDEMYTLDNDYSEPDAFMTAKKKISKLNDSSRAILGWASLLGPSFSFATVKKLCKDTDNIELNVEALQSALREGIIYATSSDDTYTFSRSIYVKAMRDLLNEAKIQIMHACLIDVCLKNRDRYNIFDIAFHINAAFDFVKGDKRSVEYCHYLHLAAEEALKIGANQEALDLYNRCIKMIPHEIPEESDDSYIRCQLIGMYVGCAEAYWVNDNFDTASEMLKLAEEKACNNSEVFPARFLYSRILFEGVHIEECTQYVLSCLKPLGYELKRHSLEDSKSIISALIPRIIDKITKSSEESQSSTDDDDRRIFEILSFLYVGSVATSYFSETAEMAIDFGIAQVEFFLSTVVNSFSAFALVYFAILANSLLEPSEDILFIGNYGEKLNREAENPIIFSRTEYLYVQSLGFIDSTTKERRLTIDYLDRNCVTCSDKHVIISLLLVSSWEKFLTSNNYSNYLADFETTHAQIMEMKPWVGDTSLITQLKRFLMCLQDNIKLDLIKSKSFLSDHNIQLSSPAAQESAKLAFSLHGWINSWYLLALVMHGEWDMAISYGENFKREFKNALLTSSRVFGIFMFTWSLVNKMLICPEFTKQKKYYEQYKENLGFFDSLCIGDNECITRVYFLLLKACGLIMNGLNFEASVMLEEVISLTEKLELFLLQAFAFETVGSIFVSMELYTSATQYLEEAIRNYAALGVKQKARHLRDKFGDLLVSNNLQVSIDEATQTDFPLVFSPERSSIDINASSMRSEKASFEIPFPEEQIDDDVSPVAQDSSLEELLISLDIIDLTSVMRSCQTIASEIELTGLLSTMTQRMLEDSSANAAVIAIRDDVGFKIAAYRTGELNEVFAPPMPITEDQTYVPSRVINYVVHTQKALFSNNINHEFDLQQERWNIENHMGRSVIAIPLYQKKEVFAILYLQGPPSAFHSRHMSVLSILGAQASFAIVNISLFHKVKEATNVNTIIIKAQREALNLVQKSEAKYRSFVDTMPCLLSKLEFDEELRIELFGSFWKEYCGELNINDPNTWKEYVHLDDHLKLQDFLLSHLHNPLPFELEIRIKRKDGVYRWNLTRCTPTTNEKNRTSFLCATIDIDDQKKARATALELARLRSNFLANISHELRTPFSGFYGMLSLLDDTNLDSEQRDIVSAARISCEMLLRVINDLLNFSKLEAGKVTLESDLEFSLESVVCDCMQSVYSACAEKGINLSYNVSPDIPFFTAGDGMKIGQMLKSILDNSVKTVNNGFIRVRAFLAGSSKKNDRDQLQIAFIVEDTREESNAIFLANMINSLNRGCNDYLPMDLSGTALGMSTCLQLCKIMGGSVSVEVSQNNPTFKICYDLKIHELGKERYDIIATPLFQNLTEFNDLIKSKVAIRVSKTSTEYDNITTYLQAARKVLHVFKGLQDLASIFDLSPDSALLRCSVVVVDVYSMDDVKAVEKILKSYPDVHVIYLCCDPSRLNIEQELQKPSGRSFACKKRWGFLQMPCTRENFLKVTLQVFKSNEDTCNFYSYVNEYGESPKPDDDMDRLNKCVGSKILIAEDNPIVRMTLKKQLEHLGMDVDAAEDGKETLQIFESHPDNYYQVCFVDYHMPVYDGLEVTRRMRKIERKHGCAPLPIFALTADMQPTMETQFQEVGITHYLSKPFKKETLIKMLLQYLVNGTDGNANTS
|
2.7.13.3
| null |
phosphorelay signal transduction system [GO:0000160]; positive regulation of p38MAPK cascade [GO:1900745]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; protein histidine kinase complex [GO:0009365]
|
ATP binding [GO:0005524]; phosphorelay sensor kinase activity [GO:0000155]
|
PF13191;PF13185;PF00512;PF08447;PF00069;PF00072;
|
1.10.287.130;3.30.450.40;3.40.50.2300;3.30.565.10;3.30.450.20;1.10.510.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:11179424}.
|
CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3;
| null | null | null | null |
FUNCTION: Involved in the control of the SAPK-dependent transcriptional response to peroxide stress. Regulates sty1 activity. {ECO:0000269|PubMed:11179424, ECO:0000269|PubMed:11758939}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74555
|
BBP_SCHPO
|
MLNSRSVGSTGSNNTPLGRRRFDEKPDSLPPLPDANGMSNGYRDSYKSNSRMDHRPDGYHDGRGRRAYRKHYWGHPTPIEEMLPSQMELETAVKSCMTMEQLELYSLNVRLEEITQKLRTGDVVPHHRERSPSPPPQYDNHGRRLNTREIRYKKKLEDERHRIIERAMKMVPGFRAPSDYRRPAKTQEKVYVPVKDYPEINFIGLLIGPRGHTLKDMEAKSGAKIAIRGKGSVKEGKGRSDPSVRGNMEEDLHCLVTADSEDKINHAIKLIDNVIQTAASVPEGQNDLKRNQLRQLATLNGTLRDDENQVCQNCGNVGHRRFDCPERINHTMNIVCRHCGSIGHIARDCPVRDQQPPMADSTADREYQSLMQELGGGSAISNGNGEPQKSIEFSESGAASPQAGHPPPWAAASTSVSSSTSSPAPWAKPASSAAPSNPAPWQQPAAPQSAPALSMNPSSLPPWQQPTQQSAVQPSNLVPSQNAPFIPGTSAPLPPTTFAPPGVPLPPIPGAPGMPNLNMSQPPMVPPGMALPPGMPAPFPGYPAVPAMPGIPGATAPPGAPGSYNTSESSNLNAPPGVSMPNGYSNR
| null | null |
mRNA cis splicing, via spliceosome [GO:0045292]; regulation of mRNA splicing, via spliceosome [GO:0048024]
|
commitment complex [GO:0000243]; cytosol [GO:0005829]; nucleus [GO:0005634]; U2-type prespliceosome [GO:0071004]
|
mRNA binding [GO:0003729]; RNA binding [GO:0003723]; zinc ion binding [GO:0008270]
|
PF00013;PF16275;PF00098;
|
6.10.140.1790;3.30.1370.10;4.10.60.10;
|
BBP/SF1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Necessary for the splicing of pre-mRNA. The BPB1(SF1)-u2af59-u2af23 complex has a role in the recognition of the branch site (5'-UACUAAC-3'), the pyrimidine tract and the 3'-splice site at the 3'-end of introns. {ECO:0000269|PubMed:12374752}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74558
|
MOB2_SCHPO
|
MFLLNSLSRITRGNRSKRHQNLSDASSSSGSFSKKSSTSQLVRTGSPSVEPTALYLQQPFVRTHLVKGNFSTIVSLPRFVDLDEWVALNVYELFTYLNHFYDVFATFCTVKTCPVMSAAANFDYTWLDNNRKPVHLPAPQYIEYVLAWIENRLHDQNVFPTKAGLPFPSNFLVIVKAIYKQMFRIFAHMYYAHYAEILHLSLEAHWNSFFAHFIAFGKEFQLLDKRDTAPLKDLIVVLENQGNI
| null | null |
cell cycle [GO:0007049]; cell division [GO:0051301]; positive regulation of protein phosphorylation [GO:0001934]; RAM/MOR signaling [GO:0062200]; regulation of establishment or maintenance of bipolar cell polarity regulating cell shape [GO:2000100]; signal transduction [GO:0007165]
|
cell cortex [GO:0005938]; cell division site [GO:0032153]; cell tip [GO:0051286]; cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
protein kinase activator activity [GO:0030295]
|
PF03637;
|
1.20.140.30;
|
MOB1/phocein family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12456722}. Cytoplasm, cell cortex {ECO:0000269|PubMed:12456722}. Note=Localizes to the cell periphery and to the division site during septation and cytokinesis.
| null | null | null | null | null |
FUNCTION: Required for coordinating polarized cell growth during interphase with the onset of mitosis. {ECO:0000269|PubMed:12456722}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74560
|
RAF2_SCHPO
|
MPPVRAEKKRKTDLIEQVCVTNKAGELVDLEDVLEYGPYSLTGILSSEKDEQEPLFDESIVLGYSIKISPVWTYNLKDVPEKETMSIWIVTPQRRYGILSPSSEYKAIYEQISEKNRLFYLIKTKFKDDMISGTLEDYDNYIEVLKEKLELPSCFQAILLVQKHIRFLLTQMVATSSLHVWSESPFFIRIRSSYEHLILQINKNIYNARQERKKSKLSSNNPSDNNTTMKSSLNQALTLINLPEQPFSISSPTATPQLGVVKRTSPLRFPLNDIWLSGLRIVDPNIESISLWKRIQVSTSPKHQRYISLQEVCSVIAQQLQITNLEALNKLSSHGETLLQIMHTAFTWRGTKLFNDIKHAIGFRSSVQQARSQFRGYCYDYLFMHCNNGEKTSLHLLRTLICMKLDFSNAQLAAKILFHFLLFDIGSGLSGSDYTYEQYINHSAVAFSFTEEIFEKNFVTVLPDFVKLFSISFGYWPAFSFYDELLKLLRNKYPKVYSSTPNLCDQVWLDRTNLFPCNRSTRSTLPYRPTKLLDLASASSCLSKKETDFKQDTGLYSYNLEKVEALKVSPDLQTGIWSCPVQNCLYFAVCDNPYKPSQVIYDHLLGHVDSKFIFKTPSNSVRSFTNKLEHIMYNIN
| null | null |
CENP-A containing chromatin assembly [GO:0034080]; regulatory ncRNA-mediated heterochromatin formation [GO:0031048]; silent mating-type cassette heterochromatin formation [GO:0030466]; siRNA-mediated pericentric heterochromatin formation [GO:0140727]; subtelomeric heterochromatin formation [GO:0031509]
|
chromosome, telomeric region [GO:0000781]; CLRC complex [GO:0043494]; cytoplasm [GO:0005737]; heterochromatin island [GO:1990342]; mating-type region heterochromatin [GO:0031934]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]
| null |
PF12047;
| null | null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Mitochondrion {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16040243, ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:18345014}. Chromosome {ECO:0000269|PubMed:16040243, ECO:0000269|PubMed:18345014}.
| null | null | null | null | null |
FUNCTION: Component of the Clr4 methyltransferase complex (ClrC) which contributes to the establishment of heterochromatin by specifically methylating histone H3 to form H3K9me (PubMed:16024659, PubMed:16040243, PubMed:16157682). ClrC preferentially ubiquitylates H3K14 and ClrC-mediated H3 ubiquitination promotes clr4 methyltransferase activity for the methylation of H3K9 (PubMed:31468675). H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin, telomeric regions and at the silent mating-type loci (PubMed:16024659, PubMed:16040243, PubMed:16157682, PubMed:18345014). Has a role in both mitotic and meiotic chromosome segregation (PubMed:16040243). {ECO:0000269|PubMed:16024659, ECO:0000269|PubMed:16040243, ECO:0000269|PubMed:16157682, ECO:0000269|PubMed:18345014, ECO:0000269|PubMed:31468675}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74562
|
SEC8_SCHPO
|
MDTRGYSETKKGRYPVGKKSLESPNGYSNYGTSMDNELSSEYASRGMHIGDLENLVNEIEDEWKDLGREDYQPISTALELLDDSSFGRDYKSFLNVYDRISAALQTIAHTHKDDFTRGISAYGEIMEGIQKCNSRIIALKQSLEASQECIGNTNSKELQQTLARSSQYKKVISVLKELNEANQLFDNFHTLVDSKQYYHASDLIRRVWDELSRSDFDGILVVEQFKSRMTGLLSHLEDILSEELVSITFLKDAVAYPIVSYCSPNPLRETSNPYFLRDFLKNNANTSTLGQSEQLRYLEEALSLKLSDCLKMDYGRDSLRDIRIVLESLNLLGKLPNAISSLKSRTSAEMFTTVDSTSRAIVNKYSLGNNVSTVNPFSKSLYDIGLHAETDREHTMISEFLTNLFTKLRCVLMHYRGISEFMTKLETKTPKHASSSHKSSIMSVNSDPTSPKVSKFDTSDSTFPFDTLLQAFESEIRLMLKDYLISKEEYIENSGNFVVGTEMSIYNLPGENEEDKLFDVTNEIAVENKSNAFYARINELVNEKAPELILNKSNASVSTIELFSGSSKEIVRLAGHVVFVGPSVFHASSVLPQTVFFLEDSVSILKNPNIPPQFAVNFMKEFLRGSYIPQLYKFMSSHFDTIMKDVGAFQLHRDWKIYSKIPIFKCHVAIVQYFHDLQDYLPIVALNLVEFYELLHTLLVRFRNHCSDYLSDLCRTAVLKEYKHVNEDTEDVDDTVRVKLLHDDVTYPQFIKFLKQKNPSLEGLNELCRMENKRLLQYEDRAITSEVKLPVSVLSKDSDLVNSVSYLHNSMEWFLQRCFSRFMNGSRRMNVLQQNQANFGGDFLPIDNLLGNNSDLMKGAYKEVFDSLQRLQFDALLLIRMEVRLQYIHSINQSVNLPDYVVEYRGRPDASIMALNSTIVTTNLKLETCLNEWERRFVFQGLSELVDSSLYSIFYKIESMNRGSCLQMLKNMSAMIQILKTVKEIHGDVEFPKSSRVFGIYQNGAKKIIEHFIAAPKKELLPDVKQMVRIYYQRLMKDAKRNGRDDLYRQYQKKIGSVLTQFDNTVGGARKNP
| null | null |
ascospore-type prospore membrane formation [GO:0032120]; division septum assembly [GO:0000917]; endocytosis [GO:0006897]; exocytosis [GO:0006887]; Golgi to plasma membrane transport [GO:0006893]; intracellular protein transport [GO:0006886]; vesicle docking involved in exocytosis [GO:0006904]; vesicle tethering involved in exocytosis [GO:0090522]
|
cell cortex of growing cell tip [GO:1902716]; cell division site [GO:0032153]; cell tip [GO:0051286]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; exocyst [GO:0000145]; meiotic spindle pole [GO:0090619]; mitotic actomyosin contractile ring [GO:0110085]
| null |
PF20652;PF04048;
| null | null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16141239, ECO:0000269|PubMed:16823372}. Cell tip {ECO:0000269|PubMed:11854409}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11854409}. Cytoplasmic vesicle {ECO:0000269|PubMed:16141239}. Note=Associated with the actinomyosin ring at the division site and at the cell tips. {ECO:0000269|PubMed:11854409}.
| null | null | null | null | null |
FUNCTION: Component of the exocyst complex involved in the delivery of secretory vesicles to the plasma membrane. Also required for polarized cell growth and division septum assembly. The exocyst complex plays an important role in the targeting of rho3, as well as the two main hydrolases required for cell separation, eng1 and agn1, to the cell wall surrounding the septum before cell separation begins. {ECO:0000269|PubMed:11854409, ECO:0000269|PubMed:12930742, ECO:0000269|PubMed:16079182, ECO:0000269|PubMed:16415366, ECO:0000269|PubMed:21148300}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74563
|
BRL2_SCHPO
|
MYQNGKPDAPTILGQKRELEDVEIQDDDIQEVSKEDLLKDVRVRSIQFDELESKIEGLQNLAEEKLKVLATLVSWWPEILQQFSVVFQGNELKDFESEGVFSILEKFPELSYFNDAVKNNKTKALSIIQKLLSTVDSSTNSVSRDPFSVLSIDDSALTEKLNTINLDIDKILDELDTTRSQLHSIIKLPDRSSSFTLQCINESVRPQSTKVKEEATTSSKGKDEEKKVSTVEQRTQLQQLSRLQDQQNGLMESRSQSLKILDSNVNEMDKLIMERENALNNVETTNLKKYSSFLALKEAVSMTSEQLRVLEHLLSECSHEINVLSQQSKNFNGVFESSYQPLINDLDHQISVMQNDEKRINNAKTELSLSLEKKLEAKKQKEKVYKDKLDELANLETMVLEKKKAVATREAANKIRLVDLNDLELQKDLSTYLSKELASTEKAFRLVKQQTVKSSHSHYQELITKFSVEKEKAEQKYFLTMKSTDSLHAEVKLLRQKYQKTNEIISKMLNSQDTAVHRIIEFEDQLARLSSVRNNSIKQSTTFQVKKSSQKSTIQNLEEKVSYLQQFMDKNNATLTDLEFQCSDLSSSIDILSKQDEEHEKEKRKLKDTGVSTSAEELKTFRAMCKCSVCNFERWKDRIISLCGHGFCYQCIQKRIETRQRRCPICGRGFGASDVIPIHL
|
2.3.2.27
| null |
epigenetic regulation of gene expression [GO:0040029]; protein ubiquitination [GO:0016567]; transcription elongation-coupled chromatin remodeling [GO:0140673]
|
HULC complex [GO:0033503]; nucleus [GO:0005634]
|
histone H2B C-terminal K residue ubiquitin ligase activity [GO:0140850]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]
|
PF08647;PF13923;
|
3.30.40.10;
|
BRE1 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000305};
| null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase which belongs to the histone H2B ubiquitin ligase complex (HULC) which mediates monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also a prerequisite for H3K4me and H3K79me formation. {ECO:0000269|PubMed:17363370, ECO:0000269|PubMed:17374714}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74627
|
CG1C_SCHPO
|
MSEVIKSVPPGSQNTSQWIISKDQLVFTPSALDGIPLDQEEIQRSKGCNFIINVGLRLKLPQTALATANIYFHRFYLRFSLKNYHYYEVAATCIFLATKVEDSVRKLRDIVINCAKVAQKNSNVLVDEQTKEYWRWRDVILYTEEVLLEALCFDFTVEHPYPYVLSFIKKFVADDKNVTKVAWTYINDSTRSIACLLYSPKTIAAAAFQFALEKNEINLSTTTDGLPVWMEESQVSYEDVKGVLTLIDSLYKKINPSKQALPIDQKNGSHASSVAPGTPSSLASVSTQATPQHQNSSGRTDSFHSLNTETPSKSTVDDQILSTAAQPKKSSDTDKEMETEAS
| null | null |
cell cycle [GO:0007049]; cell division [GO:0051301]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; regulation of transcription by RNA polymerase II [GO:0006357]; signaling [GO:0023052]
|
cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cyclin/CDK positive transcription elongation factor complex [GO:0008024]; cytosol [GO:0005829]; nucleus [GO:0005634]; P-TEFb complex [GO:0070691]
|
cyclin-dependent protein serine/threonine kinase activator activity [GO:0061575]
|
PF02984;PF00134;
|
1.10.472.10;
|
Cyclin family, Cyclin C subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Essential for progression through the whole cell cycle. {ECO:0000269|PubMed:9115279}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74630
|
ATM_SCHPO
|
MTSLNDIVNKLSSSKIKTRSDALQNLRSYIIYSRNGNSLNQEDALIIEKAIKRAFELEWQISANHGKRQISKASQEQKLQDISYLLRTCVESYILLFREPHILALLDIILRHTFTANGSICEVVCLNFSKALRLLLSHSPHLHHLRFSDWQSLVSYCCQAIEKLSIAEETYVSDSEEEPISQKNYQEISIWKSHDVIRVKQEVVELIYVMRSLVQWYAAPINFVSEQLLKFFEFFFYAYTEETDAHLPALQCLFQLCAYAIPNCNDYSASVVLLVFKILINSDKWKRLDLRLQLIQCLAISYPLWSNSETWDPHRSIRSFNLDLLNSSFFSLKNFLNFFGKRSSLSLANFRFHTVEPKNNIAKLYDPRLHLFFSLRHNSFFESYFIYFFLAKLILLKKTVLSLASTEQANKKQKTCSQIEELLLQAELANISASSFSLQLMVIITAISDNLTNDDLLSIQKMSLNFTEKKNELQSWSFFILFNICYNKAYSSMLTTSCKKEILAAASRGLLNSVTSPVCYQILTYFNMYRPLCFASIFPFIKQQFILFNDYSPMLSYEAIDYWKSLYILLNENLFVGQSSFKSVFLKWLKWHLYHLFSKEGELPFFSFTDSSIIIFDLLMMIFYRPLSLSYITTEIRSPFERNLFHLKEAWSPVTLRFPYTTDEICKQSTEGCYPFNSNHTIDCDSLQNVIKMLESSIDEISSASYDKDELDKETPSFEAVMIFSQISFLCGFLNCFIQKKGIHNVTPNNLVIFKNLFPEVLSFVKSNHSYDPIINCISTNLQFTISDEPKHLRYEIGSDLIRSTHFRDSNPLKTLVLYIMDMASKNVFIKPQEFDHDEYFSQEEEDIYRPENLIRNHQILGLMEGSLEQIRNTDLFILQKYIDYFSSHPHDSLINILHLYPIETFCFGMSAIGAYFLDVARTSEPIFYKCLEILAQKILMNYDYERDEVYLMIFIKIFQKCVHSKLQFTDATLKLIVKITKFIEKVFIETKFSSLSGRQTFLKFIFQLSPTSHVYSKFDYQKLISLTLKDSDVCVIYNFVDDLVIFLKKCDKTLIEGFVLPILSIKIEKSLYKGFCYLYLTLKVFLSISSNRSALLYQLLKLANSYETSTIFEPLLRKLHIQSANIKQLFRIYRLEIFWSFVSKDLSNTTNDFLEFPYKPIYFSLSDFLKENSDEIILVLILTKNITLAKLITSRMSVDFSEKYTQLIPVITTYTHLSEVENKKYSLRFNSIDEALDVELLNRSKAFLFCLEMLKEVKELGSTFKSISSTSFKVYSQLTIFANRVSFNNSTAIPFFSTKSVLWYCNRLFQELEGFSSIPSVIDLVLRRLAIQLHFATDEELQVTISFRLCAFLCFSDPFITSNYLVMIVLRIARQLLSIPCTQSLGLGIARFHLKKFKPTDFDYFFQLAEFCMDFLGFCYNTIGTKMEAIQDFYTWFDGYVTALLNFEYEGYGFLRCQINFVRSVMTTKNEWIEVSNKLFERGHFLKRIAMNNYLCLYFWQVLDACPRNVLHSLSLEIWKCYKAYDITEFPDSLKLFFSDIMGWNFFKSPEIADLNHYIPKTDPRLCDTKTYEESKLIIWKLICQKACSLLFKYDILLDSFIEDCIRMFFENGNHQELRKFLNFPKDSIIYDSDFKTLVSEEGSFQWVKLQPTNFDSLSNWTKEETLKLLNMMGKSSTTHSLKLLSTYMVGFSTSIIQYIIHLILLEFDFNGNNKKQKEYVTQLILSGLLNKNTNSIRKTCMNILLYLRRQLGHHALNPFEANYWVPINYSVAASTAYDCHLYEQSLLFLTIHNTKTDELDITLLSDILSQLPCPDAYYGIKRETSFKNILLKAVHEKRSPLAISYLDAANMYRSNEDEGTKMMFSNTLNNAGFFSLNEFYIDSLKANDAIDECSNEVYASAWRMQKWDIPPLSLDNKTTKDCLVFEVLHAVHNYAIYGNYLHLEEYINKKLLLINPNEEPDSLLFYALAYDLKFLIRCNQSQFNCDILQLLKENKQMSSQLHECFQLLLEIRNVLLSLLQSHKQLDLSDDLASFRKYYILELLKISESFLIVDNLQNAFSVAMLSDALYRKFDLADENLKHDIDFLSSKILWQRDEKIDAIGMLSESLSKTNSSIFPSISYAYLGNWLYTTKSEKTELVSKNYFEKSLSHMSHLNAKEKAKIYCMFAQFCDNNYSSPDLTEDFKRMEKLYFEKKNDIQQLERSIVNASNMKEEKMLKNHHSREMSSFIIDEREYLRMSTFRSKMLTQSITHYLKCLSESDENDVLISRCCTMWLSNSHLDELNNSLQHYLQNLPCKKFIPVFYQLAARLMNENSKFQQSLTSICYNVGRNHPYHSLHVLFSLVSNVPEIENLDAGSRYRAVKKILDLLKVNQGLSNLVTKLLCSFENYVSLAEWNPRSKVDSTSFSRFPGYKWFLKDAANYGLPPITMNVKVNDTGDYSNIPTVSSFDDTIHFASGINAPKVITCLGSNGHTYKQLVKGGNDDLRQDAVMEQVFEQVNGFLRSYRKTSQRNLSMRTYKVIPLALKTGVIEWVQDTIPLGEYLDSAHKVYHPKEWSLSTCRKLIAEKQMEDLETRLKVYDLVCRHYRPVFRHFFLESYADPVQWFTTQTNYARSTAVASVLGHVLGLGDRHGQNILIDKTSGEVIHIDLGIAFEQGKKLPVPECVPFRLTRDVVDGMGITGVEGVFRRCMEFTLETLRREEDSLLSVLEVLRYDPLFSWLISPLRRMKKQKMQLENFNQPESGNITTDASRDPKIQRNNVSGESEAERAILKVRQKLSSTLSVEASVGELIRIAQDPSYLALMFCGWSAFQ
|
2.7.11.1
| null |
DNA damage checkpoint signaling [GO:0000077]; DNA repair [GO:0006281]; mitotic DNA damage checkpoint signaling [GO:0044773]; negative regulation of TORC1 signaling [GO:1904262]; phosphorylation [GO:0016310]; positive regulation of initiation of premeiotic DNA replication [GO:1904514]; spatial regulation of meiotic DNA double-strand break formation involved in reciprocal meiotic recombination [GO:0062209]; telomere maintenance [GO:0000723]
|
chromosome, telomeric region [GO:0000781]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; histone H2AS121 kinase activity [GO:0072371]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF02259;PF02260;PF00454;PF11640;
|
1.10.1070.11;
|
PI3/PI4-kinase family, ATM subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, telomere {ECO:0000250}. Note=Localizes to nuclear DNA repair foci with other DNA repair proteins in response to DNA double strand breaks. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates histone H2A to form H2AS128ph (gamma-H2A) at sites of DNA damage, involved in the regulation of DNA damage response mechanism. Undirectly involved in the phosphorylation of rad32 which is necessary for its telomere function. Required for the control of telomere length and genome stability. {ECO:0000269|PubMed:10430579, ECO:0000269|PubMed:12196391, ECO:0000269|PubMed:15226425, ECO:0000269|PubMed:9771717}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74641
|
INUA_ASPNG
|
MLNPKVAYMVWMTCLGLMLPSQAQSNDYRPSYHFTPDQYWMNEPNGLIKIGSTWHLFFQHNPTANVWGNICWGHATSTDLMHWAHKPTAIADENGVEAFTGTAYYDPNNTSGLGDSANPPYLAWFTGYTTSSQTQDQRLAFSVDNGATWTKFQGNPIISTSQEAPHDITGGLESRDPKVFFHRQSGNWIMVLAHGGQDKLSFWTSADTINWTWQSDLKSTSINGLSSDITGWEVPDMFELPVEGTEETTWVVMMTPAEGSPAGGNGVLAITGSFDGKSFTADPVDASTMWLDNGRDFDGALSWVNVPASDGRRIIAAVMNSYGSNPPTTTWKGMLSFPRTLSLKKVGTQQHFVQQPITELDTISTSLQTLANQTITPGQTLLSSIRGTALDVRVAFYPDAGSVLSLAVRKGASEQTVINYTQSDATLSVDRTESGDISYDPAAGGVHTAKLEEDGTGLVSIRVLVDTCSVEVFGGQGEAVISDLIFPSDSSDGLALEVTGGNAVLQSVDVRSVSLE
|
3.2.1.7
| null |
polysaccharide catabolic process [GO:0000272]; sucrose catabolic process [GO:0005987]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]
|
inulinase activity [GO:0051670]; sucrose alpha-glucosidase activity [GO:0004575]
|
PF08244;PF00251;
| null |
Glycosyl hydrolase 32 family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (2->1)-beta-D-fructosidic linkages in inulin.; EC=3.2.1.7; Evidence={ECO:0000269|PubMed:15135402};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.57 mM for inulin {ECO:0000269|PubMed:15135402};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5. {ECO:0000269|PubMed:15135402};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:15135402};
|
FUNCTION: Endo-inulinase involved in utilization of the plant storage polymer inulin, consisting of fructooligosaccharides with a degree of polymerization (DP) value from 2 to 60. {ECO:0000269|PubMed:15135402}.
|
Aspergillus niger
|
O74653
|
POB1_SCHPO
|
MASQRFVIALHSFPGKSSDELPLVEGRKYLLIKMDEEFGDGWWEGEDEQGNRGIFPASHVELISDERSDSSDSRRGKEDFSISTAEVTRSSLSSSRSTSSRSDKDSEKLYSNNSLSSSHSSILNGPLDSLSKPSVPSNFNSMFPSSKQEGPSPLLDNQPSSDLSNFNTIDADYNNASASTSAPATSASLKKVLSAEDSVRETITDIETALQNMSTSASRTPNDSSPLPYIENRPASSLAVSEKIQNVPNWSTEEVVEWLMNAGLGSVAPNFAENEITGEILLGLDSNVLKELNITSFGKRFEVLRKIQQLKDSYEQSLYEEYPQFAEPISVSQSSDSSSSIPKKSNDEAGGSPSKSSPTRPGFNDYVNRPTSVMPSLSNMIVSPDLDSSPSTDWNQYVIPPLATPSSRNSKSTQSAVPENVSRFDSNEPSATSPILKRSSPTDSISQNSGLPSRLTEPISSPSTSSIDVDKEGTSFPGLPYHSSKGNLYAPQPSSNVPTKFTGGASESSSVPPRPIPSAMKGKAPASAISIEALEELDPPKITTIDGESPSSISSRLPSSNLEQGSSSSVTKSPESMPDPSAKASSPVTSKGVSINEKSAVNNYATPLSKPQPKDTKGSKLGNTFVAPSPAASLPASPPVGTELKTRPTLRSVASSPLNKEPIGKRKSKRDIFGRQKVLPTGISEGLSNIPAKEAIKTADCHGWMRKRSDRYGVWKSRYFVLKGTRLSYYHSLNDASEKGLIDMTSHRVTKTDDIVLSGGKTAIKLIPPAPGAAKAAVMFTPPKVHYFTCENNEELHRWSSAFLKATVERDMSVPVLTTSRMPTISLSKAKELRTRPPSLLIDDENEANLTSSIGLKKNAKQKNKKSSKQK
| null | null |
endosome organization [GO:0007032]; exocytosis [GO:0006887]; receptor recycling [GO:0001881]; retrograde transport, endosome to Golgi [GO:0042147]
|
cell cortex of cell tip [GO:0051285]; cell division site [GO:0032153]; cell tip [GO:0051286]; cytosol [GO:0005829]; early endosome [GO:0005769]; medial cortex [GO:0031097]; membrane [GO:0016020]; recycling endosome [GO:0055037]; trans-Golgi network [GO:0005802]
|
lipid binding [GO:0008289]
|
PF00169;PF07647;PF00018;
|
2.30.29.30;2.30.30.40;1.10.150.50;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10436025}. Membrane {ECO:0000269|PubMed:10436025}; Peripheral membrane protein {ECO:0000269|PubMed:10436025}. Note=Membrane-associated at the cell tips during interphase.
| null | null | null | null | null |
FUNCTION: Has a role in cell elongation and separation. {ECO:0000269|PubMed:10436025}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74700
|
TIM9_YEAST
|
MDALNSKEQQEFQKVVEQKQMKDFMRLYSNLVERCFTDCVNDFTTSKLTNKEQTCIMKCSEKFLKHSERVGQRFQEQNAALGQGLGR
| null | null |
protein insertion into mitochondrial inner membrane [GO:0045039]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial intermembrane space protein transporter complex [GO:0042719]; mitochondrion [GO:0005739]; TIM22 mitochondrial import inner membrane insertion complex [GO:0042721]
|
metal ion binding [GO:0046872]; protein transporter activity [GO:0140318]; unfolded protein binding [GO:0051082]
|
PF02953;
|
1.10.287.810;
|
Small Tim family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:9822593, ECO:0000269|PubMed:9889188}; Peripheral membrane protein {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:9822593, ECO:0000269|PubMed:9889188}; Intermembrane side {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:9822593, ECO:0000269|PubMed:9889188}. Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289}.
| null | null | null | null | null |
FUNCTION: Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. Compared to TIM10, it may have a strong structural role. {ECO:0000269|PubMed:10369662, ECO:0000269|PubMed:10995434, ECO:0000269|PubMed:11483513, ECO:0000269|PubMed:11509656, ECO:0000269|PubMed:12138093, ECO:0000269|PubMed:12391147, ECO:0000269|PubMed:14978039, ECO:0000269|PubMed:16039669, ECO:0000269|PubMed:9822593, ECO:0000269|PubMed:9889188}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
O74718
|
ERF3_SCHPO
|
MASNQPNNGEQDEQLAKQTSKLSMSAKAPTFTPKAAPFIPSFQRPGFVPVNNIAGGYPYAQYTGQGQNSNSPHPTKSYQQYYQKPTGNTVDEDKSRVPDFSKKKSFVPPKPAIPKGKVLSLGGNTSAPKSTKPISISLGGTKAPTTTKPAAPAAQSKTETPAPKVTSESTKKETAAPPPQETPTKSADAELAKTPSAPAAALKKAAEAAEPATVTEDATDLQNEVDQELLKDMYGKEHVNIVFIGHVDAGKSTLGGNILFLTGMVDKRTMEKIEREAKEAGKESWYLSWALDSTSEEREKGKTVEVGRAYFETEHRRFSLLDAPGHKGYVTNMINGASQADIGVLVISARRGEFEAGFERGGQTREHAVLARTQGINHLVVVINKMDEPSVQWSEERYKECVDKLSMFLRRVAGYNSKTDVKYMPVSAYTGQNVKDRVDSSVCPWYQGPSLLEYLDSMTHLERKVNAPFIMPIASKYKDLGTILEGKIEAGSIKKNSNVLVMPINQTLEVTAIYDEADEEISSSICGDQVRLRVRGDDSDVQTGYVLTSTKNPVHATTRFIAQIAILELPSILTTGYSCVMHIHTAVEEVSFAKLLHKLDKTNRKSKKPPMFATKGMKIIAELETQTPVCMERFEDYQYMGRFTLRDQGTTVAVGKVVKILD
|
3.6.5.-
| null |
cytoplasmic translational termination [GO:0002184]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; translation [GO:0006412]
|
cytosol [GO:0005829]; translation release factor complex [GO:0018444]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; magnesium ion binding [GO:0000287]; translation release factor activity [GO:0003747]
|
PF00009;PF03143;
|
3.40.50.300;2.40.30.10;
|
TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, ERF3 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000269|PubMed:19417105}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000269|PubMed:19417105};
| null | null | null | null |
FUNCTION: GTPase component of the eRF1-eRF3-GTP ternary complex, a ternary complex that mediates translation termination in response to the termination codons (PubMed:19417105). Sup35/eRF3 mediates sup45/ERF1 delivery to stop codons: The eRF1-eRF3-GTP complex binds to a stop codon in the ribosomal A-site (PubMed:19417105). GTP hydrolysis by sup35/eRF3 induces a conformational change that leads to its dissociation, permitting sup45/eRF1 to accommodate fully in the A-site (PubMed:19417105). {ECO:0000269|PubMed:19417105}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74736
|
ING2_SCHPO
|
MGTSGIEIFAALNDFTDAIVSVPESVCGKFTSLKEIDAQVRDIRQNVIQEIGVVLKNEKNDELSGEERCERLQKTLKEILPYSDSKICLATDAMNNIKSCIDRLDAGFEYVELEIPQQLRLGYPDDRALMNYHSTVTPQTSERRRETRRHQNNQHSQQYSSQERSSSYNNFEDASSPQSSYHTPTKRRKNAVPRKSSSPPLSSTKHAPQSTERRPVRRSESRLKQTNGEPLVKHDTLDSSDISREGEQLYCYCQQVSYGQMIGCDNENCKREWFHLPCVGLVEPPKGIWYCKECEELAKSSESRQ
| null | null |
DNA repair-dependent chromatin remodeling [GO:0140861]; regulation of DNA-templated transcription [GO:0006355]
|
cytosol [GO:0005829]; NuA4 histone acetyltransferase complex [GO:0035267]; nucleus [GO:0005634]; Rpd3L complex [GO:0033698]
|
histone acetyltransferase activity [GO:0004402]; metal ion binding [GO:0046872]; methylated histone binding [GO:0035064]
|
PF12998;
|
6.10.140.1740;3.30.40.10;
|
ING family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Component of the clr6 histone deacetylase complex I' responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Has a role in silencing of mating type genes. {ECO:0000269|PubMed:10805724, ECO:0000269|PubMed:17450151}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74739
|
PNG1_SCHPO
|
MDFHAISQRFIDMMRSKNSQNASQPPETYPFYHEVRQMSQHPWMYEDPELQDYALSILPLDKLFQDASELEKEGDGSWGYQDYVIQALLKWFKREFFVWVNQPPCEKCGGETHMTGNGPPNEEEKWNGVRNVELYQCNVCGHNQRFPRYNRIRALLDSRKGRCGEWANCFTFLCRALGSRARWIWNAEDHVWTEVYSNKQQRWVHVDSGEESFDEPLIYEQGWGKKMSYCLGFGIDSVRDVSHRYIRHPENGLPRDRCPESVLQQALHEINIEFRSRLTDSERKALEEEDKREKDELDGYMRPVSQATPTNTDLPARQTGNVEWKEKRGEAGK
|
3.5.1.52
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
|
ERAD pathway [GO:0036503]; glycoprotein catabolic process [GO:0006516]; protein quality control for misfolded or incompletely synthesized proteins [GO:0006515]
|
cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]
|
metal ion binding [GO:0046872]; misfolded protein binding [GO:0051787]; peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity [GO:0000224]
|
PF01841;
|
2.20.25.10;3.10.620.30;
|
Transglutaminase-like superfamily, PNGase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue.; EC=3.5.1.52;
| null | null | null | null |
FUNCTION: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins (By similarity). {ECO:0000250, ECO:0000269|PubMed:18279662}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74752
|
MAS5_SCHPO
|
MVKETKLYEVLNVDVTASQAELKKAYRKLALKYHPDKNPNAGDKFKEISRAYEILADEEKRATYDRFGEEGLQGGGADGGMSADDLFASFFGGGMFGGGMPRGPRKGKDLVHTIKVTLEDLYRGKTTKLALQKKVICPKCSGRGGKEGSVKSCASCNGSGVKFITRAMGPMIQRMQMTCPDCNGAGETIRDEDRCKECDGAKVISQRKILTVHVEKGMHNGQKIVFKEEGEQAPGIIPGDVIFVIDQKEHPRFKRSGDHLFYEAHVDLLTALAGGQIVVEHLDDRWLTIPIIPGECIRPNELKVLPGQGMLSQRHHQPGNLYIRFHVDFPEPNFATPEQLALLEKALPPRKIESAPKNAHTEECVLATVDPTEKVRIDNNVDPTTATSMDEDEDEEGGHPGVQCAQQ
| null | null |
cellular response to heat [GO:0034605]; cytoplasm protein quality control [GO:0140455]; protein aggregate center assembly [GO:0140454]; protein refolding [GO:0042026]; protein transport [GO:0015031]; regulatory ncRNA-mediated heterochromatin formation [GO:0031048]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; protein aggregate center [GO:0140453]
|
ATP binding [GO:0005524]; Hsp70 protein binding [GO:0030544]; metal ion binding [GO:0046872]; protein sequestering activity [GO:0140311]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082]
|
PF00226;PF01556;PF00684;
|
1.10.287.110;2.10.230.10;2.60.260.20;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Probably involved in mitochondrial protein import (By similarity). Plays a role in microtubule cytoskeleton organization. {ECO:0000250, ECO:0000269|PubMed:15797925}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74757
|
HRD1_SCHPO
|
MKFILYVLASLVLFGLSVLLSLYSSANVYSATVMISQSPVHITIGLNVCLCLFFAIANALKTLLFGSLQTFELELLYEQFWITLTEIMLAITVFREAISISFFMLLSTLMFARVFHSICSFRTERLQIQLTDQRFHIFSRLTCAYFVLSILDASLIYLCFTSEHLGDKSTRMLFVCEFSVLLLNLTIEASKLCIYLYEARHLDQVWDEKSTYLFRLEVCRDGLRLLAYSLLFMYQFPYVSVPIYSIRQMYTCFYSLFRRIREHARFRQATRDMNAMYPTATEEQLTNSDRTCTICREEMFHPDHPPENTDEMEPLPRGLDMTPKRLPCGHILHFHCLRNWLERQQTCPICRRSVIGNQSSPTGIPASPNVRATQIATQVPNPQNTPTTTAVPGITNSSNQGDPQASTFNGVPNANSSGFAAHTQDLSSVIPRRIALRDGWTMLPIPGTRRIPTYSQSTSTTNPSATPTTGDPSNSTYGGPQTFPNSGNNPNFNRGIAGIVPPGWRLVSSNTQSLSTNSAMTSLYQNASSADNNLGSSLPNVVPLSRGLTQSNETSNTFPAASSNISSQLRELHTKIDELRETVSNFRADYNSIRTSLNQLEAASGINERIQTTSADSLLNSNGMSGTEGFENTQTSITTNDNQSSILTSSDQTSPFATDEDRQNSRNVQLETVDENF
|
2.3.2.27
| null |
ERAD pathway [GO:0036503]; protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
cell cortex [GO:0005938]; cytoplasm [GO:0005737]; endomembrane system [GO:0012505]; Hrd1p ubiquitin ligase complex [GO:0000836]
|
ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]
|
PF12678;
|
3.30.40.10;
|
HRD1 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27;
| null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated E2 ligases, and transfers it to substrates promoting their degradation. Mediates the degradation of endoplasmic reticulum proteins (ERQC), also called ER-associated degradation (ERAD). Component of the hrd1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M) (By similarity). Together with ubc7, required for the degradation of the transcription factor sre1 precursor in the absence of its binding partner scp1. {ECO:0000250, ECO:0000269|PubMed:19520858}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74760
|
EIF3A_SCHPO
|
MAPPQGKPENVLRLADELIALDQHSSALQSLHETIVLKRSRNAQGFSLEPIMMRFIELCVHLRKGKIAKEGLYTYKNAVQNTSVTAIENVVKHFIELANKRVQEAQEKADKISVEYVDDLEATETPESIMMSLVSGDLSKSRTDRALVTPWLKFLWDAYRTVLDILRNNARLEVMYQLIANSAFQFCLKYQRKTEFRRLCELLRSHLGNASKFSNAPHSINLNDAETMQRHLDMRFSQLNVAVELELWQEAFRSIEDIHSLLTFSKRAPAAVMLGNYYRKLIKIFLVCDNYLLHAAAWNRYFTFTNVQKPATANFVILSALSIPIIDANKLSGPSIEAEDAKSKNARLALLLNLSKTPTRETLIKDAISRGVLSFCDQAIRDLYQILEVEFHPLSICKKLQPIIKRLAESNDTAQYIRPLQQVILTRLFQQLSQVYDSISLKYVMDLATFEEPYDFNPGQIEKFIMNGNKKGAFSIRLNHIENSISFSSDLFSNPIKSSDSVSLQSTPSELITSQLTRIAKSLSSVLMRFDTDFCLLRKQQAEAAYERAQAGVEQERKAVIAQRSLLELRRGQADTLATQREAELAAQRALKQKQESEAESLRVQEEINKRNAERIRREKEAIRINEAKKLAEELKAKGGLEVNAEDLEHLDADKLRAMQIEQVEKQNKSMNERLRVIGKRIDHLERAYRREAIPLWEEDAKQQAEHDREIFYEREKQRKEVQERKHEQAIKDKKAFAQFASYIHAYKQNIDDERDKAYQEAYAKAKNVIDAERERQRKEIFEQKLAEAIREAEEEAARAAEEEANRELHEQEEAQKRAIEERTRAAREAKEREQREMAEKLERQRRIQQERDEEISRKLAEKAAARRANIGASSPSPGAWRRGGASAGGVSRDSPRYSRGGYSRGSVPPRETLAPSKGAYVPPSRRNQQQQ
| null | null |
formation of cytoplasmic translation initiation complex [GO:0001732]; translation reinitiation [GO:0002188]
|
cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; eukaryotic translation initiation factor 3 complex, eIF3e [GO:0071540]; eukaryotic translation initiation factor 3 complex, eIF3m [GO:0071541]; multi-eIF complex [GO:0043614]
|
mRNA binding [GO:0003729]; translation initiation factor activity [GO:0003743]
| null |
1.25.40.860;4.10.860.10;
|
EIF-3 subunit A family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
| null | null | null | null | null |
FUNCTION: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. {ECO:0000255|HAMAP-Rule:MF_03000}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74774
|
HBS1_SCHPO
|
MSRHRDVKNLDLDDYELDEEPGEEELTEEQEEEFRSAVATVRETLLGVPISEKEIADTVWYYYFDVEKSVNYLLQKASSKAGAKEKQNTDSQKEKKQNKSKEALADAKDPLDESSNGIKNLSLNKNDEPAFQTNGEVKMKNSSESDNQPEKKKIKKQNPTDLVSVPEIFEQSNPKPVVHLVVTGHVDSGKSTMLGRIMFELGEINSRSMQKLHNEAANSGKGSFSYAWLLDTTEEERARGVTMDVASTTFESDKKIYEIGDAPGHRDFISGMIAGASSADFAVLVVDSSQNNFERGFLENGQTREHAYLLRALGISEIVVSVNKLDLMSWSEDRFQEIKNIVSDFLIKMVGFKTSNVHFVPISAISGTNLIQKDSSDLYKWYKGPTLLSALDQLVPPEKPYRKPLRLSIDDVYRSPRSVTVTGRVEAGNVQVNQVLYDVSSQEDAYVKNVIRNSDPSSTWAVAGDTVTLQLADIEVNQLRPGDILSNYENPVRRVRSFVAEIQTFDIHGPILSGSTLVLHLGRTVTSVSLKIVTVNNKRSRHIASRKRALVRISFLDGLFPLCLAEECPALGRFILRRSGDTVAAGIVKELC
|
3.6.5.-
| null |
cytoplasmic translational termination [GO:0002184]; endoplasmic reticulum unfolded protein response [GO:0030968]; nuclear-transcribed mRNA catabolic process, no-go decay [GO:0070966]; translation [GO:0006412]
|
cytosol [GO:0005829]; Dom34-Hbs1 complex [GO:1990533]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; translation elongation factor activity [GO:0003746]; translation release factor activity [GO:0003747]
|
PF00009;PF08938;
|
3.40.50.300;2.40.30.10;
|
TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P32769}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P32769};
| null | null | null | null |
FUNCTION: GTPase component of the Dom34-Hbs1 complex, a complex that recognizes stalled ribosomes and triggers the No-Go Decay (NGD) pathway (PubMed:20890290). The Dom34-Hbs1 complex recognizes ribosomes stalled at the 3' end of an mRNA and engages stalled ribosomes by destabilizing mRNA in the mRNA channel (By similarity). Following ribosome-binding, the Pelota-HBS1L complex promotes the disassembly of stalled ribosomes, followed by degradation of damaged mRNAs as part of the NGD pathway (By similarity). {ECO:0000250|UniProtKB:P32769, ECO:0000269|PubMed:20890290}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74791
|
GRN1_SCHPO
|
MVSLKKKSKRRTTRLRSRIEKKAAESKRKQKRADKKNPQWKSRIPKDPGIPNSFPYKDKILAEIEEQKRIREEEKLARRASGQVDAAMEEEDAVDENGSLMISKIAEAAQASNPDDEEEFVMEEDNLGEAPLLVDSESYEASVKADTSRKAYDKEFKKVVEASDVILYVLDARDPEGTRSKDVERQVLASSAEEKRLIFVINKIDLVPSEVLNKWVTYLRNFFPTIPMRSASGSGNSNLKHQSASASSTISNLLKSLKSYSAKKKLKSSLTVGVIGYPNVGKSSVINALVNRSANGRSAPCPAGNVAGMTTSLREVKLDNKLRLVDSPGIVFPSSDSKDDLYRLVMLNAVSSTKVDDPVAVASYILQFLSRVPGQLERMFQRYELPPLLNTSDIDTATDFLVNIARKRGRLGRGGIPNLNAAANIVINDWHAGRIEWWAEPEVINEKNSSEVQDTQIVTEWAKEFDLNDF
| null | null |
protein transport [GO:0015031]; rRNA processing [GO:0006364]
|
nucleolus [GO:0005730]; nucleus [GO:0005634]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; RNA binding [GO:0003723]
|
PF08701;PF01926;
|
1.10.1580.10;3.40.50.300;
|
TRAFAC class YlqF/YawG GTPase family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16251348, ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Required for optimal growth. Required for normal processing of ribosomal pre-rRNA. Required for nuclear export of ribosomal protein rpl2501. {ECO:0000269|PubMed:16251348}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74803
|
RHP23_SCHPO
|
MNLTFKNLQQQKFVISDVSADTKISELKEKIQTQQNYEVERQKLIYSGRILADDKTVGEYNIKEQDFIVCMVSRPKTSTSTPKSAASPAPNPPASVPEKKVEAPSSTVAESTSTTQTVAAAAPSNPDTTATSEAPIDANTLAVGAQRNVAVENMVEMGYERSEVERAMRAAFNNPDRAVEYLLTGIPEDILNRQREESAAALAAQQQQSEALAPTSTGQPANLFEQAALSENENQEQPSNTVGDDPLGFLRSIPQFQQLRQIVQQNPQMLETILQQIGQGDPALAQAITQNPEAFLQLLAEGAEGESALPSGGIQIQITQEESESIDRLCQLGFDRNIVIQAYLACDKNEELAANYLFEHGHESEDEP
| null | null |
ERAD pathway [GO:0036503]; nucleotide-excision repair [GO:0006289]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]
|
cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
damaged DNA binding [GO:0003684]; polyubiquitin modification-dependent protein binding [GO:0031593]; proteasome binding [GO:0070628]; ubiquitin binding [GO:0043130]
|
PF00627;PF00240;PF09280;
|
1.10.8.10;1.10.10.540;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11788722}.
| null | null | null | null | null |
FUNCTION: Involved in postreplication repair of UV-damaged DNA. Postreplication repair functions in gap-filling of a daughter strand on replication of damaged DNA. {ECO:0000269|PubMed:12560082}.; FUNCTION: Protects ubiquitin chains against dissambly by deubiquitinating enzymes thereby promoting protein degradation. {ECO:0000269|PubMed:12560082}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74804
|
EST1_SCHPO
|
MSQQLSSNEICEEQGKLVKALCEAAQGGFKHDLYEKIIAIEIEVEKKLLNRLKSIQTNTFERPDIIWSCCHYKIIQHFRSRFREIHPRHVVEKKKTKKVFFKFLKTCAIFYQTCISELISKFQLDSYRPFFCKWTSSATVSSTISNDEMSSIPEASYSRNHMEALECVYNCFIYLGDMARYSSTCLKKRGAYDRALGFYDLAHRTLPGNGMHRNQIAVVWASDECIVESIYWFSSALCSEDPPKSALLNLLKQLIAFYRRCFAVHFEFVSPMMILLFIISDCCIHSLKEIQPFKCPSIMVKDLENSLLQSNIRNVGYEKKNLYYISSAFSNLLHCRYFNCNDRLRSFYYRFSSWLFHQTLACAKEVESERAPTSYLTSCLPSIKVILARVLESSPAFGFIERNELEQLSYHFRICEKFFKESSENKMLNLFEDYNEFGLCKSFICLFKRLNEDIIGPKLNINPPDYTTHPFSESIKRFYQISKILNLLLS
| null | null |
nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; telomere maintenance via telomerase [GO:0007004]; telomere-telomerase complex assembly [GO:1905324]
|
chromosome, telomeric repeat region [GO:0140445]; nuclear periphery [GO:0034399]; nucleus [GO:0005634]; telomerase holoenzyme complex [GO:0005697]
|
single-stranded telomeric DNA binding [GO:0043047]; telomerase RNA binding [GO:0070034]
|
PF10374;PF10373;
|
1.25.40.10;
|
EST1 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12676088}. Chromosome, telomere {ECO:0000305|PubMed:12676088}.
| null | null | null | null | null |
FUNCTION: Directly involved in telomere replication. Associates with telomerase and during its interaction with trt1, telomerase activity is promoted. {ECO:0000269|PubMed:12676088}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74805
|
MYO51_SCHPO
|
MSHARLSVGSECWVSNNNGHWDAARLIEIKDNGGGKVVATVAKSSGVLETVNYQQLQNRNIGQSESPSDLTNLPYLNEPSVLHALHNRYNNKQIYTYSGIVLVSINPYQNLPEFYNDNLIKHFHKDPEAAKVPHLYSIASSCYHALTTDSKNQTIIVSGESGAGKTVAAKYIMRYLTSVQGVDHNGVVKRSVENQVLATNPIMEAFGNAKTIRNDNSSRFGKYVTISFDENLLITGANVNTYLLERSRVVSLLKGERNYHIFYQLITGCTEEQRDKWFLESASSFNYLSQGNCDEISGVDDSNDFTITCRALSTIGISESRQEDVFCLLAALLHLGNIEVCATRNEAQIQPGDGYLQKAALLLGVDSSTLAKWIVKRQLKTRSETIITSSTLEHAISIRDSVAKYLYSALFLWIVHMINASLDHNKVKRAAYKYIGVVDIYGFEHFEKNSMEQFCINYANEKLQQEFNKHVFKLEQEEYVKEGLDWRLIEYSDNQGCISLIEDKLGILSLLDEECRLPSGNHQSFLQKLNNQLPTKHSQFYKKSRFNDGSFMVKHYALDVSYQVHDFLAKNSDAIPDEFISLLQNSKNEFITYLLDFYMQLVSSQNKNPRKTAISRKPTLSSMFKSSLSQLMTTVSSTNVHYIRCIKPNEEKLPWTFSPPMVLSQLRACGVFETIRISSLGFPARFSYEEFAHRFRILLSSKEWEEDNKKLTLNIVNSVIPHDNLNFQVGRSKIFFRSNVIGNFEEAHRATCSKSTVLLQSAIRGFFTRKEYQRTVKFIIKLQSVIMGWLTRQRFEREKIERAAILIQAHWRSYIQRKRYLSLIKCAIVIQSIVRKNIAYSRYINELRESSATLLAKFWRAYNARKTFRGLKKSVIALQCVSRSVLTRRYLRRLQDSAGRTSILYEKQKNLQASITEVSKQLKSNSKKVTVLRNKLNILNNSLSKWKCLIKKPSDFSEPVSMDFTSNDEQLVQLLQAESKLRQASQQLYMAAKKSELGFVQSQTARENLSNYYQALQMTVSEKFEYDTEQLPSRVLFYAMDRYFSIHKKLKQLLELVGVENASLLPNEVVNKQTKDLLYEKRVVFLKQIKQALTVSSLFNAVGYKDGVMRLLETDQNSLLFAGVVNFLIFAGISLDLKTQISEFLSQLCSYFTKIVDGTVIENDKTLDFYEKPLQAVLYWFATLHKIRSFLVHLLSINSHGKQSVVEDLWNPLILKFSKHFSNLENSFHSLVQKLLSCCTEGSINALLNSKCLPEFIDAADENTTPTGMNIYELIDRMNLIHKLLISSALQPNLLELTISHMLQHIGQRAFQTLIHGRSPYTWKSASQVSYNASLLINWCHQKGISYVNSSLLPLMQSPLVFCLRKNDANDLDVILSVCNLLSPFEVVCLLNRYQPCAGENPLPKSFSKAVEALSCKYKQSGFTNGKITNTNGHAIPIAASKNPLLSLENNHIYEELRLSELINLLAKATL
| null | null |
actin filament bundle organization [GO:0061572]; actin filament organization [GO:0007015]; actomyosin contractile ring assembly actin filament bundle convergence [GO:0071520]; formin-nucleated actin cable assembly [GO:0070649]; mitotic actomyosin contractile ring assembly [GO:1903475]; protein transport to mating projection actin fusion focus [GO:1904601]; vesicle transport along actin filament [GO:0030050]
|
actin cytoskeleton [GO:0015629]; cell division site [GO:0032153]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; formin-nucleated actin cable [GO:0070648]; mating projection actin fusion focus [GO:1990819]; membrane [GO:0016020]; mitotic actomyosin contractile ring [GO:0110085]; mitotic actomyosin contractile ring, proximal layer [GO:0120104]; myosin complex [GO:0016459]; vesicle [GO:0031982]
|
actin filament binding [GO:0051015]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]
|
PF01843;PF00612;PF00063;
|
1.10.10.820;1.20.5.190;1.20.58.530;6.20.240.20;3.40.850.10;1.20.120.720;
|
TRAFAC class myosin-kinesin ATPase superfamily, Myosin family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11112691}. Note=Component of the cytokinetic actin ring (CAR).
| null | null | null | null | null |
FUNCTION: Involved in cytokinesis. {ECO:0000269|PubMed:11112691}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74808
|
CLR1_SCHPO
|
MAEPDISSSETLTELQQLRLLYFFCFYHAAPFNVKTLVHSLIPPGALSYLLSTYDILRPWLMALRVREGPVNDISTIVQLYEEIVKTGFFINPPPFESYSQTLVARITTLGRPKLQVQQEAQSEVYQRASTNTQQQVSNVSHGNFKPNSSVNTEPNTSILSNSKYAGIKPFDFQSSSQNPGLVCEQKTFYQHQFRPFSNLPSNKSSPVKHVSPNVKNNSKKTASSVNSNHSSIPSSITKSNISSLDVYGSEKLISSGSQQPGHGMVQTTSDKVNASASLYDRSPSKKDITSSRNTSSYNLGSMRNPSTLKNAAHANPFEGLRFQGSSAVLKEGLNSTVKKTFFDNLNSEKVCPSVSPFLTPDNIASSILYSTASFSRSKPDRPRLNLSLELKLMQNELNKGQLKKQFKGDLRNLADWNNLSLVSSKFPSLPITNLRPDGSFLKHRRFNEEIAYNRQTLEKAIKQLDLSPDKVIQLREQNGVAVNGRVCYPTRNKHSEISAQSSSSLGVTKSLASEVYSSSTVDTISKLNTDKDNYLIKSKKEPIQQKSVSSETTLVKPSSTSSYIDTTNNVLKTNSSFKSSGLTSGPRNEKELLPEGIPTSHNNSETQAQTADVSNIAASADGIYNSDQEKPPEKLDVTKRAFGREIENSNEKELLTSTFLSPSAESQVCLAEIKTIRPGLVPKKQFSVDQNNVISDNTDCSLPKPSNSKLSSISSDGDASSNRMAVPDKSPFVHAAPNSKALTKDSFSTHISVSSLLHSDNEISPIDSTRKDYFTSKDSNLQTLKEDASSTKQAKDSGTNDFDKLISGNDVSKNNSGEEQSRSALKPLISGKLSSCESINLTKDISTVKRKEYFGIESTSSKQPFHDTGSIKIPAKRSFDTIDKDFRSSNIPFADKIKEDGGDKNVISSIHITTELPKSMPVEVPTNAGAQSDQSNVVDSESLNLRENISTSVADVSLSQAGNEAVLSKKACKPLVLIDPFEEKVLKAFNMLSKGYAEYRCQWEGCLANLHSLENFIKHVLLLHHPKSCSVVKCLWASCDMVLPSEEFEMHLRGHLNNIRLNCEVSNCKKCFSNYEDMFKHLQHSHLPFKFTPESFIKIRNGNVKEEARRTRNAYTQKSGEVECFMETCTPIAKPAPANWYPVPPPGFNSSLLSRLTQSNQSKDKIIAALAKRNVYKSFAGLYDSKGKNDNTGYDFDSNYARVGRHGSFILPVSKSVPTPSLLIEGSIVQRKNIKIE
| null | null |
chromatin organization [GO:0006325]; heterochromatin formation [GO:0031507]; silent mating-type cassette heterochromatin formation [GO:0030466]
|
chromosome, subtelomeric region [GO:0099115]; mating-type region heterochromatin [GO:0031934]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]; rDNA heterochromatin [GO:0033553]; SHREC complex [GO:0070824]
|
metal ion binding [GO:0046872]
| null | null | null | null |
SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere. Chromosome, telomere. Note=Associates with major heterochromatin, centromeres, sub-telomeres, rDNA and the mat locus.
| null | null | null | null | null |
FUNCTION: Regulates silencing of the mat2 and mat3 loci. Organizes the chromatin structure of the mating-type region where it also participates in establishing the 'cold spot' for recombination. Required for proper positioning of nucleosomes at heterochromatic loci and for transcriptional gene silencing (TGS) function of the Snf2/Hdac-containing repressor complex (SHREC). {ECO:0000269|PubMed:1644273, ECO:0000269|PubMed:17289569}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74833
|
DNLI4_SCHPO
|
MDEAKETVFTKPQNHSSTLEFYDFVTTLLEPLSRIGKTRKSKTSNLDPYELKRKILLDYFNKWRQHVGPDLYPLLRLMLPDLDRERGSYGFKEFGLGKLFIRAMHLSPTSEDAKSLKNWRGSESKHTGDFSTMLQDILQRRAYRTFPGAFTVGDVNALLDQLADASSEDTRVNILEQFYRSLSPLELRWLIPILLKVRKYGTSEKFILSVFHPDAARLYRLCSSLKRICWELYDPSRSLDETETDVEVFSCFQPQLANFKKKDLHQTLEAMGNKPFWIEEKLDGERIQLHMSSGKFQFYSRNARSYTYAYGSSYFDEQSRLTQYIIGAFDKRISQIILDGEMVTWDPVLETVIPYGSLRSIFEDSSSHSSYSPYYVVFDILYLNGKSLVKYSLESRRRILEKVIVRESHRMSILPYKVGSTIEDIEAELRNVIQEGSEGLVIKKPSGSYHLGERMDDWIKVKPYYLQGFGEDLDCLILGGYFGRGKQSGKINSFLCGLRMDYTPKDHSEKFQSFVRVGGGFTYFDRDIIRKETEGKWLPWSSDALEYMELAGTKQDFEKPDMWIHPKDSLVLQIKAAEVVVSNRFKTNYTLRFPRLEKVRLDRSWKDALTINEFFTLKNAVEKQDNVSFHVNKKRKVSQKREKQKKFLYDEPTFKKEASPHSDVLKNLHFVVLPPTELHETKAGLQQIIIENGGLIHQGVGNFGKERLFLVADRVSTRVSIERSKNMCTIIRSQWVMDSVNNQRLMPQWSYLLFSKDEKYSWKTALESLSAKSLSNLLVELKQLDLSKEYSKISDDTSILNLTISKEEASFVGAFPFLKFTVFLDLKGIENSELYDVRMGQYRLTKCILLWNGATIEKDISSKKLTHVVMFVEDSTRLEQLTKACELYQIEPKFVNFEWVVNEWKKASTNILG
|
6.5.1.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P49917};
|
DNA biosynthetic process [GO:0071897]; DNA ligation involved in DNA repair [GO:0051103]; DNA recombination [GO:0006310]; double-strand break repair via classical nonhomologous end joining [GO:0097680]; double-strand break repair via nonhomologous end joining [GO:0006303]; nucleotide-excision repair, DNA gap filling [GO:0006297]
|
chromatin [GO:0000785]; DNA ligase IV complex [GO:0032807]; DNA-dependent protein kinase-DNA ligase 4 complex [GO:0005958]; nucleolus [GO:0005730]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA ligase (ATP) activity [GO:0003910]; metal ion binding [GO:0046872]
|
PF04679;PF01068;PF04675;
|
3.40.50.10190;1.10.3260.10;3.30.470.30;2.40.50.140;
|
ATP-dependent DNA ligase family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q08387}.
|
CATALYTIC ACTIVITY: Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.; EC=6.5.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10135};
| null | null | null | null |
FUNCTION: DNA ligase involved in DNA non-homologous end joining (NHEJ); required for double-strand break (DSB) repair. {ECO:0000269|PubMed:11029034, ECO:0000269|PubMed:11172711, ECO:0000269|PubMed:15226425}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74839
|
MSY1_SCHPO
|
MSSPTSPTSSPGRHHWSNSKDGMPPEYTNQDPNSDQADNENSDAKAHQPQHSPQHSTENQGHTGTSDTSSLEMELSKLHPESKQRQLPHSPEHERSRSPIASVVSYRSHMTLEDENQIFNAEMAVRGSQSLQRRPTGRSVRGSMRRLSSHRSKSMRTSKSKKSGDYERTAENEEAAQEAENHLDNFGVVTFGTEAPIKAPDHPVTIFGRIFKFIQQRSFYLRSLIYIIPLGVLLLIPVFIGRFYHPQPPYRDELGHEYERHLHVGGVDLMWMAIWWEIIWLSIWAARYAAKVIPYFFAFFVSFISNNVTKWRCMAVALEFPITLFLWMLAVYVSFLPIMTRRHIGDYGVPDHVRVKLPWQQSANNVLITLFITSIMNLVEKVLMQLIAMSLHRREYESRILYNKFAINELARLYGYARQRSFDFKDAIHRAQADVFKFADHQHGKKRAAAARVAQNALNKTTYKAISAFNFATDMVNKVAGEITNREVEKSSSPKSVVLHLLKTTRGCQSLARCLFEALVNPENPDLVLDDFIPVYTDETGEVDNATLEACYSIFDRDLNGDITCEEIELACVEIGKERKSISASLRDLNDSISKLDGICMFIVAVITLFIFLYLIARNFSGVLTSAGTTLLGLSWLFSGSAQELLSSIIFVFVKHPYDVGDRVDVMINGTVTSAMVKEISIMSTEFRLLTGKVIQAPNSLLNTLWILNMRRSDGIADPVTVNLKFGTTLQQIEQLRIKIIDFLKEEKRDYKPDLLTEVTDLPDLYSMSLCVVFFHKYNFQDEVLRMRRRNMFMCALMTYMQELDIVSPIFNSPGKSKDSPMYVNFNNGSMEGVKLSGGNDGGGTENHRDSTVGGGILKNPKAYPYREPTPPGSSDSDTASVSKKRVDFSLGTRHLMPAFDDVADIGSKRLGRDSLPDAVIENAGTEAMRREAEERRRAEEEEYERSQQESSSNEENENASRTSGARFSFSSKASRLSARPSARTVPPLQHISIQDLREPNENNTSKSARL
| null | null |
calcium ion transmembrane transport [GO:0070588]; cell volume homeostasis [GO:0006884]; intracellular calcium ion homeostasis [GO:0006874]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; perinuclear endoplasmic reticulum [GO:0097038]
|
calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; stretch-activated, monoatomic cation-selective, calcium channel activity [GO:0015275]
|
PF00924;
|
2.30.30.60;
|
MscS (TC 1.A.23) family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22910366}; Multi-pass membrane protein {ECO:0000305}. Note=Perinuclear endoplasmic reticulum. {ECO:0000269|PubMed:22910366}.
| null | null | null | null | null |
FUNCTION: Regulates intracellular calcium levels and cell volume for survival in response to hypo-osmotic shock. Acts as a mechanosensitive calcium channel in response to membrane stretch. The conductance is about 0.25 nanosiemens (PubMed:22910366). Involved in maintaining vacuole integrity and protecting the nuclear envelope upon hypo-osmotic shock (PubMed:25041276). {ECO:0000269|PubMed:22910366, ECO:0000269|PubMed:25041276}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74844
|
CENPQ_SCHPO
|
MEMKRRVRAVRRDQIQKRWRPLEDKQRQEIIIIFRTCSRLVLNTIKSETRKSLAEEWFMNILLKIEAPLRNLPVPRKRKESILFSQLLSSNMQLEQQLYSDLDHINVLQQELKVETARLENEQKSYEEMKQNMAINNSRLADLKSKLHPYLKKGLKISHDNFSDSNDFSFQKKLNTEDSNTSKTSTLDMYKEKLKPFTKTMQIHANKTVQLSQTIQKATLLLQRLNNTKNIGLNKSSKLKIKNI
| null | null |
cell division [GO:0051301]; mitotic sister chromatid segregation [GO:0000070]
|
condensed chromosome, centromeric region [GO:0000779]; cytoplasm [GO:0005737]; inner kinetochore [GO:0000939]; kinetochore [GO:0000776]; microtubule [GO:0005874]; Mis6-Sim4 complex [GO:0031511]; nucleus [GO:0005634]; spindle pole body [GO:0005816]
| null |
PF13094;
| null |
CENP-Q/OKP1 family
| null |
SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body.
| null | null | null | null | null |
FUNCTION: Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore COMA complex, which connects centromere-associated proteins and the outer kinetochore. COMA interacts with other inner kinetochore proteins to form the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly. {ECO:0000269|PubMed:16079914}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74846
|
SEC6_SCHPO
|
MTAAASDDAVYNKVADILRQCEDFHRLSTHIERFEREQASLNMHVKTELEKHVEAVELGKLALHDAQTKRVKLLQELHNMLTLCESAREMVDEFPLISRMSRIYKNCYATKQMISQLNNLVKETDVIEDMLREDLELDSDMPNLLRAHYKLSKLREFREEALYQASLEGQSDLPITLENSFSNLNTLSDNFDRLVLNFCRNIFQLVKSGHIKTIVQIFKIVEAEESSDEVLKSIRDAKSSLPDSQDGPFLSLQGMTRQLRNFRLRVLEEFQGAAAENFQRAWVSYLEDGSGELNLDFIFEDLKVAFYVLPDLTPPSYNIAKTFASIYQECLVGLVTKAVSLDTPAAVYLYLINFHREYRKFFEENAPFSVDEVEPGLEDGKDGILVREYTRLFTQKIREWSDKLFQSSVDTFMKRESEPELDSDGNYGLQGTIIFFQMITQQINIISHTNNSDVVGIVLSSIMYIMQSMQDQWKSVMRSELSQQLSGNPESVPPGLMEYLLAVANDNLKCAGFMDNTLLNTFELITSEREEDLREAFGKTVDGYILISDIGVSQIVAIISNDVKPALTSLFQPNWYQSSNMKLIVDTFRDYIVDCIEHMVPGLFDVFLLEASNALTISYLRSIFNKNACFDGDNAIQQIRSDIALAIRVFGEYMAAEHLRSTFEPIEKLLLGMLDADVETVSEYFHLLKEAYWDAPLSLVEAVLQNRTDLEKSIIKKMIDIVRHENDSLQIDTSQQPTVFSQVTSLSGSSIL
| null | null |
exocyst localization [GO:0051601]; exocytosis [GO:0006887]; intracellular protein transport [GO:0006886]; vesicle tethering involved in exocytosis [GO:0090522]
|
cell cortex of cell tip [GO:0051285]; cell cortex of growing cell tip [GO:1902716]; cell division site [GO:0032153]; cell tip [GO:0051286]; cortical dynamic polarity patch [GO:0090726]; exocyst [GO:0000145]; lateral cell cortex [GO:0097575]; nucleus [GO:0005634]; spindle pole [GO:0000922]
|
SNARE binding [GO:0000149]
|
PF06046;
|
1.10.357.50;1.10.357.70;
|
SEC6 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Cell tip {ECO:0000269|PubMed:11854409}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000269|PubMed:11854409}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74850
|
DGAT2_SCHPO
|
MSEETSIPGIIASTPPISKDSRRNVSHWLQALAVFLHSVSLTLTASWYTVLWAFLPFWPFLIVYLIWLIYDDGFVTGKDRQKRWLRNAPPYRWFCHYFPIRLHKTTELDSEKNYIFGYHPHGIISLGAFGGFASEGADFSKLFPGINVSVLTLNSNFYVPVYRDYLMALNINSVSKKSCVSILSRKPGDSVLIVIGGAQESLLSRPGQNNLVLKKRFGFVKLAFLTGSSLVPCFAFGESDIFEQVDNNPRTRIYKFQEIVKKIAGFTVPFFYGRGLLNKTFGLMPWRKPINIVVGEPIDVPKKSHPTNQEIYEVHEEYIRRLEGLWNKYKDVFLPNRISELKLSA
|
2.3.1.20
| null |
diacylglycerol metabolic process [GO:0046339]; glycerol metabolic process [GO:0006071]; lipid droplet formation [GO:0140042]; lipid storage [GO:0019915]; triglyceride biosynthetic process [GO:0019432]
|
cortical endoplasmic reticulum [GO:0032541]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; lipid droplet [GO:0005811]; perinuclear endoplasmic reticulum [GO:0097038]
|
2-acylglycerol O-acyltransferase activity [GO:0003846]; diacylglycerol O-acyltransferase activity [GO:0004144]
|
PF03982;
| null |
Diacylglycerol acyltransferase family
| null |
SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250|UniProtKB:Q08650}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12963726, ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to sites of lipid droplet biogenesis in the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q08650}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20; Evidence={ECO:0000269|PubMed:12963726}; CATALYTIC ACTIVITY: Reaction=a 2-acylglycerol + an acyl-CoA = a 1,2-diacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:32947, ChEBI:CHEBI:17389, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342; Evidence={ECO:0000269|PubMed:12963726};
| null |
PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis. {ECO:0000305|PubMed:12963726}.
| null | null |
FUNCTION: Catalyzes the terminal and only committed step in triacylglycerol (TAG) synthesis by using diacylglycerol (DAG) and fatty acyl-CoA as substrates. Required for storage lipid synthesis (PubMed:12963726, PubMed:26990381). Major DAG esterifying enzyme in stationary phase when TAG production is particularly active (PubMed:12963726). Involved in lipid particle synthesis from the endoplasmic reticulum, promoting localized TAG production at discrete ER subdomains (PubMed:26990381, PubMed:28011631). {ECO:0000269|PubMed:12963726, ECO:0000269|PubMed:26990381, ECO:0000269|PubMed:28011631}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74854
|
POF6_SCHPO
|
MKPSEAREHAIRKIKEYLERRHKQQFKALFGCLTINIYLKIFTLISTPDLCNCRLVCRKFQQLCDYNSIYVKKLLLMNAWDVTLSRKLYYESQDGMSQANMSSNTSKGFHLQSSDKKYADSDRPKLSSSSLLSLPDQKIPFPVDYSTVQGKQVVLTVLDCVSQRVEFARLDYIKVWRALAPIYRNLAYASNTIDPIAFSAFRTPEEQSKVLKYLIRFGNSYPYGTYRQAMQNAILDMASLFEQACLDEFELGLHSRNLDLLRKFSHVLHDFSGPNAYVSMYLAKQTDFVRSFFHFDPYSLFISNNLEEIHINWNILESVVNDTIKLLESESKFSEATLPEPELVQVPYAKDILGNSLKDYVISICEHIGEEETELFLVFISGFYGLCKKFFSIPNGPALVDTIFQPQIDIFISQELHYFKTVGWSLVDQWDQKLEEKEDATECFFYKNVSQNTAKNNFLETFKNVMLLPVSLFTIPSENNSASNLAEKAIEQKEEEDPELSKLDAARFVPANIYVSKDRLKHLPTTELAAQAAVLDSKLEGISTMFSLELALKIVHLCKVSLARAKVFMGTSVPQDDDIKGLSKDLFVQLLRELGQGHLKHGFDRAIEHLSSFDPRRDFSSNTVEPVVKFLELINVGDMIQQMMDSFFNEEMSPICVKDDMFDPAIAEKKKFEQLLDERAAFGLHKGINVLIEHADFLLETKTPMNLFSDQTIGSITNTIEPTAAAKNVVQFLGFHMRILVGRADHEILDVFYKEVGMRLFDSLTRYIKSHKFSVDGGLKLLSDCNLYYEFIHSLHQSSLLPYFKTLKEIAHLFIIDGKNAEEIGKLATDTSRFSSAFHTEEVYEILHSRIDWLNIKYEVDKVIHGLACCIM
| null | null |
cell cycle [GO:0007049]; endocytic recycling [GO:0032456]; exocytosis [GO:0006887]; Golgi to plasma membrane transport [GO:0006893]; septum digestion after cytokinesis [GO:0000920]
|
cell division site [GO:0032153]; cell septum [GO:0030428]; cell tip [GO:0051286]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; exocyst [GO:0000145]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]
|
protein-macromolecule adaptor activity [GO:0030674]
|
PF12937;PF07393;
|
1.20.1280.50;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Constantly expressed throughout the cell cycle. Expressed in nucleus except the nucleolus and is localized at cell tips on both sides of the septum in septated cells.
| null | null | null | null | null |
FUNCTION: Together with skp1, essential for septum processing and cell separation. {ECO:0000269|PubMed:12511573}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74856
|
CAF1_SCHPO
|
MTAMNSNFSYPALGVDGISSQISPIRDVWSTNLQQEMNLIMSLIERYPVVSMDTEFPGVVARPLGVFKSSDDYHYQTLRANVDSLKIIQIGLALSDEEGNAPVEACTWQFNFTFNLQDDMYAPESIELLTKSGIDFKKHQEVGIEPADFAELLIGSGLVLQEEVTWITFHSGYDFAYLLKAMTQIPLPAEYEEFYKILCIYFPKNYDIKYIMKSVLNNSKGLQDIADDLQIHRIGPQHQAGSDALLTARIFFEIRSRYFDGSIDSRMLNQLYGLGSTGSVLWHNNSSTPQIQFRDLPGAHPSPTPSNAGIPTTLTNTSSAPNFANSTFRFPPRVV
|
3.1.13.4
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:19307292}; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:19307292}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:19307292}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19307292}; Note=Binds 1 Zn(2+) ion per subunit. At lower physiological Zn(2+) concentrations, Mg(2+) replaces Zn(2+). The nature of the bound ion affects the speed of the RNA degradation reaction and, to a limited extent, base selectivity. {ECO:0000269|PubMed:19307292};
|
exonucleolytic catabolism of deadenylated mRNA [GO:0043928]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; regulatory ncRNA-mediated gene silencing [GO:0031047]
|
CCR4-NOT complex [GO:0030014]; CCR4-NOT core complex [GO:0030015]; cytosol [GO:0005829]; nucleus [GO:0005634]; P-body [GO:0000932]
|
chromatin binding [GO:0003682]; manganese ion binding [GO:0030145]; metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; poly(A)-specific ribonuclease activity [GO:0004535]; RNA nuclease activity [GO:0004540]; zinc ion binding [GO:0008270]
|
PF04857;
|
3.30.420.10;
|
CAF1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
|
CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
| null | null | null | null |
FUNCTION: Acts as the catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. In vivo and in vitro, caf1 has 3'-exoribonuclease activity with a preference for poly(A) RNAs. {ECO:0000269|PubMed:17452359, ECO:0000269|PubMed:19307292}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74859
|
APTX_SCHPO
|
MSVHKTNDAFKVLMNSAKEPIVEDIPKKYRKQSFRDNLKVYIESPESYKNVIYYDDDVVLVRDMFPKSKMHLLLMTRDPHLTHVHPLEIMMKHRSLVEKLVSYVQGDLSGLIFDEARNCLSQQLTNEALCNYIKVGFHAGPSMNNLHLHIMTLDHVSPSLKNSAHYISFTSPFFVKIDTPTSNLPTRGTLTSLFQEDLKCWRCGETFGRHFTKLKAHLQEEYDDWLDKSVSM
|
3.6.1.71; 3.6.1.72
| null |
mismatch repair [GO:0006298]; single strand break repair [GO:0000012]
|
cytosol [GO:0005829]; nucleus [GO:0005634]
|
DNA 5'-adenosine monophosphate hydrolase activity [GO:0033699]; DNA-3'-diphospho-5'-guanosine diphosphatase [GO:0120108]; double-stranded DNA binding [GO:0003690]; double-stranded RNA binding [GO:0003725]; GMP binding [GO:0019002]; guanosine binding [GO:1905108]; mismatched DNA binding [GO:0030983]; single-strand break-containing DNA binding [GO:1990165]; single-stranded DNA binding [GO:0003697]; zinc ion binding [GO:0008270]
|
PF01230;PF16278;
|
3.30.428.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000269|PubMed:16823372}.
|
CATALYTIC ACTIVITY: Reaction=a 5'-end adenosine-5'-diphospho-5'-2'-deoxyribonucleoside-DNA + H2O = a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + AMP + 2 H(+); Xref=Rhea:RHEA:52128, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:13181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:136413, ChEBI:CHEBI:456215; EC=3.6.1.71; Evidence={ECO:0000269|PubMed:21984210, ECO:0000269|PubMed:24362567}; CATALYTIC ACTIVITY: Reaction=a 5'-end adenosine-5'-diphospho-5'-ribonucleoside-2'-deoxyribonucleotide-DNA + H2O = a 5'-end 5'-phospho-ribonucleoside-2'-deoxyribonucleotide-DNA + AMP + 2 H(+); Xref=Rhea:RHEA:52132, Rhea:RHEA-COMP:13182, Rhea:RHEA-COMP:13183, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:136414, ChEBI:CHEBI:136415, ChEBI:CHEBI:456215; EC=3.6.1.71; Evidence={ECO:0000269|PubMed:21984210}; CATALYTIC ACTIVITY: Reaction=a 3'-end 2'-deoxyribonucleotide-3'-diphospho-5'-guanosine-DNA + H2O = a 3'-end 2'-deoxyribonucleotide 3'-phosphate-DNA + GMP + 2 H(+); Xref=Rhea:RHEA:52140, Rhea:RHEA-COMP:13186, Rhea:RHEA-COMP:13187, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58115, ChEBI:CHEBI:136419, ChEBI:CHEBI:136420; EC=3.6.1.72; Evidence={ECO:0000269|PubMed:26007660};
| null | null | null | null |
FUNCTION: DNA-binding protein involved in single-strand DNA break repair, double-strand DNA break repair and base excision repair. Resolves abortive DNA ligation intermediates formed either at base excision sites, or when DNA ligases attempt to repair non-ligatable breaks induced by reactive oxygen species (PubMed:21984208, PubMed:24362567). Catalyzes the release of adenylate groups covalently linked to 5'-phosphate termini, resulting in the production of 5'-phosphate termini that can be efficiently rejoined (PubMed:21984210, PubMed:24362567). Likewise, catalyzes the release of 3'-linked guanosine (DNAppG) and inosine (DNAppI) from DNA, but has higher specific activity with 5'-linked adenosine (AppDNA) (PubMed:26007660). {ECO:0000269|PubMed:21984210, ECO:0000269|PubMed:24362567, ECO:0000269|PubMed:26007660, ECO:0000305, ECO:0000305|PubMed:21984208}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74866
|
RIFK_SCHPO
|
MTVNLEEKRPEIVGPEKVQSPYPIRFEGKVVHGFGRGSKELGIPTANISEDAIQELLRYRDSGVYFGYAMVQKRVFPMVMSVGWNPYYKNKLRSAEVHLIERQGEDFYEEIMRVIVLGYIRPELNYAGLDKLIEDIHTDIRVALNSMDRPSYSSYKKDPFFKV
|
2.7.1.26
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.;
|
FMN biosynthetic process [GO:0009398]; phosphorylation [GO:0016310]; riboflavin biosynthetic process [GO:0009231]; riboflavin metabolic process [GO:0006771]
|
cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; riboflavin kinase activity [GO:0008531]; zinc ion binding [GO:0008270]
|
PF01687;
|
2.40.30.30;
|
Flavokinase family
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26;
| null |
PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1.
| null | null |
FUNCTION: Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) coenzyme.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74874
|
CCR4_SCHPO
|
MFNPRYTQGTIYPGAHPGLLTPDHQHAAILSVQNSPALENSNISEHWKQQIALATQSRSFSSPHQRAHNAAALARSGGPGFSMNYNARTGAFTGGPNAAGLSSLGGKYNTSSTTTTLTTSTTLNTSSGTTLNSTSKTTTSSVAVDDQKSKSDSKKERRDWTCLDLGGIGLRNVSTDLFKFSFLTELYINHNNLTRLPPEIGKLKNLVILDASGNSIKTIPPELGLLTELREVLLFDNMISVIPAELGTLFQLKILGIEGNPLQDVYKNQIMESGTAGLIAALRDGCPVGPPPPERGWEKLVSDDDDDVNDNVSTSVRDLTAADSNKPSTTSKNLKFTIMSYNVLCERYATSTLYGYTPSWALSWSYRKDLIMQELGGYNADIICLQEVDVENYDTFFAPQMSLKGYKGVHFPKSRVRTMNEVERRIVDGCATFFKTSKYVMHEKMVIEYNQAPSLRRQDIKLTSNMYNRVMTKDNISVITLLENKENGSRLIVANCHIHWDPQFRDVKVIQVAMLMDEIAQVATKFRNMPSKIPSDQLKDERPTYPEYLKIPILICGDFNSVQGSGVYDFLSSGSISQNHEDFMNNDYGEYTVNGRSHAFNLKSAYGESEALSFTNYTPGFKGAIDHIWYTGNSLEVTGLLKGVDKDYLSGVVGFPNAHFPSDHICLLAEFKVKQEKTPLPSSKFNNDKK
|
3.1.13.4
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]
|
CCR4-NOT complex [GO:0030014]; CCR4-NOT core complex [GO:0030015]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; P-body [GO:0000932]
|
metal ion binding [GO:0046872]; poly(A)-specific ribonuclease activity [GO:0004535]; RNA binding [GO:0003723]
|
PF03372;PF12799;
|
3.60.10.10;3.80.10.10;
|
CCR4/nocturin family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
|
CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
| null | null | null | null |
FUNCTION: Acts as a catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover (By similarity). Ccr4 has 3'-5' RNase activity with a strong preference for polyadenylated substrates and also low exonuclease activity towards single-stranded DNA (By similarity). Participates in the shortening of poly(A)-tails (PubMed:26942678). Erh1-mmi1 complex-mediated recruitment of CCR4-NOT to target RNAs promotes heterochromatin formation at RNAi-dependent heterochromatin domains (HOODs), including a subset of meiotic genes, lncRNAs and retrotransposons (PubMed:26942678). Recruitment of the CCR4-NOT complex to rDNA promotes rDNA heterochromatin assembly (PubMed:26942678). {ECO:0000250|UniProtKB:P31384, ECO:0000269|PubMed:26942678}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74880
|
MCES_SCHPO
|
MSSSNSRVHEEQPPTENRRYARPTAQMNRVIEQQPRRRDYFQNNDNSGRRGYNRHENNGNAQDVVRSHYNARPDLGYKKRQFSPIIQLKRFNNWIKSVLIQKFAPHASDYPILVLDMGCGKGGDLIKWDKAGIDGYIGIDIAEVSVNQAKKRYREMHASFDALFYAGDCFSSSINELLPPDQRKFDVVSLQFCMHYAFESEEKVRVLLGNVSKCLPRGGVMIGTIPNSDVIVKHIKMLKPGEKEWGNDIYKVRFPESPPRSFRPPYGIQYYFYLEDAVTDVPEYVVPFEAFRAVAEGYNLELIWVKPFLDILNEEKNSETYGPLMDRMKVVDNEGHRGIGGQEKEAAGFYLAFAFEKRGI
|
2.1.1.56
| null |
7-methylguanosine mRNA capping [GO:0006370]
|
cytosol [GO:0005829]; nucleus [GO:0005634]; P-TEFb-cap methyltransferase complex [GO:0070693]
|
mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; RNA binding [GO:0003723]
|
PF03291;
|
3.40.50.150;
|
Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0 methyltransferase family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
|
CATALYTIC ACTIVITY: Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000250|UniProtKB:O43148, ECO:0000255|PROSITE-ProRule:PRU00895};
| null | null | null | null |
FUNCTION: Responsible for methylating the 5'-cap structure of mRNAs. {ECO:0000269|PubMed:10347220}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74887
|
TPX1_SCHPO
|
MSLQIGKPAPDFKGTAVVNGAFEEIKLADYKGKWVFLGFYPLDFTFVCPTEIVAFSEAASKFAERNAQVILTSTDSEYSHLAFINTPRKEGGLGGINIPLLADPSHKVSRDYGVLIEDAGVAFRGLFLIDPKGVLRQITINDLPVGRSVDEALRLLDAFQFVEEHGEVCPANWHKGSDTIDTKNPEKYFSKH
|
1.11.1.24
| null |
cell redox homeostasis [GO:0045454]; cellular detoxification of hydrogen peroxide [GO:0061692]; hydrogen peroxide catabolic process [GO:0042744]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; removal of superoxide radicals [GO:0019430]; response to oxidative stress [GO:0006979]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
peroxidase activity [GO:0004601]; peroxiredoxin activity [GO:0051920]; thioredoxin peroxidase activity [GO:0008379]; thioredoxin-dependent peroxiredoxin activity [GO:0140824]; unfolded protein binding [GO:0051082]
|
PF10417;PF00578;
|
3.40.30.10;
|
Peroxiredoxin family, AhpC/Prx1 subfamily
|
PTM: The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its condensation to a disulfide bond. It can be reactivated by forming a transient disulfide bond with sulfiredoxin srx1, which reduces the cysteine sulfinic acid in an ATP- and Mg-dependent manner. {ECO:0000269|PubMed:15824112, ECO:0000269|PubMed:15956211}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:24316080}. Nucleus {ECO:0000269|PubMed:16823372}.
|
CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000269|PubMed:20356456};
| null | null | null | null |
FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events (PubMed:17409354, PubMed:20356456). Relays hydrogen peroxide as a signal to the transcription factor pap1 by inducing the formation of intramolecular disulfide bonds in pap1, which causes its nuclear accumulation and activation (PubMed:15824112, PubMed:24316080). Reduced by srx1 and this regulation acts as a molecular switch controlling the transcriptional response to hydrogen peroxide (PubMed:15956211). {ECO:0000269|PubMed:15824112, ECO:0000269|PubMed:15956211, ECO:0000269|PubMed:17409354, ECO:0000269|PubMed:20356456, ECO:0000269|PubMed:24316080}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74910
|
RAF1_SCHPO
|
MTNSSPRVKRRTDTQYLHSVSSKLPKVDFDTNNEEFFEEEFEIYDPFYRAELPCPKPSLSISKHSIAKVPSNVNKRLELQLLLTSGTFLPNSRPYLSERVRKHTHLLSNSITGDDKPSLIHVDFTPEECFILQEAKLKFGPVNSVQFNDAYSTHISPKLPGRAYEDCQKFEIDNPSLSPVDKHGAIILRTYKKNKKLLPDYLKSFYNAGSSYFQREQVHQLMDGESVFFLKPWKHFNETSGDTVCVAYNPLCEKFALGSTAQDGAYNRLGNLWIGDFHSETIQSLESHYKLNQVGEKEYSTISDLCFSKGNLFLYTGAFDNAVKVWDMEGNLCGIFNAPTDYIHKLALSDDDLLAVACKNGYGYLLSTDNSTGEILTSANLIYPEALEKGYSASLIEFSNFLGRSSDKVIIGYDSFHTSNNRGCLALFDASTASFVQKFNTADEAFTSLYMHPSQVGFVASSNTLSNGRVYYLDTRMYKVCLNFTTTQKDINHATISNSGILVTSSGTDNQTFVWDSRKPDKPLSLLKHGKTKMIHFDGANEEEVDAGINMAQWQPKGNLFVTGGSDGIVKVWDLRLNNPFIQNFTEMNSAITYGGFSEDASKLTVCCVGGDVNMYSLGNDNGNKFGEFRIIENRLLT
| null | null |
CENP-A containing chromatin assembly [GO:0034080]; meiotic telomere clustering [GO:0045141]; regulatory ncRNA-mediated heterochromatin formation [GO:0031048]; silent mating-type cassette heterochromatin formation [GO:0030466]; siRNA-mediated pericentric heterochromatin formation [GO:0140727]; subtelomeric heterochromatin formation [GO:0031509]
|
chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; CLRC complex [GO:0043494]; cytosol [GO:0005829]; mating-type region heterochromatin [GO:0031934]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]
| null |
PF00400;
|
2.130.10.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:18345014}. Chromosome {ECO:0000269|PubMed:18345014}.
| null | null | null | null | null |
FUNCTION: Component of the Clr4 methyltransferase complex (ClrC) which contributes to the establishment of heterochromatin by specifically methylating histone H3 to form H3K9me (PubMed:16024659, PubMed:16040243, PubMed:16157682). ClrC preferentially ubiquitylates H3K14 and ClrC-mediated H3 ubiquitination promotes clr4 methyltransferase activity for the methylation of H3K9 (PubMed:31468675). H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin, telomeric regions and at the silent mating-type loci (PubMed:16024659, PubMed:16040243, PubMed:16157682, PubMed:18345014). Has a role in both mitotic and meiotic chromosome segregation (PubMed:16040243). {ECO:0000269|PubMed:16024659, ECO:0000269|PubMed:16040243, ECO:0000269|PubMed:16157682, ECO:0000269|PubMed:18345014, ECO:0000269|PubMed:31468675}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74919
|
RNC1_SCHPO
|
MAYNHFSIPKNIEEKENSFFDVTFQDEPDETTSTATGIAKVSIPTPKPSTPLSTLTNGSTIQQSMTNQPEPTSQVPPISAKPPMDDATYATQQLTLRALLSTREAGIIIGKAGKNVAELRSTTNVKAGVTKAVPNVHDRVLTISGPLENVVRAYRFIIDIFAKNSTNPDGTPSDANTPRKLRLLIAHSLMGSIIGRNGLRIKLIQDKCSCRMIASKDMLPQSTERTVEIHGTVDNLHAAIWEIGKCLIDDWERGAGTVFYNPVSRLTQPLPSLASTASPQQVSPPAAPSTTSGEAIPENFVSYGAQVFPATQMPFLQQPKVTQNISIPADMVGCIIGRGGSKISEIRRTSGSKISIAKEPHDETGERMFTITGTHEENEKALFLLYQQLEMEKDRRSH
| null | null |
3'-UTR-mediated mRNA destabilization [GO:0061158]; 3'-UTR-mediated mRNA stabilization [GO:0070935]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of cell wall integrity MAPK cascade [GO:1903138]; negative regulation of p38MAPK cascade [GO:1903753]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
mRNA 3'-UTR AU-rich region binding [GO:0035925]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]
|
PF00013;
|
3.30.1370.10;
| null |
PTM: Phosphorylated by pmk1. Phosphorylation causes enhancement of the RNA-binding activity. {ECO:0000269|PubMed:12931193}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Binds and stabilizes pmp1 mRNA and hence acts as a negative regulator of pmk1 signaling. Overexpression suppresses the Cl(-) sensitivity of calcineurin deletion. {ECO:0000269|PubMed:12931193}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74926
|
RBD2_SCHPO
|
MIFMILGRSKEFILKLPIWTQIITYIAILVYALSFFGISTGVLSLSWIGLLQKRQLYEIITYVTLHLSMLHIVFNFVSLLPAMSQFEKKQGTLACILVTVIPYTLFPGIMHLIVYHFFLRKDYVSIAGLSGWAFAFISASCVHSPQRLISFFNLFSIPAYCFPIIYLIMTTILVPKASFIGHASGAVMGYCTPFMLGSIPLKSWAQNVDPIFQSWVKNYHSFDQLSHAQLPIAEPLSTFSSFPGKGTRLGG
|
3.4.21.105
| null |
proteolysis [GO:0006508]; SREBP signaling pathway [GO:0032933]
|
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
|
protein-macromolecule adaptor activity [GO:0030674]; serine-type endopeptidase activity [GO:0004252]
|
PF01694;
|
1.20.1540.10;
|
Peptidase S54 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:27655872}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.; EC=3.4.21.105; Evidence={ECO:0000269|PubMed:26545776, ECO:0000269|PubMed:27655872};
| null | null | null | null |
FUNCTION: Rhomboid-type serine protease that catalyzes intramembrane proteolysis (PubMed:26545776, PubMed:27655872). Upon binding to cdc48, required for sterol regulatory element-binding protein sre1 activation by mediating its release from the membrane and thereby regulating its activity under hypoxic conditions (PubMed:26545776, PubMed:27655872). Upon binding to cdc48, required for the processing of sterol regulatory element-binding protein sre2 (PubMed:27655872). {ECO:0000269|PubMed:26545776, ECO:0000269|PubMed:27655872}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74944
|
POLK_SCHPO
|
MENAKDFIGETIKENGLLTIEDDGSSSSDEEATLKRRLAGPSVLKSGQENVNQKKINEIIYEASKGSKFFEAEQKRDRELRLRIEKVQVEVEKYQSKLRFDKAFQREWTIRQESVDTTVEDFRAKRDLTQIIVHVDCDAFYASIEELKNPKLKSLPMAVGKSVLCTANYVARKFGVRSAMPEFIARKICPDLVVIPLNLSEYAIKSKEIQNVLAQYDSNLCPASIDEFYMNLTSHLRLQELAFTVENITMVVEKIRKQVHEETGVTVSCGIAANKLLAKIASNKRKPNNQFFIPFDEIGISKFMNDLPVREVSGIGRVLEQQLLGLEIKTCGDIQRNLVILSYIFLPKSFQNLLRCSYGFGTTILDEYGESKRKTIGSEATFSSNLSSPSIIEYKLRLLVQNVSENLQKRGLVTNSIAIKYKTSEFQVHTKQKSIGQFIHSESDLLKPALQLLRQSYPMTIRLLGVRATKLVSKSRCLAMQLKFQSQNTVPCPVCQKNIENELGILNQHVDLCLNVETVKSLINTDHTANPTIKKRKSNTLDTYFLE
|
2.7.7.7
| null |
DNA damage response [GO:0006974]; DNA replication [GO:0006260]; error-free translesion synthesis [GO:0070987]; error-prone translesion synthesis [GO:0042276]; meiotic cell cycle [GO:0051321]; translesion synthesis [GO:0019985]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
damaged DNA binding [GO:0003684]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]
|
PF00817;PF11799;
|
1.10.150.810;3.30.70.270;3.40.1170.60;3.30.160.60;3.30.1490.100;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Associates with chromatin.
|
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7;
| null | null | null | null |
FUNCTION: DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Has a role in meiosis. {ECO:0000269|PubMed:12514100, ECO:0000269|PubMed:16303567}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74954
|
CBF11_SCHPO
|
MGDYFAWDFANISGSNTSGSLNLNQLNLDNINNGLHNQEDGAGGRNENSERVGSGSPGSVSMQVLSLFSAVNSALATLEKSEEFPSVVKDEQSIFPAVAKASNSLDELAQNIIPAPSPPGFNRKRKTFDEDSSVEMIRRAISDHLDLLNNCCIGIANLNEDSVHKISLTRSGKPSQLVTVSCRHSSVIQKSYGSEKRYLCPPPMVYINGNYSSIFNQSFRTEISIMNDFGQCSQPISEEYTGQGCMIFRSLHISSLVAAKSKNLRLSLDMFSNVNNQLLSHLVTSSISIVSKPSKKGSKLKISNITLRSGSVVSLYNRINSQTVRTKYTSIEAGQFCLRGDRWVPLRINLLLPDENGKLKVCDDVDNPEPIKYGSIVELVDEATGTTSDPLIIRRVEKDHIAEEDGYVNQMHRIVLESAYPISNVRHLKIAEHSSLAYSNNISVRWFLGATSAQNRNASSEAILPIEWEAVGNLSSNEMTRVGDSVCWTIVGISHFDCTMMLPFNQNPVPTVTDYPYIEEPPEYLESSRSLQFKIGGYSVGLQIWLGVHGPLSYSFTAAADTSTMGTVTLGLSQISYDPSCAEQKYPLLFVIPGGIVIIGKCEILLTSSAFGN
| null | null |
cell adhesion [GO:0007155]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of lipid metabolic process [GO:0019216]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565]
|
PF09270;PF09271;
|
2.80.10.50;2.60.40.1450;
|
Su(H) family
| null |
SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
| null | null | null | null | null |
FUNCTION: Transcription factor that behaves as a negative regulator of adhesion. Recognizes specifically the canonical CSL response element GTGA/GGAA. May also play a cbf12-antagonistic role in the regulation of a number of other important processes such as extracellular material production, colony morphogenesis, ploidy maintenance, or meiosis. {ECO:0000269|PubMed:19101542}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74957
|
AGO1_SCHPO
|
MSYKPSSEIALRPGYGGLGKQITLKANFFQIISLPNETINQYHVIVGDGSRVPRKQSQLIWNSKEVKQYFGSSWMNSVYDGRSMCWSKGDIADGTIKVNIGSESHPREIEFSIQKSSKINLHTLSQFVNSKYSSDPQVLSSIMFLDLLLKKKPSETLFGFMHSFFTGENGVSLGGGVEAWKGFYQSIRPNQGFMSVNVDISSSAFWRNDSLLQILMEYTDCSNVRDLTRFDLKRLSRKFRFLKVTCQHRNNVGTDLANRVYSIEGFSSKSASDSFFVRRLNGEEQKISVAEYFLENHNVRLQYPNLPCILVKNGAMLPIEFCFVVKGQRYTAKLNSDQTANMIRFAVQRPFERVQQIDDFVHQMDWDTDPYLTQYGMKIQKKMLEVPARVLETPSIRYGGDCIERPVSGRWNLRGKRFLDPPRAPIRSWAVMCFTSTRRLPMRGIENFLQTYVQTLTSLGINFVMKKPPVLYADIRGSVEELCITLYKKAEQVGNAPPDYLFFILDKNSPEPYGSIKRVCNTMLGVPSQCAISKHILQSKPQYCANLGMKINVKVGGINCSLIPKSNPLGNVPTLILGGDVYHPGVGATGVSIASIVASVDLNGCKYTAVSRSQPRHQEVIEGMKDIVVYLLQGFRAMTKQQPQRIIYFRDGTSEGQFLSVINDELSQIKEACHSLSPKYNPKILVCTTQKRHHARFFIKNKSDGDRNGNPLPGTIIEKHVTHPYQYDFYLISHPSLQGVSVPVHYTVLHDEIQMPPDQFQTLCYNLCYVYARATSAVSLVPPVYYAHLVSNLARYQDVTADDTFVETSEASMDQEVKPLLALSSKLKTKMWYM
| null | null |
chromosome segregation [GO:0007059]; co-transcriptional gene silencing by RNA interference machinery [GO:0033562]; negative regulation of G0 to G1 transition [GO:0070317]; nuclear polyadenylation-dependent antisense transcript catabolic process [GO:0071040]; priRNA 3'-end processing [GO:1990431]; regulatory ncRNA-mediated heterochromatin formation [GO:0031048]; siRNA 3'-end processing [GO:1990432]; siRNA-mediated pericentric heterochromatin formation [GO:0140727]
|
ARC complex [GO:0033167]; chromosome, subtelomeric region [GO:0099115]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; heterochromatin island [GO:1990342]; mating-type region heterochromatin [GO:0031934]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]; RITS complex [GO:0030958]
|
miRNA binding [GO:0035198]; protein-macromolecule adaptor activity [GO:0030674]; RNA binding [GO:0003723]; RNA endonuclease activity [GO:0004521]; RNA endonuclease activity, producing 5'-phosphomonoesters [GO:0016891]; single-stranded RNA binding [GO:0003727]
|
PF08699;PF16488;PF16487;PF16486;PF02170;PF02171;
|
3.40.50.2300;2.170.260.10;3.30.420.10;
|
Argonaute family, Ago subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Chromosome, centromere. Chromosome, telomere. Note=Associates with telomeric and mating-type region heterochromatin.
| null | null | null | null | null |
FUNCTION: Required for G1 arrest and mating in response to nitrogen starvation. Ago1 regulation of cytokinesis and cell cycle checkpoints occurs downstream of dcr1. Required, indirectly, for regulated hyperphosphorylation of cdc2. Has a role in the RNA interference (RNAi) pathway which is important for heterochromatin formation, accurate chromosome segregation, centromere cohesion and telomere function during mitosis and meiosis. Required for silencing at the centromeres and for initiation of transcriptionally silent heterochromatin at the mating type locus. Promotes histone H3K9 methylation necessary for centromere function. Required for recruitment of swi6 and cohesin to an ectopic dg repeat. A member of the RNA-induced transcriptional silencing (RITS) complex which is involved in the biosynthesis of dsRNA from primer siRNAs provided by the RNA-directed RNA polymerase (RDRC) complex. Has ribonuclease H-like cleavage (slicing) activity towards target messages complementary to siRNA and can direct site-specific cleavage of RNA substrates via siRNA. Slicing activity is required for both post-transcriptional and transcriptional gene silencing as well as for histone H3 'Lys-10' methylation spreading, conversion of double-stranded siRNA to single-stranded siRNA and siRNA-dependent association of ago1 with chromatin. A member of the argonaute siRNA chaperone (ARC) complex which is required for histone H3K9 methylation, heterochromatin assembly and siRNA generation. The ARC complex contains mostly double-stranded siRNA. {ECO:0000269|PubMed:12193640, ECO:0000269|PubMed:12215653, ECO:0000269|PubMed:12509501, ECO:0000269|PubMed:12733640, ECO:0000269|PubMed:14699070, ECO:0000269|PubMed:14704433, ECO:0000269|PubMed:15371329, ECO:0000269|PubMed:15607976, ECO:0000269|PubMed:16931764, ECO:0000269|PubMed:17310250}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74958
|
MMI1_SCHPO
|
MSNTNFSTSRSSKSIPELPNLEALRSLWPPPSLNESGDTRSVWTTHTGEPVASSVLSTSGSNNFSSPLKRPAPESHDAPIGRRLMVDDPRLIKHGKYDFSRHCTDYGHSYEWPYFRSLRRESMLYHTSGSYPESQPPYSSYSTDAPHYYHAGSESSAYYDSRSRLHGIQPPPKRRTLSPPPRRLADPVVVGSSRYVEEEVYRRPPYTLASEVPSSASAYQAGYSSYPVRSSPQLSHEDTRHGIASSGSTRYPFVPANTRASHSPSLLEPYAHSLPSSVAPVGAYPEKSSYLLSNSSNDSASRKEKPKARASTPPPLNFSRASEHRNEKGERISMINPRVVLDENGISHRSRYFIMLCDNETAIAHAKKTSIWAVKKDSSKRISDAYKKASVYFIFVAQQTYNALGYAQVVSDLNSTELPFWSDSSHAGGVRIKWIKTCNLFSAEISEIVSHMDHGSEARDGMEMMYDEGSRLCTLINYAIMKRIGRDR
| null | null |
lncRNA catabolic process [GO:0110064]; mRNA destabilization [GO:0061157]; nuclear mRNA surveillance of mRNA 3'-end processing [GO:0071031]; nuclear mRNA surveillance of spliceosomal pre-mRNA splicing [GO:0071030]; nuclear ncRNA surveillance [GO:0071029]; nuclear RNA surveillance [GO:0071027]; nuclear-transcribed mRNA catabolic process, meiosis-specific transcripts [GO:0033621]; regulation of siRNA-independent facultative heterochromatin formation [GO:1902801]; regulation of termination of RNA polymerase II transcription, poly(A)-coupled [GO:2000804]; regulatory ncRNA 3'-end processing [GO:0043628]; siRNA-independent facultative heterochromatin formation [GO:1902794]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; heterochromatin island [GO:1990342]; Mei2 nuclear dot complex [GO:0033620]; nuclear exosome focus [GO:1990251]; nucleus [GO:0005634]
|
CCR4-NOT complex binding [GO:1905762]; DNA binding [GO:0003677]; lncRNA binding [GO:0106222]; mRNA binding [GO:0003729]; N6-methyladenosine-containing RNA reader activity [GO:1990247]; pre-mRNA binding [GO:0036002]; pre-mRNA intronic binding [GO:0097157]; protein-RNA adaptor activity [GO:0140517]; RNA binding [GO:0003723]
|
PF04146;
|
3.10.590.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:16823445}.
| null | null | null | null | null |
FUNCTION: RNA-binding protein that recognizes and binds N6-methyladenosine (m6A)-containing RNAs, a modification present at internal sites of mRNAs and some non-coding RNAs (By similarity). Functions alone and as part of the erh1-mmi1 complex, to recruit the CCR4-NOT complex and the NURS complex to target RNAs (PubMed:26942678, PubMed:30651569, PubMed:31974447). Suppresses the meiotic program during vegetative growth and promotes the meiotic program during mating (PubMed:31974447). Binds to DSR (determinant of selective removal) regions in meiotic mRNA, and recruits the NURS complex to targets (PubMed:16823445, PubMed:26942678). Recruitment of NURS complex to target mRNAs promotes mRNA decay by engagement of the nuclear exosome, and formation of heterochromatin islands at meiotic genes silenced by the exosome (PubMed:16823445, PubMed:26942678). Recruitment of the CCR4-NOT complex to target RNAs promotes heterochromatin formation at RNAi-dependent heterochromatin domains (HOODs), including a subset of meiotic genes, lncRNAs and retrotransposons (PubMed:26942678). Recruitment of the CCR4-NOT complex to rDNA promotes rDNA heterochromatin assembly (PubMed:26942678). Promotes non-canonical transcription termination at meiotic genes and prevents lncRNA transcription from invading and repressing adjacent genes (PubMed:16823445, PubMed:30651569). {ECO:0000250|UniProtKB:Q06390, ECO:0000269|PubMed:16823445, ECO:0000269|PubMed:26942678, ECO:0000269|PubMed:30651569, ECO:0000269|PubMed:31974447}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74966
|
RUXG_SCHPO
|
MSKAGAPDLKKYLDRQVFVQLNGSRKVYGVLRGYDIFLNIVLEDSIEEKVDGEKVKIGSVAIRGNSVIMIETLDKMT
| null | null |
mRNA 5'-splice site recognition [GO:0000395]; mRNA splicing, via spliceosome [GO:0000398]; spliceosomal snRNP assembly [GO:0000387]
|
catalytic step 2 spliceosome [GO:0071013]; cytosol [GO:0005829]; nucleus [GO:0005634]; post-mRNA release spliceosomal complex [GO:0071014]; precatalytic spliceosome [GO:0071011]; SMN-Sm protein complex [GO:0034719]; spliceosomal tri-snRNP complex [GO:0097526]; U1 snRNP [GO:0005685]; U2 snRNP [GO:0005686]; U2-type prespliceosome [GO:0071004]; U4 snRNP [GO:0005687]; U4/U6 x U5 tri-snRNP complex [GO:0046540]; U5 snRNP [GO:0005682]
|
RNA binding [GO:0003723]
|
PF01423;
|
2.30.30.100;
|
SnRNP Sm proteins family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (By similarity). {ECO:0000250|UniProtKB:P62308}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74971
|
ATG5_SCHPO
|
MNVDNNKGNIPELLWNGTISVRIDYEGNSLAYLANVPRQSYFAQILPNVQRLLAPSIPLSECWLDYNGVPLKWHWPVGLLFDLLTVFDPDTPRAPVLWRIQLRSGLFPTTKILQMETMDTFRTYFFNCLKESDYVRNGSSSGIIALSKAETDTYWNAILNHDYYDFRPIAIKILFSKSKFIPLKIYLGANAPIIQTSAPLGSSLGEFLNKRLPDLFPSCDKFLIVKPVIHGITIFLQSVLDELNRDFCYIDGFLHIVLMKV
| null | null |
autophagosome assembly [GO:0000045]; cellular response to nitrogen starvation [GO:0006995]; macroautophagy [GO:0016236]; meiotic cell cycle [GO:0051321]; mitophagy [GO:0000423]; piecemeal microautophagy of the nucleus [GO:0034727]; protein transport [GO:0015031]; reticulophagy [GO:0061709]
|
Atg12-Atg5-Atg16 complex [GO:0034274]; autophagosome [GO:0005776]; cytosol [GO:0005829]; mitochondria-associated endoplasmic reticulum membrane [GO:0044233]; nucleus [GO:0005634]; phagophore [GO:0061908]; phagophore assembly site [GO:0000407]; phagophore assembly site membrane [GO:0034045]
|
Atg8-family ligase activity [GO:0019776]
|
PF20637;PF20638;PF04106;
|
3.10.20.620;1.10.246.190;
|
ATG5 family
|
PTM: Conjugated to atg12; which is essential for autophagy.
|
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Preautophagosomal structure membrane; Peripheral membrane protein.
| null | null | null | null | null |
FUNCTION: Involved in cytoplasm to vacuole transport (Cvt) and autophagic vesicle formation. Autophagy is essential for maintenance of amino acid levels and protein synthesis under nitrogen starvation. Required for selective autophagic degradation of the nucleus (nucleophagy). Also required for mitophagy, which eliminates defective or superfluous mitochondria in order to fulfill cellular energy requirements and prevent excess ROS production. Conjugation with atg12, through a ubiquitin-like conjugating system involving atg7 as an E1-like activating enzyme and atg10 as an E2-like conjugating enzyme, is essential for its function. The atg12-atg5 conjugate acts as an E3-like enzyme which is required for lipidation of atg8 and atg8 association to the vesicle membranes (By similarity). Has a role in meiosis and sporulation. {ECO:0000250, ECO:0000269|PubMed:16303567, ECO:0000269|PubMed:19778961}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74986
|
COM1_SCHPO
|
MNEEEHNKSVHWSIVYRQLGNLLEQYEVEIARLKSQLVLEKKLRIQVEKELESVKTKQISSSASSKVSSNTIQELDSTTDEDEIPGSDTVDEEDPSLNAPFSEKNQSVKIPPHSPTLPVQNASAFVKPISVPLGNVKEEKFLDTNPIGAESFESSDGEMHLRARSPEDMILLRETQPLAPLDINTLGVSDNRQKKGTEKKRPFEPEFLNDDVIRGNKRKALPAYECPDCQKFYELHGPVKESSVAPTWNDENRLGGGSLPNCKHQPLVQKVGRHRKLNIPKPIPNGFWESDFVD
|
3.1.-.-
| null |
DNA double-strand break processing [GO:0000729]; double-strand break repair involved in meiotic recombination [GO:1990918]; double-strand break repair via homologous recombination [GO:0000724]; double-strand break repair via nonhomologous end joining [GO:0006303]; gene conversion at mating-type locus [GO:0007534]; meiotic DNA double-strand break processing [GO:0000706]; mitotic DNA replication checkpoint signaling [GO:0033314]; mitotic recombination-dependent replication fork processing [GO:1990426]; replication fork processing [GO:0031297]; stalled replication fork localization to nuclear periphery [GO:0120290]
|
nucleus [GO:0005634]; site of double-strand break [GO:0035861]
|
bubble DNA binding [GO:0000405]; DNA end binding [GO:0045027]; DNA-DNA tethering activity [GO:0106260]; double-strand/single-strand DNA junction binding [GO:0000406]; double-stranded DNA binding [GO:0003690]; endodeoxyribonuclease activator activity [GO:0140656]; endonuclease activity [GO:0004519]; flap-structured DNA binding [GO:0070336]; identical protein binding [GO:0042802]; single-stranded DNA binding [GO:0003697]; Y-form DNA binding [GO:0000403]
|
PF08573;
| null |
COM1/SAE2/CtIP family
|
PTM: Phosphorylated by tel1 in response to DNA damage; promoting interaction with nbs1 and recruitment to DSBs. {ECO:0000269|PubMed:18378696, ECO:0000269|PubMed:19804755, ECO:0000269|PubMed:19804756, ECO:0000269|PubMed:33836577}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19804755}. Chromosome {ECO:0000269|PubMed:19804755}. Note=Accumulates at DSBs; recruited to DSBs following phosphorylation and interaction with nbs1. {ECO:0000269|PubMed:19804755, ECO:0000269|PubMed:33836577}.
| null | null | null | null | null |
FUNCTION: Endonuclease that cooperates with the MRN complex in processing meiotic and mitotic double-strand breaks by allowing the endonucleolytic removal of rec12 from the break sites and ensuring both resection and intrachromosomal association of the broken ends (PubMed:16303567, PubMed:17936710, PubMed:18378696, PubMed:19139281, PubMed:33836577). Specifically promotes the endonuclease activity of the MRN complex to clear DNA ends containing protein adducts: recruited to DSBs by nbs1 following phosphorylation, and promotes the endonuclease of rad32 to clear protein-DNA adducts and generate clean double-strand break ends (PubMed:33836577). Required for the formation of RPA-coated single strand DNA adjacent to the DSBs where it functions together with the MRN complex in 5'- 3' resection (PubMed:16303567, PubMed:17936710, PubMed:18378696, PubMed:19139281). Required for the repair of programmed meiotic DSBs (PubMed:16303567, PubMed:17936710, PubMed:18378696, PubMed:19139281). Involved also in an rhp51 recombinase-dependent recombinational repair pathway (PubMed:16303567, PubMed:17936710, PubMed:18378696, PubMed:19139281). {ECO:0000269|PubMed:16303567, ECO:0000269|PubMed:17936710, ECO:0000269|PubMed:18378696, ECO:0000269|PubMed:19139281, ECO:0000269|PubMed:33836577}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74991
|
POF3_SCHPO
|
MNNYQVKAIKEKTQQYLSKRKFEDALTFITKTIEQEPNPTIDLFELRAQVYEKSGQYSQAELDAKRMIHLNARNARGYLRLGKLLQLDGFDKKADQLYTQGLRMVHKMDPLRPVLKKVSQRLNERILRTRPVLDLFRILPREVLLCILQQLNFKSIVQCMQVCKHWRDCIKKEPSLFCCLDFSCASPRSVNSRDRNVMAVARYSVYSKDNIQEVIGLEKLGILTPTKALLRSVKSLKVYKTISPLHTQSTDKLYTIWTPFSELHYFYCATPITFSIASKILSCCKKLKQVELVDLIPDLIFDSMDWDKLFNAESVPLALKSLTFIRNQKFPFHHKEQQFLKDLLSASPYLEYLEASYQSDLVAAIKKYKINLRSLIIIDEGVSNTVKDLAFLPQSLTTLIVKPCNPASTILCPYLFPTNVRMESLINLELFLYLRLSQNDIDNVVKFLTSCYKLKKLVLHDSLALAPHFFEIFASLPELEHLEIPDNVALQNKHAIHITDCCPNLKYVNFSNSISLDGSGFIAVLRGLKELKRIDIINCDSVSRDAIDWARSKGMQVTVASSLPNSQPLGTKKIRLI
| null | null |
negative regulation of mitotic cell cycle DNA replication [GO:1903464]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146]; telomere maintenance [GO:0000723]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
mitochondrion [GO:0005739]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]
|
ubiquitin ligase-substrate adaptor activity [GO:1990756]
|
PF12937;
|
1.20.1280.50;3.80.10.10;1.25.40.10;
| null | null |
SUBCELLULAR LOCATION: Mitochondrion. Nucleus.
| null | null | null | null | null |
FUNCTION: Has a role in substrate recognition in the Skp1-Cullin-1/Cdc53-F-box (SCF) ubiquitin ligase complex. Required for the maintenance of telomere length and transcriptional silencing at the telomere. Also required for chromosome segregation. {ECO:0000269|PubMed:11809834}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O75001
|
MCM7_SCHPO
|
MALPTIDLKIPEYEECQHKITDFLSHFKQEQVQDGQQNQDISMSDAGDEPFLKSKYMDILQKISNRESNVINVDLNDLYEFDPSDTQLLHNIESNAKRFVELFSQCADALMPPPTVEINYRNEVLDVIMQQRVQRNENIDPEHKGFPPELTRGYDLYFRPVTRNKKPFSVRDLRGENLGSLLTVRGIVTRTSDVKPSLTVNAYTCDRCGYEVFQEIRQKTFLPMSECPSDECKKNDAKGQLFMSTRASKFLPFQEVKIQELTNQVPIGHIPRSLTVHLYGAITRSVNPGDIVDISGIFLPTPYTGFRAMRAGLLTDTYLECHYVSQIIKNYTNIEKTPQSEAAIAELNQGGNVYEKLAKSIAPEIYGHEDVKKALLLLLVGGVTKELGDGMRIRGDINICLTGDPGVAKSQLLKYISKVAPRGVYTTGRGSSGVGLTAAVMRDPVTDEMVLEGGALVLADNGICCIDEFDKMDESDRTAIHEVMEQQTISISKAGITTTLNARTSILAAANPLYGRYNPKVAPIHNINLPAALLSRFDILFLILDTPSRETDEHLAQHVTYVHMHNEQPKMDFEPLDPNMIRHYISSARQYRPVVPKDVCDYVTGAYVQLRQNQKRDEANERQFAHTTPRTLLAILRMGQALARLRFSNRVEIGDVDEALRLMSVSKSSLYDDLDPSSHDTTITSKIYKIIRDMLNSIPDVEGNERSLTLRAIRERVLAKGFTEDHLINTIQEYTDLGVLLTTNNGQTIMFLDPDLHMEN
|
3.6.4.12
| null |
DNA replication initiation [GO:0006270]; DNA strand elongation involved in DNA replication [GO:0006271]; DNA unwinding involved in DNA replication [GO:0006268]; double-strand break repair via break-induced replication [GO:0000727]; mitotic DNA replication initiation [GO:1902975]; premeiotic DNA replication [GO:0006279]
|
chromatin [GO:0000785]; DNA replication preinitiation complex [GO:0031261]; MCM complex [GO:0042555]; MCM core complex [GO:0097373]; nuclear pre-replicative complex [GO:0005656]; nuclear replication fork [GO:0043596]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; single-stranded DNA binding [GO:0003697]; single-stranded DNA helicase activity [GO:0017116]
|
PF00493;PF17855;PF14551;PF17207;
|
2.20.28.10;3.30.1640.10;2.40.50.140;3.40.50.300;
|
MCM family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11606526}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000250|UniProtKB:P33993}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:P33993};
| null | null | null | null |
FUNCTION: Acts as a component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (By similarity). Required for the progression of S phase (PubMed:11606526). {ECO:0000250|UniProtKB:P33993, ECO:0000269|PubMed:11606526}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O75003
|
TREPH_GRIFR
|
MAPPHQFQSKPSDVIRRRLSSAVSSKRPNIPGYTSLTPMWAGIAGAVVNNNTQFEVAISIHDSVYNTDFASSVVPYSPNEPEAQAGIIEKHVLETLRKFSTEHMCKFLGAGVTVILLREAPNLCTRLWLDMDIVPIVFNIKPFHTDSITRPNVRHRISSTTGSYVPSGAETPTVYYDPAQLQDPNKLSANVQTRLPIPRTVDEQADSAARKCIMYFGPGNNPRLQIGPRNQVAVDAGGKIHLIDDIDEYRKTVGKGTWNSVIKLADELREKKIKIGFFSSTPQGGGVALMRHAIIRFFTALDVDAAWYVPNPSPSVFRTTKNNHNILQGVADPSLRLTKEAADNFDSWILKNGLRWTAEGGPLAPGGVDIAFIDDPQMPGLIPLIKRIRPDLPIIYRSHIEIRSDLVHVKGSPQEEVWNYLWNNIQHSDLFISHPVNKFVPSDVPLEKLALLGAATDWLDGLSKHLDAWDSQYYMGEFRNLCVKEKMNELGWPAREYIVQIARFDPSKGIPNVIDSYARFRKLCVDKVMEDDIPQLLLCGHGAVDDPDASIIYDQVLQLIHAKYKEYAPDIVVMRCPPSDQLLNTLMANAKFALQLSTREGFEVKVSEALHAGKPVIACRTGGIPLQIEHGKSGYLCEPGDNAAVAQHMLDLYTDEDLYDTMSEYARTHVSDEVGTVGNAAAWMYLAVMYVSRGVKLRPHGAWINDLMRTEMGEPYRPGEPRLPRGELHVQG
|
2.4.1.231
| null |
glucose 6-phosphate metabolic process [GO:0051156]; glucose metabolic process [GO:0006006]; trehalose metabolic process [GO:0005991]
| null |
alpha,alpha-trehalose phosphorylase (configuration-retaining) activity [GO:0033832]
|
PF00534;PF21269;
|
3.40.50.2000;
|
Glycosyltransferase group 1 family, Glycosyltransferase 4 subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=alpha,alpha-trehalose + phosphate = alpha-D-glucose + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:16257, ChEBI:CHEBI:16551, ChEBI:CHEBI:17925, ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.231; Evidence={ECO:0000269|PubMed:9763690, ECO:0000269|PubMed:9797287};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 for trehalose phosphorolysis activity, 6.5-6.8 for trehalose synthesis activity. {ECO:0000269|PubMed:9797287};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 32.5 degrees Celsius for trehalose phosphorolysis activity, 37.5 degrees Celsius for trehalose synthesis activity. Stable up to 35 degrees Celsius for trehalose phosphorolysis activity, 32.5 degrees Celsius for trehalose synthesis activity. {ECO:0000269|PubMed:9797287};
|
FUNCTION: Reversibly catalyzes the synthesis and degradation of trehalose from glucose and alpha-D-glucose 1-phosphate. The equilibrium lies in the direction of trehalose synthesis. {ECO:0000269|PubMed:9763690, ECO:0000269|PubMed:9797287}.
|
Grifola frondosa (Maitake) (Polyporus frondosus)
|
O75011
|
NAK1_SCHPO
|
MENNTASSPYTKLELVGRGSYGAVYRGICNLTKETVAIKILNLDTDEDEVSDIQKEVAVLSELKQSDVENIIKYHGSYLVGTNLWIIMDYCHGGSVRTLMEAGPISEPCISLILRETLQALKFIHHAGIIHRDIKAANILVSMSGNVKLCDFGVAAELNINRRKRITFIGTPYWMAPEVIRDGQEYNVMADIWSLGITAYEIATGSPPHAKEDPFRAVYLIAHTAPPRLNGNFSALLKEFIASCLQDVPQRRLDSSELLKSKFIKQYSRMSISELTNVVKRYDTWQAAGGIPQTLLLGEEADDGSDPDQETSDTAASDDGWEFGTIKQGQSNVSSITGTSTSTTTAATSSTTVTGTVIPKSSTVHEPPSSNDSHPLLQLFKDSKISDDDSPSNAEGASTEDSKGEVSYSQIELPSLDSSNLSSKKSTIQSKHTKQAEDYDLFVGRTRSNSKTSSDQSIKRPLPRVVQRQKTSLGKRGISMSPMKPGLRMPSSFDLQSRSISMGAFEQLSTPLEAPAHKHSAVLQPLEVNRSISIPPPKSISPSILHKPSLESASSTPKISSCSSTPKPFNSKLRAHLPPLSIGSPAVQPLANDNYDSLGVRGLNMELFNDYPGNMHNIKSVLSLEIDIVLGEMDACLKSLECNLLNRKAYNE
|
2.7.11.1
| null |
establishment or maintenance of actin cytoskeleton polarity [GO:0030950]; establishment or maintenance of cell polarity [GO:0007163]; phosphorylation [GO:0016310]; positive regulation of establishment or maintenance of bipolar cell polarity regulating cell shape [GO:2000247]; protein localization to medial cortex [GO:0071574]; RAM/MOR signaling [GO:0062200]; regulation of establishment or maintenance of bipolar cell polarity regulating cell shape [GO:2000100]
|
actin cortical patch [GO:0030479]; cell division site [GO:0032153]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitotic actomyosin contractile ring [GO:0110085]; mitotic spindle pole body [GO:0044732]; new mitotic spindle pole body [GO:0071958]
|
ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
|
PTM: Autophosphorylated. {ECO:0000305|PubMed:18257517}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12427731}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Has a role in the regulation of cell polarity, growth and division. {ECO:0000269|PubMed:12427731}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O75015
|
FCG3B_HUMAN
|
MWQLLLPTALLLLVSAGMRTEDLPKAVVFLEPQWYSVLEKDSVTLKCQGAYSPEDNSTQWFHNENLISSQASSYFIDAATVNDSGEYRCQTNLSTLSDPVQLEVHIGWLLLQAPRWVFKEEDPIHLRCHSWKNTALHKVTYLQNGKDRKYFHHNSDFHIPKATLKDSGSYFCRGLVGSKNVSSETVNITITQGLAVSTISSFSPPGYQVSFCLVMVLLFAVDTGLYFSVKTNI
| null | null |
antibody-dependent cellular cytotoxicity [GO:0001788]; cell surface receptor signaling pathway [GO:0007166]; immune response [GO:0006955]
|
external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]; secretory granule membrane [GO:0030667]
|
GPI anchor binding [GO:0034235]; IgG binding [GO:0019864]; IgG receptor activity [GO:0019770]
|
PF13895;
|
2.60.40.10;
| null |
PTM: Glycosylated. Glycosylation plays an inhibitory role in the interaction with IgG3.; PTM: The soluble form is produced by a proteolytic cleavage.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1825220}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:1825220}. Secreted. Note=Secreted after cleavage.
| null | null | null | null | null |
FUNCTION: Receptor for the Fc region of immunoglobulins gamma. Low affinity receptor. Binds complexed or aggregated IgG and also monomeric IgG. Contrary to III-A, is not capable to mediate antibody-dependent cytotoxicity and phagocytosis. May serve as a trap for immune complexes in the peripheral circulation which does not activate neutrophils.
|
Homo sapiens (Human)
|
O75019
|
LIRA1_HUMAN
|
MTPIVTVLICLRLSLGPRTHVQAGTLPKPTLWAEPGSVITQGSPVTLWCQGILETQEYRLYREKKTAPWITRIPQEIVKKGQFPIPSITWEHTGRYRCFYGSHTAGWSEPSDPLELVVTGAYIKPTLSALPSPVVTSGGNVTLHCVSQVAFGSFILCKEGEDEHPQCLNSQPRTHGWSRAIFSVGPVSPSRRWSYRCYAYDSNSPHVWSLPSDLLELLVLGVSKKPSLSVQPGPIVAPGESLTLQCVSDVSYDRFVLYKEGERDFLQLPGPQPQAGLSQANFTLGPVSRSYGGQYRCSGAYNLSSEWSAPSDPLDILIAGQFRGRPFISVHPGPTVASGENVTLLCQSWGPFHTFLLTKAGAADAPLRLRSIHEYPKYQAEFPMSPVTSAHSGTYRCYGSLSSNPYLLSHPSDSLELMVSGAAETLSPPQNKSDSKAGAANTLSPSQNKTASHPQDYTVENLIRMGIAGLVLVVLGILLFEAQHSQRSL
| null | null |
adaptive immune response [GO:0002250]; cell surface receptor signaling pathway [GO:0007166]; cytokine-mediated signaling pathway [GO:0019221]; defense response [GO:0006952]
|
plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]; inhibitory MHC class I receptor activity [GO:0032396]; transmembrane signaling receptor activity [GO:0004888]
|
PF13895;PF13927;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: May act as receptor for class I MHC antigens.
|
Homo sapiens (Human)
|
O75022
|
LIRB3_HUMAN
|
MTPALTALLCLGLSLGPRTRVQAGPFPKPTLWAEPGSVISWGSPVTIWCQGSQEAQEYRLHKEGSPEPLDRNNPLEPKNKARFSIPSMTEHHAGRYRCHYYSSAGWSEPSDPLEMVMTGAYSKPTLSALPSPVVASGGNMTLRCGSQKGYHHFVLMKEGEHQLPRTLDSQQLHSRGFQALFPVGPVTPSHRWRFTCYYYYTNTPWVWSHPSDPLEILPSGVSRKPSLLTLQGPVLAPGQSLTLQCGSDVGYNRFVLYKEGERDFLQRPGQQPQAGLSQANFTLGPVSPSNGGQYRCYGAHNLSSEWSAPSDPLNILMAGQIYDTVSLSAQPGPTVASGENVTLLCQSWWQFDTFLLTKEGAAHPPLRLRSMYGAHKYQAEFPMSPVTSAHAGTYRCYGSYSSNPHLLSHPSEPLELVVSGHSGGSSLPPTGPPSTPGLGRYLEVLIGVSVAFVLLLFLLLFLLLRRQRHSKHRTSDQRKTDFQRPAGAAETEPKDRGLLRRSSPAADVQEENLYAAVKDTQSEDRVELDSQSPHDEDPQAVTYAPVKHSSPRREMASPPSSLSGEFLDTKDRQVEEDRQMDTEAAASEASQDVTYAQLHSLTLRRKATEPPPSQEGEPPAEPSIYATLAIH
| null | null |
adaptive immune response [GO:0002250]; cell surface receptor signaling pathway [GO:0007166]; cytokine-mediated signaling pathway [GO:0019221]; defense response [GO:0006952]; negative regulation of osteoclast differentiation [GO:0045671]
|
plasma membrane [GO:0005886]; secretory granule membrane [GO:0030667]
|
inhibitory MHC class I receptor activity [GO:0032396]; signaling receptor activity [GO:0038023]; transmembrane signaling receptor activity [GO:0004888]
|
PF00047;PF13895;
|
2.60.40.10;
| null |
PTM: Phosphorylated on tyrosine residues by LYN. Phosphorylation at Tyr-595 and Tyr-625 is important for interaction with PTPN6/SHP-1 and PTPN11/SHP-2. {ECO:0000250|UniProtKB:P97484}.
|
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: May act as receptor for class I MHC antigens. Becomes activated upon coligation of LILRB3 and immune receptors, such as FCGR2B and the B-cell receptor. Down-regulates antigen-induced B-cell activation by recruiting phosphatases to its immunoreceptor tyrosine-based inhibitor motifs (ITIM). {ECO:0000250|UniProtKB:P97484}.
|
Homo sapiens (Human)
|
O75023
|
LIRB5_HUMAN
|
MTLTLSVLICLGLSVGPRTCVQAGTLPKPTLWAEPASVIARGKPVTLWCQGPLETEEYRLDKEGLPWARKRQNPLEPGAKAKFHIPSTVYDSAGRYRCYYETPAGWSEPSDPLELVATGFYAEPTLLALPSPVVASGGNVTLQCDTLDGLLTFVLVEEEQKLPRTLYSQKLPKGPSQALFPVGPVTPSCRWRFRCYYYYRKNPQVWSNPSDLLEILVPGVSRKPSLLIPQGSVVARGGSLTLQCRSDVGYDIFVLYKEGEHDLVQGSGQQPQAGLSQANFTLGPVSRSHGGQYRCYGAHNLSPRWSAPSDPLDILIAGLIPDIPALSVQPGPKVASGENVTLLCQSWHQIDTFFLTKEGAAHPPLCLKSKYQSYRHQAEFSMSPVTSAQGGTYRCYSAIRSYPYLLSSPSYPQELVVSGPSGDPSLSPTGSTPTPGPEDQPLTPTGLDPQSGLGRHLGVVTGVSVAFVLLLFLLLFLLLRHRHQSKHRTSAHFYRPAGAAGPEPKDQGLQKRASPVADIQEEILNAAVKDTQPKDGVEMDAPAAASEAPQDVTYAQLHSLTLRREATEPPPSQEREPPAEPSIYAPLAIH
| null | null |
adaptive immune response [GO:0002250]; cell surface receptor signaling pathway [GO:0007166]; cytokine-mediated signaling pathway [GO:0019221]; defense response [GO:0006952]
|
plasma membrane [GO:0005886]
|
inhibitory MHC class I receptor activity [GO:0032396]; transmembrane signaling receptor activity [GO:0004888]
|
PF00047;PF13895;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: May act as receptor for class I MHC antigens.
|
Homo sapiens (Human)
|
O75027
|
ABCB7_HUMAN
|
MALLAMHSWRWAAAAAAFEKRRHSAILIRPLVSVSGSGPQWRPHQLGALGTARAYQIPESLKSITWQRLGKGNSGQFLDAAKALQVWPLIEKRTCWHGHAGGGLHTDPKEGLKDVDTRKIIKAMLSYVWPKDRPDLRARVAISLGFLGGAKAMNIVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKCGAQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTQIKDKVMASPLQITPQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANPHSIYSEMWHTQSSRVQNHDNPKWEAKKENISKEEERKKLQEEIVNSVKGCGNCSC
| null | null |
intracellular iron ion homeostasis [GO:0006879]; iron ion transmembrane transport [GO:0034755]; iron-sulfur cluster assembly [GO:0016226]; iron-sulfur cluster export from the mitochondrion [GO:0140466]; negative regulation of reactive oxygen species biosynthetic process [GO:1903427]; positive regulation of heme biosynthetic process [GO:0070455]; positive regulation of iron-sulfur cluster assembly [GO:1903331]; transmembrane transport [GO:0055085]
|
mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]
|
ABC-type iron-sulfur cluster transporter activity [GO:0140481]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; heme transmembrane transporter activity [GO:0015232]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]
|
PF00664;PF00005;
|
1.20.1560.10;3.40.50.300;
|
ABC transporter superfamily, ABCB family, Heavy Metal importer (TC 3.A.1.210) subfamily
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P40416}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P40416}.
|
CATALYTIC ACTIVITY: Reaction=(glutathione)4[2Fe(III)-2S] cluster(in) + ATP + H2O = (glutathione)4[2Fe(III)-2S] cluster(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:67028, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167627, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:33157103}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67029; Evidence={ECO:0000305|PubMed:33157103};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.3 mM for Mg-ATP {ECO:0000269|PubMed:33157103}; KM=0.54 mM for Mg-ATP (in the presence of the [2Fe-2S](GS)4 cluster) {ECO:0000269|PubMed:33157103};
| null | null | null |
FUNCTION: Exports glutathione-coordinated iron-sulfur clusters such as [2Fe-2S]-(GS)4 cluster from the mitochondria to the cytosol in an ATP-dependent manner allowing the assembly of the cytosolic iron-sulfur (Fe/S) cluster-containing proteins and participates in iron homeostasis (PubMed:10196363, PubMed:17192393, PubMed:33157103). Moreover, through a functional complex formed of ABCB7, FECH and ABCB10, also plays a role in the cellular iron homeostasis, mitochondrial function and heme biosynthesis (PubMed:30765471). In cardiomyocytes, regulates cellular iron homeostasis and cellular reactive oxygen species (ROS) levels through its interaction with COX4I1 (By similarity). May also play a role in hematopoiesis (By similarity). {ECO:0000250|UniProtKB:Q61102, ECO:0000250|UniProtKB:Q704E8, ECO:0000269|PubMed:10196363, ECO:0000269|PubMed:17192393, ECO:0000269|PubMed:30765471, ECO:0000269|PubMed:33157103}.
|
Homo sapiens (Human)
|
O75030
|
MITF_HUMAN
|
MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKSSSSAEHPGASKPPISSSSMTSRILLRQQLMREQMQEQERREQQQKLQAAQFMQQRVPVSQTPAINVSVPTTLPSATQVPMEVLKVQTHLENPTKYHIQQAQRQQVKQYLSTTLANKHANQVLSLPCPNQPGDHVMPPVPGSSAPNSPMAMLTLNSNCEKEGFYKFEEQNRAESECPGMNTHSRASCMQMDDVIDDIISLESSYNEEILGLMDPALQMANTLPVSGNLIDLYGNQGLPPPGLTISNSCPANLPNIKRELTACIFPTESEARALAKERQKKDNHNLIERRRRFNINDRIKELGTLIPKSNDPDMRWNKGTILKASVDYIRKLQREQQRAKELENRQKKLEHANRHLLLRIQELEMQARAHGLSLIPSTGLCSPDLVNRIIKQEPVLENCSQDLLQHHADLTCTTTLDLTDGTITFNNNLGTGTEANQAYSVPTKMGSKLEDILMDDTLSPVGVTDPLLSSVSPGASKTSSRRSSMSMEETEHTC
| null | null |
bone remodeling [GO:0046849]; camera-type eye development [GO:0043010]; cell fate commitment [GO:0045165]; melanocyte apoptotic process [GO:1902362]; melanocyte differentiation [GO:0030318]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell migration [GO:0030336]; negative regulation of transcription by RNA polymerase II [GO:0000122]; osteoclast differentiation [GO:0030316]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of DNA-templated transcription initiation [GO:2000144]; positive regulation of gene expression [GO:0010628]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein-containing complex assembly [GO:0065003]; regulation of cell population proliferation [GO:0042127]; regulation of DNA-templated transcription [GO:0006355]; regulation of osteoclast differentiation [GO:0045670]; regulation of RNA biosynthetic process [GO:2001141]; regulation of transcription by RNA polymerase II [GO:0006357]; Wnt signaling pathway [GO:0016055]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; lysosomal membrane [GO:0005765]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
|
chromatin binding [GO:0003682]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; E-box binding [GO:0070888]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF11851;PF00010;PF15951;
|
4.10.280.10;
|
MiT/TFE family
|
PTM: When nutrients are present, phosphorylation by MTOR at Ser-5 via non-canonical mTORC1 pathway promotes ubiquitination by the SCF(BTRC) complex, followed by degradation (PubMed:36608670). Phosphorylation at Ser-405 significantly enhances the ability to bind the tyrosinase promoter (PubMed:10587587). Phosphorylation by MARK3/cTAK1 at Ser-280 promotes association with 14-3-3/YWHA adapters and retention in the cytosol (PubMed:16822840). Phosphorylated at Ser-180 and Ser-516 following KIT signaling, triggering a short live activation: Phosphorylation at Ser-180 and Ser-516 by MAPK and RPS6KA1, respectively, activate the transcription factor activity but also promote ubiquitination and subsequent degradation by the proteasome (PubMed:10673502). Phosphorylated in response to blue light (415nm) (PubMed:28842328). {ECO:0000269|PubMed:10587587, ECO:0000269|PubMed:10673502, ECO:0000269|PubMed:16822840, ECO:0000269|PubMed:28842328, ECO:0000269|PubMed:36608670}.; PTM: Ubiquitinated by the SCF(BTRC) and SCF(FBXW11) complexes following phosphorylation ar Ser-5 by MTOR, leading to its degradation by the proteasome (PubMed:36608670). Ubiquitinated following phosphorylation at Ser-180, leading to subsequent degradation by the proteasome (PubMed:10673502). Deubiquitinated by USP13, preventing its degradation (PubMed:10673502). {ECO:0000269|PubMed:10673502, ECO:0000269|PubMed:36608670}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16822840, ECO:0000269|PubMed:27889061, ECO:0000269|PubMed:28842328, ECO:0000269|PubMed:36608670}. Cytoplasm {ECO:0000269|PubMed:16822840, ECO:0000269|PubMed:28842328, ECO:0000269|PubMed:36608670}. Lysosome membrane {ECO:0000269|PubMed:23401004, ECO:0000269|PubMed:36608670}. Note=When nutrients are present, recruited to the lysosomal membrane via association with GDP-bound RagC/RRAGC (or RagD/RRAGD): it is then phosphorylated by MTOR (PubMed:23401004, PubMed:36608670). Phosphorylation by MTOR promotes ubiquitination and degradation (PubMed:36608670). Conversely, inhibition of mTORC1, starvation and lysosomal disruption, promotes dephosphorylation and translocation to the nucleus (PubMed:36608670). Phosphorylation by MARK3/cTAK1 promotes association with 14-3-3/YWHA adapters and retention in the cytosol (PubMed:16822840). {ECO:0000269|PubMed:16822840, ECO:0000269|PubMed:23401004, ECO:0000269|PubMed:36608670}.
| null | null | null | null | null |
FUNCTION: Transcription factor that acts as a master regulator of melanocyte survival and differentiation as well as melanosome biogenesis (PubMed:10587587, PubMed:22647378, PubMed:27889061, PubMed:9647758). Binds to M-boxes (5'-TCATGTG-3') and symmetrical DNA sequences (E-boxes) (5'-CACGTG-3') found in the promoter of pigmentation genes, such as tyrosinase (TYR) (PubMed:10587587, PubMed:22647378, PubMed:27889061, PubMed:9647758). Involved in the cellular response to amino acid availability by acting downstream of MTOR: in the presence of nutrients, MITF phosphorylation by MTOR promotes its inactivation (PubMed:36608670). Upon starvation or lysosomal stress, inhibition of MTOR induces MITF dephosphorylation, resulting in transcription factor activity (PubMed:36608670). Plays an important role in melanocyte development by regulating the expression of tyrosinase (TYR) and tyrosinase-related protein 1 (TYRP1) (PubMed:10587587, PubMed:22647378, PubMed:27889061, PubMed:9647758). Plays a critical role in the differentiation of various cell types, such as neural crest-derived melanocytes, mast cells, osteoclasts and optic cup-derived retinal pigment epithelium (PubMed:10587587, PubMed:22647378, PubMed:27889061, PubMed:9647758). {ECO:0000269|PubMed:10587587, ECO:0000269|PubMed:22647378, ECO:0000269|PubMed:27889061, ECO:0000269|PubMed:36608670, ECO:0000269|PubMed:9647758}.
|
Homo sapiens (Human)
|
O75031
|
HSF2B_HUMAN
|
MGEAGAAEEACRHMGTKEEFVKVRKKDLERLTTEVMQIRDFLPRILNGEVLESFQKLKIVEKNLERKEQELEQLKMDCEHFKARLETVQADNIREKKEKLALRQQLNEAKQQLLQQAEYCTEMGAAACTLLWGVSSSEEVVKAILGGDKALKFFSITGQTMESFVKSLDGDVQELDSDESQFVFALAGIVTNVAAIACGREFLVNSSRVLLDTILQLLGDLKPGQCTKLKVLMLMSLYNVSINLKGLKYISESPGFIPLLWWLLSDPDAEVCLHVLRLVQSVVLEPEVFSKSASEFRSSLPLQRILAMSKSRNPRLQTAAQELLEDLRTLEHNV
| null | null |
double-strand break repair involved in meiotic recombination [GO:1990918]; female meiosis I [GO:0007144]; male meiosis I [GO:0007141]; spermatogenesis [GO:0007283]; transcription by RNA polymerase II [GO:0006366]
|
chromosome [GO:0005694]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]
| null | null |
1.25.10.10;
| null |
PTM: Sumoylated by UBE2I in response to MEKK1-mediated stimuli. {ECO:0000269|PubMed:17709345}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9D4G2}. Chromosome {ECO:0000269|PubMed:31242413}. Note=Localizes on double-strand breaks (DSBs) in mitotic and meiotic chromosomes. {ECO:0000269|PubMed:31242413}.
| null | null | null | null | null |
FUNCTION: Meiotic recombination factor component of recombination bridges involved in meiotic double-strand break repair. Modulates the localization of recombinases DMC1:RAD51 to meiotic double-strand break (DSB) sites through the interaction with BRCA2 and its recruitment during meiotic recombination (By similarity) (PubMed:31242413). Indispensable for the DSB repair, homologous synapsis, and crossover formation that are needed for progression past metaphase I, is essential for spermatogenesis and male fertility (By similarity). Required for proper recombinase recruitment in female meiosis (By similarity). Inhibits BNC1 transcriptional activity during spermatogenesis, probably by sequestering it in the cytoplasm (By similarity). May be involved in modulating HSF2 activation in testis (PubMed:9651507). {ECO:0000250|UniProtKB:Q9D4G2, ECO:0000269|PubMed:31242413, ECO:0000269|PubMed:9651507}.
|
Homo sapiens (Human)
|
O75037
|
KI21B_HUMAN
|
MAGQGDCCVKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAYGQTGAGKTYTMGTGFDMATSEEEQGIIPRAIAHLFGGIAERKRRAQEQGVAGPEFKVSAQFLELYNEEILDLFDSTRDPDTRHRRSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMRMCTQPDLVNEAVTGLPDGTPPSSEYETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDQSKKVVHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVVVNQDKTSQQISALRAEIARLQMELMEYKAGKRVIGEDGAEGYSDLFRENAMLQKENGALRLRVKAMQEAIDAINNRVTQLMSQEANLLLAKAGDGNEAIGALIQNYIREIEELRTKLLESEAMNESLRRSLSRASARSPYSLGASPAAPAFGGSPASSMEDASEVIRRAKQDLERLKKKEVRQRRKSPEKEAFKKRAKLQQENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSDPEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKPPMLDSGAEVSASTTSSEAESGARSVSSIVRQWNRKINHFLGDHPAPTVNGTRPARKKFQKKGASQSFSKAARLKWQSLERRIIDIVMQRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEETKEELDSTDTSVVISSCSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQTDMAGSSQNHLLLDALREKAEAHPELQALIYNVQQENGYASTDEEISEFSEGSFSQSFTMKGSTSHDDFKFKSEPKLSAQMKAVSAECLGPPLDISTKNITKSLASLVEIKEDGVGFSVRDPYYRDRVSRTVSLPTRGSTFPRQSRATETSPLTRRKSYDRGQPIRSTDVGFTPPSSPPTRPRNDRNVFSRLTSNQSQGSALDKSDDSDSSLSEVLRGIISPVGGAKGARTAPLQCVSMAEGHTKPILCLDATDELLFTGSKDRSCKMWNLVTGQEIAALKGHPNNVVSIKYCSHSGLVFSVSTSYIKVWDIRDSAKCIRTLTSSGQVISGDACAATSTRAITSAQGEHQINQIALSPSGTMLYAASGNAVRIWELSRFQPVGKLTGHIGPVMCLTVTQTASQHDLVVTGSKDHYVKMFELGECVTGTIGPTHNFEPPHYDGIECLAIQGDILFSGSRDNGIKKWDLDQQELIQQIPNAHKDWVCALAFIPGRPMLLSACRAGVIKVWNVDNFTPIGEIKGHDSPINAICTNAKHIFTASSDCRVKLWNYVPGLTPCLPRRVLAIKGRATTLP
| null | null |
microtubule-based movement [GO:0007018]; mitotic spindle organization [GO:0007052]; spindle elongation [GO:0051231]
|
cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425]; growth cone [GO:0030426]; kinesin complex [GO:0005871]; microtubule [GO:0005874]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]
|
PF00225;PF00400;
|
3.40.850.10;2.130.10.10;
|
TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9QXL1}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9QXL1}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q9QXL1}. Cell projection, axon {ECO:0000250|UniProtKB:Q9QXL1}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:F1M5N7}.
| null | null | null | null | null |
FUNCTION: Plus-end directed microtubule-dependent motor protein which displays processive activity. Is involved in regulation of microtubule dynamics, synapse function and neuronal morphology, including dendritic tree branching and spine formation. Plays a role in lerning and memory. Involved in delivery of gamma-aminobutyric acid (GABA(A)) receptor to cell surface. {ECO:0000250|UniProtKB:Q9QXL1}.
|
Homo sapiens (Human)
|
O75038
|
PLCH2_HUMAN
|
MSGPWPSPDSRTKGTVAWLAEVLLWVGGSVVLSSEWQLGPLVERCMGAMQEGMQMVKLRGGSKGLVRFYYLDEHRSCIRWRPSRKNEKAKISIDSIQEVSEGRQSEVFQRYPDGSFDPNCCFSIYHGSHRESLDLVSTSSEVARTWVTGLRYLMAGISDEDSLARRQRTRDQWLKQTFDEADKNGDGSLSIGEVLQLLHKLNVNLPRQRVKQMFREADTDDHQGTLGFEEFCAFYKMMSTRRDLYLLMLTYSNHKDHLDAASLQRFLQVEQKMAGVTLESCQDIIEQFEPCPENKSKGLLGIDGFTNYTRSPAGDIFNPEHHHVHQDMTQPLSHYFITSSHNTYLVGDQLMSQSRVDMYAWVLQAGCRCVEVDCWDGPDGEPIVHHGYTLTSKILFKDVIETINKYAFIKNEYPVILSIENHCSVIQQKKMAQYLTDILGDKLDLSSVSSEDATTLPSPQMLKGKILVKGKKLPANISEDAEEGEVSDEDSADEIDDDCKLLNGDASTNRKRVENTAKRKLDSLIKESKIRDCEDPNNFSVSTLSPSGKLGRKSKAEEDVESGEDAGASRRNGRLVVGSFSRRKKKGSKLKKAASVEEGDEGQDSPGGQSRGATRQKKTMKLSRALSDLVKYTKSVATHDIEMEAASSWQVSSFSETKAHQILQQKPAQYLRFNQQQLSRIYPSSYRVDSSNYNPQPFWNAGCQMVALNYQSEGRMLQLNRAKFSANGGCGYVLKPGCMCQGVFNPNSEDPLPGQLKKQLVLRIISGQQLPKPRDSMLGDRGEIIDPFVEVEIIGLPVDCSREQTRVVDDNGFNPTWEETLVFMVHMPEIALVRFLVWDHDPIGRDFIGQRTLAFSSMMPGYRHVYLEGMEEASIFVHVAVSDISGKVKQALGLKGLFLRGPKPGSLDSHAAGRPPARPSVSQRILRRTASAPTKSQKPGRRGFPELVLGTRDTGSKGVADDVVPPGPGPAPEAPAQEGPGSGSPRDTRPLSTQRPLPPLCSLETIAEEPAPGPGPPPPAAVPTSSSQGRPPYPTGPGANVASPLEDTEEPRDSRPRPCNGEGAGGAYERAPGSQTDGRSQPRTLGHLPVIRRVKSEGQVPTEPLGGWRPLAAPFPAPAVYSDATGSDPLWQRLEPCGHRDSVSSSSSMSSSDTVIDLSLPSLGLGRSRENLAGAHMGRLPPRPHSASAARPDLPPVTKSKSNPNLRATGQRPPIPDELQPRSLAPRMAGLPFRPPWGCLSLVGVQDCPVAAKSKSLGDLTADDFAPSFEGGSRRLSHSLGLPGGTRRVSGPGVRRDTLTEQLRWLTVFQQAGDITSPTSLGPAGEGVAGGPGFVRRSSSRSHSRVRAIASRARQAQERQQRLQGLGRQGPPEEERGTPEGACSVGHEGSVDAPAPSKGALGPASAAAENLVLLRL
|
3.1.4.11
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
|
lipid catabolic process [GO:0016042]; phosphatidylinositol metabolic process [GO:0046488]; phosphatidylinositol-mediated signaling [GO:0048015]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; release of sequestered calcium ion into cytosol [GO:0051209]
|
cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; phosphatidylinositol phospholipase C activity [GO:0004435]
|
PF00168;PF09279;PF16457;PF00388;PF00387;
|
2.60.40.150;1.10.238.10;3.20.20.190;2.30.29.30;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2AP18}. Cell membrane {ECO:0000250|UniProtKB:A2AP18}. Note=Localized predominantly at the plasma membrane. {ECO:0000250|UniProtKB:A2AP18}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456, ChEBI:CHEBI:203600; EC=3.1.4.11; Evidence={ECO:0000269|PubMed:18361507}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180; Evidence={ECO:0000305|PubMed:18361507};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14.4 uM for 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) {ECO:0000269|PubMed:18361507}; Vmax=12.6 umol/min/mg enzyme {ECO:0000269|PubMed:18361507};
| null | null | null |
FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes (PubMed:18361507). This phospholipase activity is very sensitive to calcium. May be important for formation and maintenance of the neuronal network in the postnatal brain (By similarity). {ECO:0000250|UniProtKB:A2AP18, ECO:0000269|PubMed:18361507}.
|
Homo sapiens (Human)
|
O75044
|
SRGP2_HUMAN
|
MTSPAKFKKDKEIIAEYDTQVKEIRAQLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTRSTKDQQFKKDQNVLSPVNCWNLLLNQVKRESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKKSKEVGQQLQDDLMKVLNELYSVMKTYHMYNADSISAQSKLKEAEKQEEKQIGKSVKQEDRQTPRSPDSTANVRIEEKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVFKYYIHDLSDLIDQCCDLGYHASLNRALRTFLSAELNLEQSKHEGLDAIENAVENLDATSDKQRLMEMYNNVFCPPMKFEFQPHMGDMASQLCAQQPVQSELVQRCQQLQSRLSTLKIENEEVKKTMEATLQTIQDIVTVEDFDVSDCFQYSNSMESVKSTVSETFMSKPSIAKRRANQQETEQFYFTKMKEYLEGRNLITKLQAKHDLLQKTLGESQRTDCSLARRSSTVRKQDSSQAIPLVVESCIRFISRHGLQHEGIFRVSGSQVEVNDIKNAFERGEDPLAGDQNDHDMDSIAGVLKLYFRGLEHPLFPKDIFHDLMACVTMDNLQERALHIRKVLLVLPKTTLIIMRYLFAFLNHLSQFSEENMMDPYNLAICFGPSLMSVPEGHDQVSCQAHVNELIKTIIIQHENIFPSPRELEGPVYSRGGSMEDYCDSPHGETTSVEDSTQDVTAEHHTSDDECEPIEAIAKFDYVGRTARELSFKKGASLLLYQRASDDWWEGRHNGIDGLIPHQYIVVQDTEDGVVERSSPKSEIEVISEPPEEKVTARAGASCPSGGHVADIYLANINKQRKRPESGSIRKTFRSDSHGLSSSLTDSSSPGVGASCRPSSQPIMSQSLPKEGPDKCSISGHGSLNSISRHSSLKNRLDSPQIRKTATAGRSKSFNNHRPMDPEVIAQDIEATMNSALNELRELERQSSVKHTPDVVLDTLEPLKTSPVVAPTSEPSSPLHTQLLKDPEPAFQRSASTAGDIACAFRPVKSVKMAAPVKPPATRPKPTVFPKTNATSPGVNSSTSPQSTDKSCTV
| null | null |
actin filament severing [GO:0051014]; dendritic spine development [GO:0060996]; excitatory synapse assembly [GO:1904861]; extension of a leading process involved in cell motility in cerebral cortex radial glia guided migration [GO:0021816]; filopodium assembly [GO:0046847]; inhibitory synapse assembly [GO:1904862]; lamellipodium assembly involved in ameboidal cell migration [GO:0003363]; negative regulation of cell migration [GO:0030336]; negative regulation of neuron migration [GO:2001223]; neuron projection morphogenesis [GO:0048812]; positive regulation of GTPase activity [GO:0043547]; regulation of small GTPase mediated signal transduction [GO:0051056]; signal transduction [GO:0007165]; substrate adhesion-dependent cell spreading [GO:0034446]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine head [GO:0044327]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]
|
GTPase activator activity [GO:0005096]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; small GTPase binding [GO:0031267]
|
PF00611;PF00620;PF00018;
|
1.20.1270.60;1.10.555.10;2.30.30.40;
| null |
PTM: Methylation at Arg-927 is required for the stimulation of cell migration, dimerization and localization at the plasma membrane protrusions. {ECO:0000269|PubMed:20810653}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21148482}. Cell projection, dendritic spine {ECO:0000303|PubMed:22559944}. Postsynaptic density {ECO:0000250|UniProtKB:Q91Z67}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q91Z67}. Cell projection, lamellipodium {ECO:0000269|PubMed:20810653}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q91Z67}. Nucleus {ECO:0000250|UniProtKB:D4A208}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q91Z67}. Note=Recruited to actin-rich phagosomes during phagocytosis (By similarity). Translocates from nucleus to cytoplasm during development (By similarity). {ECO:0000250|UniProtKB:D4A208, ECO:0000250|UniProtKB:Q91Z67}.
| null | null | null | null | null |
FUNCTION: Postsynaptic RAC1 GTPase activating protein (GAP) that plays a key role in neuronal morphogenesis and migration mainly during development of the cerebral cortex (PubMed:20810653, PubMed:27373832, PubMed:28333212). Regulates excitatory and inhibitory synapse maturation and density in cortical pyramidal neurons (PubMed:22559944, PubMed:27373832). SRGAP2/SRGAP2A limits excitatory and inhibitory synapse density through its RAC1-specific GTPase activating activity, while it promotes maturation of both excitatory and inhibitory synapses through its ability to bind to the postsynaptic scaffolding protein HOMER1 at excitatory synapses, and the postsynaptic protein GPHN at inhibitory synapses (By similarity). Mechanistically, acts by binding and deforming membranes, thereby regulating actin dynamics to regulate cell migration and differentiation (PubMed:27373832). Promotes cell repulsion and contact inhibition of locomotion: localizes to protrusions with curved edges and controls the duration of RAC1 activity in contact protrusions (By similarity). In non-neuronal cells, may also play a role in cell migration by regulating the formation of lamellipodia and filopodia (PubMed:20810653, PubMed:21148482). {ECO:0000250|UniProtKB:Q91Z67, ECO:0000269|PubMed:20810653, ECO:0000269|PubMed:21148482, ECO:0000269|PubMed:22559944, ECO:0000269|PubMed:27373832, ECO:0000269|PubMed:28333212}.
|
Homo sapiens (Human)
|
O75051
|
PLXA2_HUMAN
|
MEQRRPWPRALEVDSRSVVLLSVVWVLLAPPAAGMPQFSTFHSENRDWTFNHLTVHQGTGAVYVGAINRVYKLTGNLTIQVAHKTGPEEDNKSCYPPLIVQPCSEVLTLTNNVNKLLIIDYSENRLLACGSLYQGVCKLLRLDDLFILVEPSHKKEHYLSSVNKTGTMYGVIVRSEGEDGKLFIGTAVDGKQDYFPTLSSRKLPRDPESSAMLDYELHSDFVSSLIKIPSDTLALVSHFDIFYIYGFASGGFVYFLTVQPETPEGVAINSAGDLFYTSRIVRLCKDDPKFHSYVSLPFGCTRAGVEYRLLQAAYLAKPGDSLAQAFNITSQDDVLFAIFSKGQKQYHHPPDDSALCAFPIRAINLQIKERLQSCYQGEGNLELNWLLGKDVQCTKAPVPIDDNFCGLDINQPLGGSTPVEGLTLYTTSRDRMTSVASYVYNGYSVVFVGTKSGKLKKIRADGPPHGGVQYEMVSVLKDGSPILRDMAFSIDQRYLYVMSERQVTRVPVESCEQYTTCGECLSSGDPHCGWCALHNMCSRRDKCQQAWEPNRFAASISQCVSLAVHPSSISVSEHSRLLSLVVSDAPDLSAGIACAFGNLTEVEGQVSGSQVICISPGPKDVPVIPLDQDWFGLELQLRSKETGKIFVSTEFKFYNCSAHQLCLSCVNSAFRCHWCKYRNLCTHDPTTCSFQEGRINISEDCPQLVPTEEILIPVGEVKPITLKARNLPQPQSGQRGYECVLNIQGAIHRVPALRFNSSSVQCQNSSYQYDGMDISNLAVDFAVVWNGNFIIDNPQDLKVHLYKCAAQRESCGLCLKADRKFECGWCSGERRCTLHQHCTSPSSPWLDWSSHNVKCSNPQITEILTVSGPPEGGTRVTIHGVNLGLDFSEIAHHVQVAGVPCTPLPGEYIIAEQIVCEMGHALVGTTSGPVRLCIGECKPEFMTKSHQQYTFVNPSVLSLNPIRGPESGGTMVTITGHYLGAGSSVAVYLGNQTCEFYGRSMSEIVCVSPPSSNGLGPVPVSVSVDRAHVDSNLQFEYIDDPRVQRIEPEWSIASGHTPLTITGFNLDVIQEPRIRVKFNGKESVNVCKVVNTTTLTCLAPSLTTDYRPGLDTVERPDEFGFVFNNVQSLLIYNDTKFIYYPNPTFELLSPTGVLDQKPGSPIILKGKNLCPPASGGAKLNYTVLIGETPCAVTVSETQLLCEPPNLTGQHKVMVHVGGMVFSPGSVSVISDSLLTLPAIVSIAAGGSLLLIIVIIVLIAYKRKSRENDLTLKRLQMQMDNLESRVALECKEAFAELQTDINELTSDLDRSGIPYLDYRTYAMRVLFPGIEDHPVLRELEVQGNGQQHVEKALKLFAQLINNKVFLLTFIRTLELQRSFSMRDRGNVASLIMTGLQGRLEYATDVLKQLLSDLIDKNLENKNHPKLLLRRTESVAEKMLTNWFAFLLHKFLKECAGEPLFMLYCAIKQQMEKGPIDAITGEARYSLSEDKLIRQQIEYKTLILNCVNPDNENSPEIPVKVLNCDTITQVKEKILDAVYKNVPYSQRPRAVDMDLEWRQGRIARVVLQDEDITTKIEGDWKRLNTLMHYQVSDRSVVALVPKQTSSYNIPASASISRTSISRYDSSFRYTGSPDSLRSRAPMITPDLESGVKVWHLVKNHDHGDQKEGDRGSKMVSEIYLTRLLATKGTLQKFVDDLFETLFSTVHRGSALPLAIKYMFDFLDEQADRHSIHDTDVRHTWKSNCLPLRFWVNVIKNPQFVFDIHKGSITDACLSVVAQTFMDSCSTSEHRLGKDSPSNKLLYAKDIPSYKSWVERYYADIAKLPAISDQDMNAYLAEQSRLHAVEFNMLSALNEIYSYVSKYSEELIGALEQDEQARRQRLAYKVEQLINAMSIES
| null | null |
centrosome localization [GO:0051642]; cerebellar granule cell precursor tangential migration [GO:0021935]; limb bud formation [GO:0060174]; negative regulation of cell adhesion [GO:0007162]; neural tube development [GO:0021915]; pharyngeal system development [GO:0060037]; positive regulation of axonogenesis [GO:0050772]; regulation of cell migration [GO:0030334]; regulation of cell shape [GO:0008360]; semaphorin-plexin signaling pathway [GO:0071526]; semaphorin-plexin signaling pathway involved in axon guidance [GO:1902287]; somitogenesis [GO:0001756]
|
plasma membrane [GO:0005886]; semaphorin receptor complex [GO:0002116]
|
identical protein binding [GO:0042802]; semaphorin receptor activity [GO:0017154]
|
PF08337;PF20170;PF01437;PF01403;PF01833;PF18020;PF17960;
|
2.60.40.10;2.130.10.10;
|
Plexin family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Coreceptor for SEMA3A and SEMA6A. Necessary for signaling by SEMA6A and class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm (By similarity). {ECO:0000250, ECO:0000269|PubMed:10520995}.
|
Homo sapiens (Human)
|
O75052
|
CAPON_HUMAN
|
MPSKTKYNLVDDGHDLRIPLHNEDAFQHGICFEAKYVGSLDVPRPNSRVEIVAAMRRIRYEFKAKNIKKKKVSIMVSVDGVKVILKKKKKLLLLQKKEWTWDESKMLVMQDPIYRIFYVSHDSQDLKIFSYIARDGASNIFRCNVFKSKKKSQAMRIVRTVGQAFEVCHKLSLQHTQQNADGQEDGESERNSNSSGDPGRQLTGAERASTATAEETDIDAVEVPLPGNDVLEFSRGVTDLDAVGKEGGSHTGSKVSHPQEPMLTASPRMLLPSSSSKPPGLGTETPLSTHHQMQLLQQLLQQQQQQTQVAVAQVHLLKDQLAAEAAARLEAQARVHQLLLQNKDMLQHISLLVKQVQELELKLSGQNAMGSQDSLLEITFRSGALPVLCDPTTPKPEDLHSPPLGAGLADFAHPAGSPLGRRDCLVKLECFRFLPPEDTPPPAQGEALLGGLELIKFRESGIASEYESNTDESEERDSWSQEELPRLLNVLQRQELGDGLDDEIAV
| null | null |
nitric oxide biosynthetic process [GO:0006809]; positive regulation of membrane repolarization during ventricular cardiac muscle cell action potential [GO:1905026]; positive regulation of peptidyl-cysteine S-nitrosylation [GO:2000170]; positive regulation of potassium ion transmembrane transport [GO:1901381]; postsynaptic actin cytoskeleton organization [GO:0098974]; regulation of calcium ion transmembrane transport via high voltage-gated calcium channel [GO:1902514]; regulation of cardiac muscle cell action potential [GO:0098901]; regulation of heart rate by chemical signal [GO:0003062]; regulation of high voltage-gated calcium channel activity [GO:1901841]; regulation of nitric oxide biosynthetic process [GO:0045428]; regulation of nitric-oxide synthase activity [GO:0050999]; regulation of ventricular cardiac muscle cell membrane repolarization [GO:0060307]
|
anchoring junction [GO:0070161]; caveola [GO:0005901]; cytosol [GO:0005829]; filopodium [GO:0030175]; glutamatergic synapse [GO:0098978]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; podosome [GO:0002102]; sarcolemma [GO:0042383]; sarcoplasmic reticulum membrane [GO:0033017]; T-tubule [GO:0030315]; Z disc [GO:0030018]
|
nitric-oxide synthase binding [GO:0050998]; nitric-oxide synthase regulator activity [GO:0030235]; signaling adaptor activity [GO:0035591]
|
PF00640;
|
2.30.29.30;
| null | null |
SUBCELLULAR LOCATION: Cell projection, filopodium {ECO:0000250|UniProtKB:O54960}. Cell projection, podosome {ECO:0000250|UniProtKB:O54960}.
| null | null | null | null | null |
FUNCTION: Adapter protein involved in neuronal nitric-oxide (NO) synthesis regulation via its association with nNOS/NOS1. The complex formed with NOS1 and synapsins is necessary for specific NO and synapsin functions at a presynaptic level. Mediates an indirect interaction between NOS1 and RASD1 leading to enhance the ability of NOS1 to activate RASD1. Competes with DLG4 for interaction with NOS1, possibly affecting NOS1 activity by regulating the interaction between NOS1 and DLG4 (By similarity). In kidney podocytes, plays a role in podosomes and filopodia formation through CDC42 activation (PubMed:33523862). {ECO:0000250|UniProtKB:O54960, ECO:0000269|PubMed:33523862}.
|
Homo sapiens (Human)
|
O75054
|
IGSF3_HUMAN
|
MKCFFPVLSCLAVLGVVSAQRQVTVQEGPLYRTEGSHITIWCNVSGYQGPSEQNFQWSIYLPSSPEREVQIVSTMDSSFPYAIYTQRVRGGKIFIERVQGNSTLLHITDLQARDAGEYECHTPSTDKQYFGSYSAKMNLVVIPDSLQTTAMPQTLHRVEQDPLELTCEVASETIQHSHLSVAWLRQKVGEKPVEVISLSRDFMLHSSSEYAQRQSLGEVRLDKLGRTTFRLTIFHLQPSDQGEFYCEAAEWIQDPDGSWYAMTRKRSEGAVVNVQPTDKEFTVRLETEKRLHTVGEPVEFRCILEAQNVPDRYFAVSWAFNSSLIATMGPNAVPVLNSEFAHREARGQLKVAKESDSVFVLKIYHLRQEDSGKYNCRVTEREKTVTGEFIDKESKRPKNIPIIVLPLKSSISVEVASNASVILEGEDLRFSCSVRTAGRPQGRFSVIWQLVDRQNRRSNIMWLDRDGTVQPGSSYWERSSFGGVQMEQVQPNSFSLGIFNSRKEDEGQYECHVTEWVRAVDGEWQIVGERRASTPISITALEMGFAVTAISRTPGVTYSDSFDLQCIIKPHYPAWVPVSVTWRFQPVGTVEFHDLVTFTRDGGVQWGDRSSSFRTRTAIEKAESSNNVRLSISRASDTEAGKYQCVAELWRKNYNNTWTRLAERTSNLLEIRVLQPVTKLQVSKSKRTLTLVENKPIQLNCSVKSQTSQNSHFAVLWYVHKPSDADGKLILKTTHNSAFEYGTYAEEEGLRARLQFERHVSGGLFSLTVQRAEVSDSGSYYCHVEEWLLSPNYAWYKLAEEVSGRTEVTVKQPDSRLRLSQAQGNLSVLETRQVQLECVVLNRTSITSQLMVEWFVWKPNHPERETVARLSRDATFHYGEQAAKNNLKGRLHLESPSPGVYRLFIQNVAVQDSGTYSCHVEEWLPSPSGMWYKRAEDTAGQTALTVMRPDASLQVDTVVPNATVSEKAAFQLDCSIVSRSSQDSRFAVAWYSLRTKAGGKRSSPGLEEQEEEREEEEEEDDDDDDDPTERTALLSVGPDAVFGPEGSPWEGRLRFQRLSPVLYRLTVLQASPQDTGNYSCHVEEWLPSPQKEWYRLTEEESAPIGIRVLDTSPTLQSIICSNDALFYFVFFYPFPIFGILIITILLVRFKSRNSSKNSDGKNGVPLLWIKEPHLNYSPTCLEPPVLSIHPGAID
| null | null |
lacrimal gland development [GO:0032808]
|
cell surface [GO:0009986]; membrane [GO:0016020]
| null |
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
| null | null | null | null | null | null |
Homo sapiens (Human)
|
O75056
|
SDC3_HUMAN
|
MKPGPPHRAGAAHGAGAGAGAAAGPGARGLLLPPLLLLLLAGRAAGAQRWRSENFERPVDLEGSGDDDSFPDDELDDLYSGSGSGYFEQESGIETAMRFSPDVALAVSTTPAVLPTTNIQPVGTPFEELPSERPTLEPATSPLVVTEVPEEPSQRATTVSTTMATTAATSTGDPTVATVPATVATATPSTPAAPPFTATTAVIRTTGVRRLLPLPLTTVATARATTPEAPSPPTTAAVLDTEAPTPRLVSTATSRPRALPRPATTQEPDIPERSTLPLGTTAPGPTEVAQTPTPETFLTTIRDEPEVPVSGGPSGDFELPEEETTQPDTANEVVAVGGAAAKASSPPGTLPKGARPGPGLLDNAIDSGSSAAQLPQKSILERKEVLVAVIVGGVVGALFAAFLVTLLIYRMKKKDEGSYTLEEPKQASVTYQKPDKQEEFYA
| null | null |
cell migration [GO:0016477]
|
cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; Golgi lumen [GO:0005796]; lysosomal lumen [GO:0043202]; membrane [GO:0016020]; microspike [GO:0044393]; plasma membrane [GO:0005886]
|
identical protein binding [GO:0042802]
|
PF01034;
| null |
Syndecan proteoglycan family
|
PTM: O-glycosylated within the Thr/Ser-rich region which could interact with lectin domains on other molecules. {ECO:0000305}.
|
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Cell surface proteoglycan that may bear heparan sulfate (By similarity). May have a role in the organization of cell shape by affecting the actin cytoskeleton, possibly by transferring signals from the cell surface in a sugar-dependent mechanism. {ECO:0000250, ECO:0000269|PubMed:11527150}.
|
Homo sapiens (Human)
|
O75061
|
AUXI_HUMAN
|
MKDSENKGASSPDMEPSYGGGLFDMVKGGAGRLFSNLKDNLKDTLKDTSSRVIQSVTSYTKGDLDFTYVTSRIIVMSFPLDNVDIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQAPSLHNLFAVCRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAIRLLYAKRPGIGLSPSHRRYLGYMCDLLADKPYRPHFKPLTIKSITVSPIPFFNKQRNGCRPYCDVLIGETKIYSTCTDFERMKEYRVQDGKIFIPLNITVQGDVVVSMYHLRSTIGSRLQAKVTNTQIFQLQFHTGFIPLDTTVLKFTKPELDACDVPEKYPQLFQVTLDVELQPHDKVIDLTPPWEHYCTKDVNPSILFSSHQEHQDTLALGGQAPIDIPPDNPRHYGQSGFFASLCWQDQKSEKSFCEEDHAALVNQESEQSDDELLTLSSPHGNANGDKPHGVKKPSKKQQEPAAPPPPEDVDLLGLEGSAMSNSFSPPAAPPTNSELLSDLFGGGGAAGPTQAGQSGVEDVFHPSGPASTQSTPRRSATSTSASPTLRVGEGATFDPFGAPSKPSGQDLLGSFLNTSSASSDPFLQPTRSPSPTVHASSTPAVNIQPDVSGGWDWHAKPGGFGMGSKSAATSPTGSSHGTPTHQSKPQTLDPFADLGTLGSSSFASKPTTPTGLGGGFPPLSSPQKASPQPMGGGWQQGGAYNWQQPQPKPQPSMPHSSPQNRPNYNVSFSAMPGGQNERGKGSSNLEGKQKAADFEDLLSGQGFNAHKDKKGPRTIAEMRKEEMAKEMDPEKLKILEWIEGKERNIRALLSTMHTVLWAGETKWKPVGMADLVTPEQVKKVYRKAVLVVHPDKATGQPYEQYAKMIFMELNDAWSEFENQGQKPLY
|
3.1.3.-
| null |
clathrin coat disassembly [GO:0072318]; clathrin-dependent endocytosis [GO:0072583]; dephosphorylation [GO:0016311]; intracellular transport [GO:0046907]; regulation of clathrin coat assembly [GO:1905443]; regulation of clathrin-dependent endocytosis [GO:2000369]; synaptic vesicle recycling [GO:0036465]; synaptic vesicle uncoating [GO:0016191]
|
clathrin-coated vesicle [GO:0030136]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extrinsic component of presynaptic endocytic zone membrane [GO:0098894]; intracellular membrane-bounded organelle [GO:0043231]; postsynaptic density [GO:0014069]; vesicle [GO:0031982]
|
clathrin binding [GO:0030276]; clathrin heavy chain binding [GO:0032050]; heat shock protein binding [GO:0031072]; protein tyrosine phosphatase activity [GO:0004725]; SH3 domain binding [GO:0017124]
|
PF10409;
|
2.60.40.1110;1.10.287.110;3.90.190.10;
| null |
PTM: Phosphorylation at Ser-570 modulates its ability to bind CLTC and therefore the synaptic vesicle endocytosis (SVE). {ECO:0000269|PubMed:29735704}.; PTM: The N-terminus is blocked. {ECO:0000250|UniProtKB:Q27974}.
|
SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q27974}. Note=Appears on coated vesicles in successive transient bursts, immediately after the vesicle release from the plasma membrane. Recruitment to clathrin-coated vesicles depends on temporal variations in phosphoinositide composition of clathrin-coated vesicles. {ECO:0000250|UniProtKB:Q27974}.
| null | null | null | null | null |
FUNCTION: May act as a protein phosphatase and/or a lipid phosphatase. Co-chaperone that recruits HSPA8/HSC70 to clathrin-coated vesicles (CCVs) and promotes the ATP-dependent dissociation of clathrin from CCVs and participates in clathrin-mediated endocytosis of synaptic vesicles and their recycling and also in intracellular trafficking (PubMed:18489706). Firstly, binds tightly to the clathrin cages, at a ratio of one DNAJC6 per clathrin triskelion. The HSPA8:ATP complex then binds to the clathrin-auxilin cage, initially at a ratio of one HSPA8 per triskelion leading to ATP hydrolysis stimulation and causing a conformational change in the HSPA8. This cycle is repeated three times to drive to a complex containing the clathrin-auxilin cage associated to three HSPA8:ADP complex. The ATP hydrolysis of the third HSPA8:ATP complex leads to a concerted dismantling of the cage into component triskelia. Then, dissociates from the released triskelia and be recycled to initiate another cycle of HSPA8's recruitment. Also acts during the early steps of clathrin-coated vesicle (CCV) formation through its interaction with the GTP bound form of DNM1 (By similarity). {ECO:0000250|UniProtKB:Q27974, ECO:0000269|PubMed:18489706}.
|
Homo sapiens (Human)
|
O75063
|
XYLK_HUMAN
|
MKLKQRVVLLAILLVIFIFTKVFLIDNLDTSAANREDQRAFHRMMTGLRVELAPKLDHTLQSPWEIAAQWVVPREVYPEETPELGAVMHAMATKKIIKADVGYKGTQLKALLILEGGQKVVFKPKRYSRDHVVEGEPYAGYDRHNAEVAAFHLDRILGFHRAPLVVGRFVNLRTEIKPVATEQLLSTFLTVGNNTCFYGKCYYCRETEPACADGDIMEGSVTLWLPDVWPLQKHRHPWGRTYREGKLARWEYDESYCDAVKKTSPYDSGPRLLDIIDTAVFDYLIGNADRHHYESFQDDEGASMLILLDNAKSFGNPSLDERSILAPLYQCCIIRVSTWNRLNYLKNGVLKSALKSAMAHDPISPVLSDPHLDAVDQRLLSVLATVKQCTDQFGMDTVLVEDRMPLSHL
|
2.7.1.-
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9XTW2};
|
phosphorylation [GO:0016310]; proteoglycan biosynthetic process [GO:0030166]
|
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nucleoplasm [GO:0005654]
|
ATP binding [GO:0005524]; kinase activity [GO:0016301]; metal ion binding [GO:0046872]; phosphotransferase activity, alcohol group as acceptor [GO:0016773]
|
PF06702;
| null |
FAM20 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:19473117}; Single-pass type II membrane protein {ECO:0000269|PubMed:19473117}.
|
CATALYTIC ACTIVITY: Reaction=3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + ATP = 3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-2-O-phosphoxylosyl)-L-seryl-[protein] + ADP + H(+); Xref=Rhea:RHEA:19461, Rhea:RHEA-COMP:12571, Rhea:RHEA-COMP:14558, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:132090, ChEBI:CHEBI:140494, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:19473117};
| null | null | null | null |
FUNCTION: Responsible for the 2-O-phosphorylation of xylose in the glycosaminoglycan-protein linkage region of proteoglycans thereby regulating the amount of mature GAG chains. Sulfated glycosaminoglycans (GAGs), including heparan sulfate and chondroitin sulfate, are synthesized on the so-called common GAG-protein linkage region (GlcUAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser) of core proteins, which is formed by the stepwise addition of monosaccharide residues by the respective specific glycosyltransferases. Xylose 2-O-phosphorylation may influence the catalytic activity of B3GAT3 (GlcAT-I) which completes the precursor tetrasaccharide of GAG-protein linkage regions on which the repeating disaccharide region is synthesized. {ECO:0000269|PubMed:19473117, ECO:0000269|PubMed:24425863}.
|
Homo sapiens (Human)
|
O75069
|
TMCC2_HUMAN
|
MKRCRSDELQQQQGEEDGAGLEDAASHLPGADLRPGETTGANSAGGPTSDAGAAAAPNPGPRSKPPDLKKIQQLSEGSMFGHGLKHLFHSRRRSREREHQTSQDSQQHQQQQGMSDHDSPDEKERSPEMHRVSYAMSLHDLPARPTAFNRVLQQIRSRPSIKRGASLHSSSGGGSSGSSSRRTKSSSLEPQRGSPHLLRKAPQDSSLAAILHQHQCRPRSSSTTDTALLLADGSNVYLLAEEAEGIGDKVDKGDLVALSLPAGHGDTDGPISLDVPDGAPDPQRTKAAIDHLHQKILKITEQIKIEQEARDDNVAEYLKLANNADKQQVSRIKQVFEKKNQKSAQTIAQLHKKLEHYRRRLKEIEQNGPSRQPKDVLRDMQQGLKDVGANVRAGISGFGGGVVEGVKGSLSGLSQATHTAVVSKPREFASLIRNKFGSADNIAHLKDPLEDGPPEEAARALSGSATLVSSPKYGSDDECSSASASSAGAGSNSGAGPGGALGSPKSNALYGAPGNLDALLEELREIKEGQSHLEDSMEDLKTQLQRDYTYMTQCLQEERYRYERLEEQLNDLTELHQNEMTNLKQELASMEEKVAYQSYERARDIQEAVESCLTRVTKLELQQQQQQVVQLEGVENANARALLGKFINVILALMAVLLVFVSTIANFITPLMKTRLRITSTTLLVLVLFLLWKHWDSLTYLLEHVLLPS
| null | null |
amyloid precursor protein metabolic process [GO:0042982]
|
endomembrane system [GO:0012505]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]
| null |
PF10267;
| null |
TEX28 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21593558, ECO:0000269|PubMed:24454821, ECO:0000269|PubMed:30220460}; Multi-pass membrane protein {ECO:0000255}. Note=Concentrates in discrete patches along peripheral endoplasmic reticulum tubules. {ECO:0000269|PubMed:30220460}.
| null | null | null | null | null |
FUNCTION: May be involved in the regulation of the proteolytic processing of the amyloid precursor protein (APP) possibly also implicating APOE. {ECO:0000269|PubMed:21593558}.
|
Homo sapiens (Human)
|
O75072
|
FKTN_HUMAN
|
MSRINKNVVLALLTLTSSAFLLFQLYYYKHYLSTKNGAGLSKSKGSRIGFDSTQWRAVKKFIMLTSNQNVPVFLIDPLILELINKNFEQVKNTSHGSTSQCKFFCVPRDFTAFALQYHLWKNEEGWFRIAENMGFQCLKIESKDPRLDGIDSLSGTEIPLHYICKLATHAIHLVVFHERSGNYLWHGHLRLKEHIDRKFVPFRKLQFGRYPGAFDRPELQQVTVDGLEVLIPKDPMHFVEEVPHSRFIECRYKEARAFFQQYLDDNTVEAVAFRKSAKELLQLAAKTLNKLGVPFWLSSGTCLGWYRQCNIIPYSKDVDLGIFIQDYKSDIILAFQDAGLPLKHKFGKVEDSLELSFQGKDDVKLDVFFFYEETDHMWNGGTQAKTGKKFKYLFPKFTLCWTEFVDMKVHVPCETLEYIEANYGKTWKIPVKTWDWKRSPPNVQPNGIWPISEWDEVIQLY
|
2.7.8.-
| null |
muscle organ development [GO:0007517]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of JNK cascade [GO:0046329]; nervous system development [GO:0007399]; protein glycosylation [GO:0006486]; protein O-linked glycosylation [GO:0006493]; protein O-linked mannosylation [GO:0035269]; regulation of protein glycosylation [GO:0060049]
|
cis-Golgi network [GO:0005801]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nucleus [GO:0005634]
|
phosphotransferase activity, for other substituted phosphate groups [GO:0016780]
|
PF19737;PF04991;
| null |
LicD transferase family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:25279699, ECO:0000269|PubMed:29477842, ECO:0000305|PubMed:26923585}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q8R507}. Nucleus {ECO:0000250|UniProtKB:Q8R507}. Note=In retinal tissue, does not localize with the Golgi apparatus. {ECO:0000250|UniProtKB:Q8R507}.
|
CATALYTIC ACTIVITY: Reaction=3-O-[beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + CDP-L-ribitol = 3-O-[Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + CMP + H(+); Xref=Rhea:RHEA:36551, Rhea:RHEA-COMP:13309, Rhea:RHEA-COMP:17480, ChEBI:CHEBI:15378, ChEBI:CHEBI:57608, ChEBI:CHEBI:60377, ChEBI:CHEBI:136710, ChEBI:CHEBI:177331; Evidence={ECO:0000269|PubMed:26923585, ECO:0000269|PubMed:29477842}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36552; Evidence={ECO:0000269|PubMed:26923585};
| null |
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:25279699, ECO:0000269|PubMed:26923585, ECO:0000269|PubMed:27194101, ECO:0000269|PubMed:29477842}.
| null | null |
FUNCTION: Catalyzes the transfer of a ribitol-phosphate from CDP-ribitol to the distal N-acetylgalactosamine of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1) (PubMed:26923585, PubMed:27194101, PubMed:29477842). This constitutes the first step in the formation of the ribitol 5-phosphate tandem repeat which links the phosphorylated O-mannosyl trisaccharide to the ligand binding moiety composed of repeats of 3-xylosyl-alpha-1,3-glucuronic acid-beta-1 (PubMed:17034757, PubMed:25279699, PubMed:26923585, PubMed:27194101, PubMed:29477842). Required for normal location of POMGNT1 in Golgi membranes, and for normal POMGNT1 activity (PubMed:17034757). May interact with and reinforce a large complex encompassing the outside and inside of muscle membranes (PubMed:25279699). Could be involved in brain development (Probable). {ECO:0000269|PubMed:17034757, ECO:0000269|PubMed:25279699, ECO:0000269|PubMed:26923585, ECO:0000269|PubMed:27194101, ECO:0000269|PubMed:29477842, ECO:0000305|PubMed:11115853}.
|
Homo sapiens (Human)
|
O75074
|
LRP3_HUMAN
|
MEKRAAAGLEGAPGARAQLAVVCLVNIFLTGRLSSAVPALAACSGKLEQHTERRGVIYSPAWPLNYPPGTNCSWYIQGDRGDMITISFRNFDVEESHQCSLDWLLLGPAAPPRQEAFRLCGSAIPPAFISARDHVWIFFHSDASSSGQAQGFRLSYIRGKLGQASCQADEFRCDNGKCLPGPWQCNTVDECGDGSDEGNCSAPASEPPGSLCPGGTFPCSGARSTRCLPVERRCDGLQDCGDGSDEAGCPDLACGRRLGSFYGSFASPDLFGAARGPSDLHCTWLVDTQDSRRVLLQLELRLGYDDYVQVYEGLGERGDRLLQTLSYRSNHRPVSLEAAQGRLTVAYHARARSAGHGFNATYQVKGYCLPWEQPCGSSSDSDGGSLGDQGCFSEPQRCDGWWHCASGRDEQGCPACPPDQYPCEGGSGLCYTPADRCNNQKSCPDGADEKNCFSCQPGTFHCGTNLCIFETWRCDGQEDCQDGSDEHGCLAAVPRKVITAALIGSLVCGLLLVIALGCAFKLYSLRTQEYRAFETQMTRLEAEFVRREAPPSYGQLIAQGLIPPVEDFPVYSASQASVLQNLRTAMRRQMRRHASRRGPSRRRLGRLWNRLFHRPRAPRGQIPLLTAARPSQTVLGDGFLQPAPGAAPDPPAPLMDTGSTRAAGDRPPSAPGRAPEVGPSGPPLPSGLRDPECRPVDKDRKVCREPLVDGPAPADAPREPCSAQDPHPQVSTASSTLGPHSPEPLGVCRNPPPPCSPMLEASDDEALLVC
| null | null |
negative regulation of fat cell differentiation [GO:0045599]; negative regulation of gene expression [GO:0010629]; positive regulation of gene expression [GO:0010628]; positive regulation of osteoblast differentiation [GO:0045669]; receptor-mediated endocytosis [GO:0006898]; transport across blood-brain barrier [GO:0150104]
|
clathrin-coated pit [GO:0005905]; membrane [GO:0016020]; plasma membrane [GO:0005886]
| null |
PF00431;PF00057;
|
4.10.400.10;2.60.120.290;
|
LDLR family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Membrane, coated pit {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Probable receptor, which may be involved in the internalization of lipophilic molecules and/or signal transduction. Its precise role is however unclear, since it does not bind to very low density lipoprotein (VLDL) or to LRPAP1 in vitro.
|
Homo sapiens (Human)
|
O75077
|
ADA23_HUMAN
|
MKPPGSSSRQPPLAGCSLAGASCGPQRGPAGSVPASAPARTPPCRLLLVLLLLPPLAASSRPRAWGAAAPSAPHWNETAEKNLGVLADEDNTLQQNSSSNISYSNAMQKEITLPSRLIYYINQDSESPYHVLDTKARHQQKHNKAVHLAQASFQIEAFGSKFILDLILNNGLLSSDYVEIHYENGKPQYSKGGEHCYYHGSIRGVKDSKVALSTCNGLHGMFEDDTFVYMIEPLELVHDEKSTGRPHIIQKTLAGQYSKQMKNLTMERGDQWPFLSELQWLKRRKRAVNPSRGIFEEMKYLELMIVNDHKTYKKHRSSHAHTNNFAKSVVNLVDSIYKEQLNTRVVLVAVETWTEKDQIDITTNPVQMLHEFSKYRQRIKQHADAVHLISRVTFHYKRSSLSYFGGVCSRTRGVGVNEYGLPMAVAQVLSQSLAQNLGIQWEPSSRKPKCDCTESWGGCIMEETGVSHSRKFSKCSILEYRDFLQRGGGACLFNRPTKLFEPTECGNGYVEAGEECDCGFHVECYGLCCKKCSLSNGAHCSDGPCCNNTSCLFQPRGYECRDAVNECDITEYCTGDSGQCPPNLHKQDGYACNQNQGRCYNGECKTRDNQCQYIWGTKAAGSDKFCYEKLNTEGTEKGNCGKDGDRWIQCSKHDVFCGFLLCTNLTRAPRIGQLQGEIIPTSFYHQGRVIDCSGAHVVLDDDTDVGYVEDGTPCGPSMMCLDRKCLQIQALNMSSCPLDSKGKVCSGHGVCSNEATCICDFTWAGTDCSIRDPVRNLHPPKDEGPKGPSATNLIIGSIAGAILVAAIVLGGTGWGFKNVKKRRFDPTQQGPI
| null | null |
cell adhesion [GO:0007155]; cellular response to leukemia inhibitory factor [GO:1990830]; central nervous system development [GO:0007417]; proteolysis [GO:0006508]
|
extracellular region [GO:0005576]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]
|
integrin binding [GO:0005178]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]
|
PF08516;PF00200;PF07974;PF01562;PF01421;
|
3.40.390.10;4.10.70.10;2.10.25.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform Gamma]: Secreted.
| null | null | null | null | null |
FUNCTION: May play a role in cell-cell and cell-matrix interactions. This is a non-catalytic metalloprotease-like protein.
|
Homo sapiens (Human)
|
O75078
|
ADA11_HUMAN
|
MRLLRRWAFAALLLSLLPTPGLGTQGPAGALRWGGLPQLGGPGAPEVTEPSRLVRESSGGEVRKQQLDTRVRQEPPGGPPVHLAQVSFVIPAFNSNFTLDLELNHHLLSSQYVERHFSREGTTQHSTGAGDHCYYQGKLRGNPHSFAALSTCQGLHGVFSDGNLTYIVEPQEVAGPWGAPQGPLPHLIYRTPLLPDPLGCREPGCLFAVPAQSAPPNRPRLRRKRQVRRGHPTVHSETKYVELIVINDHQLFEQMRQSVVLTSNFAKSVVNLADVIYKEQLNTRIVLVAMETWADGDKIQVQDDLLETLARLMVYRREGLPEPSDATHLFSGRTFQSTSSGAAYVGGICSLSHGGGVNEYGNMGAMAVTLAQTLGQNLGMMWNKHRSSAGDCKCPDIWLGCIMEDTGFYLPRKFSRCSIDEYNQFLQEGGGSCLFNKPLKLLDPPECGNGFVEAGEECDCGSVQECSRAGGNCCKKCTLTHDAMCSDGLCCRRCKYEPRGVSCREAVNECDIAETCTGDSSQCPPNLHKLDGYYCDHEQGRCYGGRCKTRDRQCQVLWGHAAADRFCYEKLNVEGTERGSCGRKGSGWVQCSKQDVLCGFLLCVNISGAPRLGDLVGDISSVTFYHQGKELDCRGGHVQLADGSDLSYVEDGTACGPNMLCLDHRCLPASAFNFSTCPGSGERRICSHHGVCSNEGKCICQPDWTGKDCSIHNPLPTSPPTGETERYKGPSGTNIIIGSIAGAVLVAAIVLGGTGWGFKNIRRGRSGGA
| null | null |
behavioral response to acetic acid induced pain [GO:0061367]; behavioral response to formalin induced pain [GO:0061368]; establishment of protein localization [GO:0045184]; integrin-mediated signaling pathway [GO:0007229]; multicellular organismal response to stress [GO:0033555]; proteolysis [GO:0006508]
|
axon [GO:0030424]; collagen-containing extracellular matrix [GO:0062023]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]
|
integrin binding [GO:0005178]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]
|
PF08516;PF00200;PF07974;PF01562;PF01421;
|
3.40.390.10;4.10.70.10;2.10.25.10;
| null |
PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Presynaptic cell membrane {ECO:0000250|UniProtKB:Q9R1V4}; Single-pass type I membrane protein. Perikaryon {ECO:0000250|UniProtKB:Q9R1V4}. Cell projection, axon {ECO:0000250|UniProtKB:Q9R1V4}. Note=Localizes to basket cell terminals and pinceaux. {ECO:0000250|UniProtKB:Q9R1V4}.
| null | null | null | null | null |
FUNCTION: Probable ligand for integrin in the brain. This is a non catalytic metalloprotease-like protein. Required for localization of the potassium channel subunit proteins KCNA1/KV1.1 and KCNA2/KV1.2 at cerebellar cortex basket cell distal terminals, is thereby involved in ephaptic inhibitory synchronization of Purkinje cell firing and response to stress (By similarity). Plays a role in spatial learning and motor coordination (By similarity). Involved in the nociceptive pain response to chemical-derived stimulation (By similarity). {ECO:0000250|UniProtKB:Q9R1V4}.
|
Homo sapiens (Human)
|
O75081
|
MTG16_HUMAN
|
MPASRLRDRAASSASGSTCGSMSQTHPVLESGLLASAGCSAPRGPRKGGPAPVDRKAKASAMPDSPAEVKTQPRSTPPSMPPPPPAASQGATRPPSFTPHTHREDGPATLPHGRFHGCLKWSMVCLLMNGSSHSPTAINGAPCTPNGFSNGPATSSTASLSTQHLPPACGARQLSKLKRFLTTLQQFGSDISPEIGERVRTLVLGLVNSTLTIEEFHSKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARLAKQTPAQYLAQHEQLLLDASASSPIDSSELLLEVNENGKRRTPDRTKENGSDRDPLHPEHLSKRPCTLNPAQRYSPSNGPPQPTPPPHYRLEDIAMAHHFRDAYRHPDPRELRERHRPLVVPGSRQEEVIDHKLTEREWAEEWKHLNNLLNCIMDMVEKTRRSLTVLRRCQEADREELNHWARRYSDAEDTKKGPAPAAARPRSSSAGPEGPQLDVPREFLPRTLTGYVPEDIWRKAEEAVNEVKRQAMSELQKAVSDAERKAHELITTERAKMERALAEAKRQASEDALTVINQQEDSSESCWNCGRKASETCSGCNAARYCGSFCQHRDWEKHHHVCGQSLQGPTAVVADPVPGPPEAAHSLGPSLPVGAASPSEAGSAGPSRPGSPSPPGPLDTVPR
| null | null |
DNA-templated transcription [GO:0006351]; granulocyte differentiation [GO:0030851]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of glycolytic process [GO:0045820]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; regulation of aerobic respiration [GO:1903715]; response to hypoxia [GO:0001666]
|
Golgi membrane [GO:0000139]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
metal ion binding [GO:0046872]; transcription corepressor activity [GO:0003714]
|
PF08788;PF07531;PF01753;
|
6.10.140.2220;6.10.250.230;1.20.120.1110;
|
CBFA2T family
| null |
SUBCELLULAR LOCATION: [Isoform 1]: Nucleus, nucleolus. Note=The RUNX1-CBFA2T3 fusion protein localizes to the nucleoplasm.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus, nucleoplasm {ECO:0000269|PubMed:11823486}. Golgi apparatus membrane {ECO:0000269|PubMed:11823486}.
| null | null | null | null | null |
FUNCTION: Transcriptional corepressor which facilitates transcriptional repression via its association with DNA-binding transcription factors and recruitment of other corepressors and histone-modifying enzymes (PubMed:12559562, PubMed:15203199). Can repress the expression of MMP7 in a ZBTB33-dependent manner (PubMed:23251453). Reduces the protein levels and stability of the transcriptinal regulator HIF1A; interacts with EGLN1 and promotes the HIF1A prolyl hydroxylation-dependent ubiquitination and proteasomal degradation pathway (PubMed:25974097). Contributes to inhibition of glycolysis and stimulation of mitochondrial respiration by down-regulating the expression of glycolytic genes including PFKFB3, PFKFB4, PDK1, PFKP, LDHA and HK1 which are direct targets of HIF1A (PubMed:23840896, PubMed:25974097). Regulates the proliferation and the differentiation of erythroid progenitors by repressing the expression of TAL1 target genes (By similarity). Plays a role in granulocyte differentiation (PubMed:15231665). {ECO:0000250|UniProtKB:O54972, ECO:0000269|PubMed:12183414, ECO:0000269|PubMed:15231665, ECO:0000269|PubMed:16966434, ECO:0000269|PubMed:23251453, ECO:0000269|PubMed:23840896, ECO:0000269|PubMed:25974097, ECO:0000303|PubMed:12559562, ECO:0000303|PubMed:15203199}.; FUNCTION: Isoform 2 functions as an A-kinase-anchoring protein (PubMed:11823486). {ECO:0000269|PubMed:11823486}.
|
Homo sapiens (Human)
|
O75083
|
WDR1_HUMAN
|
MPYEIKKVFASLPQVERGVSKIIGGDPKGNNFLYTNGKCVILRNIDNPALADIYTEHAHQVVVAKYAPSGFYIASGDVSGKLRIWDTTQKEHLLKYEYQPFAGKIKDIAWTEDSKRIAVVGEGREKFGAVFLWDSGSSVGEITGHNKVINSVDIKQSRPYRLATGSDDNCAAFFEGPPFKFKFTIGDHSRFVNCVRFSPDGNRFATASADGQIYIYDGKTGEKVCALGGSKAHDGGIYAISWSPDSTHLLSASGDKTSKIWDVSVNSVVSTFPMGSTVLDQQLGCLWQKDHLLSVSLSGYINYLDRNNPSKPLHVIKGHSKSIQCLTVHKNGGKSYIYSGSHDGHINYWDSETGENDSFAGKGHTNQVSRMTVDESGQLISCSMDDTVRYTSLMLRDYSGQGVVKLDVQPKCVAVGPGGYAVVVCIGQIVLLKDQRKCFSIDNPGYEPEVVAVHPGGDTVAIGGVDGNVRLYSILGTTLKDEGKLLEAKGPVTDVAYSHDGAFLAVCDASKVVTVFSVADGYSENNVFYGHHAKIVCLAWSPDNEHFASGGMDMMVYVWTLSDPETRVKIQDAHRLHHVSSLAWLDEHTLVTTSHDASVKEWTITY
| null | null |
actin filament depolymerization [GO:0030042]; actin filament fragmentation [GO:0030043]; apical junction assembly [GO:0043297]; cortical cytoskeleton organization [GO:0030865]; establishment of planar polarity of follicular epithelium [GO:0042247]; locomotion [GO:0040011]; maintenance of epithelial cell apical/basal polarity [GO:0045199]; neutrophil mediated immunity [GO:0002446]; neutrophil migration [GO:1990266]; platelet formation [GO:0030220]; positive regulation of actin filament depolymerization [GO:0030836]; regulation of actin filament depolymerization [GO:0030834]; regulation of cell shape [GO:0008360]; regulation of oligodendrocyte differentiation [GO:0048713]; regulation of ventricular cardiac muscle cell membrane repolarization [GO:0060307]; sarcomere organization [GO:0045214]; sensory perception of sound [GO:0007605]
|
cell junction [GO:0030054]; cell projection [GO:0042995]; cell-cell junction [GO:0005911]; cortical actin cytoskeleton [GO:0030864]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]; podosome [GO:0002102]
|
actin filament binding [GO:0051015]
|
PF00400;
|
2.130.10.10;
|
WD repeat AIP1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27994071}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q5RKI0}. Cell projection, podosome {ECO:0000269|PubMed:22721921}. Cell junction {ECO:0000269|PubMed:25792565}.
| null | null | null | null | null |
FUNCTION: Induces disassembly of actin filaments in conjunction with ADF/cofilin family proteins (PubMed:15629458, PubMed:27557945, PubMed:29751004). Enhances cofilin-mediated actin severing (By similarity). Involved in cytokinesis. Involved in chemotactic cell migration by restricting lamellipodial membrane protrusions (PubMed:18494608). Involved in myocardium sarcomere organization. Required for cardiomyocyte growth and maintenance (By similarity). Involved in megakaryocyte maturation and platelet shedding. Required for the establishment of planar cell polarity (PCP) during follicular epithelium development and for cell shape changes during PCP; the function seems to implicate cooperation with CFL1 and/or DSTN/ADF. Involved in the generation/maintenance of cortical tension (By similarity). Involved in assembly and maintenance of epithelial apical cell junctions and plays a role in the organization of the perijunctional actomyosin belt (PubMed:25792565). {ECO:0000250|UniProtKB:O88342, ECO:0000250|UniProtKB:Q9W7F2, ECO:0000269|PubMed:15629458, ECO:0000269|PubMed:18494608, ECO:0000269|PubMed:25792565, ECO:0000269|PubMed:27557945, ECO:0000269|PubMed:29751004}.
|
Homo sapiens (Human)
|
O75084
|
FZD7_HUMAN
|
MRDPGAAAPLSSLGLCALVLALLGALSAGAGAQPYHGEKGISVPDHGFCQPISIPLCTDIAYNQTILPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELRFFLCSMYAPVCTVLDQAIPPCRSLCERARQGCEALMNKFGFQWPERLRCENFPVHGAGEICVGQNTSDGSGGPGGGPTAYPTAPYLPDLPFTALPPGASDGRGRPAFPFSCPRQLKVPPYLGYRFLGERDCGAPCEPGRANGLMYFKEEERRFARLWVGVWSVLCCASTLFTVLTYLVDMRRFSYPERPIIFLSGCYFMVAVAHVAGFLLEDRAVCVERFSDDGYRTVAQGTKKEGCTILFMVLYFFGMASSIWWVILSLTWFLAAGMKWGHEAIEANSQYFHLAAWAVPAVKTITILAMGQVDGDLLSGVCYVGLSSVDALRGFVLAPLFVYLFIGTSFLLAGFVSLFRIRTIMKHDGTKTEKLEKLMVRIGVFSVLYTVPATIVLACYFYEQAFREHWERTWLLQTCKSYAVPCPPGHFPPMSPDFTVFMIKYLMTMIVGITTGFWIWSGKTLQSWRRFYHRLSHSSKGETAV
| null | null |
canonical Wnt signaling pathway [GO:0060070]; cellular response to retinoic acid [GO:0071300]; mesenchymal to epithelial transition [GO:0060231]; negative regulation of cardiac muscle cell differentiation [GO:2000726]; negative regulation of cell-substrate adhesion [GO:0010812]; negative regulation of ectodermal cell fate specification [GO:0042666]; neuron differentiation [GO:0030182]; non-canonical Wnt signaling pathway [GO:0035567]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of epithelial cell proliferation involved in wound healing [GO:0060054]; positive regulation of JNK cascade [GO:0046330]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of phosphorylation [GO:0042327]; regulation of canonical Wnt signaling pathway [GO:0060828]; regulation of DNA-templated transcription [GO:0006355]; skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration [GO:0014834]; somatic stem cell division [GO:0048103]; stem cell population maintenance [GO:0019827]; substrate adhesion-dependent cell spreading [GO:0034446]; T cell differentiation in thymus [GO:0033077]; Wnt signaling pathway, planar cell polarity pathway [GO:0060071]
|
intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]
|
frizzled binding [GO:0005109]; G protein-coupled receptor activity [GO:0004930]; PDZ domain binding [GO:0030165]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; Wnt receptor activity [GO:0042813]; Wnt-protein binding [GO:0017147]
|
PF01534;PF01392;
|
1.10.2000.10;1.20.1070.10;
|
G-protein coupled receptor Fz/Smo family
|
PTM: Ubiquitinated by ZNRF3, leading to its degradation by the proteasome. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27386966}; Multi-pass membrane protein {ECO:0000269|PubMed:27386966}. Endosome membrane {ECO:0000269|PubMed:27386966}; Multi-pass membrane protein {ECO:0000269|PubMed:27386966}. Note=Associated to the plasma membrane in the presence of FZD7 and phosphatidylinositol 4,5-bisphosphate (PIP2). Localized in recycling endosomes in other conditions. {ECO:0000269|PubMed:27386966}.
| null | null | null | null | null |
FUNCTION: Receptor for Wnt proteins. Most frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. Activation by WNT8 induces expression of beta-catenin target genes (By similarity). Following ligand activation, binds to CCDC88C/DAPLE which displaces DVL1 from FZD7 and leads to inhibition of canonical Wnt signaling, activation of G-proteins by CCDC88C and triggering of non-canonical Wnt responses (PubMed:26126266). May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. {ECO:0000250|UniProtKB:Q61090, ECO:0000269|PubMed:26126266}.; FUNCTION: (Microbial infection) Acts as a receptor for C.difficile toxin TcdB in the colonic epithelium. {ECO:0000269|PubMed:27680706}.
|
Homo sapiens (Human)
|
O75093
|
SLIT1_HUMAN
|
MALTPGWGSSAGPVRPELWLLLWAAAWRLGASACPALCTCTGTTVDCHGTGLQAIPKNIPRNTERLELNGNNITRIHKNDFAGLKQLRVLQLMENQIGAVERGAFDDMKELERLRLNRNQLHMLPELLFQNNQALSRLDLSENAIQAIPRKAFRGATDLKNLQLDKNQISCIEEGAFRALRGLEVLTLNNNNITTIPVSSFNHMPKLRTFRLHSNHLFCDCHLAWLSQWLRQRPTIGLFTQCSGPASLRGLNVAEVQKSEFSCSGQGEAGRVPTCTLSSGSCPAMCTCSNGIVDCRGKGLTAIPANLPETMTEIRLELNGIKSIPPGAFSPYRKLRRIDLSNNQIAEIAPDAFQGLRSLNSLVLYGNKITDLPRGVFGGLYTLQLLLLNANKINCIRPDAFQDLQNLSLLSLYDNKIQSLAKGTFTSLRAIQTLHLAQNPFICDCNLKWLADFLRTNPIETSGARCASPRRLANKRIGQIKSKKFRCSAKEQYFIPGTEDYQLNSECNSDVVCPHKCRCEANVVECSSLKLTKIPERIPQSTAELRLNNNEISILEATGMFKKLTHLKKINLSNNKVSEIEDGAFEGAASVSELHLTANQLESIRSGMFRGLDGLRTLMLRNNRISCIHNDSFTGLRNVRLLSLYDNQITTVSPGAFDTLQSLSTLNLLANPFNCNCQLAWLGGWLRKRKIVTGNPRCQNPDFLRQIPLQDVAFPDFRCEEGQEEGGCLPRPQCPQECACLDTVVRCSNKHLRALPKGIPKNVTELYLDGNQFTLVPGQLSTFKYLQLVDLSNNKISSLSNSSFTNMSQLTTLILSYNALQCIPPLAFQGLRSLRLLSLHGNDISTLQEGIFADVTSLSHLAIGANPLYCDCHLRWLSSWVKTGYKEPGIARCAGPQDMEGKLLLTTPAKKFECQGPPTLAVQAKCDLCLSSPCQNQGTCHNDPLEVYRCACPSGYKGRDCEVSLDSCSSGPCENGGTCHAQEGEDAPFTCSCPTGFEGPTCGVNTDDCVDHACANGGVCVDGVGNYTCQCPLQYEGKACEQLVDLCSPDLNPCQHEAQCVGTPDGPRCECMPGYAGDNCSENQDDCRDHRCQNGAQCMDEVNSYSCLCAEGYSGQLCEIPPHLPAPKSPCEGTECQNGANCVDQGNRPVCQCLPGFGGPECEKLLSVNFVDRDTYLQFTDLQNWPRANITLQVSTAEDNGILLYNGDNDHIAVELYQGHVRVSYDPGSYPSSAIYSAETINDGQFHTVELVAFDQMVNLSIDGGSPMTMDNFGKHYTLNSEAPLYVGGMPVDVNSAAFRLWQILNGTGFHGCIRNLYINNELQDFTKTQMKPGVVPGCEPCRKLYCLHGICQPNATPGPMCHCEAGWVGLHCDQPADGPCHGHKCVHGQCVPLDALSYSCQCQDGYSGALCNQAGALAEPCRGLQCLHGHCQASGTKGAHCVCDPGFSGELCEQESECRGDPVRDFHQVQRGYAICQTTRPLSWVECRGSCPGQGCCQGLRLKRRKFTFECSDGTSFAEEVEKPTKCGCALCA
| null | null |
axon extension involved in axon guidance [GO:0048846]; axon guidance [GO:0007411]; dorsal/ventral axon guidance [GO:0033563]; forebrain morphogenesis [GO:0048853]; motor neuron axon guidance [GO:0008045]; negative chemotaxis [GO:0050919]; negative regulation of axon extension involved in axon guidance [GO:0048843]; negative regulation of synapse assembly [GO:0051964]; nuclear migration [GO:0007097]; retinal ganglion cell axon guidance [GO:0031290]; spinal cord development [GO:0021510]; tangential migration from the subventricular zone to the olfactory bulb [GO:0022028]
|
extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; Roundabout binding [GO:0048495]
|
PF00008;PF12661;PF02210;PF13855;PF01463;PF01462;
|
2.60.120.200;2.10.25.10;3.80.10.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Thought to act as molecular guidance cue in cellular migration, and function appears to be mediated by interaction with roundabout homolog receptors. During neural development involved in axonal navigation at the ventral midline of the neural tube and projection of axons to different regions (By similarity). SLIT1 and SLIT2 together seem to be essential for midline guidance in the forebrain by acting as repulsive signal preventing inappropriate midline crossing by axons projecting from the olfactory bulb. {ECO:0000250}.
|
Homo sapiens (Human)
|
O75094
|
SLIT3_HUMAN
|
MAPGWAGVGAAVRARLALALALASVLSGPPAVACPTKCTCSAASVDCHGLGLRAVPRGIPRNAERLDLDRNNITRITKMDFAGLKNLRVLHLEDNQVSVIERGAFQDLKQLERLRLNKNKLQVLPELLFQSTPKLTRLDLSENQIQGIPRKAFRGITDVKNLQLDNNHISCIEDGAFRALRDLEILTLNNNNISRILVTSFNHMPKIRTLRLHSNHLYCDCHLAWLSDWLRQRRTVGQFTLCMAPVHLRGFNVADVQKKEYVCPAPHSEPPSCNANSISCPSPCTCSNNIVDCRGKGLMEIPANLPEGIVEIRLEQNSIKAIPAGAFTQYKKLKRIDISKNQISDIAPDAFQGLKSLTSLVLYGNKITEIVKGLFDGLVSLQLLLLNANKINCLRVNTFQDLQNLNLLSLYDNKLQTISKGLFAPLQSIQTLHLAQNPFVCDCHLKWLADYLQDNPIETSGARCSSPRRLANKRISQIKSKKFRCSGSEDYRSRFSSECFMDLVCPEKCRCEGTIVDCSNQKLVRIPSHLPEYVTDLRLNDNEVSVLEATGIFKKLPNLRKINLSNNKIKEVREGAFDGAASVQELMLTGNQLETVHGRVFRGLSGLKTLMLRSNLIGCVSNDTFAGLSSVRLLSLYDNRITTITPGAFTTLVSLSTINLLSNPFNCNCHLAWLGKWLRKRRIVSGNPRCQKPFFLKEIPIQDVAIQDFTCDGNEESSCQLSPRCPEQCTCMETVVRCSNKGLRALPRGMPKDVTELYLEGNHLTAVPRELSALRHLTLIDLSNNSISMLTNYTFSNMSHLSTLILSYNRLRCIPVHAFNGLRSLRVLTLHGNDISSVPEGSFNDLTSLSHLALGTNPLHCDCSLRWLSEWVKAGYKEPGIARCSSPEPMADRLLLTTPTHRFQCKGPVDINIVAKCNACLSSPCKNNGTCTQDPVELYRCACPYSYKGKDCTVPINTCIQNPCQHGGTCHLSDSHKDGFSCSCPLGFEGQRCEINPDDCEDNDCENNATCVDGINNYVCICPPNYTGELCDEVIDHCVPELNLCQHEAKCIPLDKGFSCECVPGYSGKLCETDNDDCVAHKCRHGAQCVDTINGYTCTCPQGFSGPFCEHPPPMVLLQTSPCDQYECQNGAQCIVVQQEPTCRCPPGFAGPRCEKLITVNFVGKDSYVELASAKVRPQANISLQVATDKDNGILLYKGDNDPLALELYQGHVRLVYDSLSSPPTTVYSVETVNDGQFHSVELVTLNQTLNLVVDKGTPKSLGKLQKQPAVGINSPLYLGGIPTSTGLSALRQGTDRPLGGFHGCIHEVRINNELQDFKALPPQSLGVSPGCKSCTVCKHGLCRSVEKDSVVCECRPGWTGPLCDQEARDPCLGHRCHHGKCVATGTSYMCKCAEGYGGDLCDNKNDSANACSAFKCHHGQCHISDQGEPYCLCQPGFSGEHCQQENPCLGQVVREVIRRQKGYASCATASKVPIMECRGGCGPQCCQPTRSKRRKYVFQCTDGSSFVEEVERHLECGCLACS
| null | null |
aortic valve morphogenesis [GO:0003180]; apoptotic process involved in luteolysis [GO:0061364]; atrioventricular valve morphogenesis [GO:0003181]; axon extension involved in axon guidance [GO:0048846]; axon guidance [GO:0007411]; cellular response to hormone stimulus [GO:0032870]; negative chemotaxis [GO:0050919]; negative regulation of cell growth [GO:0030308]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of chemokine-mediated signaling pathway [GO:0070100]; negative regulation of gene expression [GO:0010629]; response to cortisol [GO:0051414]; Roundabout signaling pathway [GO:0035385]; ventricular septum morphogenesis [GO:0060412]
|
extracellular space [GO:0005615]; mitochondrion [GO:0005739]
|
calcium ion binding [GO:0005509]; heparin binding [GO:0008201]; Roundabout binding [GO:0048495]
|
PF00008;PF12661;PF02210;PF13855;PF01463;PF01462;
|
2.60.120.200;2.10.25.10;3.80.10.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May act as molecular guidance cue in cellular migration, and function may be mediated by interaction with roundabout homolog receptors.
|
Homo sapiens (Human)
|
O75096
|
LRP4_HUMAN
|
MRRQWGALLLGALLCAHGLASSPECACGRSHFTCAVSALGECTCIPAQWQCDGDNDCGDHSDEDGCILPTCSPLDFHCDNGKCIRRSWVCDGDNDCEDDSDEQDCPPRECEEDEFPCQNGYCIRSLWHCDGDNDCGDNSDEQCDMRKCSDKEFRCSDGSCIAEHWYCDGDTDCKDGSDEENCPSAVPAPPCNLEEFQCAYGRCILDIYHCDGDDDCGDWSDESDCSSHQPCRSGEFMCDSGLCINAGWRCDGDADCDDQSDERNCTTSMCTAEQFRCHSGRCVRLSWRCDGEDDCADNSDEENCENTGSPQCALDQFLCWNGRCIGQRKLCNGVNDCGDNSDESPQQNCRPRTGEENCNVNNGGCAQKCQMVRGAVQCTCHTGYRLTEDGHTCQDVNECAEEGYCSQGCTNSEGAFQCWCETGYELRPDRRSCKALGPEPVLLFANRIDIRQVLPHRSEYTLLLNNLENAIALDFHHRRELVFWSDVTLDRILRANLNGSNVEEVVSTGLESPGGLAVDWVHDKLYWTDSGTSRIEVANLDGAHRKVLLWQNLEKPRAIALHPMEGTIYWTDWGNTPRIEASSMDGSGRRIIADTHLFWPNGLTIDYAGRRMYWVDAKHHVIERANLDGSHRKAVISQGLPHPFAITVFEDSLYWTDWHTKSINSANKFTGKNQEIIRNKLHFPMDIHTLHPQRQPAGKNRCGDNNGGCTHLCLPSGQNYTCACPTGFRKISSHACAQSLDKFLLFARRMDIRRISFDTEDLSDDVIPLADVRSAVALDWDSRDDHVYWTDVSTDTISRAKWDGTGQEVVVDTSLESPAGLAIDWVTNKLYWTDAGTDRIEVANTDGSMRTVLIWENLDRPRDIVVEPMGGYMYWTDWGASPKIERAGMDASGRQVIISSNLTWPNGLAIDYGSQRLYWADAGMKTIEFAGLDGSKRKVLIGSQLPHPFGLTLYGERIYWTDWQTKSIQSADRLTGLDRETLQENLENLMDIHVFHRRRPPVSTPCAMENGGCSHLCLRSPNPSGFSCTCPTGINLLSDGKTCSPGMNSFLIFARRIDIRMVSLDIPYFADVVVPINITMKNTIAIGVDPQEGKVYWSDSTLHRISRANLDGSQHEDIITTGLQTTDGLAVDAIGRKVYWTDTGTNRIEVGNLDGSMRKVLVWQNLDSPRAIVLYHEMGFMYWTDWGENAKLERSGMDGSDRAVLINNNLGWPNGLTVDKASSQLLWADAHTERIEAADLNGANRHTLVSPVQHPYGLTLLDSYIYWTDWQTRSIHRADKGTGSNVILVRSNLPGLMDMQAVDRAQPLGFNKCGSRNGGCSHLCLPRPSGFSCACPTGIQLKGDGKTCDPSPETYLLFSSRGSIRRISLDTSDHTDVHVPVPELNNVISLDYDSVDGKVYYTDVFLDVIRRADLNGSNMETVIGRGLKTTDGLAVDWVARNLYWTDTGRNTIEASRLDGSCRKVLINNSLDEPRAIAVFPRKGYLFWTDWGHIAKIERANLDGSERKVLINTDLGWPNGLTLDYDTRRIYWVDAHLDRIESADLNGKLRQVLVSHVSHPFALTQQDRWIYWTDWQTKSIQRVDKYSGRNKETVLANVEGLMDIIVVSPQRQTGTNACGVNNGGCTHLCFARASDFVCACPDEPDSRPCSLVPGLVPPAPRATGMSEKSPVLPNTPPTTLYSSTTRTRTSLEEVEGRCSERDARLGLCARSNDAVPAAPGEGLHISYAIGGLLSILLILVVIAALMLYRHKKSKFTDPGMGNLTYSNPSYRTSTQEVKIEAIPKPAMYNQLCYKKEGGPDHNYTKEKIKIVEGICLLSGDDAEWDDLKQLRSSRGGLLRDHVCMKTDTVSIQASSGSLDDTETEQLLQEEQSECSSVHTAATPERRGSLPDTGWKHERKLSSESQV
| null | null |
amyloid-beta clearance by cellular catabolic process [GO:0150094]; dendrite morphogenesis [GO:0048813]; dorsal/ventral pattern formation [GO:0009953]; embryonic digit morphogenesis [GO:0042733]; enzyme-linked receptor protein signaling pathway [GO:0007167]; generation of neurons [GO:0048699]; hair follicle development [GO:0001942]; kidney development [GO:0001822]; limb development [GO:0060173]; negative regulation of axonogenesis [GO:0050771]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of ossification [GO:0030279]; odontogenesis of dentin-containing tooth [GO:0042475]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of presynaptic membrane organization [GO:1901631]; positive regulation of Rac protein signal transduction [GO:0035022]; positive regulation of skeletal muscle acetylcholine-gated channel clustering [GO:1904395]; postsynaptic membrane assembly [GO:0097104]; presynaptic membrane assembly [GO:0097105]; proximal/distal pattern formation [GO:0009954]; receptor-mediated endocytosis [GO:0006898]; skeletal muscle acetylcholine-gated channel clustering [GO:0071340]; synapse organization [GO:0050808]; synaptic assembly at neuromuscular junction [GO:0051124]; Wnt signaling pathway [GO:0016055]
|
apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; dendrite [GO:0030425]; neuromuscular junction [GO:0031594]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; plasma membrane raft [GO:0044853]; postsynaptic density [GO:0014069]; receptor complex [GO:0043235]; synaptic membrane [GO:0097060]
|
apolipoprotein binding [GO:0034185]; calcium ion binding [GO:0005509]; coreceptor activity [GO:0015026]; hormone binding [GO:0042562]; protein homodimerization activity [GO:0042803]; receptor tyrosine kinase binding [GO:0030971]; scaffold protein binding [GO:0097110]
|
PF12662;PF14670;PF00057;PF00058;
|
2.10.25.10;4.10.400.10;2.120.10.30;
|
LDLR family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8VI56}; Single-pass type I membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Mediates SOST-dependent inhibition of bone formation. Functions as a specific facilitator of SOST-mediated inhibition of Wnt signaling. Plays a key role in the formation and the maintenance of the neuromuscular junction (NMJ), the synapse between motor neuron and skeletal muscle. Directly binds AGRIN and recruits it to the MUSK signaling complex. Mediates the AGRIN-induced phosphorylation of MUSK, the kinase of the complex. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Alternatively, may be involved in the negative regulation of the canonical Wnt signaling pathway, being able to antagonize the LRP6-mediated activation of this pathway. More generally, has been proposed to function as a cell surface endocytic receptor binding and internalizing extracellular ligands for degradation by lysosomes. May play an essential role in the process of digit differentiation (By similarity). {ECO:0000250|UniProtKB:Q8VI56, ECO:0000269|PubMed:20381006, ECO:0000269|PubMed:21471202}.
|
Homo sapiens (Human)
|
O75106
|
AOC2_HUMAN
|
MHLKIVLAFLALSLITIFALAYVLLTSPGGSSQPPHCPSVSHRAQPWPHPGQSQLFADLSREELTAVMRFLTQRLGPGLVDAAQAQPSDNCIFSVELQLPPKAAALAHLDRGSPPPAREALAIVLFGGQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLRAEFTQMWRHLKEVELPKAPIFLSSTFNYNGSTLAAVHATPRGLRSGDRATWMALYHNISGVGLFLHPVGLELLLDHRALDPAHWTVQQVFYLGHYYADLGQLEREFKSGRLEVVRVPLPPPNGASSLRSRNSPGPLPPLQFSPQGSQYSVQGNLVVSSLWSFTFGHGVFSGLRIFDVRFQGERIAYEVSVQECVSIYGADSPKTMLTRYLDSSFGLGRNSRGLVRGVDCPYQATMVDIHILVGKGAVQLLPGAVCVFEEAQGLPLRRHHNYLQNHFYGGLASSALVVRSVSSVGNYDYIWDFVLYPNGALEGRVHATGYINTAFLKGGEEGLLFGNRVGERVLGTVHTHAFHFKLDLDVAGLKNWVVAEDVVFKPVAAPWNPEHWLQRPQLTRQVLGKEDLTAFSLGSPLPRYLYLASNQTNAWGHQRGYRIQIHSPLGIHIPLESDMERALSWGRYQLVVTQRKEEESQSSSIYHQNDIWTPTVTFADFINNETLLGEDLVAWVTASFLHIPHAEDIPNTVTLGNRVGFLLRPYNFFDEDPSIFSPGSVYFEKGQDAGLCSINPVACLPDLAACVPDLPPFSYHGF
|
1.4.3.21
|
COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:Q16853}; Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:Q16853}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q16853}; Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:Q16853}; COFACTOR: Name=L-topaquinone; Xref=ChEBI:CHEBI:79027; Evidence={ECO:0000250|UniProtKB:Q16853}; Note=Contains 1 topaquinone per subunit. {ECO:0000250|UniProtKB:Q16853};
|
amine metabolic process [GO:0009308]; catecholamine metabolic process [GO:0006584]; visual perception [GO:0007601]; xenobiotic metabolic process [GO:0006805]
|
cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
|
aliphatic amine oxidase activity [GO:0052595]; copper ion binding [GO:0005507]; electron transfer activity [GO:0009055]; primary amine oxidase activity [GO:0008131]; quinone binding [GO:0048038]
|
PF01179;PF02727;PF02728;
|
3.10.450.40;2.70.98.20;
|
Copper/topaquinone oxidase family
|
PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. {ECO:0000250|UniProtKB:Q16853}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:19588076}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q16853}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:19588076}. Note=Either not translocated to the plasma membrane or below detection level. {ECO:0000269|PubMed:19588076}.
|
CATALYTIC ACTIVITY: Reaction=2-phenylethylamine + H2O + O2 = 2-phenylacetaldehyde + H2O2 + NH4(+); Xref=Rhea:RHEA:25265, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16424, ChEBI:CHEBI:28938, ChEBI:CHEBI:225237; EC=1.4.3.21; Evidence={ECO:0000269|PubMed:19588076}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25266; Evidence={ECO:0000305|PubMed:19588076}; CATALYTIC ACTIVITY: Reaction=H2O + O2 + tryptamine = H2O2 + indole-3-acetaldehyde + NH4(+); Xref=Rhea:RHEA:59416, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18086, ChEBI:CHEBI:28938, ChEBI:CHEBI:57887; Evidence={ECO:0000269|PubMed:19588076}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59417; Evidence={ECO:0000305|PubMed:19588076}; CATALYTIC ACTIVITY: Reaction=H2O + O2 + tyramine = (4-hydroxyphenyl)acetaldehyde + H2O2 + NH4(+); Xref=Rhea:RHEA:30591, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:15621, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:327995; Evidence={ECO:0000269|PubMed:19588076}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30592; Evidence={ECO:0000305|PubMed:19588076};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.056 mM for tryptamine {ECO:0000269|PubMed:19588076}; KM=0.077 mM for 2-phenylethylamine {ECO:0000269|PubMed:19588076}; KM=0.167 mM for benzylamine {ECO:0000269|PubMed:19588076}; KM=0.178 mM for p-tyramine {ECO:0000269|PubMed:19588076}; KM=1.7 mM for methylamine {ECO:0000269|PubMed:19588076}; Vmax=28 nmol/h/mg enzyme with tryptamine as substrate {ECO:0000269|PubMed:19588076}; Vmax=44 nmol/h/mg enzyme with 2-phenylethylamine as substrate {ECO:0000269|PubMed:19588076}; Vmax=11 nmol/h/mg enzyme with benzylamine as substrate {ECO:0000269|PubMed:19588076}; Vmax=43 nmol/h/mg enzyme with p-tyramine as substrate {ECO:0000269|PubMed:19588076}; Vmax=2.4 nmol/h/mg enzyme with methylamine as substrate {ECO:0000269|PubMed:19588076};
| null | null | null |
FUNCTION: Catalyzes the oxidative deamination of primary amines to the corresponding aldehydes with the concomitant production of hydrogen peroxide and ammonia (PubMed:19588076). Has a preference for 2-phenylethylamine, tryptamine and tyramine (PubMed:19588076). Could also act on methylamine and benzylamine but much less efficiently (PubMed:19588076). {ECO:0000269|PubMed:19588076}.
|
Homo sapiens (Human)
|
O75110
|
ATP9A_HUMAN
|
MTDNIPLQPVRQKKRMDSRPRAGCCEWLRCCGGGEARPRTVWLGHPEKRDQRYPRNVINNQKYNFFTFLPGVLFNQFKYFFNLYFLLLACSQFVPEMRLGALYTYWVPLGFVLAVTVIREAVEEIRCYVRDKEVNSQVYSRLTARGTVKVKSSNIQVGDLIIVEKNQRVPADMIFLRTSEKNGSCFLRTDQLDGETDWKLRLPVACTQRLPTAADLLQIRSYVYAEEPNIDIHNFVGTFTREDSDPPISESLSIENTLWAGTVVASGTVVGVVLYTGRELRSVMNTSNPRSKIGLFDLEVNCLTKILFGALVVVSLVMVALQHFAGRWYLQIIRFLLLFSNIIPISLRVNLDMGKIVYSWVIRRDSKIPGTVVRSSTIPEQLGRISYLLTDKTGTLTQNEMIFKRLHLGTVAYGLDSMDEVQSHIFSIYTQQSQDPPAQKGPTLTTKVRRTMSSRVHEAVKAIALCHNVTPVYESNGVTDQAEAEKQYEDSCRVYQASSPDEVALVQWTESVGLTLVGRDQSSMQLRTPGDQILNFTILQIFPFTYESKRMGIIVRDESTGEITFYMKGADVVMAGIVQYNDWLEEECGNMAREGLRVLVVAKKSLAEEQYQDFEARYVQAKLSVHDRSLKVATVIESLEMEMELLCLTGVEDQLQADVRPTLETLRNAGIKVWMLTGDKLETATCTAKNAHLVTRNQDIHVFRLVTNRGEAHLELNAFRRKHDCALVISGDSLEVCLKYYEYEFMELACQCPAVVCCRCAPTQKAQIVRLLQERTGKLTCAVGDGGNDVSMIQESDCGVGVEGKEGKQASLAADFSITQFKHLGRLLMVHGRNSYKRSAALSQFVIHRSLCISTMQAVFSSVFYFASVPLYQGFLIIGYSTIYTMFPVFSLVLDKDVKSEVAMLYPELYKDLLKGRPLSYKTFLIWVLISIYQGSTIMYGALLLFESEFVHIVAISFTSLILTELLMVALTIQTWHWLMTVAELLSLACYIASLVFLHEFIDVYFIATLSFLWKVSVITLVSCLPLYVLKYLRRRFSPPSYSKLTS
|
7.6.2.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P40527};
|
endocytosis [GO:0006897]; negative regulation of exosomal secretion [GO:1903542]; neuron projection morphogenesis [GO:0048812]; phospholipid translocation [GO:0045332]; regulation of endocytic recycling [GO:2001135]; regulation of retrograde transport, endosome to Golgi [GO:1905279]; retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum [GO:0006890]
|
early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; trans-Golgi network [GO:0005802]; trans-Golgi network membrane [GO:0032588]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; magnesium ion binding [GO:0000287]; protease binding [GO:0002020]
|
PF13246;PF00122;PF00702;PF16212;PF16209;
|
3.40.1110.10;2.70.150.10;3.40.50.1000;
|
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IV subfamily
| null |
SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:27733620, ECO:0000269|PubMed:30213940}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:27733620}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:36604604}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:27733620, ECO:0000269|PubMed:30213940}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:30947313}; Multi-pass membrane protein. Note=Efficient exit from the endoplasmic reticulum does not require TMEM30A, nor TMEM30B (PubMed:21914794). Transiently expressed in the cell membrane (PubMed:30947313). {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:30947313}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000305|PubMed:30213940};
| null | null | null | null |
FUNCTION: Plays a role in regulating membrane trafficking of cargo proteins, namely endosome to plasma membrane recycling, probably acting through RAB5 and RAB11 activation (PubMed:27733620, PubMed:30213940, PubMed:36604604). Also involved in endosome to trans-Golgi network retrograde transport (PubMed:27733620, PubMed:30213940). In complex with MON2 and DOP1B, regulates SNX3 retromer-mediated endosomal sorting of WLS, a transporter of Wnt morphogens in developing tissues. Participates in the formation of endosomal carriers that direct WLS trafficking back to Golgi, away from lysosomal degradation (PubMed:30213940). Appears to be implicated in intercellular communication by negatively regulating the release of exosomes (PubMed:30947313). The flippase activity towards membrane lipids and its role in membrane asymmetry remains to be proved (PubMed:30947313). Required for the maintenance of neurite morphology and synaptic transmission (By similarity). {ECO:0000250|UniProtKB:O70228, ECO:0000269|PubMed:27733620, ECO:0000269|PubMed:30213940, ECO:0000269|PubMed:30947313, ECO:0000269|PubMed:36604604}.
|
Homo sapiens (Human)
|
O75112
|
LDB3_HUMAN
|
MSYSVTLTGPGPWGFRLQGGKDFNMPLTISRITPGSKAAQSQLSQGDLVVAIDGVNTDTMTHLEAQNKIKSASYNLSLTLQKSKRPIPISTTAPPVQTPLPVIPHQKDPALDTNGSLVAPSPSPEARASPGTPGTPELRPTFSPAFSRPSAFSSLAEASDPGPPRASLRAKTSPEGARDLLGPKALPGSSQPRQYNNPIGLYSAETLREMAQMYQMSLRGKASGVGLPGGSLPIKDLAVDSASPVYQAVIKSQNKPEDEADEWARRSSNLQSRSFRILAQMTGTEFMQDPDEEALRRSSTPIEHAPVCTSQATTPLLPASAQPPAAASPSAASPPLATAAAHTAIASASTTAPASSPADSPRPQASSYSPAVAASSAPATHTSYSEGPAAPAPKPRVVTTASIRPSVYQPVPASTYSPSPGANYSPTPYTPSPAPAYTPSPAPAYTPSPVPTYTPSPAPAYTPSPAPNYNPAPSVAYSGGPAEPASRPPWVTDDSFSQKFAPGKSTTSISKQTLPRGGPAYTPAGPQVPPLARGTVQRAERFPASSRTPLCGHCNNVIRGPFLVAMGRSWHPEEFTCAYCKTSLADVCFVEEQNNVYCERCYEQFFAPLCAKCNTKIMGEVMHALRQTWHTTCFVCAACKKPFGNSLFHMEDGEPYCEKDYINLFSTKCHGCDFPVEAGDKFIEALGHTWHDTCFICAVCHVNLEGQPFYSKKDRPLCKKHAHTINL
| null | null |
actin cytoskeleton organization [GO:0030036]; heart development [GO:0007507]; muscle structure development [GO:0061061]; sarcomere organization [GO:0045214]
|
adherens junction [GO:0005912]; cytoskeleton [GO:0005856]; filamentous actin [GO:0031941]; perinuclear region of cytoplasm [GO:0048471]; pseudopodium [GO:0031143]; stress fiber [GO:0001725]; Z disc [GO:0030018]
|
actin binding [GO:0003779]; cytoskeletal protein binding [GO:0008092]; metal ion binding [GO:0046872]; muscle alpha-actinin binding [GO:0051371]; protein kinase C binding [GO:0005080]
|
PF15936;PF00412;PF00595;
|
2.30.42.10;2.10.110.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10427098}. Cell projection, pseudopodium {ECO:0000269|PubMed:10427098}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10427098}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:10427098}. Note=Localized to the cytoplasm around nuclei and pseudopodia of undifferentiated cells and detected throughout the myotubes of differentiated cells. Colocalizes with ACTN2 at the Z-lines.
| null | null | null | null | null |
FUNCTION: May function as an adapter in striated muscle to couple protein kinase C-mediated signaling via its LIM domains to the cytoskeleton. {ECO:0000305}.
|
Homo sapiens (Human)
|
O75113
|
N4BP1_HUMAN
|
MAARAVLDEFTAPAEKAELLEQSRGRIEGLFGVSLAVLGALGAEEPLPARIWLQLCGAQEAVHSAKEYIKGICEPELEERECYPKDMHCIFVGAESLFLKSLIQDTCADLCILDIGLLGIRGSAEAVVMARSHIQQFVKLFENKENLPSSQKESEVKREFKQFVEAHADNYTMDLLILPTSLKKELLTLTQGEENLFETGDDEVIEMRDSQQTEFTQNAATGLNISRDETVLQEEARNKAGTPVSELTKQMDTVLSSSPDVLFDPINGLTPDEEALSNERICQKRRFSDSEERHTKKQFSLENVQEGEILHDAKTLAGNVIADLSDSSADSENLSPDIKETTEEMEYNILVNFFKTMGYSQEIVEKVIKVYGPSTEPLLLLEEIEKENKRFQEDREFSAGTVYPETNKTKNKGVYSSTNELTTDSTPKKTQAHTQQNMVEKFSQLPFKVEAKPCTSNCRINTFRTVPIEQKHEVWGSNQNYICNTDPETDGLSPSVASPSPKEVNFVSRGASSHQPRVPLFPENGLHQQPEPLLPNNMKSACEKRLGCCSSPHSKPNCSTLSPPMPLPQLLPSVTDARSAGPSDHIDSSVTGVQRFRDTLKIPYKLELKNEPGRTDLKHIVIDGSNVAITHGLKKFFSCRGIAIAVEYFWKLGNRNITVFVPQWRTRRDPNVTEQHFLTQLQELGILSLTPARMVFGERIASHDDRFLLHLADKTGGIIVTNDNFREFVNESVSWREIITKRLLQYTFVGDIFMVPDDPLGRSGPRLEEFLQKEVCLRDMQPLLSALPNVGMFDPSFRVPGTQAASTSHQPPTRIQGAPSSHWLPQQPHFPLLPALPSLQQNLPMPAQRSSAETNELREALLKIFPDSEQRLKIDQILVAHPYMKDLNALSAMVLD
|
3.1.-.-
| null |
cellular response to UV [GO:0034644]; innate immune response [GO:0045087]; negative regulation of cytokine production [GO:0001818]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of viral genome replication [GO:0045071]; regulation of innate immune response [GO:0045088]
|
cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleus [GO:0005634]; PML body [GO:0016605]
|
mRNA binding [GO:0003729]; RNA nuclease activity [GO:0004540]; ubiquitin binding [GO:0043130]
|
PF11977;
|
3.40.50.11980;
|
N4BP1 family
|
PTM: Proteolytically cleaved by CASP8 downstream of TLR3 or TLR4, leading to its inactivation. Mainly cleaved at Asp-490 by CASP8 (By similarity). Cleaved by caspase-like protein MALT1 in T-cells following TCR-mediated activation, leading to its inactivation and subsequent viral reactivation during HIV-1 infection (PubMed:31133753). {ECO:0000250|UniProtKB:Q6A037, ECO:0000269|PubMed:31133753}.; PTM: Mono- and polyubiquitinated on the CoCUN region (PubMed:31319543). Monoubiquitinated by NEDD4 (By similarity). Polyubiquitinated, leading to its degradation by the proteasome (By similarity). Sumoylated with SUMO1, abrogating polyubiquitination and subsequent degradation (By similarity). Desumoylated by SENP1, leading to accumulation in PML nuclear bodies (By similarity). {ECO:0000250|UniProtKB:Q6A037, ECO:0000269|PubMed:31319543}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q6A037}. Nucleus {ECO:0000250|UniProtKB:Q6A037}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q6A037}. Nucleus, PML body {ECO:0000250|UniProtKB:Q6A037}. Note=Primarily localizes to the nucleolus. Also localizes to the PML nuclear bodies, when desumoylated. {ECO:0000250|UniProtKB:Q6A037}.
| null | null | null | null | null |
FUNCTION: Potent suppressor of cytokine production that acts as a regulator of innate immune signaling and inflammation. Acts as a key negative regulator of select cytokine and chemokine responses elicited by TRIF-independent Toll-like receptors (TLRs), thereby limiting inflammatory cytokine responses to minor insults. In response to more threatening pathogens, cleaved by CASP8 downstream of TLR3 or TLR4, leading to its inactivation, thereby allowing production of inflammatory cytokines (By similarity). Acts as a restriction factor against some viruses, such as HIV-1: restricts HIV-1 replication by binding to HIV-1 mRNAs and mediating their degradation via its ribonuclease activity (PubMed:31133753). Also acts as an inhibitor of the E3 ubiquitin-protein ligase ITCH: acts by interacting with the second WW domain of ITCH, leading to compete with ITCH's substrates and impairing ubiquitination of substrates (By similarity). {ECO:0000250|UniProtKB:Q6A037, ECO:0000269|PubMed:31133753}.
|
Homo sapiens (Human)
|
O75116
|
ROCK2_HUMAN
|
MSRPPPTGKMPGAPETAPGDGAGASRQRKLEALIRDPRSPINVESLLDGLNSLVLDLDFPALRKNKNIDNFLNRYEKIVKKIRGLQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKHGHLKLADFGTCMKMDETGMVHCDTAVGTPDYISPEVLKSQGGDGFYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMDHKNSLCFPEDAEISKHAKNLICAFLTDREVRLGRNGVEEIRQHPFFKNDQWHWDNIRETAAPVVPELSSDIDSSNFDDIEDDKGDVETFPIPKAFVGNQLPFIGFTYYRENLLLSDSPSCRETDSIQSRKNEESQEIQKKLYTLEEHLSNEMQAKEELEQKCKSVNTRLEKTAKELEEEITLRKSVESALRQLEREKALLQHKNAEYQRKADHEADKKRNLENDVNSLKDQLEDLKKRNQNSQISTEKVNQLQRQLDETNALLRTESDTAARLRKTQAESSKQIQQLESNNRDLQDKNCLLETAKLKLEKEFINLQSALESERRDRTHGSEIINDLQGRICGLEEDLKNGKILLAKVELEKRQLQERFTDLEKEKSNMEIDMTYQLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQALHIGLDSSSIGSGPGDAEADDGFPESRLEGWLSLPVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEQSNPYMVLDIDKLFHVRPVTQTDVYRADAKEIPRIFQILYANEGESKKEQEFPVEPVGEKSNYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVYYDISTAKNLLLLANSTEEQQKWVSRLVKKIPKKPPAPDPFARSSPRTSMKIQQNQSIRRPSRQLAPNKPS
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
actin cytoskeleton organization [GO:0030036]; actomyosin structure organization [GO:0031032]; aortic valve morphogenesis [GO:0003180]; blood vessel diameter maintenance [GO:0097746]; canonical NF-kappaB signal transduction [GO:0007249]; cellular response to acetylcholine [GO:1905145]; cellular response to testosterone stimulus [GO:0071394]; centrosome duplication [GO:0051298]; cortical actin cytoskeleton organization [GO:0030866]; embryonic morphogenesis [GO:0048598]; epithelial to mesenchymal transition [GO:0001837]; mitotic cytokinesis [GO:0000281]; modulation by host of viral process [GO:0044788]; mRNA destabilization [GO:0061157]; negative regulation of angiogenesis [GO:0016525]; negative regulation of bicellular tight junction assembly [GO:1903347]; negative regulation of biomineral tissue development [GO:0070168]; negative regulation of gene expression [GO:0010629]; negative regulation of myosin-light-chain-phosphatase activity [GO:0035509]; negative regulation of nitric oxide biosynthetic process [GO:0045019]; negative regulation of protein localization to lysosome [GO:0150033]; positive regulation of amyloid precursor protein catabolic process [GO:1902993]; positive regulation of amyloid-beta formation [GO:1902004]; positive regulation of cardiac muscle hypertrophy [GO:0010613]; positive regulation of cell migration [GO:0030335]; positive regulation of centrosome duplication [GO:0010825]; positive regulation of connective tissue growth factor production [GO:0032723]; positive regulation of connective tissue replacement [GO:1905205]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of fibroblast growth factor production [GO:0090271]; positive regulation of gene expression [GO:0010628]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of protein localization to early endosome [GO:1902966]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of stress fiber assembly [GO:0051496]; protein localization to plasma membrane [GO:0072659]; protein phosphorylation [GO:0006468]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of angiotensin-activated signaling pathway [GO:0110061]; regulation of cell adhesion [GO:0030155]; regulation of cell junction assembly [GO:1901888]; regulation of cell motility [GO:2000145]; regulation of cellular response to hypoxia [GO:1900037]; regulation of circadian rhythm [GO:0042752]; regulation of establishment of cell polarity [GO:2000114]; regulation of establishment of endothelial barrier [GO:1903140]; regulation of focal adhesion assembly [GO:0051893]; regulation of keratinocyte differentiation [GO:0045616]; regulation of nervous system process [GO:0031644]; regulation of stress fiber assembly [GO:0051492]; response to angiotensin [GO:1990776]; response to ischemia [GO:0002931]; response to transforming growth factor beta [GO:0071559]; Rho protein signal transduction [GO:0007266]; rhythmic process [GO:0048511]; smooth muscle contraction [GO:0006939]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; endopeptidase activator activity [GO:0061133]; metal ion binding [GO:0046872]; protease binding [GO:0002020]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; Rho-dependent protein serine/threonine kinase activity [GO:0072518]; RNA binding [GO:0003723]; small GTPase binding [GO:0031267]; structural molecule activity [GO:0005198]; tau protein binding [GO:0048156]; tau-protein kinase activity [GO:0050321]
|
PF00069;PF08912;
|
1.20.5.340;3.30.60.20;2.30.29.30;1.20.5.730;1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family
|
PTM: Phosphorylation at Tyr-722 reduces its binding to RHOA and is crucial for focal adhesion dynamics. Dephosphorylation by PTPN11 stimulates its RHOA binding activity. {ECO:0000269|PubMed:18559669, ECO:0000269|PubMed:20826462}.; PTM: Cleaved by granzyme B during apoptosis. This leads to constitutive activation of the kinase and membrane blebbing.
|
SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Cytoplasmic, and associated with actin microfilaments and the plasma membrane. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of ADD1, BRCA2, CNN1, EZR, DPYSL2, EP300, MSN, MYL9/MLC2, NPM1, RDX, PPP1R12A and VIM. Phosphorylates SORL1 and IRF4. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Positively regulates the activation of p42/MAPK1-p44/MAPK3 and of p90RSK/RPS6KA1 during myogenic differentiation. Plays an important role in the timely initiation of centrosome duplication. Inhibits keratinocyte terminal differentiation. May regulate closure of the eyelids and ventral body wall through organization of actomyosin bundles. Plays a critical role in the regulation of spine and synaptic properties in the hippocampus. Plays an important role in generating the circadian rhythm of the aortic myofilament Ca(2+) sensitivity and vascular contractility by modulating the myosin light chain phosphorylation. {ECO:0000269|PubMed:10579722, ECO:0000269|PubMed:15699075, ECO:0000269|PubMed:16574662, ECO:0000269|PubMed:17015463, ECO:0000269|PubMed:19131646, ECO:0000269|PubMed:19997641, ECO:0000269|PubMed:21084279, ECO:0000269|PubMed:21147781}.
|
Homo sapiens (Human)
|
O75121
|
MFA3L_HUMAN
|
MDRLKSHLTVCFLPSVPFLILVSTLATAKSVTNSTLNGTNVVLGSVPVIIARTDHIIVKEGNSALINCSVYGIPDPQFKWYNSIGKLLKEEEDEKERGGGKWQMHDSGLLNITKVSFSDRGKYTCVASNIYGTVNNTVTLRVIFTSGDMGVYYMVVCLVAFTIVMVLNITRLCMMSSHLKKTEKAINEFFRTEGAEKLQKAFEIAKRIPIITSAKTLELAKVTQFKTMEFARYIEELARSVPLPPLIMNCRTIMEEIMEVVGLEEQGQNFVRHTPEGQEAADRDEVYTIPNSLKRSDSPAADSDASSLHEQPQQIAIKVSVHPQSKKEHADDQEGGQFEVKDVEETELSAEHSPETAEPSTDVTSTELTSEEPTPVEVPDKVLPPAYLEATEPAVTHDKNTCIIYESHV
| null | null | null |
cell junction [GO:0030054]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
| null |
PF07679;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24735981}; Single-pass type I membrane protein {ECO:0000305}. Nucleus {ECO:0000269|PubMed:24735981}. Cytoplasm {ECO:0000269|PubMed:24735981}. Note=Mainly localized in the nucleus (PubMed:24735981). {ECO:0000269|PubMed:24735981}.
| null | null | null | null | null |
FUNCTION: May participate in the nuclear signaling of EGFR and MAPK1/ERK2. May a have a role in metastasis. {ECO:0000269|PubMed:24735981}.
|
Homo sapiens (Human)
|
O75122
|
CLAP2_HUMAN
|
MAMGDDKSFDDEESVDGNRPSSAASAFKVPAPKTSGNPANSARKPGSAGGPKVGGASKEGGAGAVDEDDFIKAFTDVPSIQIYSSRELEETLNKIREILSDDKHDWDQRANALKKIRSLLVAGAAQYDCFFQHLRLLDGALKLSAKDLRSQVVREACITVAHLSTVLGNKFDHGAEAIVPTLFNLVPNSAKVMATSGCAAIRFIIRHTHVPRLIPLITSNCTSKSVPVRRRSFEFLDLLLQEWQTHSLERHAAVLVETIKKGIHDADAEARVEARKTYMGLRNHFPGEAETLYNSLEPSYQKSLQTYLKSSGSVASLPQSDRSSSSSQESLNRPFSSKWSTANPSTVAGRVSAGSSKASSLPGSLQRSRSDIDVNAAAGAKAHHAAGQSVRSGRLGAGALNAGSYASLEDTSDKLDGTASEDGRVRAKLSAPLAGMGNAKADSRGRSRTKMVSQSQPGSRSGSPGRVLTTTALSTVSSGVQRVLVNSASAQKRSKIPRSQGCSREASPSRLSVARSSRIPRPSVSQGCSREASRESSRDTSPVRSFQPLASRHHSRSTGALYAPEVYGASGPGYGISQSSRLSSSVSAMRVLNTGSDVEEAVADALKKPARRRYESYGMHSDDDANSDASSACSERSYSSRNGSIPTYMRQTEDVAEVLNRCASSNWSERKEGLLGLQNLLKNQRTLSRVELKRLCEIFTRMFADPHGKRVFSMFLETLVDFIQVHKDDLQDWLFVLLTQLLKKMGADLLGSVQAKVQKALDVTRESFPNDLQFNILMRFTVDQTQTPSLKVKVAILKYIETLAKQMDPGDFINSSETRLAVSRVITWTTEPKSSDVRKAAQSVLISLFELNTPEFTMLLGALPKTFQDGATKLLHNHLRNTGNGTQSSMGSPLTRPTPRSPANWSSPLTSPTNTSQNTLSPSAFDYDTENMNSEDIYSSLRGVTEAIQNFSFRSQEDMNEPLKRDSKKDDGDSMCGGPGMSDPRAGGDATDSSQTALDNKASLLHSMPTHSSPRSRDYNPYNYSDSISPFNKSALKEAMFDDDADQFPDDLSLDHSDLVAELLKELSNHNERVEERKIALYELMKLTQEESFSVWDEHFKTILLLLLETLGDKEPTIRALALKVLREILRHQPARFKNYAELTVMKTLEAHKDPHKEVVRSAEEAASVLATSISPEQCIKVLCPIIQTADYPINLAAIKMQTKVIERVSKETLNLLLPEIMPGLIQGYDNSESSVRKACVFCLVAVHAVIGDELKPHLSQLTGSKMKLLNLYIKRAQTGSGGADPTTDVSGQS
| null | null |
cell division [GO:0051301]; establishment of mitotic spindle localization [GO:0040001]; establishment or maintenance of cell polarity [GO:0007163]; exit from mitosis [GO:0010458]; Golgi organization [GO:0007030]; microtubule anchoring [GO:0034453]; microtubule cytoskeleton organization [GO:0000226]; microtubule nucleation [GO:0007020]; microtubule organizing center organization [GO:0031023]; mitotic spindle assembly [GO:0090307]; mitotic spindle organization [GO:0007052]; negative regulation of focal adhesion assembly [GO:0051895]; negative regulation of microtubule depolymerization [GO:0007026]; negative regulation of stress fiber assembly [GO:0051497]; negative regulation of wound healing, spreading of epidermal cells [GO:1903690]; platelet-derived growth factor receptor-beta signaling pathway [GO:0035791]; positive regulation of basement membrane assembly involved in embryonic body morphogenesis [GO:1904261]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of exocytosis [GO:0045921]; positive regulation of extracellular matrix disassembly [GO:0090091]; protein localization to plasma membrane [GO:0072659]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of axon extension [GO:0030516]; regulation of epithelial to mesenchymal transition [GO:0010717]; regulation of gastrulation [GO:0010470]; regulation of microtubule polymerization [GO:0031113]; regulation of microtubule polymerization or depolymerization [GO:0031110]; regulation of microtubule-based process [GO:0032886]; vesicle targeting [GO:0006903]
|
axonal growth cone [GO:0044295]; basal cortex [GO:0045180]; cell cortex [GO:0005938]; cell leading edge [GO:0031252]; centrosome [GO:0005813]; cortical microtubule plus-end [GO:1903754]; cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; membrane [GO:0016020]; microtubule [GO:0005874]; microtubule organizing center [GO:0005815]; mitotic spindle [GO:0072686]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587]; spindle microtubule [GO:0005876]; trans-Golgi network [GO:0005802]
|
actin filament binding [GO:0051015]; dystroglycan binding [GO:0002162]; microtubule binding [GO:0008017]; microtubule plus-end binding [GO:0051010]; protein tyrosine kinase binding [GO:1990782]
|
PF21040;PF12348;
|
1.25.10.10;
|
CLASP family
|
PTM: Phosphorylated by GSK3B. Phosphorylation reduces MAPRE1 binding (PubMed:26003921). Phosphorylation by GSK3B may negatively regulate binding to microtubule lattices in lamella. {ECO:0000269|PubMed:15955847, ECO:0000305|PubMed:26003921}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15631994, ECO:0000269|PubMed:20937854}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:16914514}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:16866869, ECO:0000269|PubMed:16914514}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16866869, ECO:0000269|PubMed:16914514}. Golgi apparatus {ECO:0000250|UniProtKB:Q8BRT1}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:17543864}. Cell membrane {ECO:0000269|PubMed:20937854}. Cell projection, ruffle membrane {ECO:0000269|PubMed:20937854}. Note=Localizes to microtubule plus ends (PubMed:15631994). Localizes to centrosomes, kinetochores and the mitotic spindle from prometaphase. Subsequently localizes to the spindle midzone from anaphase and to the midbody from telophase (PubMed:16866869, PubMed:16914514). In migrating cells localizes to the plus ends of microtubules within the cell body and to the entire microtubule lattice within the lamella. Localizes to the cell cortex and this requires ERC1 and PHLDB2 (PubMed:16824950). The MEMO1-RHOA-DIAPH1 signaling pathway controls localization of the phosphorylated form to the cell membrane. {ECO:0000269|PubMed:15631994, ECO:0000269|PubMed:16824950, ECO:0000269|PubMed:16866869, ECO:0000269|PubMed:16914514, ECO:0000269|PubMed:20937854}.
| null | null | null | null | null |
FUNCTION: Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules (PubMed:26003921). Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2 (PubMed:16824950). This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle (PubMed:16866869, PubMed:16914514). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. {ECO:0000269|PubMed:11290329, ECO:0000269|PubMed:15631994, ECO:0000269|PubMed:16824950, ECO:0000269|PubMed:16866869, ECO:0000269|PubMed:16914514, ECO:0000269|PubMed:17543864, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:26003921}.
|
Homo sapiens (Human)
|
O75127
|
PTCD1_HUMAN
|
MDFVRLARLFARARPMGLFILQHLDPCRARWAGGREGLMRPMWAPFSSSSSQLPLGQERQENTGSLGSDPSHSNSTATQEEDEEEEESFGTLSDKYSSRRLFRKSAAQFHNLRFGERRDEQMEPEPKLWRGRRNTPYWYFLQCKHLIKEGKLVEALDLFERQMLKEERLQPMESNYTVLIGGCGRVGYLKKAFNLYNQMKKRDLEPSDATYTALFNVCAESPWKDSALQSALKLRQQLQAKNFELNLKTYHALLKMAAKCADLRMCLDVFKEIIHKGHVVTEETFSFLLMGCIQDKKTGFRYALQVWRLMLSLGLQPSRDSYNLLLVAARDCGLGDPQVASELLLKPREEATVLQPPVSRQRPRRTAQAKAGNLMSAMLHVEALERQLFLEPSQALGPPEPPEARVPGKAQPEVDTKAEPSHTAALTAVALKPPPVELEVNLLTPGAVPPTVVSFGTVTTPADRLALIGGLEGFLSKMAEHRQQPDIRTLTLLAEVVESGSPAESLLLALLDEHQVEADLTFFNTLVRKKSKLGDLEGAKALLPVLAKRGLVPNLQTFCNLAIGCHRPKDGLQLLTDMKKSQVTPNTHIYSALINAAIRKLNYTYLISILKDMKQNRVPVNEVVIRQLEFAAQYPPTFDRYQGKNTYLEKIDGFRAYYKQWLTVMPAEETPHPWQKFRTKPQGDQDTGKEADDGCALGGR
| null | null |
mitochondrial translation [GO:0032543]; tRNA 3'-end processing [GO:0042780]
|
mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
|
RNA binding [GO:0003723]; tRNA binding [GO:0000049]
|
PF13812;PF17177;
|
1.25.40.10;
|
PTCD1 family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19651879, ECO:0000269|PubMed:21857155}. Mitochondrion matrix {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Mitochondrial protein implicated in negative regulation of leucine tRNA levels, as well as negative regulation of mitochondria-encoded proteins and COX activity. Affects also the 3'-processing of mitochondrial tRNAs. {ECO:0000269|PubMed:21857155}.
|
Homo sapiens (Human)
|
O75128
|
COBL_HUMAN
|
MDAPRASAAKPPTGRKMKARAPPPPGKAATLHVHSDQKPPHDGALGSQQNLVRMKEALRASTMDVTVVLPSGLEKRSVLNGSHAMMDLLVELCLQNHLNPSHHALEIRSSETQQPLSFKPNTLIGTLNVHTVFLKEKVPEEKVKPGPPKVPEKSVRLVVNYLRTQKAVVRVSPEVPLQNILPVICAKCEVSPEHVVLLRDNIAGEELELSKSLNELGIKELYAWDNRRETFRKSSLGNDETDKEKKKFLGFFKVNKRSNSKGCLTTPNSPSMHSRSLTLGPSLSLGSISGVSVKSEMKKRRAPPPPGSGPPVQDKASEKVSLGSQIDLQKKKRRAPAPPPPQPPPPSPLIPNRTEDKEENRKSTMVSLPLGSGSHCSPDGAPQVLSEAEETVSVGSCFASEDTTEDSGVMSSPSDIVSLDSQQDSMKYKDKWATDQEDCSDQDLAGTPDLGPQKSPLWEKNGSENSHLRTEKAVTASNDEEDLLIAGEFRKTLAELDEDLEEMEDSYETDTSSLTSSIHGASNHCPQDAMIPHGDTDAIPVTFIGEVSDDPVDSGLFSNRNNNAGSFDSEGVASRRDSLAPLQAEHSQPHEKAREEVPALHPASHDVGKGIRVALSNISKDGNLMETAPRVTSFASNLHTDNLNAKVKDKVYGCADGERTQATERVNSQPVNEKDSNDKNAALAPTSWHQRGQNPGKSYRLKHGLTTYKIIPPKSEMRCYDRDVSLSTGAIKIDELGNLVSPHATGIRIISLSSSVPEAESQPIGKVREFWRCNSVEKHLGRPSESSARGPPSTPVPTQTQNPESRLQADPKPISPQQKSAHHEGRNPLGEGRNQPPTMGMGHVRVPAAHTTEVTFLKPQRRTSSQYVASAIAKRIGAPKVHADVVRPHGYAEKGYAGKAPVLAAPPVTVKDDRTSSPHSETQGWKDGAQWPCVTPPNNHGEDLAVGAPPRGEVIGPHRKLSTQDRPAAIHRSSCFSLVQSSQRDRVSVGQSCGFSGKQSTSSQEASSASEPRRAPDGTDPPPPHTSDTQACSRELVNGSVRAPGHGEPSHPPGGSGTESHILLEREEKPSVFSTDGNETDSIWPPSIFGPKKKFKPVVQRPVPKDTSLHSALMEAIHSAGGKDRLRKTAEHTGEGRPAKLSYTEAEGERSALLAAIRGHSGTCSLRKVASSASEELQSFRDAALSAQGSESPLLEDLGLLSPPAIPPPPPPPSQALSAPRTASRFSTGTLSNTADARQALMDAIRSGTGAARLRKVPLLV
| null | null |
actin filament network formation [GO:0051639]; actin filament polymerization [GO:0030041]; collateral sprouting in absence of injury [GO:0048669]; digestive tract development [GO:0048565]; embryonic axis specification [GO:0000578]; floor plate development [GO:0033504]; liver development [GO:0001889]; neural tube closure [GO:0001843]; notochord development [GO:0030903]; positive regulation of dendrite development [GO:1900006]; positive regulation of ruffle assembly [GO:1900029]; somite specification [GO:0001757]
|
actin filament [GO:0005884]; axon [GO:0030424]; axonal growth cone [GO:0044295]; cell cortex [GO:0005938]; dendrite [GO:0030425]; dendritic growth cone [GO:0044294]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; terminal web [GO:1990357]
|
actin monomer binding [GO:0003785]
|
PF09469;PF02205;
| null | null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Recruited to the cell membrane via interaction with PACSIN1. Colocalizes with the actin cytoskeleton. Detected throughout the neuron cell body, as well as in axons and dendrites (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Plays an important role in the reorganization of the actin cytoskeleton. Regulates neuron morphogenesis and increases branching of axons and dendrites. Regulates dendrite branching in Purkinje cells (By similarity). Binds to and sequesters actin monomers (G actin). Nucleates actin polymerization by assembling three actin monomers in cross-filament orientation and thereby promotes growth of actin filaments at the barbed end. Can also mediate actin depolymerization at barbed ends and severing of actin filaments. Promotes formation of cell ruffles. {ECO:0000250, ECO:0000269|PubMed:21816349}.
|
Homo sapiens (Human)
|
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