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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O41933
|
MIR1_MHV68
|
MDSTGEFCWICHQPEGPLKRFCGCKGSCAVSHQDCLRGWLETSRRQTCALCGTPYSMKWKTKPLREWTWGEEEVLAAMEACLPLVLIPLAVLMIVMGTWLLVNHNGFLSPRMQVVLVVIVLLAMIVFSASASYVMVEGPGCLDTCTAKNSTVTVNSIDEAIATQQPTKTDLGLARETLSTRFRRGKCRSCCRLGCVRLCCV
|
2.3.2.36
| null |
protein ubiquitination [GO:0016567]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell endoplasmic reticulum membrane [GO:0044167]; membrane [GO:0016020]
|
ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]
|
PF12906;
|
3.30.40.10;
| null | null |
SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:11672544}; Multi-pass membrane protein {ECO:0000269|PubMed:11672544}.
|
CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine.; EC=2.3.2.36; Evidence={ECO:0000250|UniProtKB:P90495};
| null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of host surface class I (MHC-I) H-2D(b)/H2-D1 and H-2K(b)/H2-K1 molecules before they exit the endoplasmic reticulum, leading to their degradation by the endoplasmic reticulum-associated degradation (ERAD) system, thus blocking the immune detection of virus-infected cells. Mediates ubiquitination of lysine, as well as serine and threonine residues present in the cytoplasmic tail of surface class I molecules. Promotes ubiquitination of hydroxylated serine or threonine residues via ester bonds instead of the classical isopeptide linkage. {ECO:0000269|PubMed:10890918, ECO:0000269|PubMed:11672544, ECO:0000269|PubMed:17502423, ECO:0000269|PubMed:19531064, ECO:0000269|PubMed:19951915}.
|
Murid herpesvirus 4 (MuHV-4) (Murine gammaherpesvirus 68)
|
O42043
|
ENK18_HUMAN
|
MVTPVTWMDNPIEVYVNDSVWVPGPTDDRCPAKPEEEGMMINISIGYHYPPICLGRAPGCLMPAVQNWLVEVPTVSPNSRFTYHMVSGMSLRPRVNCLQDFSYQRSLKFRPKGKTCPKEIPKGSKNTEVLVWEECVANSVVILQNNEFGTIIDWAPRGQFYHNCSGQTQSCPSAQVSPAVDSDLTESLDKHKHKKLQSFYLWEWEEKGISTPRPKIISPVSGPEHPELWRLTVASHHIRIWSGNQTLETRYRKPFYTIDLNSILTVPLQSCVKPPYMLVVGNIVIKPASQTITCENCRLFTCIDSTFNWQHRILLVRAREGMWIPVSTDRPWEASPSIHILTEILKGVLNRSKRFIFTLIAVIMGLIAVTATAAVAGVALHSSVQSVNFVNYWQKNSTRLWNSQSSIDQKLASQINDLRQTVIWMGDRLMTLEHHFQLQCDWNTSDFCITPQIYNESEHHWDMVRRHLQGREDNLTLDISKLKEQIFEASKAHLNLVPGTEAIAGVADGLANLNPVTWIKTIRSTMIINLILIVVCLFCLLLVCRCTQQLRRDSDIENGP
| null | null | null |
plasma membrane [GO:0005886]
|
structural molecule activity [GO:0005198]
|
PF00517;PF13804;
| null |
Beta type-B retroviral envelope protein family, HERV class-II K(HML-2) env subfamily
|
PTM: Specific enzymatic cleavages in vivo yield the mature SU and TM proteins. {ECO:0000250}.
|
SUBCELLULAR LOCATION: [Transmembrane protein]: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Surface protein]: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=The surface protein is not anchored to the membrane, but localizes to the extracellular surface through its binding to TM. {ECO:0000250}.; SUBCELLULAR LOCATION: [Endogenous retrovirus group K member 18 Env polyprotein]: Virion {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This envelope protein has superantigenic properties.; FUNCTION: SU mediates receptor recognition. {ECO:0000250}.; FUNCTION: TM anchors the envelope heterodimer to the viral membrane through one transmembrane domain. The other hydrophobic domain, called fusion peptide, mediates fusion of the viral membrane with the target cell membrane (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O42123
|
FKB1A_XENLA
|
MGVQVETITEGDGRTFPKKGQTVVVHYVGSLENGKKFDSSRDRNKPFKFIIGRCEVIRGWEEGVAQMSVGQRARLTCSPDFAYGATGHPGIIPPNATLTFDVELLRLE
|
5.2.1.8
| null |
amyloid fibril formation [GO:1990000]; cytokine-mediated signaling pathway [GO:0019221]; heart morphogenesis [GO:0003007]; heart trabecula formation [GO:0060347]; muscle contraction [GO:0006936]; negative regulation of phosphoprotein phosphatase activity [GO:0032515]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of release of sequestered calcium ion into cytosol [GO:0051280]; negative regulation of ryanodine-sensitive calcium-release channel activity [GO:0060315]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of protein binding [GO:0032092]; positive regulation of protein ubiquitination [GO:0031398]; protein peptidyl-prolyl isomerization [GO:0000413]; regulation of activin receptor signaling pathway [GO:0032925]; regulation of amyloid precursor protein catabolic process [GO:1902991]; regulation of immune response [GO:0050776]; regulation of protein localization [GO:0032880]; regulation of ryanodine-sensitive calcium-release channel activity [GO:0060314]; release of sequestered calcium ion into cytosol [GO:0051209]; supramolecular fiber organization [GO:0097435]; T cell proliferation [GO:0042098]; ventricular cardiac muscle tissue morphogenesis [GO:0055010]
|
cytoplasm [GO:0005737]; cytoplasmic side of membrane [GO:0098562]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; ryanodine receptor complex [GO:1990425]; sarcoplasmic reticulum membrane [GO:0033017]; terminal cisterna [GO:0014802]; Z disc [GO:0030018]
|
activin binding [GO:0048185]; calcium channel inhibitor activity [GO:0019855]; FK506 binding [GO:0005528]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; protein homodimerization activity [GO:0042803]; SMAD binding [GO:0046332]; transmembrane transporter binding [GO:0044325]
|
PF00254;
|
3.10.50.40;
|
FKBP-type PPIase family, FKBP1 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8;
| null | null | null | null |
FUNCTION: Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
|
Xenopus laevis (African clawed frog)
|
O42127
|
FGFR3_XENLA
|
MVSVNGVPAARLPVTLPGEDRASRKAPDYLMVEQPPFDELMYTIGETIELSCAAEDASTTTKWCKDGIGIVPNNRTSTRQGLLKIINVSSDDSGIYSCRLWHSTEILRNFTIRVTDLPSSGDDEDDDDDDDDETEDREPPRWTQPERMEKKLIAVPAANTIRFRCPAAGNPTPTIHWLKNGKEFRGEHRIGGIKLRHQQWSLVMESVVPSDKGNYTCVVENKYGSIRQTYQLDVLERSSHRPILQAGLPGNQTVVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKYGPDGDPYVSVLQSFINGTEVDSTLSLKNVTETNEGQYVCRANNFIGVAEASFWLHIYKPAPAEPVEKALTTSSSSITVLIVVTSTIVFILLVIIVITHLMKVPSKKSMTAPPVHKVSKFPLKRQQVSLESNSSMNSNTPLVRITHLSSSDGTMLANVSELGLPLDPKWELLRSRLTLGKPLGEGCFGQVVMAEAIGIDKERPNKPATVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVLVEYASKGSLREYLKARRPPGMDYSFDACKIPAEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTDDNVMKIADFGLARDIHNIDYYKKTTNGRLPVKWMAPEALFDRIYTHHSDVWSYGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTHELYMIMRECWHAVPSQRPAFKQLVEDLDRVLTVTSTNEYLDLSVAFEQYSPPSQDSHSTCSSGDDSVFAHDILPDEPCLPKHQQHNGAIPT
|
2.7.10.1
| null |
apoptotic process [GO:0006915]; phosphorylation [GO:0016310]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of MAPK cascade [GO:0043410]
|
plasma membrane [GO:0005886]; receptor complex [GO:0043235]
|
ATP binding [GO:0005524]; fibroblast growth factor binding [GO:0017134]; fibroblast growth factor receptor activity [GO:0005007]
|
PF07679;PF13927;PF07714;
|
2.60.40.10;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, Fibroblast growth factor receptor subfamily
|
PTM: Autophosphorylated. Binding of FGF family members together with heparan sulfate proteoglycan or heparin promotes receptor dimerization and autophosphorylation on tyrosine residues. Autophosphorylation occurs in trans between the two FGFR molecules present in the dimer (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
| null | null | null | null |
FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation and apoptosis. Plays an essential role in the regulation of chondrocyte differentiation, proliferation and apoptosis, and is required for normal skeleton development. Regulates both osteogenesis and postnatal bone mineralization by osteoblasts. Promotes apoptosis in chondrocytes, but can also promote cancer cell proliferation. Phosphorylates PLCG1, CBL and FRS2. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway (By similarity). {ECO:0000250}.
|
Xenopus laevis (African clawed frog)
|
O42130
|
TOP2A_CHICK
|
MELLDSPAPLRPLHDNPRLPKADGAQKRLSVERIYQKKTQLEHILLRPDTYIGSVETVTQQMWVFDEDVGLNCRDVTFVPGLYKIFDEILVNAADNKQRDKSMSCIKVTIDPENNTISVWNNGKGIPVVEHKVEKVYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETACREYKKLFKQTWTDNMGKAGEMTLKHFDGEDYTCVTFQPDLSKFKMTILDKDIVALMSRRAYDIAGSTKDVKVFLNGKRLPVKGFRSYVDLYLKDKVDETGNALKVIHEEVNSRWEVCLTLSEKGFQQVSFVNSIATTKGGRHVDYVADQIVTKLIDVVKKKNKNGVGVKPFQVKNHMWIFVNSLIENPTFDSQTKENMTLQAKSFGSTCKLSEKFIKGAVGCGIVESILNWVKFKAQTQLNKKCSAVKHTKIKGVPKLDDANDAGSKNSIDCTLILTEGDSAKTLAVSGLGVVGRDKYGVFPLRGKMLNVREASHKQIMENAEINNIIKIVGLQYKKNYEDRESLKSLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLRHNFLEEFITPIIKVSKNKEEIPFYSIPEFEEWKSSTQNYNSWKIKYYKGLGTSTSKEAKEYFADMARHRIGFKYSGPEDDAAITLAFSKKKVEERKEWLTNFMEDRRQRNVHGLPEDYLYGKDTNYLTYNDFINKELVLFSNSDNERSIPSLVDGLKPGQRKVLFTCFKRNDKREVKGAQLAGSVAEMSSYHHGEASLMMTIINLAQNFVGSNNLNLLQPIGQFGTRLHGGKDSASPRYIFTMLSPLARLLFPPVDDNVLRFLYDDNQRVEPEWYMPIIPMVLINGAEGIGTGWSCKIPNFDIRETVNNIRCLLDGKEPLPMLPSYKNFKGTIDELGPNQYVISGEVSILDSTTIEITELPVRTWTQTYKEQVLEPMLNGTEKTPPLITDYKEYHTDTTVKFVVKMSEEKLAEAEAVGLHKVFKLQTNLTCNSMVLFDHVGFLKKYESPQDILKEFFELRLRYYGLRKEWLIGMLGAESAKLNNQARFILEKIDGKIVIENKPKKELIQVLIQRGYESDPVKAWKELQNKEEEEGDESGEESAAATGPDFNYLLNMPLWYLTKEKKDELCKQRDNKDKELEDLKHKSPSDLWKEDLAAFVEELDAVEAKQMQDEMAGITGKPLKVKGGKQGGKQKVTKAQLAEVMPSPHGIRVVPRVTAEMKAEAEKRIKKKIKSEKNESDEKQEGNSSGDKEPSSLKQRLAQKRKAEQGTKRQTTLPFKPIKKMKRNPWSDSESDSESDDFEVPSKRERVVRQAAAKIKPMVNSDSDADLTSSDEDSEYQENSEGNTDSDTTSKKKPPKAKAVPKEKKGKAPKEKPLPDAVPVRVQNVAAESASQDPAAPPVSVPRAQAVPKKPAAAKKGSTAKDNQPSIMDILTKKKAAPKAPRRAQREESPPSEATAAVAKKPGPPRGRKATKRLTSSSDSDSDFGSRPSKSVAAKKSKRDDDDSYSIDLTADSPAAAAPRTRPGRLKKPVQYLESSDEDDMF
|
5.6.2.2
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995}; Note=Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+). {ECO:0000255|PROSITE-ProRule:PRU00995};
|
apoptotic chromosome condensation [GO:0030263]; cell division [GO:0051301]; chromosome segregation [GO:0007059]; DNA damage response [GO:0006974]; DNA ligation [GO:0006266]; DNA replication [GO:0006260]; DNA topological change [GO:0006265]; negative regulation of DNA duplex unwinding [GO:1905463]; positive regulation of apoptotic process [GO:0043065]; resolution of meiotic recombination intermediates [GO:0000712]; rhythmic process [GO:0048511]; sister chromatid segregation [GO:0000819]
|
chromosome [GO:0005694]; condensed chromosome [GO:0000793]; cytoplasm [GO:0005737]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex [GO:0009330]; heterochromatin [GO:0000792]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]
|
ATP binding [GO:0005524]; ATP-dependent activity, acting on DNA [GO:0008094]; cyclin binding [GO:0030332]; DNA binding [GO:0003677]; DNA binding, bending [GO:0008301]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity [GO:0003918]; magnesium ion binding [GO:0000287]
|
PF00204;PF00521;PF08070;PF02518;PF01751;PF16898;
|
3.30.1360.40;3.30.1490.30;3.30.230.10;3.40.50.670;3.30.565.10;3.90.199.10;1.10.268.10;
|
Type II topoisomerase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11388}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P11388}. Nucleus {ECO:0000250|UniProtKB:P11388}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P11388}.
|
CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
| null | null | null | null |
FUNCTION: Key decatenating enzyme that alters DNA topology by binding to two double-stranded DNA molecules, generating a double-stranded break in one of the strands, passing the intact strand through the broken strand, and religating the broken strand (By similarity). May play a role in the regulation of circadian rhythm (By similarity). {ECO:0000250|UniProtKB:P11388, ECO:0000250|UniProtKB:Q01320}.
|
Gallus gallus (Chicken)
|
O42131
|
TOP2B_CHICK
|
MAKSGGGGGGGGGGGGGGGGSGGLTCVTLFDNQINASKKEESESVNKNDTSKKMSVERVYQKKTQLEHILLRPDTYIGSVEPLTQLMWVYDEDVGMNCREVTFVPGLYKIFDEILVNAADNKQRDKNMTCIKISIDPESNIISIWNNGKGIPVVEHKVEKVYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETACKEYKHSFKQTWMNNMMKTSEPKIKHFEGDDYTCITFQPDLSKFKMENLDKDIVSLMTRRAYDLAGSCKGVKVMLNGKKLPVNGFRSYVDLYVKDKLDETGVALKVIHEVVNERWDVCLTLSEKGFQQISFVNSIATTKGGRHVDYVVDQVVGKLIEVVKKKNKAGVSVKPFQVKNHIWVFVNCLIENPSFDSQTKENMTLQPKSFGSKCQLSEKFFKAASNCGIIESILNWVKFKAQTQLNKKCSSVKHSKIKGIPKLDDANDAGGKHSLDCTLILTEGDSAKSLAVSGLGVIGRDRYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKSYEDPESLKSLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLKHGFLEEFITPIVKASKNKQELSFYSIPEFDEWKKHMENHKAWKIKYYKGLGTSTAKEAKEYFADMERHRILFRYAGPEDDAAITLAFSKKKIDDRKEWLTNFMEDRRQRRLHGLPEQFLYGTATKHLTYNDFINKELILFSNSDNERSIPSLVDGLKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSAYHHGEQALMMTIVNLAQNFVGSNNVNLLQPIGQFGTRLHGGKDAASPRYIFTMLSPLARLLFPSVDDNLLKFLYDDNQRVEPEWYIPIIPMVLVNGAEGIGTGWACKLPNYDTREIVNNVRRMLDGLDPHPMLPNYKNFRGTIQELGQNQYVVSGEIFVVDRNTVEITELPVRTWTQVYKEQVLEPMLNGTEKTPALISDYKEYHTDTTVKFVVKMTEEKLAQAEAAGLHKVFKLQTSLTCNSMVLFDHMGCLKKYETVQDILKEFFDLRLHYYSLRKEWLVGMLGAESTKLNNQARFILEKIQGKITIENRSKRDLIQMLVQRGYESDPVKAWKEAQEKAAEEEDPQNANDDASSASGSTSGPDFNYILNMSLWSLTKEKVEELIKHRDSKERELNDLKRKSASDLWKEDLAAFVEELEKVEAQEREDVLAGMVGKPIKGKVGKPKMKKLQLEETMPSPFGRRIVPQITSAMKADASRKLLKKKKGDADSVAIKMEFDEEFGGVQAEGGGDDTVNTAASGTKTPKLKREKKEPGTRVRRAPSSTKSSAKKVKKRNPWSDDESKSESDLEESEPVIIPRDSLLRRAAADRAKYTFDFSKEEDDAHDDDDANNNNDLDELKVKASPVINDREDEFVPSDSVEKDEYDFSPVKSKPSPEKMSQEKKNQDFGNIFSFPSYSQKTDDDTTKLDSDEEDSTPVFSSPFAPKQTEKMLSKTVAAKKAKVDVPPKPKRAPKAKKMETVNSDSDSEFGIPKKTAAPKGKGRGAKKRKTSGSENEGEYNPGKKAPKSTPCKKSKKAAFDQDSDVEIFQSGFASETAPKPRTGRARKEVKYFAESDEDDDFDMFN
|
5.6.2.2
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995}; Note=Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+). {ECO:0000255|PROSITE-ProRule:PRU00995};
|
B cell differentiation [GO:0030183]; DNA topological change [GO:0006265]; resolution of meiotic recombination intermediates [GO:0000712]; sister chromatid segregation [GO:0000819]
|
nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]
|
ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA topoisomerase activity [GO:0003916]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity [GO:0003918]; metal ion binding [GO:0046872]
|
PF00204;PF00521;PF08070;PF02518;PF01751;PF16898;
|
3.30.1360.40;3.30.1490.30;3.30.230.10;3.40.50.670;3.30.565.10;3.90.199.10;1.10.268.10;
|
Type II topoisomerase family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q02880}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q02880}. Nucleus {ECO:0000269|PubMed:11453553}.
|
CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
| null | null | null | null |
FUNCTION: Key decatenating enzyme that alters DNA topology by binding to two double-stranded DNA molecules, generating a double-stranded break in one of the strands, passing the intact strand through the broken strand, and religating the broken strand. Plays a role in B-cell differentiation. {ECO:0000250|UniProtKB:Q64511}.
|
Gallus gallus (Chicken)
|
O42145
|
C19AA_DANRE
|
MAGDLLQPCGMKPVRLGEAVVDLLIQRAHNGTERAQDNACGATATILLLLLCLLLAIRHHRPHKSHIPGPSFFFGLGPVVSYCRFIWSGIGTASNYYNSKYGDIVRVWINGEETLILSRSSAVYHVLRKSLYTSRFGSKLGLQCIGMHEQGIIFNSNVALWKKVRAFYAKALTGPGLQRTMEICTTSTNSHLDDLSQLTDAQGQLDILNLLRCIVVDVSNRLFLGVPLNEHDLLQKIHKYFDTWQTVLIKPDVYFRLDWLHRKHKRDAQELQDAITALIEQKKVQLAHAEKLDHLDFTAELIFAQSHGELSAENVRQCVLEMVIAAPDTLSISLFFMLLLLKQNPDVELKILQEMDSVLAGQSLQHSHLSKLQILESFINESLRFHPVVDFTMRRALDDDVIEGYNVKKGTNIILNVGRMHRSEFFSKPNQFSLDNFHKNVPSRFFQPFGSGPRSCVGKHIAMVMMKSILVALLSRFSVCPMKACTVENIPQTNNLSQQPVEEPSSLSV
|
1.14.14.14
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
|
female germ-line sex determination [GO:0019099]; female gonad development [GO:0008585]; female sex determination [GO:0030237]; female sex differentiation [GO:0046660]; male germ-line sex determination [GO:0019100]; ovarian follicle development [GO:0001541]; regulation of estrogen biosynthetic process [GO:1904076]; response to estradiol [GO:0032355]; response to xenobiotic stimulus [GO:0009410]
|
endoplasmic reticulum [GO:0005783]; membrane [GO:0016020]
|
aromatase activity [GO:0070330]; heme binding [GO:0020037]; iron ion binding [GO:0005506]
|
PF00067;
|
1.10.630.10;
|
Cytochrome P450 family
| null |
SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
|
CATALYTIC ACTIVITY: Reaction=3 O2 + 3 reduced [NADPH--hemoprotein reductase] + testosterone = 17beta-estradiol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:38191, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:16469, ChEBI:CHEBI:17347, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.14; Evidence={ECO:0000250|UniProtKB:P11511}; CATALYTIC ACTIVITY: Reaction=androst-4-ene-3,17-dione + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = estrone + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:38195, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:16422, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.14; Evidence={ECO:0000250|UniProtKB:P11511};
| null | null | null | null |
FUNCTION: Catalyzes the formation of aromatic C18 estrogens from C19 androgens. {ECO:0000250}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O42164
|
LEP_CHICK
|
MCWRPLCRLWSYLVYVQAVPCQIFQDDTKTLIKTIVTRINDISHTSVSAKQRVTGLDFIPGLHPILSLSKMDQTLAVYQQVLTSLPSQNVLQIANDLENLRDLLHLLAFSKSCSLPQTSGLQKPESLDGVLEASLYSTEVVALSRLQGSLQDILQQLDISPEC
| null | null |
cellular response to leptin stimulus [GO:0044320]; energy reserve metabolic process [GO:0006112]; lipid metabolic process [GO:0006629]; negative regulation of apoptotic process [GO:0043066]; negative regulation of appetite [GO:0032099]; negative regulation of appetite by leptin-mediated signaling pathway [GO:0038108]; negative regulation of gene expression [GO:0010629]; ovarian follicle atresia [GO:0001552]; phagocytosis [GO:0006909]; positive regulation of estradiol secretion [GO:2000866]; positive regulation of female gonad development [GO:2000196]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of luteinizing hormone secretion [GO:0033686]; positive regulation of p38MAPK cascade [GO:1900745]; positive regulation of progesterone secretion [GO:2000872]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; positive regulation of TOR signaling [GO:0032008]; positive regulation of tumor necrosis factor production [GO:0032760]; response to insulin [GO:0032868]
|
extracellular space [GO:0005615]
|
hormone activity [GO:0005179]; peptide hormone receptor binding [GO:0051428]
|
PF02024;
|
1.20.1250.10;
|
Leptin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Key player in the regulation of energy balance and body weight control. Once released into the circulation, has central and peripheral effects by binding LEPR, found in many tissues, which results in the activation of several major signaling pathways. {ECO:0000250|UniProtKB:P41159}.
|
Gallus gallus (Chicken)
|
O42173
|
PV1_XENLA
|
MVQQGFSIDLILARSREEAADGKDSMSSRPHIPCAPQPLPPNKYAKEMPRRKDGQDVQEHSSWSLGEQGKKLQYSSPSSAALHRSWGSSDDFSSVGSEDDSTEGSPSPMRNSQETETDHRGESPKSDLQRHLRTAFTPQQISKLEQAFNKQRYLGASERKKLATSLRLSEIQVKTWFQNRRMKLKRQIQDQQHNMVPPPVCYPQTFPYYPGVLPVPLNSGSFYQPPAHPFQAPQNSYIPDPRFIPQPLPHHIRMSVALQQQYPPLGLPPGRYFTGLASKNDG
| null | null |
BMP signaling pathway [GO:0030509]; cell differentiation [GO:0030154]; determination of ventral identity [GO:0048264]; mesoderm formation [GO:0001707]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of erythrocyte differentiation [GO:0045647]; negative regulation of neurogenesis [GO:0050768]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of epidermal cell differentiation [GO:0045606]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]
|
PF00046;
|
1.10.10.60;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Transcriptional repressor. Acts in a ventral signaling pathway downstream of bmp4, which suppresses dorsal mesoderm formation and leads to both ventral mesoderm and ventral ectoderm formation. Acts in the ectoderm to simultaneously specify epidermal lineages and restrict neuralization. Represses transcription of dorsal-specific genes. Binds to DNA, with preference for the target sequences 5'-TAATGC-3' and 5'-TAATTG-3'. Acts in a pathway downstream of bmp4 and fgf to negatively regulate erythroid specification. {ECO:0000269|PubMed:10191050, ECO:0000269|PubMed:10926781, ECO:0000269|PubMed:11944926, ECO:0000269|PubMed:12890483, ECO:0000269|PubMed:8692829, ECO:0000269|PubMed:9405105}.
|
Xenopus laevis (African clawed frog)
|
O42182
|
FBLN1_DANRE
|
MDLYMIVLLSLCGLLRAQETTDTISLDNCCEDGKKRGLESQDCSSLPLISESTTCRVVQEQCCSAVLEDSICTSGINMAKDQSSCDALLSGSSTCETKTTKMCCECCLLGSSRCRIRVSPVSSVCRWSISRGPGVRSCCVDKQPAHGVQPSKGDAQNTEDQCRAAGCAQRCLNGTCSCLDGFKLKTDGKHCEDINECLLGPHHCVTGERCINTLGSYRCQREISCGTGYELTDNNKCKDIDECDLGTHNCAAEMECQNTAGSFRCRPRMQCAAGFIQDALGSCIDINECVSVTALSRGQMCFNTVGSFICQRHSVTCGRGYHLNAEGTRCVDIDECAGPDNSCDGHGCINLVGSYRCECRTGFIFNSISRSCEDIDECRNYPGRLCAHKCENILGSYKCSCTAGFKLADDGRNCDDVNECESSPCSQGCANVYGSYQSYCRRGYQLSDADGITCEDIDECALPTGGHICSYRCHNTPGSFHCTCPASGYTLAANGRSCQDIDECLTGTHSCSESESCFNIQGGFRCLSFDCPANYRRSGDTRPRVDRADIIRCVKSCQHNDISCVLNPILSHSHTAISLPTFREFNKPEEIVFLRSPTPTHLPHMDSPEIVYDILEGNIQNSFDIIKRLDHGMIVGVVKQVRPLVGPVRTVLKLAMNYVTNGVVSHRNIINVRIYVSEFWF
| null | null |
embryonic medial fin morphogenesis [GO:0035122]; extracellular matrix organization [GO:0030198]; mesenchymal cell migration [GO:0090497]; skin morphogenesis [GO:0043589]
|
extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; peptidase activator activity [GO:0016504]
|
PF01821;PF12662;PF07645;
|
2.10.25.10;
|
Fibulin family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix.
| null | null | null | null | null |
FUNCTION: Incorporated into fibronectin-containing matrix fibers. May play a role in cell adhesion and migration along protein fibers within the extracellular matrix (ECM). Could be important for certain developmental processes and contribute to the supramolecular organization of ECM architecture, in particular to those of basement membranes.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O42187
|
PA2BB_GLOHA
|
MRALWIVAVLLLGVEGSLLQFRKMIKKMTGKEPVVSYAFYGCYCGSGGRGKPKDATDRCCFVHDCCYEKLTGCDPKWDDYTYSWKNGTIVCGGDDPCKKEVCECDKAAAICFRDNLKTYKKRYMTYPNILCSSKSEKC
|
3.1.1.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305|PubMed:9761847}; Note=Binds 1 Ca(2+) ion. {ECO:0000305|PubMed:9761847};
|
arachidonic acid secretion [GO:0050482]; fatty acid biosynthetic process [GO:0006633]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]; positive regulation of fibroblast proliferation [GO:0048146]
|
extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102]; toxin activity [GO:0090729]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family, Group II subfamily, D49 sub-subfamily
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036};
| null | null | null | null |
FUNCTION: Snake venom phospholipase A2 (PLA2) that shows potent hemolytic activity, and exhibits medium anticoagulant effects by binding to factor Xa (F10) and inhibiting the prothrombinase activity (IC(50) is 90 nM). It is one of the few phospholipases A2 capable of hydrolyzing the phospholipids of E.coli membranes in the presence of a bactericidal/permeability-increasing protein (BPI) of neutrophils. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:10728829, ECO:0000269|PubMed:18062812}.
|
Gloydius halys (Chinese water mocassin) (Agkistrodon halys)
|
O42202
|
NDF1_DANRE
|
MTKSYSEESMMLESQSSSNWTDKCHSSSQDERDVDKTSEPMLNDMEDDDDAGLNRLEDEDDEEEEEEEEDGDDTKPKRRGPKKKKMTKARMQRFKMRRMKANARERNRMHGLNDALESLRKVVPCYSKTQKLSKIETLRLAKNYIWALSEILRSGKSPDLMSFVQALCKGLSQPTTNLVAGCLQLNPRTFLPEQSQEMPPHMQTASASFSALPYSYQTPGLPSPPYGTMDSSHIFHVKPHAYGSALEPFFDTTLTDCTSPSFDGPLSPPLSVNGNFSFKHEPSSEFEKNYAFTMHYQAAGLAGAQGHAASLYAGSTQRCDIPMENIMSYDGHSHHERVMNAQLNAIFHDS
| null | null |
axon development [GO:0061564]; camera-type eye photoreceptor cell development [GO:0062139]; endocrine pancreas development [GO:0031018]; inner ear receptor cell development [GO:0060119]; negative regulation of Notch signaling pathway [GO:0045746]; positive regulation of transcription by RNA polymerase II [GO:0045944]; posterior lateral line neuromast hair cell differentiation [GO:0048923]; regeneration [GO:0031099]; sensory organ development [GO:0007423]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; E-box binding [GO:0070888]; protein dimerization activity [GO:0046983]
|
PF00010;PF12533;
|
4.10.280.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q64289}. Nucleus {ECO:0000250|UniProtKB:Q64289, ECO:0000255|PROSITE-ProRule:PRU00981}.
| null | null | null | null | null |
FUNCTION: May act as a transcriptional activator. Differentiation factor required for neurogenesis. Acts as an upstream activator of isl1. {ECO:0000269|PubMed:12044886}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O42220
|
GDF8_CHICK
|
MQKLAVYVYIYLFMQIAVDPVALDGSSQPTENAEKDGLCNACTWRQNTKSSRIEAIKIQILSKLRLEQAPNISRDVIKQLLPKAPPLQELIDQYDVQRDDSSDGSLEDDDYHATTETIITMPTESDFLVQMEGKPKCCFFKFSSKIQYNKVVKAQLWIYLRQVQKPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMNPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKAFDETGRDLAVTFPGPGEDGLNPFLEVRVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS
| null | null |
cellular response to dexamethasone stimulus [GO:0071549]; embryo development ending in birth or egg hatching [GO:0009792]; muscle cell cellular homeostasis [GO:0046716]; muscle cell proliferation [GO:0033002]; myoblast migration involved in skeletal muscle regeneration [GO:0014839]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of myoblast differentiation [GO:0045662]; negative regulation of myoblast proliferation [GO:2000818]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; negative regulation of satellite cell differentiation [GO:1902725]; negative regulation of skeletal muscle satellite cell proliferation [GO:1902723]; negative regulation of skeletal muscle tissue growth [GO:0048632]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of lamellipodium assembly [GO:0010592]; positive regulation of macrophage chemotaxis [GO:0010759]; regulation of cell differentiation [GO:0045595]; regulation of growth [GO:0040008]; skeletal muscle satellite cell differentiation [GO:0014816]; skeletal muscle tissue development [GO:0007519]; transforming growth factor beta receptor signaling pathway [GO:0007179]
|
extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; protein homodimerization activity [GO:0042803]
|
PF00019;PF00688;
|
2.60.120.970;2.10.90.10;
|
TGF-beta family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Acts specifically as a negative regulator of skeletal muscle growth.
|
Gallus gallus (Chicken)
|
O42221
|
GDF8_MELGA
|
MQKLAVYVYIYLFMQILVHPVALDGSSQPTENAEKDGLCNACTWRQNTKSSRIEAIKIQILSKLRLEQAPNISRDVIKQLLPKAPPLQELIDQYDVQRDDSSDGSLEDDDYHATTETIITMPTESDFLVQMEGKPKCCFFKFSSKIQYNKVVKAQLWIYLRQVQKPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMNPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKAFDENGRDLAVTFPGPGEDGLNPFLEVRVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS
| null | null |
cellular response to dexamethasone stimulus [GO:0071549]; muscle cell cellular homeostasis [GO:0046716]; muscle cell proliferation [GO:0033002]; myoblast migration involved in skeletal muscle regeneration [GO:0014839]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of myoblast differentiation [GO:0045662]; negative regulation of myoblast proliferation [GO:2000818]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; negative regulation of satellite cell differentiation [GO:1902725]; negative regulation of skeletal muscle satellite cell proliferation [GO:1902723]; negative regulation of skeletal muscle tissue growth [GO:0048632]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of lamellipodium assembly [GO:0010592]; positive regulation of macrophage chemotaxis [GO:0010759]; skeletal muscle satellite cell differentiation [GO:0014816]; transforming growth factor beta receptor signaling pathway [GO:0007179]
|
extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; protein homodimerization activity [GO:0042803]
|
PF00019;PF00688;
|
2.60.120.970;2.10.90.10;
|
TGF-beta family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Acts specifically as a negative regulator of skeletal muscle growth.
|
Meleagris gallopavo (Wild turkey)
|
O42222
|
GDF8_DANRE
|
MHFTQVLISLSVLIACGPVGYGDITAHQQPSTATEESEQCSTCEFRQHSKLMRLHAIKSQILSKLRLKQAPNISRDVVKQLLPKAPPLQQLLDQYDVLGDDSKDGAVEEDDEHATTETIMTMATEPDPIVQVDRKPKCCFFSFSPKIQANRIVRAQLWVHLRPAEEATTVFLQISRLMPVKDGGRHRIRSLKIDVNAGVTSWQSIDVKQVLTVWLKQPETNRGIEINAYDAKGNDLAVTSTETGEDGLLPFMEVKISEGPKRIRRDSGLDCDENSSESRCCRYPLTVDFEDFGWDWIIAPKRYKANYCSGECDYMYLQKYPHTHLVNKASPRGTAGPCCTPTKMSPINMLYFNGKEQIIYGKIPSMVVDRCGCS
| null | null |
cardiac muscle myoblast proliferation [GO:0110021]; immune response [GO:0006955]; muscle organ development [GO:0007517]; negative regulation of cardiac muscle myoblast proliferation [GO:0110023]; negative regulation of growth [GO:0045926]; negative regulation of growth rate [GO:0045967]; negative regulation of skeletal muscle tissue development [GO:0048642]; negative regulation of striated muscle tissue development [GO:0045843]; regulation of muscle hyperplasia [GO:0014738]; skeletal muscle tissue development [GO:0007519]; transforming growth factor beta receptor signaling pathway [GO:0007179]; ventricular trabecula myocardium morphogenesis [GO:0003222]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; growth factor activity [GO:0008083]
|
PF00019;PF00688;
|
2.60.120.970;2.10.90.10;
|
TGF-beta family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Acts specifically as a negative regulator of skeletal muscle growth. May down-regulate muscle-specific transcription factors such as myod and myog. {ECO:0000269|PubMed:14555747, ECO:0000269|PubMed:15042708, ECO:0000269|PubMed:16005092}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O42226
|
I4A3B_XENLA
|
MAAAAVAGVAGLTTAHAKRLLREEDMTTVEFQTSEEVDVTPTFDTMGLREDLLRGIYAYGFEKPSAIQQKAIKQIIKGRDVIAQSQSGTGKTATFCVSVLQCLDIQIRETQALILAPTKELARQIQKVLLALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQVCLISATLPHEILEMTNKFMTDPIRILVKRDELTLEGIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLPNNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQIDEMPMNVADLI
|
3.6.4.13
| null |
mRNA processing [GO:0006397]; mRNA transport [GO:0051028]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of translation [GO:0006417]; RNA splicing [GO:0008380]
|
catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; mRNA binding [GO:0003729]; RNA helicase activity [GO:0003724]
|
PF00270;PF00271;
|
3.40.50.300;
|
DEAD box helicase family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3B8Q2}. Nucleus speckle {ECO:0000250|UniProtKB:P38919}. Cytoplasm {ECO:0000250|UniProtKB:Q3B8Q2}. Note=Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. {ECO:0000250|UniProtKB:Q3B8Q2}.
|
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; Evidence={ECO:0000250|UniProtKB:P38919};
| null | null | null | null |
FUNCTION: ATP-dependent RNA helicase. Involved in pre-mRNA splicing as component of the spliceosome. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions (By similarity). Involved in craniofacial development (By similarity). When overexpressed, induces epidermis in dissociated cells that would otherwise adopt a neural fate, a process that requires an active BMP signaling pathway (PubMed:9334272). {ECO:0000250|UniProtKB:P38919, ECO:0000269|PubMed:9334272}.
|
Xenopus laevis (African clawed frog)
|
O42227
|
HDA1B_XENLA
|
MALSQGTKKKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKASAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDISVNWSGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVVYIDIDIHHGDGVEEAFYTTDRVMSVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMTKVMEMFQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEFIKTFNLPMLMLGGGGYTIRNVARCWTYETAVALDSEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDSVHDDSGEEDEEDPDKRISIRSSDKRIACDEEFSDSEDEGEGGRKNVANFKKVKRVKTEEEKEGEDKKDVKEEEKAKDEKTDSKRVKEETKSV
|
3.5.1.-; 3.5.1.98
| null |
negative regulation of transcription by RNA polymerase II [GO:0000122]
|
cytoplasm [GO:0005737]; NuRD complex [GO:0016581]
|
histone deacetylase activity [GO:0004407]; histone decrotonylase activity [GO:0160009]; protein lysine deacetylase activity [GO:0033558]
|
PF00850;
|
3.40.800.20;
|
Histone deacetylase family, HD type 1 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10454532}. Cytoplasm {ECO:0000269|PubMed:10454532}.
|
CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; EC=3.5.1.98; Evidence={ECO:0000269|PubMed:10454532}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197; Evidence={ECO:0000269|PubMed:10454532}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] = acetate + L-lysyl-[protein]; Xref=Rhea:RHEA:58108, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; Evidence={ECO:0000250|UniProtKB:Q13547}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58109; Evidence={ECO:0000250|UniProtKB:Q13547}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(2E)-butenoyl-L-lysyl-[protein] = (2E)-2-butenoate + L-lysyl-[protein]; Xref=Rhea:RHEA:69172, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:35899, ChEBI:CHEBI:137954; Evidence={ECO:0000250|UniProtKB:Q13547}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69173; Evidence={ECO:0000250|UniProtKB:Q13547};
| null | null | null | null |
FUNCTION: Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (PubMed:10454532). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed:10454532). Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Also functions as a deacetylase for non-histone proteins. In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl) of histones (By similarity). {ECO:0000250|UniProtKB:Q13547, ECO:0000269|PubMed:10454532}.
|
Xenopus laevis (African clawed frog)
|
O42248
|
GBLP_DANRE
|
MTEQMTVRGTLKGHSGWVTQIATTPQFPDMILSASRDKTIIMWKLTRDETNYGIPQRALRGHSHFVSDVVISSDGQFALSGSWDGTLRLWDLTTGTTTRRFVGHTKDVLSVAFSADNRQIVSGSRDKTIKLWNTLGVCKYTIQDDSHTEWVSCVRFSPNSSNPIIVSCGWDKMVKVWNLANCKLKTNHIGHTGYLNTVTVSPDGSLCASGGKDGQAMLWDLNEGKHLYTLDGGDTINALCFSPNRYWLCAATGPSIKIWDLEGKIIVDELRQDIITTNSKAEPPQCTSLAWSADGQTLFAGYTDNLIRVWQVTIGTR
| null | null |
angiogenesis [GO:0001525]; convergent extension involved in gastrulation [GO:0060027]; negative regulation of Wnt signaling pathway [GO:0030178]; positive regulation of gastrulation [GO:2000543]; positive regulation of protein phosphorylation [GO:0001934]; regulation of cell division [GO:0051302]; regulation of establishment of cell polarity [GO:2000114]; regulation of protein localization [GO:0032880]; rescue of stalled ribosome [GO:0072344]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]; ribosome [GO:0005840]
|
protein kinase C binding [GO:0005080]; ribosome binding [GO:0043022]; translation regulator activity [GO:0045182]
|
PF00400;
|
2.130.10.10;
|
WD repeat G protein beta family, Ribosomal protein RACK1 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21262816}.
| null | null | null | null | null |
FUNCTION: Involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes (By similarity). Required for VANGL2 membrane localization, inhibits Wnt signaling and regulates cellular polarization and oriented cell division during gastrulation. {ECO:0000250, ECO:0000269|PubMed:21262816}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O42250
|
VSX1_DANRE
|
MTGREEATDEKPKVKLYPSFGIDKSRLNGSGFRSKGFAITDLLGLESELQPHQSGPGAGPNGEGQSAAVGGFSFPGGSLPLGLGFLCSLAAQQPPGAPCFLPSHIPLLQSRTESHFMQNLEQQRDVYSDDDCLSGDRNDGKNSGNSQKRKKRRHRTVFTSHQLEELEKAFNEAHYPDVYAREMLAMKTELPEDRIQVWFQNRRAKWRKREKCWGRSSVMAEYGLYGAMVRHSIPLPESIINSAKSGMMGSCAPWLLGEPAGMHKKSMEIVKKAPGTPESTHSDTYSEEHKGKDSDTTWSSGANGADDSEDMAIDLSSTSKQENKSTLKRSPPRTENSSDSENES
| null | null |
axial mesoderm development [GO:0048318]; forebrain development [GO:0030900]; negative regulation of axial mesodermal cell fate specification [GO:0048329]; negative regulation of DNA-templated transcription [GO:0045892]; neuron development [GO:0048666]; paraxial mesoderm development [GO:0048339]; paraxial mesodermal cell fate specification [GO:0048348]; prechordal plate formation [GO:0021501]; regulation of DNA-templated transcription [GO:0006355]; response to stimulus [GO:0050896]; visual perception [GO:0007601]
|
nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; transcription cis-regulatory region binding [GO:0000976]
|
PF00046;
|
1.10.10.60;
|
Paired homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:11331779}.
| null | null | null | null | null |
FUNCTION: May be involved in maintenance as well as cellular differentiation of retinal interneurons, such as bipolar cells. May play a role in establishing interneuronal cell classes in nonsensory as well as sensory systems.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O42252
|
LDB1_CHICK
|
MSVGCACPGCSSKSFKLYSPKEPPNGNAFPPFHPGTMLDRDVGPTPMYPPTYLEPGIGRHTPYGNQTDYRIFELNKRLQNWTEECDNLWWDAFTTEFFEDDAMLTITFCLEDGPKRYTIGRTLIPRYFRSIFEGGATELYYVLKHPKESFHNNFVSLDCDQCTMVTQHGKPMFTQVCVEGRLYLEFMFDDMMRIKTWHFSIRQHRELIPRSILAMHAQDPQMLDQLSKNITRCGLSNSTLNYLRLCVILEPMQELMSRHKTYSLSPRDCLKTCLFQKWQRMVAPPAEPARQQPSKRRKRKMSGGSTMSSGGGNTNNSNSKKKSPASTFALSSQVPDVMVVGEPTLMGGEFGDEDERLITRLENTQFDAANGIDDEDSFNNSPALGANSPWNSKPPSSQESKSENPTSQASQ
| null | null |
anterior/posterior axis specification [GO:0009948]; negative regulation of erythrocyte differentiation [GO:0045647]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nervous system development [GO:0007399]; neuron differentiation [GO:0030182]; positive regulation of transcription by RNA polymerase II [GO:0045944]; Wnt signaling pathway [GO:0016055]
|
nucleus [GO:0005634]; protein-containing complex [GO:0032991]; transcription regulator complex [GO:0005667]
|
LIM domain binding [GO:0030274]; protein homodimerization activity [GO:0042803]
|
PF17916;PF01803;
|
2.10.110.10;
|
LDB family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Binds to the LIM domain of a wide variety of LIM domain-containing transcription factors. {ECO:0000305}.
|
Gallus gallus (Chicken)
|
O42254
|
IF2B1_CHICK
|
MNKLYIGNLNESVTPADLEKVFNDHKISFSGQFLVKSGYAFVDCPDEQWAMKAIETFSGKVELHGKQLEIEHSVPKKQRSRKIQIRNIPPQLRWEVLDGLLAQYGTVENCEQVNTDSETAVVNVTYTNREQTRQAIMKLNGHQLENHVLKVSYIPDEQSVQGPENGRRGGFGARGAPRQGSPVTAGAPVKQQPVDIPLRLLVPTQYVGAIIGKEGATIRNITKQTQSKIDVHRKENAGAAEKAISIHSTPEGCSAACKMILEIMQKEAKDTKTADEVPLKILAHNNFVGRLIGKEGRNLKKVEQDTETKITISSLQDLTLYNPERTITVKGSIENCCKAEQEIMKKVREAYENDVAAMSLQSHLIPGLNLAAVGLFPASSNAVPPPPSSVSGAAPYSSFMPPEQETVHVFIPAQAVGAIIGKKGQHIKQLSRFASASIKIAPPETPDSKVRMVVITGPPEAQFKAQGRIYGKLKEENFFGPKEEVKLETHIRVPASAAGRVIGKGGKTVNELQNLTAAEVVVPRDQTPDENEQVIVKIIGHFYASQMAQRKIRDILAQVKQQHQKGQSGQLQARRK
| null | null |
CRD-mediated mRNA stabilization [GO:0070934]; mRNA transport [GO:0051028]; negative regulation of translation [GO:0017148]; nervous system development [GO:0007399]; positive regulation of neuron projection development [GO:0010976]; regulation of gene expression [GO:0010468]
|
CRD-mediated mRNA stability complex [GO:0070937]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; filopodium [GO:0030175]; growth cone [GO:0030426]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; P-body [GO:0000932]; perinuclear region of cytoplasm [GO:0048471]
|
mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]; N6-methyladenosine-containing RNA reader activity [GO:1990247]
|
PF00013;PF00076;
|
3.30.310.210;3.30.70.330;3.30.1370.10;
|
RRM IMP/VICKZ family
|
PTM: Phosphorylated by SRC at Tyr-396. This residue is involved in ACTB mRNA binding, its phosphorylation impairs association with ACTB mRNA and hence abolishes translational repression. Phosphorylation occurs in close proximity to filopodia and in the growth cones of differentiated neuroglioblastoma cells. {ECO:0000269|PubMed:16306994}.
|
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q9NZI8}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q9NZI8}. Cell projection, growth cone. Cell projection, filopodium. Cell projection, lamellipodium. Note=In the nucleus, located in discrete foci, coinciding with the sites of ACTB transcription. Export from the nucleus is mediated by XPO1. In the cytoplasm, colocalizes with ACTB mRNA at the leading edge, in growth cone filopodia and along neurites. In these locations, also colocalizes with microtubules. Colocalization with ACTB mRNA is partially lost at the cell periphery, suggesting release of the transcript. In neuronal processes, exhibits fast retrograde and anterograde movements, when associated with ACTB mRNA; this motility is lost when the association is inhibited. In migrating fibroblasts, localizes not only to leading edges, but also to retracting tails. In response to cellular stress, such as oxidative stress or heat shock, recruited to stress granules.
| null | null | null | null | null |
FUNCTION: RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Preferentially binds to N6-methyladenosine (m6A)-containing mRNAs and increases their stability (By similarity). Plays a direct role in the transport and translation of transcripts required for axonal regeneration in adult sensory neurons (By similarity). Regulates localized beta-actin/ACTB mRNA translation in polarized cells, a crucial process for cell migration and neurite outgrowth. Co-transcriptionally associates with the ACTB mRNA in the nucleus. This binding involves by a conserved 54-nucleotide element in the ACTB mRNA 3'-UTR, known as the 'zipcode'. The ribonucleoparticle (RNP) thus formed is exported to the cytoplasm, binds to a motor protein and is transported along the cytoskeleton to the cell periphery. During transport, IGF2BP1 prevents beta-actin mRNA from being translated into protein. When the RNP complex reaches its destination near the plasma membrane, IGF2BP1 is phosphorylated by SRC. This releases the mRNA, allowing ribosomal 40S and 60S subunits to assemble and initiate ACTB protein synthesis. The monomeric ACTB protein then assembles into the subcortical actin cytoskeleton, which pushes the leading edge onwards. Binds MYC mRNA. Binding to MYC mRNA is enhanced by m6A-modification of the CRD (By similarity). Promotes the directed movement of cells by fine-tuning intracellular signaling networks. Binds to MAPK4 3'-UTR and inhibits its translation. Interacts with PTEN transcript open reading frame (ORF) and prevents mRNA decay. This combined action on MAPK4 (down-regulation) and PTEN (up-regulation) antagonizes HSPB1 phosphorylation, consequently it prevents G-actin sequestration by phosphorylated HSPB1, allowing F-actin polymerization. Hence enhances the velocity of cell migration and stimulates directed cell migration by PTEN-modulated polarization. {ECO:0000250|UniProtKB:Q9NZI8, ECO:0000269|PubMed:11502257, ECO:0000269|PubMed:12507992, ECO:0000269|PubMed:12573215, ECO:0000269|PubMed:16306994, ECO:0000269|PubMed:22279049, ECO:0000269|PubMed:23640942, ECO:0000269|PubMed:9121465}.
|
Gallus gallus (Chicken)
|
O42259
|
G3P_ONCMY
|
MSDLCVGINGFGRIGRLVLRACLQKGIKVVAINDPFIDLQYMVYMFKYDSTHGRYKGEVSMEDGKLIVDDHSISVFQCMKPHEIPWGKAGADYVVESTGVFLSIDKASSHIQGGAKRVVVSAPSPDAPMFVMGVNEDKFDPSSMTIVSNASCTTNCLAPLAKVIHDNFGIEEALMTTVHAYTATQKTVDGPSAKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVADVSVVELTCRLSRPGSYAEIKGAVKKAAEGPMKGYVGYTEYSVVSSDFIGDTHSSMFDAGAGISFNDNFVKLISWYDNEFGYSHRVADLLLYMHFKE
|
1.2.1.12; 2.6.99.-
| null |
glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; microtubule cytoskeleton organization [GO:0000226]; neuron apoptotic process [GO:0051402]; peptidyl-cysteine S-trans-nitrosylation [GO:0035606]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of type I interferon production [GO:0032481]; protein stabilization [GO:0050821]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634]
|
glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; microtubule binding [GO:0008017]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; peptidyl-cysteine S-nitrosylase activity [GO:0035605]
|
PF02800;PF00044;
|
3.40.50.720;
|
Glyceraldehyde-3-phosphate dehydrogenase family
|
PTM: S-nitrosylation of Cys-152 leads to translocation to the nucleus. {ECO:0000250|UniProtKB:P04797}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P04797}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P04797}. Nucleus {ECO:0000250|UniProtKB:P04797}.
|
CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000250|UniProtKB:P04406, ECO:0000255|PROSITE-ProRule:PRU10009}; CATALYTIC ACTIVITY: Reaction=L-cysteinyl-[protein] + S-nitroso-L-cysteinyl-[GAPDH] = L-cysteinyl-[GAPDH] + S-nitroso-L-cysteinyl-[protein]; Xref=Rhea:RHEA:66684, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:17089, Rhea:RHEA-COMP:17090, Rhea:RHEA-COMP:17091, ChEBI:CHEBI:29950, ChEBI:CHEBI:149494; Evidence={ECO:0000250|UniProtKB:P04797}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66685; Evidence={ECO:0000250|UniProtKB:P04797};
| null |
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
| null | null |
FUNCTION: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (By similarity). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity). {ECO:0000250|UniProtKB:P04406, ECO:0000250|UniProtKB:P04797}.
|
Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
|
O42261
|
IRX3_XENLA
|
MSFPQLGYQYIRPLYPSDRQSVGVTRSGTELSPAGTLSNVLSSVYGAPYAAAAAAQAYGAFLPYSAELPIFPQLGSQYDMKDSPGVQHAAFSHPHPAFYPYGQYQFGDPSRPKNATRESTSTLKAWLNEHRKNPYPTKGEKIMLAIITKMTLTQVSTWFANARRRLKKENKMTWAPRSRTDEEGNAYGSDHEEDKHEDEEEIDLENIDTEDIESKEDLDDPDTDIHSDSKTDTRSDSEVSDGFEDLNVPEDRLLKSVVGQRQLLNEEPQDKCALSSDAKVPQPACEQIKLNRLPPSPPQENNMPVAHKPKIWSLAETATTPDNPRNSPNTGGSVNTQNLIAQHRLIASPGSRFQGWTGRAFSAQQLSLLNSAHFLQGLGVSHTAPCSGNASFPKAAESKCSTNSLTDRPSTVDIEKTIPVLNTAFQPVQRRSQNHLDAAMILSALSSS
| null | null |
brain development [GO:0007420]; cell development [GO:0048468]; dorsal/ventral pattern formation [GO:0009953]; kidney development [GO:0001822]; maintenance of kidney identity [GO:0072005]; mesoderm development [GO:0007498]; metanephros development [GO:0001656]; negative regulation of neuron differentiation [GO:0045665]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neural plate development [GO:0001840]; neuron differentiation [GO:0030182]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of transcription by RNA polymerase II [GO:0045944]; pronephros development [GO:0048793]; proximal/distal pattern formation [GO:0009954]; proximal/distal pattern formation involved in nephron development [GO:0072047]; proximal/distal pattern formation involved in pronephric nephron development [GO:0072196]; specification of loop of Henle identity [GO:0072086]; specification of pronephric tubule identity [GO:0039005]
|
axon [GO:0030424]; cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF05920;
|
1.10.10.60;
|
TALE/IRO homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255, ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Acts partially redundantly with other irx members in neural patterning. Required for formation of the posterior forebrain, midbrain, hindbrain, and to a lesser extent, spinal cord. Both up-regulates and down-regulates gene expression during neural development. Acts early in neural plate development to induce proneural gene expression and specify a neural precursor state. Also up-regulates repressors that prevent neuronal differentiation. Required during at least two stages of pronephros kidney development; during neurula stages, maintains transcription of key renal genes to define the size and identity of the pronephric anlage, probably in part through regulation of bmp-signaling. Subsequently required for proper formation of the intermediate tubule segment of the pronephros. {ECO:0000269|PubMed:12385755, ECO:0000269|PubMed:17875669, ECO:0000269|PubMed:18715948, ECO:0000269|PubMed:19268445, ECO:0000269|PubMed:9427753}.
|
Xenopus laevis (African clawed frog)
|
O42287
|
ITSN1_XENLA
|
MAQFGTPFGGNLDIWAITVEERAKHDQQFHGLKPTAGYITGDQARNFFLQSGLPQPVLAQIWALADMNNDGRMDQLEFSIAMKLIKLKLQGYPLPSILPSNMLKQPVAMPAAAVAGFGMSGIVGIPPLAAVAPVPMPSIPVVGMSPPLVSSVPTVPPLSNGAPAVIQSHPAFAHSATLPKSSSFGRSVAGSQINTKLQKAQSFDVPAPPLVVEWAVPSSSRLKYRQLFNSQDKTMSGNLTGPQARTILMQSSLPQSQLATIWNLSDIDQDGKLTAEEFILAMHLIDVAMSGQPLPPILPPEYIPPSFRRVRSGSGLSIMSSVSVDQRLPEEPEEEEPQNADKKLPVTFEDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQDQERKRQQDLEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNREQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIRCRLTTQRHEIESTNKSRELRIAEITHLQQQLQESQQLLGKMIPEKQSLNDQLKQVQQNSLHRDSLLTLKRALETKEIGRQQLRDQLDEVEKETRAKLQEIDVFNNQLKELRELYNKQQFQKQQDFETEKIKQKELERKTSELDKLKEEDKRRMLEHDKLWQDRVKQEEERYKFQDEEKEKREESIQKCEVEKKPEIQEKPNKPFHQPPEPGKLGGQIPWMNTEKAPLTINQGDVKVVYYRALYPFDARSHDEITIEPGDIIMVDESQTGEPGWLGGELKGKTGWFPANYAERMPESEFPSTTKPAAETTAKPTVHVAPSPVAPAAFTNTSTNSNNWADFSSTWPTNNTDKVESDNWDTWAAQPSLTVPSAGQHRQRSAFTPATVTGSSPSPVLGQGEKVEGLQAQALYPWRAKKDNHLNFNKNDVITVLEQQDMWWFGEVQGQKGWFPKSYVKLISGPLRKSTSIDSTSSESPASLKRVSSPAFKPAIQGEEYISMYTYESNEQGDLTFQQGDLIVVIKKDGDWWTGTVGEKTGVFPSNYVRPKDSEAAGSGGKTGSLGKKPEIAQVIASYAATGPEQLTLAPGQLILIRKKNPGGWWEGELQARGKKRQIGWFPANYVKLLSPGTNKSTPTEPPKPTSLPPTCQVIGMYDYIAQNDDELAFSKGQVINVLNKEDPDWWKGELNGHVGLFPSNYVKLTTDMDPSQQWCADLHLLDMLSPTERKRQGYIHELIVTEENYVSDLQLVTETFQKPLLESDLLTEKEVAMIFVNWKELIMCNIKLLKALRVRKKMSGEKMPVKMIGDILTAQLPHMQPYIRFCSCQLNGAALIQQKTDEVPEFKEFVKRLAMDPRCKGMPLSSFLLKPMQRVTRYPLIIKNIIENTPENHPDHSHLKQALEKAEELCSQVNEGVREKENSDRLEWIQGHVQCEGLSEQLVFNSVTNCLGPRKFLHSGKLYKAKSNKELYGFLFNDFLLLTQIIKPLGSSGNDKVFSPKSNLQYKMYKTPIFLNEVLVKLPTDPSGDEPIFHISHIDRVYTLRAESINERTAWVQKIKAASELYIETEKKKREKAYLVRSQRATGIGRLMVNIVEGIELKPCRTHGKSNPYCEITMGSQCHITKTIQDTLNPKWNSNCQFFIKDLEQDVLCITVFERDQFSPDDFLGRTEIRVADIKKDQGSKGPVTKCLLLHEVPTGEIVVRLDLQLFDEP
| null |
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
|
endocytosis [GO:0006897]; exocytosis [GO:0006887]; intracellular signal transduction [GO:0035556]; positive regulation of Rho protein signal transduction [GO:0035025]; protein transport [GO:0015031]
|
clathrin-coated pit [GO:0005905]; cytoplasm [GO:0005737]; lamellipodium [GO:0030027]; neuron projection [GO:0043005]; nuclear envelope [GO:0005635]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; synapse [GO:0045202]
|
calcium ion binding [GO:0005509]; guanyl-nucleotide exchange factor activity [GO:0005085]
|
PF00168;PF12763;PF16617;PF16652;PF00621;PF00018;PF07653;PF14604;
|
2.60.40.150;1.20.900.10;1.10.238.10;2.30.29.30;2.30.30.40;
| null | null |
SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250|UniProtKB:Q15811}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q9WVE9}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q15811}. Cell membrane {ECO:0000250|UniProtKB:Q15811}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q15811}. Recycling endosome {ECO:0000250|UniProtKB:Q15811}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000250|UniProtKB:Q15811}. Nucleus envelope {ECO:0000250|UniProtKB:Q15811}. Note=Shuttles between the cytoplasm and nucleus in an XPO1/CRM1-dependent manner. {ECO:0000250|UniProtKB:Q15811}.
| null | null | null | null | null |
FUNCTION: Adapter protein that provides a link between the endocytic membrane traffic and the actin assembly machinery. Acts as a guanine nucleotide exchange factor (GEF) for cdc42, and thereby stimulates actin nucleation mediated by wasl and the arp2/3 complex (By similarity). Involved in endocytosis of activated egfr, and probably also other growth factor receptors (By similarity). {ECO:0000250|UniProtKB:Q15811, ECO:0000250|UniProtKB:Q9Z0R4}.
|
Xenopus laevis (African clawed frog)
|
O42342
|
SOX7_XENLA
|
MTTLMGSYSWTESLDCSPMDGDLSDGLSPHRSPREKGSETRIRRPMNAFMVWAKDERKRLAVQNPDLHNAELSKMLGKSWKALSPAQKRPYVEEAERLRVQHMQDYPNYKYRPRRKKQIKRICKRVDTGFLLGSLSKDQNSVPDTRGCRTAMEKEENGGYPGAALSDIRHYRETPSNGNKYDQTYPYGLPTPPEMSPLEAIDQDQSFYSTSCSEDCHSHINGAVYPPEYSRSPILCSHLSQVPIPQPGSSMIPPVPTCPPAYYSSSYHSIHNYHAHLGQLSPPPEHPHYDTIDQISQAELLGEMDRNEFDQYLNTSLQDPTEMTIHGHVQVSQASDIQPSETSLISVLADATATYYNSYSVS
| null | null |
cell differentiation [GO:0030154]; endoderm formation [GO:0001706]; heart development [GO:0007507]; negative regulation of Wnt signaling pathway [GO:0030178]; positive regulation of transcription by RNA polymerase II [GO:0045944]; pronephros development [GO:0048793]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976]
|
PF00505;PF12067;
|
1.10.30.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Transcription factor. Binds to the DNA sequence 5'-AACAAT-3'. Acts downstream of vegt and upstream of nodal signaling to promote endodermal and mesodermal differentiation by promoting vegt-induced expression of both endodermal genes (including endodermin) and mesodermal genes (including snai1/snail and snai2/slug). Induces expression of multiple nodal genes (including nodal, nodal2, nodal4, nodal5 and nodal6) and binds directly to sites within the promoter of the nodal5 gene. The endodermal and mesodermal specification pathways then interact to initiate cardiogenesis. Acts partially redundantly with sox18 during cardiogenesis. Also acts as an antagonist of beta-catenin signaling. Regulates (possibly indirectly) development of the pronephros, the functional larval kidney. {ECO:0000250|UniProtKB:Q28GD5, ECO:0000269|PubMed:15680368, ECO:0000269|PubMed:16193513, ECO:0000269|PubMed:17608734, ECO:0000269|PubMed:8950180}.
|
Xenopus laevis (African clawed frog)
|
O42350
|
CO1A2_AQUCT
|
MLSFVDLRSVLLLAVTLYLVTCQEVRRGPRGDKGPPGEQGPPGIPGRDGEDGLPGLPGPPGVPGLGGNFAAQYDPSKSAEPGQQGIMGPRGPPGPPGSPGSQGFQGLPGENGEPGQTGPVGSRGPSGAPGKAGEDGHPGKSGRPGERGPVGPQGARGFPGTPGLPGFKGIRGHTGSDGQKGAPGAAGVKGENGANGDNGSPGQAGARGLPGERGRIGPAGSAGSRGSDGSSGPVGPAGPIGSAGAPGLPGAPGAKGELGPAGNNGPTGAAGGRGEPGPPGSLGPAGPPGNPGTNGVNGAKGTAGLPGVGGAPGLPGGRGIPGPAGPAGPSGARGLAGDPGIAGGKGDTGSKGEPGSVGQQGPAGPSGEEGKRGPNGEAGSSGPSGNAGIRGVPGTRGLPGPDGRAGGIGPAGSRGSSGPPGARGPNGDAGRPGEPGLLGARGLPGFSGSNGPQGKEGPAGPQGIEGRSGAAGPAGARGEPGAIGFPGPKGPNGEPGKNGDKGNQGPSGNRGAPGPDGNNGAQGPAGLGGATGEKGEQGPSGAPGFQGLPGPGGPPGEVGKPGERGAPGDFGPPGSAGTRGERGAPGESGGAGPHGPSGSRGPSGAPGPDGQKGEPGAAGLNGGLGPSGPAGIPGERGTAGTPGTKGEKGDAGNSGDYGNPGRDGARGPAGAAGAPGPAGGPGDRGESGPAGPSGVAGPRGAPGERGEAGPAGPTGFAGPPGAAGHTGAKGDRGAKGPKGEAGSPGPLGAHGSAGPAGPNGPAGSTGARGDAGPSGATGFPGPAGRAGAPGPPGNVGPSGPTGHPGKDGSRGPRGDSGPVGRPGEQGQHGPVGLAGDKGPSGEAGPAGPPGAAGPSGVLGARGILGLPGTRGERGLPGGPGSNGEPGPSGLAGSSGPRGPPGSVGSPGPVGHSGEAGRDGHPGNDGPPGRDGLPGAKGERGYPGNTGPSGLAGAPGPAGSAGPAGKSGNRGEGGPSGPAGITGPSGPRGPAGPQGVRGDKGEAGERGARGLDGRKGHNGLSGLPGPSGTPGETGPSGSVGPVGPRGPSGPSGPPGKEGRSGHPGAMGPVGPRGPAGFTGPAGPPGPPGPPGHAGPSGGGYDGGDGGEYYRADQPERKPKDYEVDATLKSLNQQIEVILTPEGSRKNPARTCRDLRLSHPEWTSGFYWIDPNQGCTSDAIRVFCDFSSGETCIHANPDEITQKNWYINTSNKDKKHLWFGEILNGGTQFEYHDEGLTAKDMATQLAFMRLLANQASQNITYHCKNSIAYMDEETGNLKKAVILQGSNDVELRAEGNTRFTYSVLEDGCTKHTGEWGKTVIEYRTNKPSRLPILDIAPLDIGGHDQEIGFEIGPVCFK
| null | null |
collagen fibril organization [GO:0030199]; notochord development [GO:0030903]; skeletal system development [GO:0001501]
|
collagen type II trimer [GO:0005585]; extracellular space [GO:0005615]
|
extracellular matrix structural constituent conferring tensile strength [GO:0030020]; metal ion binding [GO:0046872]
|
PF01410;PF01391;
|
2.60.120.1000;
|
Fibrillar collagen family
|
PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
| null | null | null | null | null |
FUNCTION: Type I collagen is a member of group I collagen (fibrillar forming collagen).
|
Aquarana catesbeiana (American bullfrog) (Rana catesbeiana)
|
O42354
|
MDM2_DANRE
|
MATESCLSSSQISKVDNEKLVRPKVQLKSLLEDAGADKDVFTMKEVMFYLGKYIMSKELYDKQQQHIVHCGEDPLGAVLGVKSFSVKEPRALFALINRNLVTVKNPESQSTFSEPRSQSEPDRGPGDTDSDSRSSTSQQQRRRRRSSDPESSSAEDESRERRKRHKSDSFSLTFDDSLSWCVIGGLHRERGNSESSDANSNSDVGISRSEGSEESEDSDSDSDNFSVEFEVESINSDAYSENDVDSVPGENEIYEVTIFAEDEDSFDEDTEITEADYWKCPKCDQFNPPLPRHCKSCWTVRADWLPETHSNWENLSRNTRTNPEDTSVTTTPNTTFEKKLSKPSSPLPETDDGVDVPTPPLLRRGSSQEETPELERFNSLEACLPATCLEPCVICQSRPKNGCIVHGRTGHLMACYTCAKKLKNRNKLCPVCREPIQSVVLTYMS
|
2.3.2.27
| null |
apoptotic process [GO:0006915]; cell cycle [GO:0007049]; negative regulation of apoptotic process [GO:0043066]; negative regulation of epithelial cell apoptotic process [GO:1904036]; negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator [GO:1902254]; pronephric glomerulus morphogenesis [GO:0035775]; protein ubiquitination [GO:0016567]; regulation of cell cycle [GO:0051726]; regulation of gene expression [GO:0010468]; regulation of protein stability [GO:0031647]; response to X-ray [GO:0010165]
|
cytoplasm [GO:0005737]; endosome [GO:0005768]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; p53 binding [GO:0002039]; ubiquitin protein ligase activity [GO:0061630]
|
PF02201;PF13920;
|
1.10.245.10;3.30.40.10;2.30.30.380;
|
MDM2/MDM4 family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P23804}. Cytoplasm {ECO:0000250|UniProtKB:P23804}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P23804}. Nucleus {ECO:0000250|UniProtKB:Q00987}.
|
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:0000250|UniProtKB:Q00987};
| null | null | null | null |
FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:Q00987}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O42358
|
RX3_DANRE
|
MRLVGSQYKDMEDRLSPSARLVRSPGSQTRIHSIESILGFKGETLFHPAFPYGSGKTGKDTEHLSPKKDSNKHFDGVCRSTVMVSPDLPDADGGKLSDDENPKKKHRRNRTTFTTFQLHELERAFEKSHYPDVYSREELALKVNLPEVRVQVWFQNRRAKWRRQEKLEVSSIKLQESSMLSIPRSGPLSLGSGLPLEPWLTGPISTSSSPLQSLPSFITPQQAVPASYTPPQFLSSSTLNHSLPHIGAVCPPYQCSGFMDKFSLQEADPRNTSIASLRMKAKEHIQSIGKTW
| null | null |
adenohypophysis development [GO:0021984]; camera-type eye morphogenesis [GO:0048593]; cell fate specification [GO:0001708]; embryonic camera-type eye morphogenesis [GO:0048596]; eye development [GO:0001654]; eye field cell fate commitment involved in camera-type eye formation [GO:0060898]; forebrain development [GO:0030900]; hypothalamus development [GO:0021854]; neural crest cell migration [GO:0001755]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; retina development in camera-type eye [GO:0060041]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00046;PF03826;
|
1.10.10.60;
|
Paired homeobox family, Bicoid subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00138}.
| null | null | null | null | null |
FUNCTION: Plays a critical role in eye formation by regulating the initial specification of retinal cells and/or their subsequent proliferation. {ECO:0000250}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O42363
|
APOA1_DANRE
|
MKFVALALTLLLALGSQANLFQADAPTQLEHYKAAALVYLNQVKDQAEKALDNLDGTDYEQYKLQLSESLTKLQEYAQTTSQALTPYAETISTQLMENTKQLRERVMTDVEDLRSKLEPHRAELYTALQKHIDEYREKLEPVFQEYSALNRQNAEQLRAKLEPLMDDIRKAFESNIEETKSKVVPMVEAVRTKLTERLEDLRTMAAPYAEEYKEQLVKAVEEAREKIAPHTQDLQTRMEPYMENVRTTFAQMYETIAKAIQA
| null | null |
acylglycerol homeostasis [GO:0055090]; cholesterol efflux [GO:0033344]; cholesterol metabolic process [GO:0008203]; lipoprotein metabolic process [GO:0042157]; phosphatidylcholine metabolic process [GO:0046470]; phospholipid efflux [GO:0033700]; regulation of intestinal cholesterol absorption [GO:0030300]
|
chylomicron [GO:0042627]; extracellular region [GO:0005576]; extracellular vesicle [GO:1903561]; high-density lipoprotein particle [GO:0034364]; low-density lipoprotein particle [GO:0034362]; very-low-density lipoprotein particle [GO:0034361]
|
cholesterol transfer activity [GO:0120020]; high-density lipoprotein particle receptor binding [GO:0070653]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipid binding [GO:0005543]; protein homodimerization activity [GO:0042803]
|
PF01442;
|
1.20.5.20;6.10.250.2890;1.20.120.20;
|
Apolipoprotein A1/A4/E family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). {ECO:0000250|UniProtKB:P02647}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O42364
|
APOEB_DANRE
|
MRSLVVFFALAVLTGCQARSLFQADAPQPRWEEMVDRFWQYVSELNTQTDGMVQNIKGSQLSRELDTLITDTMAELSSYSENLQTQMTPYASDAAGQLSKDLQLLAGKLQTDMTDAKERSTQYLQELKTMMEQNADDVKNRVGTYTRKLKKRLNKDTEEIRNTVATYMSEMQSRASQNADAVKDRFQPYMSQAQDGATQKLGAISELMKAQAQEVSEQLEVQAGALKEKLEETAENLRTSLEGRVDELTSLLAPYSQKIREQLQEVMDKIKEATAALPTQA
| null | null |
acylglycerol homeostasis [GO:0055090]; cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; cholesterol metabolic process [GO:0008203]; chylomicron remnant clearance [GO:0034382]; high-density lipoprotein particle assembly [GO:0034380]; intermediate-density lipoprotein particle clearance [GO:0071831]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process [GO:0042159]; negative regulation of neuron apoptotic process [GO:0043524]; phospholipid efflux [GO:0033700]; regulation of amyloid-beta clearance [GO:1900221]; triglyceride-rich lipoprotein particle clearance [GO:0071830]; very-low-density lipoprotein particle clearance [GO:0034447]
|
chylomicron [GO:0042627]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; low-density lipoprotein particle [GO:0034362]; very-low-density lipoprotein particle [GO:0034361]
|
amyloid-beta binding [GO:0001540]; cholesterol transfer activity [GO:0120020]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; low-density lipoprotein particle receptor binding [GO:0050750]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipid binding [GO:0005543]; very-low-density lipoprotein particle receptor binding [GO:0070326]
|
PF01442;
|
1.20.5.20;1.20.120.20;
|
Apolipoprotein A1/A4/E family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}.
| null | null | null | null | null |
FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. {ECO:0000250|UniProtKB:P02649}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O42392
|
VDR_CHICK
|
MSELRGSWDEQQQSMAYLPDADMDTVAASTSLPDPAGDFDRNVPRICGVCGDRATGFHFNAMTCEGCKGFFRRSMKRKAMFTCPFNGDCKITKDNRRHCQACRLKRCVDIGMMKEFILTDEEVQRKREMILKRKEEEALKESLKPKLSEEQQKVIDTLLEAHHKTFDTTYSDFNKFRPPVRSKFSSRMATHSSSVVSQDFSSEDSNDVFGSDAFAAFPEPMEPQMFSNLDLSEESDESPSMNIELPHLPMLPHLADLVSYSIQKVIGFAKMIPGFRDLTAEDQIALLKSSAIEVIMLRSNQSFTMEDMSWTCGSNDFKYKVSDVTQAGHSMDLLEPLVKFQVGLKKLNLHEEEHVLLMAICILSPDRPGVQDTSLVESIQDRLSDILQTYIRCRHPPPGSRLLYAKMIQKLADLRSLNEEHSKQYRCLSFQPEHSMQLTPLVLEVFGNEIS
| null | null |
calcium ion transport [GO:0006816]; cell differentiation [GO:0030154]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; response to vitamin D [GO:0033280]; vitamin D receptor signaling pathway [GO:0070561]
|
caveola [GO:0005901]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; vitamin D binding [GO:0005499]; vitamin D response element binding [GO:0070644]; zinc ion binding [GO:0008270]
|
PF00104;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family, NR1 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P11473, ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm {ECO:0000250|UniProtKB:P11473}. Note=Localizes mainly to the nucleus. Translocated into the nucleus via both ligand-dependent and ligand-independent pathways; ligand-independent nuclear translocation is mediated by IPO4. {ECO:0000250|UniProtKB:P11473}.
| null | null | null | null | null |
FUNCTION: Nuclear receptor for calcitriol, the active form of vitamin D3 which mediates the action of this vitamin on cells. Enters the nucleus upon vitamin D3 binding where it forms heterodimers with the retinoid X receptor/RXR. The VDR-RXR heterodimers bind to specific response elements on DNA and activate the transcription of vitamin D3-responsive target genes (By similarity). Plays a central role in calcium homeostasis (By similarity). Also functions as a receptor for the secondary bile acid lithocholic acid (LCA) and its metabolites (By similarity). {ECO:0000250|UniProtKB:P11473, ECO:0000250|UniProtKB:P13053}.
|
Gallus gallus (Chicken)
|
O42406
|
SIX3_CHICK
|
MVFRSPLELYPTHFFLPNFAADPHHRSLLLASGGSGSGSGCSPGAGGGGGSSRAPHEELSMFQLPTLNFSPEQVASVCETLEETGDIERLGRFLWSLPVAPGACEAINKHESILRARAVVAFHTGNFRDLYHILENHKFTKESHGKLQAMWLEAHYQEAEKLRGRPLGPVDKYRVRKKFPLPRTIWDGEQKTHCFKERTRSLLREWYLQDPYPNPSKKRELAQATGLTPTQVGNWFKNRRQRDRAAAAKNRLQHQAIGQSGMRSLAEPGCPTHSSAESPSTAASPTTSVSSLTERAETGTSILSVTSSDSECDV
| null | null |
apoptotic process involved in development [GO:1902742]; brain development [GO:0007420]; cell proliferation in forebrain [GO:0021846]; epithelial cell maturation [GO:0002070]; eye development [GO:0001654]; forebrain dorsal/ventral pattern formation [GO:0021798]; lens development in camera-type eye [GO:0002088]; lens fiber cell apoptotic process [GO:1990086]; lens fiber cell differentiation [GO:0070306]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of neuron differentiation [GO:0045665]; negative regulation of Wnt signaling pathway [GO:0030178]; neuroblast differentiation [GO:0014016]; neuroblast migration [GO:0097402]; optic vesicle morphogenesis [GO:0003404]; pituitary gland development [GO:0021983]; proximal/distal axis specification [GO:0009946]; regulation of cell cycle phase transition [GO:1901987]; regulation of cell population proliferation [GO:0042127]; regulation of neural precursor cell proliferation [GO:2000177]; regulation of neural retina development [GO:0061074]; regulation of neuroblast proliferation [GO:1902692]; regulation of transcription by RNA polymerase II [GO:0006357]; telencephalon development [GO:0021537]; telencephalon regionalization [GO:0021978]
|
nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00046;PF16878;
|
1.10.10.60;
|
SIX/Sine oculis homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q62233, ECO:0000255|PROSITE-ProRule:PRU00108}.
| null | null | null | null | null |
FUNCTION: Transcriptional regulator which can act as both a transcriptional repressor and activator by binding a ATTA homeodomain core recognition sequence on these target genes. During forebrain development represses WNT1 expression allowing zona limitans intrathalamica formation and thereby ensuring proper anterio-posterior patterning of the diencephalon and formation of the rostral diencephalon (PubMed:12569128). Acts as a direct upstream activator of SHH expression in the rostral diencephalon ventral midline and that in turn SHH maintains its expression. In addition, Six3 activity is required for the formation of the telencephalon. During postnatal stages of brain development is necessary for ependymal cell maturation by promoting the maturation of radial glia into ependymal cells through regulation of neuroblast proliferation and migration. Acts on the proliferation and differentiation of neural progenitor cells through activating transcription of CCND1 and CCND2. During early lens formation plays a role in lens induction and specification by activating directly PAX6 in the presumptive lens ectoderm. In turn PAX6 activates SIX3 resulting in activation of PDGFRA and CCND1 promoting cell proliferation. Also is required for the neuroretina development by directly suppressing WNT8B expression in the anterior neural plate territory. Its action during retina development and lens morphogenesis is AES and TLE4-dependent manner (PubMed:12050133). Furthermore, during eye development regulates several genes expression. Before and during early lens development represses the CRYGF promoter by binding a SIX repressor element. Directly activates RHO transcription, or cooperates with CRX or NRL. Six3 functions also in the formation of the proximodistal axis of the optic cup, and promotes the formation of optic vesicles-like structures. During pituitary development, acts in parallel or alternatively with HESX1 to control cell proliferation through Wnt/beta-catenin pathway. Plays a role in eye development by suppressing WNT1 expression and in dorsal-ventral patterning by repressing BMP signaling pathway (By similarity). {ECO:0000250|UniProtKB:O95343, ECO:0000250|UniProtKB:Q62233, ECO:0000269|PubMed:12050133, ECO:0000269|PubMed:12569128}.
|
Gallus gallus (Chicken)
|
O42410
|
IKZF1_CHICK
|
METDEAQDMSQVSGKESPPISDVPDDADEPMPVPEDLSTTTGGQQSVKNERVLAGNIKIETQSDEENGRACEMNGEECAEDLRMLDASGDKMNGSHNGPGSKAMSGVGGIRLPNGKLKCDICGIICIGPNVLMVHNRSHTGERPFQCNQCGASFTQKGNLLRHIKLHSGEKPFKCHLCNYACRRRDALTGHLRTHSVGKPHKCGYCGRSYKQRSSLEEHKERCHNYLQTMSISSNLYSVIKEETNQSEMAEDLCKIGSERSLVLDRLASNVAKRKSSMPQKFVGEKCLSDLPYDATTNYEKENEIMQTHVIDQAINNAISYLGAESLRPLVQTPPVGSEVVPVISPMYQLHKPLGDNQTRSNHTAQDSAVENLLLLSKAKSVSSERDASPSNSCQDSTDTESNNEERSGLIYLTNHIGPHARNGISVKEESRQFDVLRAGTDNSQDAFKVISSNGEQVRVYKCEHCRVLFLDHVMYTIHMGCHGFRDPFECNMCGYHSQDRYEFSSHITRGEHRFHMS
| null | null |
cell growth [GO:0016049]; immunoglobulin production [GO:0002377]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleus [GO:0005634]; protein-DNA complex [GO:0032993]
|
DNA-binding transcription factor activity [GO:0003700]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription cis-regulatory region binding [GO:0000976]
|
PF00096;
|
3.30.160.60;
|
Ikaros C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13422}.
| null | null | null | null | null |
FUNCTION: Binds and activates the enhancer (delta-A element) of the CD3-delta gene. Functions in the specification and the maturation of the T-lymphocyte. Also interacts with a critical control element in the TDT (terminal deoxynucleotidyltransferase) promoter as well as with the promoters for other genes expressed during early stages of B- and T-cell development. Function is isoform-specific and is modulated by dominant-negative inactive isoforms (By similarity). {ECO:0000250|UniProtKB:Q03267, ECO:0000250|UniProtKB:Q13422}.
|
Gallus gallus (Chicken)
|
O42414
|
NFASC_CHICK
|
MVLHSHQLTYAGIAFALCLHHLISAIEVPLDSNIQSELPQPPTITKQSVKDYIVDPRDNIFIECEAKGNPVPTFSWTRNGKFFNVAKDPKVSMRRRSGTLVIDFHGGGRPDDYEGEYQCFARNDYGTALSSKIHLQVSRSPLWPKEKVDVIEVDEGAPLSLQCNPPPGLPPPVIFWMSSSMEPIHQDKRVSQGQNGDLYFSNVMLQDAQTDYSCNARFHFTHTIQQKNPYTLKVKTKKPHNETSLRNHTDMYSARGVTETTPSFMYPYGTSSSQMVLRGVDLLLECIASGVPAPDIMWYKKGGELPAGKTKLENFNKALRISNVSEEDSGEYFCLASNKMGSIRHTISVRVKAAPYWLDEPQNLILAPGEDGRLVCRANGNPKPSIQWLVNGEPIEGSPPNPSREVAGDTIVFRDTQIGSSAVYQCNASNEHGYLLANAFVSVLDVPPRILAPRNQLIKVIQYNRTRLDCPFFGSPIPTLRWFKNGQGNMLDGGNYKAHENGSLEMSMARKEDQGIYTCVATNILGKVEAQVRLEVKDPTRIVRGPEDQVVKRGSMPRLHCRVKHDPTLKLTVTWLKDDAPLYIGNRMKKEDDGLTIYGVAEKDQGDYTCVASTELDKDSAKAYLTVLAIPANRLRDLPKERPDRPRDLELSDLAERSVKLTWIPGDDNNSPITDYIVQFEEDRFQPGTWHNHSRYPGNVNSALLSLSPYVNYQFRVIAVNDVGSSLPSMPSERYQTSGARPEINPTGVQGAGTQKNNMEITWTPLNATQAYGPNLRYIVRWRRRDPRGSWYNETVKAPRHVVWNTPIYVPYEIKVQAENDFGRAPEPETYIGYSGEDYPKAAPTDVRIRVLNSTAIALTWTRVHLDTIQGQLKEYRAYFWRDSSLLKNLWVSKKRQYVSFPGDRNRGIVSRLFPYSNYKLEMVVTNGRGDGPRSEVKEFPTPEGVPSSPRYLRIRQPNLESINLEWDHPEHPNGVLTGYNLRYQASCLSSPVNGSKTGRTLVENFSPNQTRFTVQRTDPISRYRFFLRARTQVGDGEVIVEESPALLNEATPTPASTWLPPPTTELTPAATIATTTTTATPTTETPPTEIPTTAIPTTTTTTTTTAASTVASTTTTAERAAAATTKQELATNGSSIWDIRAWANSNWANITWSHNYSAGTDFVVKYITSNKTEKSIPVKAQTPSSVQLANLTPGMVYKLWVFPIWSSPSEHSYITFTTSSAYTKNHVDIATQGWFIGLMCAIALLVLILLIVCFIKRSRGGKYPVRDNKDEHLNPEDKNVEDGSFDYRSLESDEDNKPLPNSQTSLDGTIKQQESDDSLVDYGEGGEGQFNEDGSFIGQYTVKKDKEETEGNESSEATSPVNAIYSLA
| null | null |
axon guidance [GO:0007411]; brain development [GO:0007420]; dendrite self-avoidance [GO:0070593]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]
|
axon [GO:0030424]; plasma membrane [GO:0005886]
|
cell-cell adhesion mediator activity [GO:0098632]
|
PF13882;PF00041;PF07679;PF00047;PF13927;
|
2.60.40.10;
|
Immunoglobulin superfamily, L1/neurofascin/NgCAM family
|
PTM: N-glycosylated and O-glycosylated. {ECO:0000269|PubMed:1377696}.; PTM: May be proteolytically cleaved at Arg-636. {ECO:0000269|PubMed:1377696}.
|
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Cell adhesion, ankyrin-binding protein which may be involved in neurite extension, axonal guidance, synaptogenesis, myelination and neuron-glial cell interactions. {ECO:0000250}.
|
Gallus gallus (Chicken)
|
O42422
|
EPHA7_CHICK
|
MVLRSRLPPWIMLCSVWLLRFAHTGEAQAAKEVILLDSKAQQTELEWISSPPNGWEEISGLDENYTPIRTYQVCQVMESNQNNWLRTNWIAKSNAQRIFVELKFTLRDCNSLPGVLGTCKETFNLYYYETDYDTGRNIRENQYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDVGACIALVSVKVYYKKCWSIIENLAIFPDTVTGSEFSSLVEVRGTCVSSAEEEAENSPKMHCSAEGEWLVPIGKCICKAGYQQKGDTCEPCGRGFYKSSSQDLQCSRCPTHSFSDKEGSSRCDCEDSYYRAPSDPPYVACTRPPSAPQNLIFNINQTTVSLEWSPPADNGGRNDVTYRILCKRCSWEQGECVPCGSNIGYMPQQTGLVDNYVTVMDLLAHANYTFEVEAVNGVSDLSRSQRLFAAVSITTGQAAPSQVSGVMKERVLQRSVELSWQEPEHPNGVITEYEIKYYEKDQRERTYSTVKTKSTSASINNLKPGTVYVFQIRAFTAAGYGNYSPRLDVATLEEATATAVSSEQNPVIIIAVVAVAGTIILVFMVFGFIIGRRHCGYSKADQEGDEELYFHFKFPGTKTYIDPETYEDPNRAVHQFAKELDASCIKIERVIGAGEFGEVCSGRLKLPGKRDVAVAIKTLKVGYTEKQRRDFLCEASIMGQFDHPNVVHLEGVVTRGKPVMIVIEYMENGALDAFLRKHDGQFTVIQLVGMLRGIAAGMRYLADMGYVHRDLAARNILVNSNLVCKVSDFGLSRVIEDDPEAVYTTTGGKIPVRWTAPEAIQYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVIKAIEEGYRLPAPMDCPAGLHQLMLDCWQKERGERPKFEQIVGILDKMIRNPNSLKTPLGTCSRPISPLLDQNTPDFTTFCSVGEWLQAIKMERYKDNFTAAGYNSLESVARMTIEDVMSLGITLVGHQKKIMSSIQTMRAQMLHLHGTGIQV
|
2.7.10.1
| null |
apoptotic process [GO:0006915]; axon guidance [GO:0007411]; brain development [GO:0007420]; ephrin receptor signaling pathway [GO:0048013]; phosphorylation [GO:0016310]; regulation of cell-cell adhesion [GO:0022407]; regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043281]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of peptidyl-tyrosine phosphorylation [GO:0050730]; regulation of protein autophosphorylation [GO:0031952]
|
dendrite [GO:0030425]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; axon guidance receptor activity [GO:0008046]; GPI-linked ephrin receptor activity [GO:0005004]; protein tyrosine kinase activity [GO:0004713]; transmembrane-ephrin receptor activity [GO:0005005]
|
PF14575;PF01404;PF07699;PF00041;PF07714;PF00536;
|
2.60.40.1770;2.60.120.260;2.60.40.10;1.10.150.50;1.10.510.10;2.10.50.10;
|
Protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily
|
PTM: Phosphorylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
| null | null | null | null |
FUNCTION: Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Among GPI-anchored ephrin-A ligands, EFNA5 is a cognate/functional ligand for EPHA7 and their interaction regulates brain development modulating cell-cell adhesion and repulsion. Has a repellent activity on axons and is for instance involved in the guidance of corticothalamic axons and in the proper topographic mapping of retinal axons to the colliculus. May also regulate brain development through a caspase(CASP3)-dependent proapoptotic activity. Forward signaling may result in activation of components of the ERK signaling pathway including MAP2K1, MAP2K2, MAPK1 and MAPK3 which are phosphorylated upon activation of EPHA7 (By similarity). {ECO:0000250}.
|
Gallus gallus (Chicken)
|
O42425
|
HBA2_GADMO
|
MSLSSKQKATVKDFFSKMSTRSDDIGAEALSRLVAVYPQTKSYFSHWKDASPGSAPVRKHGITTMGGVYDAVGKIDDLKGGLLSLSELHAFMLRVDPVNFKLLAHCMLVCMSMIFPEEFTPQVHVAVDKFLAQLALALAEKYR
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from gills to the various peripheral tissues. {ECO:0000269|PubMed:16717098}.
|
Gadus morhua (Atlantic cod)
|
O42446
|
DNAS1_OREMO
|
MQTYRSRMHLVCSLGLFLTLLHLSNSLLLGAFNIKSFGDTKASNATLMNIITKIVKRYDVILIQEVRDSDLSATQTLMNYVNKDSPQYKYIVSEPLGASTYKERYLFLYREALVSVVKSYTYDDGPEETGQDTFSREPFVVMFSSKNTAVRDFTLIPQHTSPDLAVRELNALYDVVLDVRARWNTNDIVLLGDFNAGCSYVSGSAWQQIRIFTDKTFHWLITDAADTTVSQTVCPYDRIVVTTDMMRGVVQNSAKVYNYMTDLNLKQDLALAVSDHFPVEVKLS
|
3.1.21.1
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:9395327}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9395327}; Note=Divalent metal cations. Prefers Ca(2+) or Mg(2+) which have a synergistic effect on activation. {ECO:0000269|PubMed:9395327};
|
DNA catabolic process [GO:0006308]; neutrophil activation involved in immune response [GO:0002283]; regulation of acute inflammatory response [GO:0002673]; regulation of neutrophil mediated cytotoxicity [GO:0070948]
|
extracellular region [GO:0005576]; nuclear envelope [GO:0005635]; zymogen granule [GO:0042588]
|
deoxyribonuclease I activity [GO:0004530]; DNA binding [GO:0003677]
|
PF03372;
|
3.60.10.10;
|
DNase I family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P24855}. Zymogen granule {ECO:0000250|UniProtKB:P24855}. Nucleus envelope {ECO:0000250|UniProtKB:P24855}. Note=Secretory protein, stored in zymogen granules and found in the nuclear envelope. {ECO:0000250|UniProtKB:P24855}.
|
CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products.; EC=3.1.21.1; Evidence={ECO:0000269|PubMed:9395327};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:9395327};
| null |
FUNCTION: Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs (PubMed:9395327). Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA (By similarity). Among other functions, seems to be involved in cell death by apoptosis (By similarity). Binds specifically to G-actin and blocks actin polymerization. Preferentially attacks double-stranded DNA and produces oligonucleotides with 5'-phospho and 3'-hydroxy termini (PubMed:9395327). {ECO:0000250|UniProtKB:P21704, ECO:0000269|PubMed:9395327}.
|
Oreochromis mossambicus (Mozambique tilapia) (Tilapia mossambica)
|
O42477
|
VSX2_DANRE
|
MTGKDGAVLSESLNKSKSLCATENGGNNNPHLSKSSITHPPKCTGFGIQEILGLNKEPSSAPRSTLDSFPAGAHLLASRSMLGPAGVGVGVGMGLIGPGGIPSFYSQPAFLEVLSDAQNVHLQPLSRTVGPLEHNQSASSDSDDVSSSERKMSKSSLSQSKKRKKRRHRTIFTSYQLEELEKAFNEAHYPDVYAREMLAMKTELPEDRIQVWFQNRRAKWRKREKCWGRSSVMAEYGLYGAMVRHSIPLPVQDGFPTTSCFSKHEYPPFFAESILKSAKDGIMDSCAPWLLGMHKKSLETAGHQSNEKSDVTQTPTNPKPDEAEAEERRTESPMSKEELRENSIAALRAKAQEHSAKVLGTVSSERLEHNMETTATEEKSSEQIDAKEEEKSS
| null | null |
negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of neural retina development [GO:0061074]; regulation of transcription by RNA polymerase II [GO:0006357]; response to stimulus [GO:0050896]; visual perception [GO:0007601]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00046;PF03826;
|
1.10.10.60;
|
Paired homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q61412}.
| null | null | null | null | null |
FUNCTION: Acts as a transcriptional regulator (By similarity). Mediates the differentiation of V2a interneurons (By similarity). Plays a role in eye development and organization of the neuroretina (PubMed:17919464, PubMed:9203137). {ECO:0000250|UniProtKB:Q61412, ECO:0000269|PubMed:17919464, ECO:0000269|PubMed:9203137}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O42478
|
TLE4_XENLA
|
MIRDLSKMYPQTRHPAPPHQPAQPFKFTISESCDRIKEEFQFLQAQYHSLKLECEKLASEKTEMQRHYVMYYEMSYGLNIEMHKQAEIVKRLNAICAQVIPFLSQEHQQQVVQAVERAKQVTMAELNAIIGQQLQAQHLSHAHGLPVPLTPHPSGLQPPAIPSIGSSAGLLALSSALGGQSHLPIKDEKKHHDSDHQRDRDSIKSSSVSPSASFRAAEKHRNSTDYSSESKKQKTEEKDIAARYDSDGEKSDDNLVVDVSNEDPSSPRGSPAHSPRENGLDKPRLLKKDAPISPASIASSSSTPSSKSKEHSHNEKSTTPVSKSNTPTPRTDAPTPGSNSSGLRPVPGKPPGVDPLTGLRTPMAVPCPYPTPFGIVPHAGMNGDLTSPGPAYASLHSISPQMSAAAAAAAAAAAYGRSPVVGFDPHHHMRVPGIPPNLTGIPGGKPAYSFHVSADGQMQPVPFPPDALIGPGIPRHARQINTLNHGEVVCAVTISNPTRHVYTGGKGCVKVWDISHPGNKSPVSQLDCLNRDNYIRSCRLLPDGRTLIVGGEASTLSIWDLAAPTPRIKAELTSSAPACYALAISPDSKVCFSCCSDGNIAVWDLHNQTLVRQFQGHTDGASCIDISNDGTKLWTGGLDNTVRSWDLREGRQLQQHDFTSQIFSLGYCPTGEWLAVGMENSNVEVLHVTKPDKYQLHLHESCVLSLKFAHCGKWFVSTGKDNLLNAWRTPYGASIFQSKESSSVLSCDISVDDKYIVTGSGDKKATVYEVIY
| null | null |
mesoderm formation [GO:0001707]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of transcription by RNA polymerase II [GO:0000122]
|
nucleoplasm [GO:0005654]; transcription repressor complex [GO:0017053]
|
transcription corepressor activity [GO:0003714]
|
PF03920;PF00400;
|
2.130.10.10;
|
WD repeat Groucho/TLE family
|
PTM: Ubiquitinated by XIAP/BIRC4. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Transcriptional corepressor. Functions with ripply2.2/bowline to down regulate transcription of tbx6-dependent gene expression. Represses transcription of siamois and nodal3. {ECO:0000269|PubMed:9783587}.
|
Xenopus laevis (African clawed frog)
|
O42579
|
FZD3_XENLA
|
MAAYLISFIWVSVILAQKSMGHSLFACEPITLRMCQDLPYNSTFMPNLLNHYDQQTAALAMEPFHPMVNLECSRDLRPFLCALYTPVCMEYGRMTLPCRKLCQRAYNECFKLMEMFGVPWPEEMECSRFPDCDEPYPRIVDISLSGEPSEETPLAVQRDYGFWCPRELKIDPDLRSSFLGVRDCSPPCPHMYFRREELSFARYFIGVISIVCLSATLFTFLTFLIDVTRFRYPERPIIFYAVCYMMVSLIFFIGFLLEDKVACNGANPSQYKASTVTQGSHNKACTMLFMVLYFFTMAGSVWWVILTITWFLAAVPKWGSEAIEKKALLFHASAWGIPGTLTIILLAMNKIEGDNISGVCFVGLYDVHALRYFVLAPLCLDVVVGVSLLLAGIISLNRVRIEIPLEKENQDKLVKFMIRIGVFSILYLVPLLVVIGCYFYEQAYRGVWETTWVQERCREYHIPCPYKVTQTSRPDLILFLMKYLMLLVVGIPSVFWVGSKKTCFEWASFFHGRKKKAGVNESRQVLQEPDFAQSLLRDPNTPIVRKSRGTSTQGTSTHASSTQLAMLDDQRSKAGSVQSKVSSYHGSLHRSRDGRYTPCSYRGIEERLPHGSMSHLTDHSRHSSTHRLNEQSHQGSIRDLSNPLAHISHGTSMNRVIEADATSA
| null | null |
canonical Wnt signaling pathway [GO:0060070]; nervous system development [GO:0007399]; neural crest cell fate specification [GO:0014036]; non-canonical Wnt signaling pathway [GO:0035567]; regulation of protein localization [GO:0032880]
|
apical plasma membrane [GO:0016324]; cell surface [GO:0009986]
|
G protein-coupled receptor activity [GO:0004930]; 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
| null |
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell surface {ECO:0000250|UniProtKB:Q61086}. Apical cell membrane {ECO:0000250|UniProtKB:Q61086}; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Receptor for Wnt proteins. Most of 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. Activated by Wnt8. Involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Plays a role in controlling early axon growth and guidance processes necessary for the formation of a subset of central and peripheral major fiber tracts. Involved in the migration of cranial neural crest cells. May also be implicated in the transmission of sensory information from the trunk and limbs to the brain. Controls commissural sensory axons guidance after midline crossing along the anterior-posterior axis in the developing spinal cord in a Wnt-dependent signaling pathway. Together with FZD6, is involved in the neural tube closure and plays a role in the regulation of the establishment of planar cell polarity (PCP). Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle in a beta-catenin-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q61086}.
|
Xenopus laevis (African clawed frog)
|
O42601
|
S17B1_XENLA
|
MSSPDCGYSSDDQIQGSCSVPMMMGQYQWTEPLTVFQDLKPKRDEGSADSRSKAEGRIRRPMNAFMVWAKDERKRLAQQNPDLHNAELSKMLGKSWKSLTLATKRPFVEEAERLRVQHIQDYPDYKYRPRRKKQVKRMKREEDGFLPSANFPGSQIMDNNVMVGENYRMQYSAQNHQQNQLPPAGYFEGHNSMGYYYRDYSVPNYHISQNSSGYDSPPAQDEYQALSYSFNSSYMPYQQNATTPVMAKQMAVTQNIPQESPEHGMMASPQMYNRQMYVSECAKTHPMAQTEQHFPSYQSQKTVRQNYLQSQQDGHLESDIDKTEFDQYLMYEPKADMEIIYTIDQDSGAYSTNLLPSLITEANNVCYYDYCGV
| null | null |
cell differentiation [GO:0030154]; endoderm development [GO:0007492]; gastrulation [GO:0007369]; midgut development [GO:0007494]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of Wnt signaling pathway [GO:0030178]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; Wnt signaling pathway [GO:0016055]
|
nucleus [GO:0005634]
|
beta-catenin binding [GO:0008013]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]
|
PF00505;
|
1.10.30.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:9363948}.
| null | null | null | null | null |
FUNCTION: Transcription activator. Doesn't appear to bind to the consensus 5'-AACAAT-3' DNA binding site, but binds 5'-ATTGTT-3'. All of the sox17 proteins are required for embryonic endoderm development and gastrulation movements, and show some redundancy in function. In addition, the sox17 proteins have distinct but overlapping roles in later gut development. Acts downstream of vegt-signaling in endoderm differentiation to induce a range of endodermal genes both directly and indirectly. Also represses wnt-responsive genes to inhibit wnt/beta-catenin-mediated signaling. {ECO:0000269|PubMed:10549281, ECO:0000269|PubMed:11091074, ECO:0000269|PubMed:12591603, ECO:0000269|PubMed:15157240, ECO:0000269|PubMed:15163629, ECO:0000269|PubMed:15302595, ECO:0000269|PubMed:16193513, ECO:0000269|PubMed:16278889, ECO:0000269|PubMed:16651540, ECO:0000269|PubMed:17719026, ECO:0000269|PubMed:18651654, ECO:0000269|PubMed:19003160, ECO:0000269|PubMed:9363948}.
|
Xenopus laevis (African clawed frog)
|
O42606
|
NGN1_DANRE
|
MEIVYSDMETSSCDYSFSHTDDEDSRSSLHPASPASSCGKPPASPAGLQQKKRRRGRARNETTVHVVKKNRRLKANDRERNRMHNLNDALDALRSVLPAFPDDTKLTKIETLRFAHNYIWALSETIRIADQKQGKSRDGPLLLPGLSCMADAPSPGSDSCSWPSGASSSSSSPSYCNSDPGSPAAMDDFGYLQTDVVYSYRNFVPSIY
| null | null |
anterior lateral line nerve development [GO:0048909]; axon development [GO:0061564]; axon regeneration [GO:0031103]; axonal fasciculation [GO:0007413]; dorsal spinal cord development [GO:0021516]; forebrain development [GO:0030900]; forebrain neuron development [GO:0021884]; generation of neurons [GO:0048699]; habenula development [GO:0021986]; hindbrain morphogenesis [GO:0021575]; negative regulation of neurogenesis [GO:0050768]; nervous system development [GO:0007399]; neuromast development [GO:0048884]; olfactory bulb development [GO:0021772]; olfactory placode development [GO:0071698]; peripheral nervous system development [GO:0007422]; peripheral nervous system neuron development [GO:0048935]; positive regulation of DNA-binding transcription factor activity [GO:0051091]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of transcription by RNA polymerase II [GO:0045944]; posterior lateral line nerve development [GO:0048918]; sensory organ development [GO:0007423]
|
nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; E-box binding [GO:0070888]; protein dimerization activity [GO:0046983]
|
PF00010;
|
4.10.280.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Transcriptional regulator. Activates transcription by binding to the E box-containing promoter (By similarity). Mediates neuronal differentiation. Required for the development of Rohon-Beard spinal sensory neurons and dorsal root ganglion neurons, but not for primary motoneurons or autonomic neurons. Required for development of all cranial ganglia but not associated glial cells. Regulates epiphysial neurogenesis, acting partially redundantly with ascl1a and downstream of flh. Required for the development of basal forebrain dopaminergic neurons; involved in the specification of dopaminergic progenitor cells. May be involved in maintaining rhombomere boundaries in the hindbrain. {ECO:0000250, ECO:0000269|PubMed:12015292, ECO:0000269|PubMed:12413897, ECO:0000269|PubMed:12702659, ECO:0000269|PubMed:15659486, ECO:0000269|PubMed:16549779, ECO:0000269|PubMed:9409673, ECO:0000269|PubMed:9469669}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O42634
|
DMC1_SCHPO
|
MEEFAEGNDDEQMIFSDIEDLTAHGIGMTDIIKLKQAGVCTVQGVHMSTKRFLLKIKGFSEAKVDKLKEAASKMCPANFSTAMEISQNRKKVWSISTGSEALNGILGGGIQSMSITEVFGEFRCGKTQMSHTLCVTAQLPRDMGGAEGKVAFIDTEGTFRPDRIKAIAERFGVDADQAMENIIVSRAYNSEQQMEYITKLGTIFAEDGQYRLLIVDSIMALFRVDYSGRGELSERQQKLNIMLARLNHISEEFNVAVFVTNQVQADPGAAMMFASNDRKPVGGHVMAHASATRLLLRKGRGEERVAKLNDSPDMPEAECSYVITPGGIADVS
| null | null |
chromosome organization involved in meiotic cell cycle [GO:0070192]; DNA recombinase assembly [GO:0000730]; DNA strand invasion [GO:0042148]; meiotic gene conversion [GO:0006311]; meiotic joint molecule formation [GO:0000709]; meiotic strand invasion involved in reciprocal meiotic recombination [GO:0010774]; mitotic recombination [GO:0006312]; protein homooligomerization [GO:0051260]; reciprocal meiotic recombination [GO:0007131]
|
condensed nuclear chromosome [GO:0000794]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; ATP-dependent DNA damage sensor activity [GO:0140664]; DNA strand exchange activity [GO:0000150]; double-stranded DNA binding [GO:0003690]; identical protein binding [GO:0042802]; single-stranded DNA binding [GO:0003697]; Swi5-Sfr1 complex binding [GO:1905334]
|
PF08423;
|
1.10.150.20;3.40.50.300;
|
RecA family, DMC1 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Required for meiotic recombination and cell cycle progression. Binds to single and double-stranded DNA, in the presence of magnesium, and exhibits DNA-dependent ATPase activity. Promotes DNA strand annealing and strand exchange via DNA recombinase activity and forms helical and stacked ring nucleoprotein filaments. {ECO:0000269|PubMed:10908327, ECO:0000269|PubMed:15899844}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O42649
|
SMC3_SCHPO
|
MYITKIVIQGFKSYKDYTVIEPLSPHHNVIVGRNGSGKSNFFAAIRFVLSDAYTHLSREERQALLHEGPGATVMSAYVEVTFANADNRFPTGKSEVVLRRTIGLKKDEYSLDKKTVSKTEVINLLESAGFSRSNPYYIVPQGRVTSLTNAKDSERLELLKEVAGTQIYENRRAESNKIMDETIQKSEKIDELLQYIEERLRELEEEKNDLAVYHKKDNERRCLEYAIYSREHDEINSVLDALEQDRIAALERNDDDSGAFIQREERIERIKAEITELNHSLELLRVEKQQNDEDYTNIMKSKVALELQSSQLSRQIEFSKKDESSKLNILSELESKISEKENELSEILPKYNAIVSEADDLNKRIMLLKNQKQSLLDKQSRTSQFTTKKERDEWIRNQLLQINRNINSTKENSDYLKTEYDEMENELKAKLSRKKEIEISLESQGDRMSQLLANITSINERKENLTDKRKSLWREEAKLKSSIENVKDDLSRSEKALGTTMDRNTSNGIRAVKDIAERLKLEGYYGPLCELFKVDNRFKVAVEATAGNSLFHIVVDNDETATQILDVIYKENAGRVTFMPLNKLRPKAVTYPDASDALPLIQYLEFDPKFDAAIKQVFSKTIVCPSIETASQYARSHQLNGITLSGDRSDKKGALTAGYRDYRNSRLDAIKNVKTYQIKFSDLQESLEKCRSEIESFDQKITACLDDLQKAQLSLKQFERDHIPLKDELVTITGETTDLQESMHHKSRMLELVVLELHTLEQQANDLKSELSSEMDELDPKDVEALKSLSGQIENLSHEFDAIIKERAHIEARKTALEYELNTNLYLRRNPLKAEIGSDNRIDESELNSVKRSLLKYENKLQIIKSSSSGLEEQMQRINSEISDKRNELESLEELQHEVATRIEQDAKINERNAAKRSLLLARKKECNEKIKSLGVLPEEAFIKYVSTSSNAIVKKLHKINEALKDYGSVNKKAYEQFNNFTKQRDSLLARREELRRSQESISELTTVLDQRKDEAIERTFKQVAKSFSEIFVKLVPAGRGELVMNRRSELSQSIEQDISMDIDTPSQKSSIDNYTGISIRVSFNSKDDEQLNINQLSGGQKSLCALTLIFAIQRCDPAPFNILDECDANLDAQYRSAIAAMVKEMSKTSQFICTTFRPEMVKVADNFYGVMFNHKVSTVESISKEEAMAFVEG
| null | null |
cell division [GO:0051301]; chromatin looping [GO:0140588]; mitotic sister chromatid cohesion [GO:0007064]
|
chromosome [GO:0005694]; cohesin complex [GO:0008278]; condensed chromosome, centromeric region [GO:0000779]; cytosol [GO:0005829]; meiotic cohesin complex [GO:0030893]; mitotic cohesin complex [GO:0030892]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cohesin loader activity [GO:0061775]; DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]
|
PF06470;PF02463;
|
1.20.1060.20;3.30.70.1620;3.40.50.300;
|
SMC family, SMC3 subfamily
|
PTM: Acetylation at Lys-105 and Lys-106 by ECO1 is important for genome stability and S phase sister chromatid cohesion. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11069892}. Chromosome {ECO:0000269|PubMed:11069892}. Note=Associates with chromatin. Before prophase it is scattered along chromosome arms. At anaphase, the rad21 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation.
| null | null | null | null | null |
FUNCTION: Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. {ECO:0000269|PubMed:11069892}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O42661
|
SMD1_SCHPO
|
MKLVRFLMKLTNETVSIELKNGTIVHGTITSVDMQMNTHLKAVKMTVKGREPVPVETLSIRGNNIRYYILPDSLPLDTLLIDDSTKPKQKKKEVVRGRGRGRGRGTRGRGRGASRGF
| null | null |
mRNA 5'-splice site recognition [GO:0000395]; spliceosomal snRNP assembly [GO:0000387]
|
catalytic step 2 spliceosome [GO:0071013]; commitment complex [GO:0000243]; cytosol [GO:0005829]; nucleus [GO:0005634]; pICln-Sm protein complex [GO:0034715]; 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]
|
mRNA binding [GO:0003729]; RNA binding [GO:0003723]
|
PF01423;
|
2.30.30.100;
|
SnRNP core protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:24298023}. Cytoplasm {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:24298023}. Note=Localizes to the nucleus predominantly. {ECO:0000269|PubMed:24298023}.
| 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:P62314}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O42667
|
SSM4_SCHPO
|
MSYLSVGDEVLIRGELGIVRFAGSTDFESGIWLGVELLNGKGKNDGSVKGKRYFSCEKGKGIFVRACSSNVMKRPSVVKSRKKGSENISNFMEKTKAIKQKSRREPSKFERSLARPLCITPIDSSTPTKTATFYTSSTTENLDELNFSTEELSSFDTTLLNSDTSKLSGLDDSSFMEEEFVWQVDNVLQECEKKFTPHSKGSYLKENLKSELRKGRLDELMCENTALKEKIDKLNKELEKVEPQLTFLRSKNSIEKPRNFRREKFLKKFLAMQKEIKYLRKRKLQIRKIPNYKYSDRSLNSKTPKSQDNWTTQVTPSSLLGVSEVSKVLQLKQVQVDITELVKIPKNPFSEKLTISNVNRYLNIVPGSLDLQFSLTNENFVHWNSTVYQELLNLKSNNSSVDGVKTRRQLLEENALLSHKVLKLTEEIQDLETLNQLNTEIEARQSEKLNEVQEETQRLSQLLISSQPALTEVKHLKLCLSDSQEELLQLNAKLEKANIVIDELNSAKLKLSKQVEEESSMKDDLTEMNQRLKEQIESYENEVNSEITSRTLKEFETLKTQYEKNLCNLREQLKTARMKLADKYPQGDNTSENIDWLKHSLRDSNTENSIPSPLTFACKEIRKLVADIKPVSVEKQLALNWKKDIERPSFHHNQQLFNYCQLTDILSKKC
| null | null |
cytoplasmic microtubule organization [GO:0031122]; dynein-driven meiotic oscillatory nuclear movement [GO:0030989]; establishment of mitotic spindle orientation [GO:0000132]; meiosis I [GO:0007127]; nuclear migration involved in conjugation with cellular fusion [GO:0000743]
|
cell cortex of cell tip [GO:0051285]; cell tip [GO:0051286]; cortical microtubule plus-end [GO:1903754]; cytoplasmic microtubule [GO:0005881]; dynactin complex [GO:0005869]; kinetochore [GO:0000776]; meiotic spindle pole body [GO:0035974]; microtubule associated complex [GO:0005875]; microtubule cytoskeleton [GO:0015630]; mitotic spindle [GO:0072686]; nucleus leading edge [GO:0110092]; spindle [GO:0005819]; spindle pole [GO:0000922]; spindle pole body [GO:0005816]
|
microtubule plus-end binding [GO:0051010]
|
PF01302;
|
2.30.30.190;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle. Note=Mitotic spindle.
| null | null | null | null | null |
FUNCTION: Binds to nuclear microtubules with the effect of either modifying their structure or function. This then promotes meiotic nuclear division.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O42709
|
MCM10_SCHPO
|
MHDPFIAEENDLDLEEKRLQRQLNEIQEKKRLRSAQKEASSENAEVIQVPRSPPQQVRVLTVSSPSKLKSPKRLILGIDKGKTGKDVSLGKGPRGPLPKPFHERLAEARNQERKRSDKLKTMKKNRKQSFQRKRNILEDGKSEEEKFPMKCDEIDPYSRQAIVIRYISDEVAKENIGGNQVYLIHQLLKLVRAPKFEAPEVDNYVVMGIVASNSGTRETVNGNKYCMLTLTDLKWQLECFLFGKAFERYWKIQSGTVIALLNPEVLKPKNPDIGRFSLKLDSEYDVLLEIGRSKHLGYCSSRRKSGELCKHWLDKRAGDVCEYHVDLAVQRSMSTRTEFASSMATMHEPRARREKRFRGQGFQGYFAGEKYSAIPNAVAGLYDAEDAVQTERERKERYKKQRAQAEREREILVRLSKRCCASSSSSSNSNNLSTGMSMRTLGHQYLNLQGSGVKNLHDKGNPTALSKDSEIDSSTKKPSVLASFNASIMNPKSSLPSFSNSAILGTNDAASGTPVPQDTTSTKVSPAVVFTSSPRIFSPQSLRKIGFDPTHSADASTTHSTATGLSRSGSLKNIKFRYEFTESDDEDDLEIVP
| null | null |
cell division [GO:0051301]; DNA replication initiation [GO:0006270]; mitotic DNA replication initiation [GO:1902975]
|
chromatin [GO:0000785]; nuclear replication fork [GO:0043596]; site of double-strand break [GO:0035861]
|
DNA primase activity [GO:0003896]; DNA replication origin binding [GO:0003688]; MCM complex binding [GO:1904931]; metal ion binding [GO:0046872]; single-stranded DNA binding [GO:0003697]
|
PF09329;
|
2.40.50.140;
|
MCM10 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10783164}. Note=Associates with chromatin.
| null | null | null | null | null |
FUNCTION: Required for DNA synthesis. Required for entry into or completion of S phase. Involved in DNA replication and seems to participate in the activation of the pre-replication complex (pre-RC) and in transcription elongation. May play a role as key coordinator in assembling the replication fork. Proposed to function at replication origins following the binding of the mcm2-7 complex prior to the recruitment of sna41. Probably is required to stimulate phosphorylation of the mcm2-7 complex by the dfp1-hsk1 kinase complex. May recruit the DNA polymerase alpha:primase complex to replication origins and is required to maintain it on chromatin independently of sna41. May have primase activity. Binds to single-stranded DNA. {ECO:0000269|PubMed:10783164, ECO:0000269|PubMed:12604790, ECO:0000269|PubMed:14766746, ECO:0000269|PubMed:16720577, ECO:0000269|PubMed:9745018}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O42721
|
MP1_TALMA
|
MKFLSSLVVLGLSAQALASPYVDHQATKDQRDVNVFKQVLQDINLDVQKFDQDITQYQGGDPTVLLADSDAIIKTTEEGIQRIGPQPPLSVTEALALVGPVQGVNKLIMKAVDHLIEKKGPLVGGGYGPQVKDSLERQAHAASKLSELVSSKVPSPLAPISKQLSDQVAQALQKGIQAFSISARQATKVKREATKVQRDISAFKKVIQNISLAVNKFNVDIERYVGGDASHLLADGNVLIKATLDGVQSLQNEPPLSSMEALALVGPVQDLSNQILLAIQNLIDKKEPLVQAGFGGKVENNLRQQEEAAQKLSELVSTKVPHELADISRQLSDGIAAGIKKGIDAFAGTGPAPTTSSTPEASTAPAPSTPPQTPEDTLVPATSTPAPGPAPTAPDSSMVWPTSTTASPDVQPTITSSGTSVPAAPTGGNSSPAVPAFTGAASANQVSGAVGLAAGLLAVLAF
| null | null |
fungal-type cell wall organization [GO:0031505]
|
extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]; hyphal cell wall [GO:0030446]; yeast-form cell wall [GO:0030445]
|
fatty acid binding [GO:0005504]; structural constituent of cell wall [GO:0005199]
|
PF12296;
|
1.20.1280.140;6.10.140.790;
|
Cell wall mannoprotein 1 family
|
PTM: Mannoprotein, glycosylated. {ECO:0000269|PubMed:9488383}.
|
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:10074513, ECO:0000269|PubMed:9488383}. Note=Associated with the entire thickness of the cell walls of yeast and conidia found in mold form. Localizes on the outer layers of the hyphal cell walls. {ECO:0000269|PubMed:9488383}.
| null | null | null | null | null |
FUNCTION: Constitutive protein of the cell wall. Binds fatty acids and may thus serve as a fatty acid transporter between P.marneffei and host cells during infection (PubMed:20053994). Abundant antigen target of host humoral immune response (PubMed:9488383). {ECO:0000269|PubMed:20053994, ECO:0000269|PubMed:9488383}.
|
Talaromyces marneffei (Penicillium marneffei)
|
O42766
|
1433_CANAL
|
MPASREDSVYLAKLAEQAERYEEMVENMKAVASSGQELSVEERNLLSVAYKNVIGARRASWRIVSSIEQKEEAKGNESQVALIRDYRAKIEAELSKICEDILSVLSDHLITSAQTGESKVFYYKMKGDYHRYLAEFAIAEKRKEAADLSLEAYKAASDVAVTELPPTHPIRLGLALNFSVFYYEILNSPDRACHLAKQAFDDAVADLETLSEDSYKDSTLIMQLLRDNLTLWTDLSEAPAATEEQQQSSQAPAAQPTEGKADQE
| null | null |
cellular response to heat [GO:0034605]; cellular response to neutral pH [GO:0036244]; chlamydospore formation [GO:0001410]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms [GO:0044182]; filamentous growth of a population of unicellular organisms in response to biotic stimulus [GO:0036180]; filamentous growth of a population of unicellular organisms in response to heat [GO:0036168]; filamentous growth of a population of unicellular organisms in response to neutral pH [GO:0036178]; positive regulation of filamentous growth of a population of unicellular organisms in response to biotic stimulus [GO:1900445]; positive regulation of filamentous growth of a population of unicellular organisms in response to neutral pH [GO:1900442]; regulation of carbohydrate metabolic process [GO:0006109]; regulation of mitotic cell cycle [GO:0007346]; signal transduction [GO:0007165]
|
cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular vesicle [GO:1903561]; plasma membrane [GO:0005886]; yeast-form cell wall [GO:0030445]
|
phosphoserine residue binding [GO:0050815]
|
PF00244;
|
1.20.190.20;
|
14-3-3 family
| null | null | null | null | null | null | null | null |
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
|
O42773
|
PP2B1_CRYNH
|
MASPATQTANAIAAINNRSNLVIPEIDFTQHQLENGEIVSTTERVIKDVQAPAMYVPTDDQFWSKVDKTKPDIAFLKNHFYREGRLTEEQALYILEKGGELLRSEPNLLEVDAPITVCGDIHGQYYDLMKLFEVGGNPADTRYLFLGDYVDRGYFSIECVLYLWSLKMWYPDTLFLLRGNHECRHLTDYFTFKLECKHKYSETVYNACMESFCNLPLAAVMNKQFLCIHGGLSPELHTLDDLRSINRFREPPTQGLMCDILWADPLEDFGSEKTNENFLHNHVRGCSYFFTYNAACQFLERNNLLSIIRAHEAQDAGYRMYRKTKTTGFPSVMTIFSAPNYLDVYSNKAAVLKYESNVMNIRQFNCTPHPYWLPNFMDVFTWSLPFVGEKITDMLIAILNCCTKEELEEEDEEFPLNAPEPTDAESAAERRQIIKNKILAVGRMSRVFSLLREESERVSELKSISGSNALPAGMLASGAEGIKEAIQGFEDARKSDIENERLPPDIIDPDEDKPASPSASPIMPATPEEIPSEIPYDSPITGTPRTPISSAIASGSPGSPGTPTSPSIGGPPLTAWRPGHGRRTSLGTTKTSPSTRRRSLENTMHLIRDVVGGKDAQGDGQLERLAEVISSPTKGGQGE
|
3.1.3.16
|
COFACTOR: Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000250}; Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
|
calcineurin-mediated signaling [GO:0097720]; cellular response to calcium ion [GO:0071277]; fungal-type cell wall organization [GO:0031505]; intracellular signal transduction [GO:0035556]; negative regulation of calcium ion import across plasma membrane [GO:1905949]; positive regulation of mitotic actomyosin contractile ring contraction [GO:1903473]; positive regulation of mitotic division septum assembly [GO:0140281]; positive regulation of protein localization to nucleus [GO:1900182]; regulation of cell morphogenesis [GO:0022604]
|
calcineurin complex [GO:0005955]; mitotic actomyosin contractile ring, intermediate layer [GO:0120105]
|
calmodulin binding [GO:0005516]; calmodulin-dependent protein phosphatase activity [GO:0033192]; ferric iron binding [GO:0008199]; myosin phosphatase activity [GO:0017018]; zinc ion binding [GO:0008270]
|
PF00149;
|
3.60.21.10;
|
PPP phosphatase family, PP-2B subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16;
| null | null | null | null |
FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin (By similarity). {ECO:0000250}.
|
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
|
O42777
|
TREB_EMENI
|
MDDSALPSNTSNGINGRTAHRRSSSGGDPFQHPDIYYGNPESVERIKNRRRAFSSSLKSFNRQDFHEMLGDRNTRRGSMDPTSGNPRKFLIDVDATLHSLLEREDSDRNMQITIEDVGPKVFSLGTAASHGYNRFDVRGTYMLSNLLQELTIAKDYGRKQIVLDEERLSENPVSRLSRLIKNSFWNSLTRRIDGRNIEVAGRDPKDWTDDPRPRIYVPPGAPEQLEYYRRIAEEKPELRLDVQELAAEITPEYVRDLNEKPGLLALAMEEKYDEKTGKTDFAGVPFVVPGGRFNELYGWDSYMESLGLLASNRVDLAKAMVINFCFCIKHYGKILNANRSYYLTRSQPPFLTDMALRVYDRIQNEPGAMDFLRHAILAAIKEYYSVWMAEPRLDPVSGLSRYRSPGIGVPPETEASHFLHLLTPYAEKHGMEFKEFVQAYNYGKVKEPELDEYFMHDRAVRESGHDTSYRLERVCGNLATVDLNSLLYKYEVDIARVIRVYFKDKLEIPVEFRTPATKDIQSESSSVWDRRARRRKMRMDTYLWDEEKGMYFDYDTVKQERTNYESATTLWAMWAGLVTPRQASAMITKALPRFEEFGGIVSGTEESRGAVGLNRPTRQWDYPYGWAPQQMLAWTGFARYGYQEEAERLAYKWLYMITKAFVDFNGVVVEKYDVTRPIDPHRVDAEYGNQGVDFKGAPREGFGWVNASYVYGLEMLNAHQRRALGAVTPWETYSKAVSAQGSDTVLENRSE
|
3.2.1.28
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P32356};
|
ascospore formation [GO:0030437]; cellular response to heat [GO:0034605]; cellular response to starvation [GO:0009267]; trehalose catabolic process [GO:0005993]
|
alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) [GO:0005946]
|
alpha,alpha-trehalase activity [GO:0004555]; calcium ion binding [GO:0005509]; trehalase activity [GO:0015927]
|
PF01204;PF07492;
|
1.50.10.10;
|
Glycosyl hydrolase 37 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32356}.
|
CATALYTIC ACTIVITY: Reaction=alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-glucose; Xref=Rhea:RHEA:32675, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903, ChEBI:CHEBI:16551, ChEBI:CHEBI:17925; EC=3.2.1.28; Evidence={ECO:0000305|PubMed:10320571};
| null |
PATHWAY: Carbohydrate degradation. {ECO:0000305}.
| null | null |
FUNCTION: Hydrolyzes intracellular trehalose to glucose (Probable). The disaccharide trehalose serves as a storage carbohydrate that is mobilized during conidial germination (PubMed:10320571). Regulates the level of trehalose as a protectant for cell integrity during heat stress (PubMed:10320571). {ECO:0000269|PubMed:10320571, ECO:0000305|PubMed:10320571}.
|
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
|
O42779
|
CARP9_CANAX
|
MRLNSVALLSLVATALAAKAPFKIDFEVRRGESKDDLSPEDDSNPRFVKRDGSLDMTLTNKQTFYMATLKIGSNEDENRVLEDTGSSDLWVMSHDLKCVSAPISKRNERSFGHGTGVKLNERELMQKRKNLYQPSRTIETDEEKEASEKIHNKLFGFGSIYSTVYITEGPGAYSTFSPLVGTEGGSGGSGGSNTCRSYGSFNTENSDTFKKNNTNDFEIQYADDTSAIGIWGYDDVTISNVTVKDLSFAIANETSSDVGVLGIGLPGLEVTTQLRYTYQNLPLKLKADGIIAKSLYSLYLNTADAKAGSILFGAIDHAKYQGDLVTVKMMRTYSQISYPVRIQVPVLKIDVESSSGSTTNILSGTTGVVLDTGSTLSYVFSDTLQSLGKALNGQYSNSVGAYVVNCNLADSSRTVDIEFGGNKTIKVPISDLVLQASKSTCILGVMQQSSSSSYMLFGDNILRSAYIVYDLDDYEVSLAQVSYTNKESIEVIGASGITNSSGSGTTSSSGTSTSTSTRHSAGSIISNPVYGLLLSLLISYYVLV
|
3.4.23.24
| null |
fungal-type cell wall organization [GO:0031505]; proteolysis [GO:0006508]
|
extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
|
aspartic-type endopeptidase activity [GO:0004190]
|
PF00026;
|
2.40.70.10;
|
Peptidase A1 family
|
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer. {ECO:0000269|PubMed:21646240}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. Secreted, cell wall {ECO:0000269|PubMed:16269404, ECO:0000269|PubMed:21622905}.
|
CATALYTIC ACTIVITY: Reaction=Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 of insulin B chain. Activates trypsinogen, and degrades keratin.; EC=3.4.23.24; Evidence={ECO:0000269|PubMed:21646240, ECO:0000269|PubMed:27390786, ECO:0000269|PubMed:29143452, ECO:0000269|PubMed:31675138};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5 using casein-resorufin as substrate, and 6.0-7.0, the pH of the saliva, for cleavage of Hst 5. {ECO:0000269|PubMed:21646240, ECO:0000269|PubMed:27390786, ECO:0000269|PubMed:29143452};
| null |
FUNCTION: Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors (PubMed:15820985, PubMed:16269404, PubMed:19805528). These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense (PubMed:15820985, PubMed:16269404, PubMed:19805528). Moreover, acts toward human hemoglobin though limited proteolysis to generate a variety of antimicrobial hemocidins, enabling to compete with the other microorganisms of the same physiological niche using the microbicidal peptides generated from the host protein (PubMed:23927842). {ECO:0000269|PubMed:15820985, ECO:0000269|PubMed:16269404, ECO:0000269|PubMed:19805528, ECO:0000269|PubMed:23927842}.; FUNCTION: Plays a key role in defense against host by cleaving histatin-5 (Hst 5), a peptide from human saliva that carries out fungicidal activity (PubMed:27390786, PubMed:29143452, PubMed:31675138). The cleavage rate decreases in an order of SAP2 > SAP9 > SAP3 > SAP7 > SAP4 > SAP1 > SAP8 (PubMed:27390786). The first cleavage occurs between residues 'Lys-17' and 'His-18' of Hst 5, giving DSHAKRHHGYKRKFHEK and HHSHRGY peptides (PubMed:27390786). Simultaneously, the DSHAKRHHGYKRK peptide is also formed (PubMed:27390786). Further fragmentation by SAP9 results in FHEK product (PubMed:27390786). {ECO:0000269|PubMed:27390786, ECO:0000269|PubMed:29143452, ECO:0000269|PubMed:31675138}.
|
Candida albicans (Yeast)
|
O42781
|
MAPK2_PNECA
|
MTASSRNVRFNVSDDYEILDVIGEGAYGIVCSAIHKPSGQKVAIKKISPFDHSMFCLRTLREMKLLRYFNHENIISILDIQQPQDFESFSEVYLIQELMETDMHRVIRTQDLSDDHCQYFIYQILRALKAMHSADILHRDLKPSNLLLNANCDLKVCDFGLARSAVSTEDSSSFMTEYVATRWYRAPEIMLTFKEYTKAIDIWSVGCILAEMLSGRPLFPGKDYHHQLMLILDVLGTPTMEDYYGIKSRRAREYIRSLPFKKRVSFASIFPRANPLALDLLEKLLAFNPAKRVTAEEALQHNYLEPYHDPDDEPTAPPISPSFFDFDRIKDSLTKNDLKILIYKEIMSMNN
|
2.7.11.24
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:12965219}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:12965219}; Note=Divalent cations including magnesium and manganese. {ECO:0000269|PubMed:12965219};
|
mitotic cell cycle G1 arrest in response to pheromone [GO:0000751]; pheromone-dependent signal transduction involved in conjugation with cellular fusion [GO:0000750]; phosphorylation [GO:0016310]; response to pheromone [GO:0019236]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily
|
PTM: Dually phosphorylated on Thr-176 and Tyr-178, which activates the enzyme. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P27638}.
|
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=2.7.11.24; Evidence={ECO:0000269|PubMed:9688951}; 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=2.7.11.24; Evidence={ECO:0000269|PubMed:9688951};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:12965219};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30-35 degrees Celsius. {ECO:0000269|PubMed:12965219};
|
FUNCTION: Serine-threonine protein kinase which may be involved in pheromone signaling. Functionally complements the MAPK pheromone signaling pathway in S.cerevisiae. {ECO:0000269|PubMed:12965219, ECO:0000269|PubMed:9688951}.
|
Pneumocystis carinii
|
O42807
|
FAEA_ASPNG
|
MKQFSAKYALILLATAGQALAASTQGISEDLYNRLVEMATISQAAYADLCNIPSTIIKGEKIYNAQTDINGWILRDDTSKEIITVFRGTGSDTNLQLDTNYTLTPFDTLPQCNDCEVHGGYYIGWISVQDQVESLVKQQASQYPDYALTVTGHSLGASMAALTAAQLSATYDNVRLYTFGEPRSGNQAFASYMNDAFQVSSPETTQYFRVTHSNDGIPNLPPADEGYAHGGVEYWSVDPYSAQNTFVCTGDEVQCCEAQGGQGVNDAHTTYFGMTSGACTW
|
3.1.1.73
| null |
cell wall macromolecule catabolic process [GO:0016998]; cellulose catabolic process [GO:0030245]; lipid metabolic process [GO:0006629]; pectin catabolic process [GO:0045490]; xylan catabolic process [GO:0045493]
|
extracellular region [GO:0005576]
|
cellulose binding [GO:0030248]; feruloyl esterase activity [GO:0030600]
|
PF01764;
|
3.40.50.1820;
|
AB hydrolase superfamily, FaeA family
|
PTM: Glycosylated. {ECO:0000305|PubMed:17027758}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9406381, ECO:0000269|Ref.5}.
|
CATALYTIC ACTIVITY: Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.; EC=3.1.1.73;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.31 mM for methyl ferulate {ECO:0000269|PubMed:17027758};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0. {ECO:0000269|PubMed:17027758};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55-60 degrees Celsius. {ECO:0000269|PubMed:17027758};
|
FUNCTION: Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-galactose ester bond in pectin. Binds to cellulose. {ECO:0000269|PubMed:11931668, ECO:0000269|PubMed:15081808, ECO:0000269|PubMed:17027758, ECO:0000269|PubMed:7805053, ECO:0000269|PubMed:9406381, ECO:0000269|PubMed:9649839, ECO:0000269|Ref.5}.
|
Aspergillus niger
|
O42844
|
KCC2_SCHPO
|
MSILAGFKNLLKHSKSSKGRSNASKSVDVSVNRDVAAYTELAAKNVNAGGDEEIRVANYPGLEKYQLIENLGDGAFSQVYKAYSIDRKEHVAVKVIRKYEMNKKQRQGVFKEVNIMRRVKHKNVVNLFDFVETEDFYHLVMELAEGGELFHQIVNFTYFSENLARHIIIQVAEAVKHLHDVCGIVHRDIKPENLLFQPIEYLPSQNYTPPSLEPNKLDEGMFLEGIGAGGIGRILIADFGFSKVVWNSKTATPCGTVGYAAPEIVNDELYSKNVDMWAMGCVLHTMLCGFPPFFDENIKDLASKVVNGEFEFLSPWWDDISDSAKDLITHLLTVDPRERYDIHQFFQHPWIKGESKMPENFTYKPKLHGTPGGPKLSLPRSLVSKGEIDIPTTPIKSATHPLLSSYSEPKTPGVSSVHEAMGVAYDIRRLNHLGFSPEQLSKKSMNTGSIKELILDEETTTDDDDYIISSFPLNDTLGSEGKDPFSLNLKESSLYSRRSAKRVN
|
2.7.11.17
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:12135745};
|
cellular response to oxidative stress [GO:0034599]; mitotic DNA damage checkpoint signaling [GO:0044773]; negative regulation of G2/M transition of mitotic cell cycle [GO:0010972]; phosphorylation [GO:0016310]
|
ascus epiplasm [GO:0072324]; cell cortex [GO:0005938]; cell cortex of cell tip [GO:0051285]; cytoplasm [GO:0005737]; division septum [GO:0000935]; nucleus [GO:0005634]; prospore membrane [GO:0005628]
|
ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; 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, CAMK Ser/Thr protein kinase family, CaMK subfamily
|
PTM: Autophosphorylated. {ECO:0000269|PubMed:12135745, ECO:0000269|PubMed:18257517}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12135745, ECO:0000269|PubMed:12589433}. Barrier septum {ECO:0000269|PubMed:12589433}. Forespore membrane {ECO:0000269|PubMed:12589433}. Ascus epiplasm {ECO:0000269|PubMed:12589433}.
|
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=2.7.11.17; Evidence={ECO:0000269|PubMed:12135745}; 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=2.7.11.17; Evidence={ECO:0000269|PubMed:12135745};
| null | null | null | null |
FUNCTION: Has a role in the regulation of G2/M transition during the mitotic cell cycle. {ECO:0000269|PubMed:12135745, ECO:0000269|PubMed:12589433}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O42860
|
BUB3_SCHPO
|
MNFSKTLLKNSKDGISSVIFSPSVKNELIAGCWDGSLLHYQISENPELLGKYDLSSPILSLEYTDEKTALVGNLDGTVTTLDLNTRNHEFLGNHGKGVSCISKLRLENCFISGSWDKSFRVWDVRVKQPVEGQDIGKKIFASSSRDNILVLGCSERENLVYDIRNLKLPFQRRPSSFKYMTRSVCCNQNFEGFVSSSIEGRTSVEYINPSQEAQSKNFTFKCHRQIQKDYDIVYPVNDLKFHPIHQTLATAGGDGVVAFWDIQVRKRLRVLNPSKINISSISFNVDGSMLAIATCAQEEAAGNIYVHALESNFAAPKLKS
| null | null |
cell division [GO:0051301]; mitotic metaphase chromosome recapture [GO:1990942]; mitotic sister chromatid biorientation [GO:1990758]; mitotic spindle assembly checkpoint signaling [GO:0007094]; negative regulation of mitotic spindle assembly checkpoint signaling [GO:0140499]
|
bub1-bub3 complex [GO:1990298]; kinetochore [GO:0000776]; mitotic checkpoint complex [GO:0033597]; nucleoplasm [GO:0005654]
|
ubiquitin binding [GO:0043130]
|
PF00400;
|
2.130.10.10;
|
WD repeat BUB3 family
|
PTM: Phosphorylated by bub1. {ECO:0000269|PubMed:15509783}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15509783}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:15509783}. Chromosome, centromere {ECO:0000269|PubMed:15509783}. Note=Associates with kinetochores and centromeres during the early stages of mitosis.
| null | null | null | null | null |
FUNCTION: Involved in cell cycle checkpoint enforcement. Involved in recruitment of checkpoint proteins bub1 and mad3 to the kinetochores, ensuring correct spindle checkpoint function. {ECO:0000269|PubMed:15509783}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O42861
|
FFT3_SCHPO
|
MDGKRKIEHTADGTHYDATSNVKRKPIFPPFIADSLSEATEKANVMGGGMNSRLQILSEMSKRVQATAPISSLEHFKQLSDISPSFTSSANSINQPYNYSGSLENLVPTPSAGTPSQFMDAQNPYGAVYNALSQFSETEPKMPSYMDDEEASDSLPLSLSSQSLSSQVTNQKPAPHRLTMRERYAANNLTNGLQFTLPLSSRKTYEPEADDDSNDDMYSDDDSNADRWASRIDTAALKEEVLKYMNRCSTQDLADMTGCTLAEAEFMVAKRPFPDLESALVVKQPRPVIPKGRRGRREKTPLGPRLVGICMEIMRGYFVVDALIRQCEQLGGKIQRGIEAWGLSNTATSDEGETSLVNFDQMKSFGTPANSSFITTPPASFSPDIKLQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMDKNINGPHLVIAPASTMENWLREFAKFCPKLKIELYYGSQVEREEIRERINSNKDSYNVMLTTYRLAATSKADRLFLRNQKFNVCVYDEGHYLKNRASERYRHLMSIPADFRVLLTGTPLQNNLKELISLLAFILPHVFDYGLKSLDVIFTMKKSPESDFERALLSEQRVSRAKMMMAPFVLRRKKSQVLDALPKKTRIIEFCEFSEEERRRYDDFASKQSVNSLLDENVMKTNLDTNANLAKKKSTAGFVLVQLRKLADHPMLFRIHYKDDILRQMAKAIMNEPQYKKANELYIFEDMQYMSDIELHNLCCKFPSINSFQLKDEPWMDATKVRKLKKLLTNAVENGDRVVLFSQFTQVLDILQLVMKSLNLKFLRFDGSTQVDFRQDLIDQFYADESINVFLLSTKAGGFGINLACANMVILYDVSFNPFDDLQAEDRAHRVGQKKEVTVYKFVVKDTIEEHIQRLANAKIALDATLSGNAETVEAEDDDD
|
3.6.4.12
| null |
attachment of telomeric heterochromatin to nuclear envelope [GO:0140698]; chromatin remodeling [GO:0006338]; replication fork processing [GO:0031297]; transcription elongation-coupled chromatin remodeling [GO:0140673]
|
chromatin [GO:0000785]; heterochromatin [GO:0000792]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; ATP-dependent H3-H4 histone complex chaperone activity [GO:0140665]; chromatin binding [GO:0003682]; damaged DNA binding [GO:0003684]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; histone chaperone activity [GO:0140713]
|
PF00271;PF00176;
|
3.40.50.300;3.40.50.10810;
|
SNF2/RAD54 helicase family
| null |
SUBCELLULAR LOCATION: Nucleus. Chromosome.
|
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;
| null | null | null | null |
FUNCTION: DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is required for heterochromatin organization. Required for maintaining a heterochromatin chromatin structure at centromeres and subtelomeres by protecting these regions from euchromatin assembly. Enhances the nucleotide exchange activity of the pim1 guanine nucleotide exchange factor and abolishes histone-H3-mediated RanGAP inhibition. Involved in the construction of the centromeres. {ECO:0000269|PubMed:15317843, ECO:0000269|PubMed:18422602, ECO:0000269|PubMed:21437270}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O42868
|
SSU72_SCHPO
|
MAPKTNLQISVICASNQNRSMEAHNVLKNAGYQVDSFGTGSAVRLPGPSIDKPNIYQFGYPYDEIYKELEAQDSRLYTANGLLKMLDRNRRIKRAPCRWQDQDSIYNIVITCEERCYDAICEDLYRRGETLNRPVYLINVDIKDNHEEASVGGKAILDLVNKLTEAQDKLEELFPSIMADFQSNHPKLPVLYTIHFF
|
3.1.3.16
| null |
co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway [GO:0180010]; mRNA polyadenylation [GO:0006378]; positive regulation of telomere maintenance via semi-conservative replication [GO:0032215]; regulation of pericentric heterochromatin formation [GO:0090052]; regulation of siRNA-independent facultative heterochromatin formation [GO:1902801]; signaling [GO:0023052]; termination of RNA polymerase II transcription [GO:0006369]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; mRNA cleavage and polyadenylation specificity factor complex [GO:0005847]; nucleus [GO:0005634]
|
myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722]; RNA polymerase II CTD heptapeptide repeat phosphatase activity [GO:0008420]
|
PF04722;
|
3.40.50.2300;
|
SSU72 phosphatase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16;
| null | null | null | null |
FUNCTION: Processively dephosphorylates Ser-5 of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit (rpb1). {ECO:0000250}.; FUNCTION: Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Ssu72 is required for 3'-end formation of snoRNAs (By similarity). {ECO:0000250}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O42872
|
RRP41_SCHPO
|
MSHFEILSLEGLRNDGRRWDEMRNFQCRIGIEPSENGSAFIELGNTKVLCIVDGPSEPVIKSKARADRTFVNVEINIASFSTIDVKKRFKSDRRIQLQCLALQNTFEEIIQTELYPRSQISVYLHVLQDDGAVMASCINATTLALIDAGIPVKDFVCCSTAGIVESDMLLDLNSLEESALSWLTVAVLGNIKKVVYMQLETSMHLDYLESVMNMAIAGSEHIYNTMQSAVRQSAKPALASLS
| 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]; nonfunctional rRNA decay [GO:0070651]; nuclear mRNA surveillance [GO:0071028]; nuclear mRNA surveillance of mRNA 3'-end processing [GO:0071031]; nuclear polyadenylation-dependent mRNA catabolic process [GO:0071042]; nuclear polyadenylation-dependent rRNA catabolic process [GO:0071035]; nuclear polyadenylation-dependent tRNA catabolic process [GO:0071038]; nuclear RNA surveillance [GO:0071027]; nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay [GO:0070478]; nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5' [GO:0034427]; nuclear-transcribed mRNA catabolic process, non-stop decay [GO:0070481]; polyadenylation-dependent snoRNA 3'-end processing [GO:0071051]; rRNA catabolic process [GO:0016075]; termination of RNA polymerase II transcription, exosome-dependent [GO:0030847]; U4 snRNA 3'-end processing [GO:0034475]
|
chromatin [GO:0000785]; cytoplasmic exosome (RNase complex) [GO:0000177]; cytosol [GO:0005829]; exosome (RNase complex) [GO:0000178]; nuclear exosome (RNase complex) [GO:0000176]; nucleolus [GO:0005730]; nucleus [GO:0005634]
|
RNA binding [GO:0003723]
|
PF01138;PF03725;
|
3.30.230.70;
|
RNase PH family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. ski6 is part of the hexameric ring of RNase PH domain-containing subunits proposed to form a central channel which threads RNA substrates for degradation (By similarity). {ECO:0000250}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O42874
|
STU1_SCHPO
|
MADKDAQDFLKFLKSNASTDEKTRCLDTLRSFFNKNNIPNADLGLFVECFRLALTTVNPLLLRSSVACFETFLRRLRAQYPTWLKFRVPMLKNLVIDHIASRDLQKRVLNILIDLWHFNPSEIEKSLIHLSTTSKSAETRIQCFKWFVLAHNAHLSFDVKSLRPALYINLENANPSVREEAKEVLLLIYKNLSTSAKMQFITDVETTSGLRREILQSLVEELSLISSSSEVIIVQNSASSFQPAPFMTAVATLYPGVELENVKPLLANFSKQLEQDSASMLPAFEGRETEQNWSVRQDSVLRLRQYLRGNACIDYLPELLSVLKTLLPGILLALLSLRTTLSSSAIQLIKEMAIILKSNIDPFLELILPNLLKVCSVTKKLASQAANVTFAAILVNCGVLSRNLSFISLAAHDTNAQLRVFSSNWIFMLISLSPELKNLASLQTNLKAFEKLICRGLADSNSQVREVYRKSFWKLSEYFPSVQEELTNTLEPSVLKQLHLANPNRQAASFNFSGPKRAPIRPLSNLRSFSKSQKEETSSNSSNSSGTRRLGLPQRATPASRERVLPYTRSQAFHSTSLPPSLPSGHSPSIAIPSKRSVSATIKDESKTFELLKNIQRKYELILSGSSVDLPSAEFLSSNLTDALYSGSSICYSLIFSHSLLDLTFQYVDIASLLSQFLLCVYDPSNVGHSFALASFPYVKSHYDAHKYFPIVFDVLMNISNMAPHVKVFPFNTNQKRLIIHGCLLWLKEISDTKLNQLENKPFFVTDKLRYYSSKILAMTAKTKLTSKNWIPLSGLLFSLRAHDTFMFDGLLDRLNEESRTKLVSSWSKQDAFDYSKSSTHQEHLSKNLPTLNTSSSSNSSQTDLLVPHGKGETKETEMQSPIESKEGLLSKDTHIESPQGTSLEKENEEEGKNPVESNCSEESLDDHNIDQTLVNKKETLAQDSESLLQKNNALNEKGFENQFGLSSSAAKVLNKDTLDHVSGPISNSVSSSFKDFTRTPFKEINGERETGFELTSYVNALSKKDDINVQKTENVDESVGLNAMFMDNVNQDSLNSVDQSSGKDKLLLTSSTPNKPTTFFMPANEEILGSPAKDYDIHDQSYSVHELHSENMRENVGQSSLIYNNRDYMNTPMNDFSLSFSEIKGGILESPVESPMTGTISPIDADESVLHDIPAYESLNKSESNKYQEQAYSTPLHHTLNVLPKNKWILSRMHKMENGSPINVDKNLDDAVAALEAAVKELNDGSVNTKTLKFCIKVCKETPSMLYHSHGLLPAILHYIESNNSAMHISDCLILLHEFLVQGYQGVDMHTYHNIICILIEKAEKCKDEPVILAGIEDNITLIAEIADLQGLYEFTQQRLQSLNTETGEKSAPLLLMLLSAILMRLKDLEFLETKDLLRHVVLKYIDHTNPEIRKATFNVCLAVNTIVNNVDETFSILGGLNEGQRLLFMHYLKMKSDEKN
| null | null |
astral microtubule depolymerization [GO:0060172]; cell division [GO:0051301]; establishment of mitotic spindle localization [GO:0040001]; microtubule bundle formation [GO:0001578]; mitotic spindle assembly [GO:0090307]; mitotic spindle formation (spindle phase one) [GO:0061804]; mitotic spindle midzone assembly [GO:0051256]
|
cytoplasmic microtubule [GO:0005881]; cytosol [GO:0005829]; kinetochore [GO:0000776]; microtubule associated complex [GO:0005875]; microtubule cytoskeleton [GO:0015630]; microtubule organizing center [GO:0005815]; mitotic spindle [GO:0072686]; mitotic spindle midzone [GO:1990023]; mitotic spindle pole body [GO:0044732]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; spindle microtubule [GO:0005876]; static microtubule bundle [GO:0099070]
|
microtubule binding [GO:0008017]
|
PF12348;
|
1.25.10.10;
|
CLASP family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16951255}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16951255}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:16951255}. Note=Colocalizes with cytoplasmic microtubules and associates with the mitotic spindle throughout mitosis.
| null | null | null | null | null |
FUNCTION: Microtubule binding protein that regulates the stability of dynamic microtubules. Required for mitotic spindle formation. {ECO:0000269|PubMed:16951255}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O42893
|
TREA_SCHPO
|
MPSKFSSKYVDTEAISNDDDNPFATAKSYYSKDTDLSTRVSAGRPRTLSTSMEASAAPTIPELKNLRRRGSLDEHKQPRKFLVDVDKTLNALLESEDTDRNMQITIEDTGPKVVSLGSASSGGYRLYELRGTYQLSNLLQELTLAKDYGRRYILLDERRLNENPVNRLSRLIKGTFWDALTRRIDASVLDVICRDTKDRSGSHVNRIYVPKAEQEMYEYYVRAAKERPYLNLQVEYLPEEITPEWVRDVNDKPGLLALAMEKYQDDEGNTHLRGVPFVVPGGRFNELYGWDSYFESLGLLVDDRVDLAKGMVENFIFEITYYGKILNANRTYYLLRSQPPFLTDMALRVYERIKNEEGSLDFLHRAFSATIKEYHTVWTATPRLDPKTGLSRYRPGGLGIPPETEASHFEHLLRPYMEKYHMTLEEFTHAYNYQQIHEPALDEYFVHDRAVRESGHDTTYRLEKVCADLATVDLNSLLYKYETDISHVILEYFDDKFVLPNGTIETSAIWDRRARARRAAMEKYLWSEADSMWYDYNTKLETKSTYESATAFWALWAGVATPRQAAKFVDVSLPKFEVAGGIVAGTKRSLGKVGLDNPSRQWDYPNGWSPQQILAWYGLIRYGYEEETRRLVYRWLYTITKSFVDFNGIVVEKYDLTRPVDPHRVEAEYGNQGVNIKGVAREGFGWVNASYEVGLTFCNSHMRRALGACTTPDVFFAGIKEESLPAFENLSIHKN
|
3.2.1.28
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:12943532};
|
ascospore formation [GO:0030437]; trehalose catabolic process [GO:0005993]; trehalose metabolic process [GO:0005991]; trehalose metabolism in response to stress [GO:0070413]
|
alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) [GO:0005946]; cytosol [GO:0005829]
|
alpha,alpha-trehalase activity [GO:0004555]; calcium ion binding [GO:0005509]
|
PF01204;PF07492;
|
1.50.10.10;
|
Glycosyl hydrolase 37 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
|
CATALYTIC ACTIVITY: Reaction=alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-glucose; Xref=Rhea:RHEA:32675, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903, ChEBI:CHEBI:16551, ChEBI:CHEBI:17925; EC=3.2.1.28; Evidence={ECO:0000269|PubMed:12153582, ECO:0000305|PubMed:12943532};
| null |
PATHWAY: Carbohydrate degradation. {ECO:0000305}.
| null | null |
FUNCTION: Hydrolyzes intracellular trehalose to glucose (PubMed:12153582). The disaccharide trehalose serves as a storage carbohydrate that is mobilized during nutrient stress and spore germination (PubMed:11094289). Together with tps1, regulates the level of trehalose as a protectant for cell integrity during heat, osmotic and oxidative stresses (PubMed:12943532, PubMed:15965643, PubMed:9495778, PubMed:9974219). {ECO:0000269|PubMed:11094289, ECO:0000269|PubMed:12153582, ECO:0000269|PubMed:12943532, ECO:0000269|PubMed:15965643, ECO:0000269|PubMed:9495778, ECO:0000269|PubMed:9974219}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O42900
|
PPK19_SCHPO
|
MGIQLSTIQTPQFHELFEEELPEYHNERSLGDSHFLRTFRMQDRKGYDVLIKVFVNKLPEISLSSIVNLLKEEQENISYRVPNAVPYIKTLVTLRAAYLVRPYVTHNLYDRISTRPFLELTEKKWIMFQLLKGISDCHRLGVCHGDIKSENILITSWNWAYLSDFSSFKPTYLPEDNPADYGYFFDTSSRRVCNIAPERFVPASQLQPAPLSPAMDIFSLGCVFAELLLEESPLFTLSQLFSYKAHGSYDLQSVLEQIEDKSTQNMILSMLDRDPSQRLSADAYLQKYRGTVFPACFYDTLYDYCIGLVDPSGILSAKQPNDACSLYGSRIDDIYRDIMPPNNNDISNLMHTPHEYNGIDSYSVPLFTTLDEFYNKNPAAKNWYLRLYNTMQEKKGFEDKEQGSTPAPSPSVIEDISSIETDENHLYGAAVLLPIVLSTIRHVNTRESKINALSLVQILSRNICDESKLDTVLPFVMTLLRDQYADVRISALITITRLVSNVTSIAPINAFLFQEYLFPDLQHFLFDMNSRTRATYASCLPILAKQASKFLNLAQSLRNAGILSFPESEYENINHGKAELLFETGRHDLVVTVERHVSTLLADSSSIVRRSLLNALAPLCVFFGKAKSNDLILSHLITYLNDTDWMLRCAFFESITGLSIFIGPRSVDEYILPLMLQALVDPEPAVLESVLGSFSGLIELHLFEKLVVVDILQLVLPLVAVPNAYIRRAALSVIYSAYQSFDDIDRDCIVTPLLRPYLMSNLCDINSLEKLDQFILPMVSDSVWSTLTRWYEESENSSFWKCDKDASYSSLDVSNDSLLGRTKNLQKREIMHHAEVYTHKKISLTGHVIITSTEMLELSEDDQKWADIIKEMGVDVKHLWVLANLRDYVKKTKINLNGINYKRQSGLRELNTYPNAPLHILPETIFWNPERPPSSSIANETFLDRNSYAESIQTSRSYNDDLIARDPIAYVGTDMTNAFGTTTKPKDVSQSDIKVDINRESNSDNGETITGTHDVYRQTDNPEIKLPSDTASSKVDTHNPTVTQPTDDTGGLNSYNTENPLLTNNTLEPSSVEAIVSSKDSDKHAKESKGKSLAPLISSRVSTNDTTNVAGIRSQRSFTTHIDLKKLTTRQNGAKKSSYTGTNPCVLNYLNKIYAEAAASTLNVGAAVSPSWASNIPLRRRTKVSAKAANKIVQTHEWHPEGSRVAQIYLGSLLDGGTKKVLVSPDSSFFVTLGSDGVVRAWQLVESVRHISTMRCECRLSYGHTRRNGERNRFSVVNGCFLGNTYAFASVTQDGSVEVHRLDVNNQRHTLISAGRIPNLDFSDSVTSMEASTFHDGSIRLVVVTKWSRIVYLDVGMMRVLSSDQLPLQCGSATSVVVSEGCNWALIGTTKGWLLLWDLRFGTLSCSWHMPARIDQMHLLLDVTKKRSNVNEYTSGNNNSPVTKVPGSSSTSSSSTQPINSTIPINPLENHGMLNSFGSTTVSISFSVLTNLDNKEVNLEDAVPASHRSASGIVNFDVEKGKTEEVFLENWNSSLTSPIPVSVGIDAFNEKKKFDIDSGNDMGLRDLNTKFDSPWPCISSPIYRYRGPSAGSVEREPLFLIAASGSPHAFIWNPHNVSASSSVTNDSESSKLSLIHNKPPIYQKVSEQQNVRPKSSGVSRPLLFLQQQKNLPSENRLHPIVDMAFLYQPYAIVLIVDAFGSLELWT
|
2.7.11.1
| null |
late endosome to vacuole transport [GO:0045324]; macroautophagy [GO:0016236]; phosphorylation [GO:0016310]; protein targeting to vacuole [GO:0006623]; retrograde transport, endosome to Golgi [GO:0042147]; signaling [GO:0023052]
|
cytosol [GO:0005829]; late endosome [GO:0005770]; nucleus-vacuole junction [GO:0071561]; phosphatidylinositol 3-kinase complex, class III, type I [GO:0034271]; phosphatidylinositol 3-kinase complex, class III, type II [GO:0034272]
|
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.25.10.10;1.10.510.10;2.130.10.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
| 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=2.7.11.1; 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 | null |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O42916
|
ALE1_SCHPO
|
MAYLIDIPFEYFSSFLGVHPDQLKLLFCFLSAYPFAGILKRLPSAPWIRNLFSISIGLFYLIGVHHLYDGVLVLLFDALFTYFVAAFYRSSRMPWIIFIVILGHTFSSHVIRYIYPSENTDITASQMVLCMKLTAFAWSVYDGRLPSSELSSYQKDRALRKIPNILYFLGYVFFFPSLLVGPAFDYVDYERFITLSMFKPLADPYEKQITPHSLEPALGRCWRGLLWLILFITGSSIYPLKFLLTPKFASSPILLKYGYVCITAFVARMKYYGAWELSDGACILSGIGYNGLDSSKHPRWDRVKNIDPIKFEFADNIKCALEAWNMNTNKWLRNYVYLRVAKKGKRPGFKSTLSTFTVSAMWHGVSAGYYLTFVSAAFIQTVAKYTRRHVRPFFLKPDMETPGPFKRVYDVIGMVATNLSLSYLIISFLLLNLKESIHVWKELYFIVHIYILIALAVFNSPIRSKLDNKIRSRVNSYKLKSYEQSMKSTSDTDMLNMSVPKREDFENDE
|
2.3.1.23; 2.3.1.51
| null |
glycerophospholipid biosynthetic process [GO:0046474]; lipid modification [GO:0030258]; phosphatidylethanolamine biosynthetic process [GO:0006646]; triglyceride biosynthetic process [GO:0019432]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]
|
1-acylglycerol-3-phosphate O-acyltransferase activity [GO:0003841]; 1-acylglycerophosphocholine O-acyltransferase activity [GO:0047184]; 1-acylglycerophosphoethanolamine O-acyltransferase activity [GO:0106262]
|
PF03062;
| null |
Membrane-bound acyltransferase family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Microsome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709, ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342, ChEBI:CHEBI:58608; EC=2.3.1.51; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937, ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168, ChEBI:CHEBI:58342; EC=2.3.1.23; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:32995, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64381, ChEBI:CHEBI:64612;
| null | null | null | null |
FUNCTION: Membrane-bound O-acyltransferase that mediates the incorporation of unsaturated acyl chains into the sn-2 position of phospholipids. {ECO:0000269|PubMed:17890783}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O42917
|
ESO1_SCHPO
|
MELGKSKFSWKDLQYCDKAGTQNSPLRVVAHIDQDAFYAQVESVRLGLDHSVPLAVQQWQGLIAVNYAARAANISRHETVTEAKKKCPELCTAHVKTWKAGESEAKYHENPNPNYYKTCLDPYRHESVKILNIIKKHAPVVKKASIDECFIELTSDVKRIVLEEYPYLKIPSEDSNVALPQAPVLLWPAEFGMVIEEEVVDRTKEDYERDWDDVFLFYAAKIVKEIRDDIYLQLKYTCSAGVSFNPMLSKLVSSRNKPNKQTILTKNAIQDYLVSLKITDIRMLGGKFGEEIINLLGTDSIKDVWNMSMDFLIDKLGQTNGPLVWNLCHGIDNTEITTQVQIKSMLSAKNFSQQKVKSEEDAINWFQVFASDLRSRFLELEGMRRPKTICLTVVSRFLRKSRSSQIPMNVDISTQFIVEATSKLLRQLQQEFDVYPISNLSISFQNIIEVDRNSRGIEGFLKKSNDEIYMSTSVSPSIEGRAKLLNENMRENNSFELSSEKDIKSPKRLKRGKGKGIFDMLQQTAVSKPTENSADETYTCEECEQKITLSERNEHEDYHIALSISRKERYNNLVPPSHDKPKQVKPKTYGRKTGSKHYAPLSDETNNKRAFLDAFLGNGGNLTPNWKKQTPKAISNSSDNMTQLHLDLANSTVTCSECSMEYNSTSEEDILLHSRFHSRVLGGVTVSFQCSPIYRVNYGLSSDCIYSINSESSLIDQRKAEEALSFVNNELSSEPIETIGVDKYTTFLFISDKKCVGLLLAERISSAYIVDELELNNNNSTSSAVYIKNENLRKGFVLGISRIWVSASRRKQGIASLLLDNALKKFIYGYVISPAEVAFSQPSESGKQFIISWHRSRNNGSSKSLRYAVYES
|
2.3.1.-
| null |
error-free translesion synthesis [GO:0070987]; error-prone translesion synthesis [GO:0042276]; meiotic sister chromatid cohesion [GO:0051177]; mitotic sister chromatid cohesion [GO:0007064]; response to radiation [GO:0009314]; translesion synthesis [GO:0019985]
|
chromatin [GO:0000785]; nuclear replication fork [GO:0043596]; nucleus [GO:0005634]; replication fork [GO:0005657]; site of double-strand break [GO:0035861]
|
damaged DNA binding [GO:0003684]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; peptidyl-lysine acetyltransferase activity [GO:0052858]
|
PF13880;PF00817;PF11799;PF21704;PF13878;PF18439;
|
3.30.70.270;3.40.1170.60;1.10.150.20;3.30.1490.100;
|
Acetyltransferase family, ECO subfamily; DNA polymerase type-Y family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Probable acetyltransferase required for the establishment of sister chromatid cohesion and couple the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. In contrast to the structural cohesins, the deposition and establishment factors are required only during S phase. The relevance of acetyltransferase function remains unclear (By similarity). {ECO:0000250}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O42930
|
VPS10_SCHPO
|
MFFLTKILPLRGRIFPMFGCLLLIVSLITGCIASPAAEVAETVFDSKPVDFMTFKDSTNTLFLNAEFGDVYLSQDNGQSWRNGVISGQVCPIKKLIKHSFENSRVFALTECDTVYYSYDNGENWDYFTIDHPISITQLPFHFHAKNPDYVIFNNQYCSSSGTWVGKICKPDLYYTKDGFQSDPEPMPVGSSYCIFADSSEKMVVSSEEQIICISLNPNSAARPPFSHHIVYSDDWFQSIVPVQLHNFLGSDGAYGILSTGSFLVAALIDAATRKLFVYVSQDGYYWEEALKFHKGFEFDAFTILPSTEYSFFIDSLDSHPNNPTGILYSLDSESNTFVIRQMNTNRYVDGYTDFMLIDYLDGLQFVNVVENVDEIEVDPQVDKVLSSRITFDGGKTWSTVASPESSCNSMKQCSLHLFLDPHVSHASIASSKFAPGILLASGSVGDRLLSENQMDLFVSEDGGRNWTLSRDGMHLFAMSGFGSIFFASEYLDVINEVYYSLDHGQSWVTVTLDKTIVPIKLFASEDPYAEIFYLLAMTDDGEQSNYSLFSFNFGKFLPKECQFSNSESNKNDFEKWYTRYANGSPICSEMGKKEFFWRKKATSVCSVPKSITDLHGSFDACECTDEDYECNTQFISNDQGECKLLDFIGSLLCASEDLDTFQKIPYRLVPGNKCTPNKRDSHREPQTFNCDSFNEPGTEITSFLYDFDEKIVDVVYLEGTVPEENTFLIGISVNSHVYFSEDEGKTWDKFSKEEFSSVLPHAYNKNSVYMVTSKNIVYFTTNRGKNFYKFKAPSPPNQNGKSLFSFHPSRPAWLLYAGSENCEKNPFADDCRDVVFVSLDFGDTWSRLPSNLEYCSWAKAEKLVVDDTLIFCIRQNTNDPFKKELISSIDFFEYEQDEILNDVVGFMIEDEYVIVAVQDEEGTSLSLDVSINGLNFASCSFPAYLNVHPKQAYTILDSQTHSLFIHVTTNTHLGSEWGDILKSNSNGTYFMTSLANVNRDSVGYVDFERLEGIQGIALANIVSNTKELTDGGTKKLQTLITFNDGLDWSYLNLVGGEKIVPKCGKNCYLHLHGYTERNQFSDPTSTNAAVGLIIGVGSFSPFLIPYEESQTFISRDAGVTWYRIFDSPHLWAFLDSGSIIIAVESISPTNVIKYSADEGRTWQEYQFSEKSKVVVDVSTKPSGVGHQVLLLTTDDENAPISSVLIDFDALYRRTCVFDEENSEESDFVRWVPTDISGKPLCLRGRISSFYRKSIHKKCRVGSSLLVKEEVLSKCECTRADFECDYNYRRLKDGTCVLVSGLQPPDTREEQCSVDDAFEWRQPTGYKRTPLTECEGGVPLDAGTLHPCPGKEDDYYKAHPKPGGWSIFLTIIFSILLAAVAGCILYYYSRRFLKGAIRLGSDSATENPLESGISYTRGAFSSIPIFFSALYQSVRSLFIRSTPTNGEFENAAFLQNYEIDDDDEESV
| null | null |
Golgi to endosome transport [GO:0006895]; Golgi to vacuole transport [GO:0006896]; protein targeting to vacuole [GO:0006623]
|
cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; membrane [GO:0016020]; trans-Golgi network [GO:0005802]
|
nucleotide binding [GO:0000166]; signal sequence binding [GO:0005048]
|
PF15902;PF15901;
|
3.30.60.270;2.130.10.10;
|
VPS10-related sortilin family
| null |
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:16622069}; Single-pass type I membrane protein {ECO:0000269|PubMed:16622069}. Prevacuolar compartment membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Cycles between the Golgi apparatus and the prevacuolar compartment. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Functions as a sorting receptor in the Golgi compartment required for the intracellular sorting and delivery of soluble vacuolar proteins, like carboxypeptidase Y (CPY) and proteinase A. Executes multiple rounds of sorting by cycling between the late Golgi and a prevacuolar endosome-like compartment. {ECO:0000269|PubMed:16622069}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O42934
|
CHP2_SCHPO
|
MVKSADLDLMNSIISESDENFSPPPFTVEEAENSINNKSSTASLESPQNGSWHPSLYGLSVPEKTHIQNSLDLYSHGNSGSQKTHNVSFSCEIRKVKSSKLSPISNMEDSEDKKEEDESSSYKNEFKSSSSASVSSNFEKTSGSDDHNSQSPVPLNEGFEYIASSGSEDKNSDEEFAVEMILDSRMKKDGSGFQYYLKWEGYDDPSDNTWNDEEDCAGCLELIDAYWESRGGKPDLSSLIRLTRSRARSSNEASYVEKDESSNSDDSISYKRRRSRNAANRITDYVDSDLSESSMKEKQSKIEKYMKSDKSSKNFKPPFQKKSWEDLVDCVKTVQQLDNGKLIAKIKWKNGYVSTHDNIIIHQKCPLKIIEYYEAHIKFT
| null | null |
chromatin organization [GO:0006325]; negative regulation of transcription by RNA polymerase II [GO:0000122]; pericentric heterochromatin formation [GO:0031508]; rDNA heterochromatin formation [GO:0000183]; regulatory ncRNA-mediated heterochromatin formation [GO:0031048]; silent mating-type cassette heterochromatin formation [GO:0030466]; subtelomeric heterochromatin formation [GO:0031509]
|
chromosome, subtelomeric region [GO:0099115]; mating-type region heterochromatin [GO:0031934]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; histone binding [GO:0042393]; methylated histone binding [GO:0035064]
|
PF00385;PF01393;
|
2.40.50.40;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Component of the kinetochore which plays a role in stabilizing microtubules and so allowing accurate chromosome segregation. {ECO:0000269|PubMed:10835380}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O42938
|
PFKA_SCHPO
|
MSGETVHGISCYSVVANTEDTYNQTLDFYQKLGFKKVASFGTSDSDNARVCNESLREDWMHVAGNNSAESVTIKFRLVPGELSLSPAAEDSEWRGQKSSLVFYYPNLLDLLKQLSADAIKYQAFPNEKKPDEVYVEDPLGNLIGFSDRYNPFAHANLKKSEESGAASNLESGLATPVVETLKKATTSDKPAGVKKKIAVMTSGGDSPGMNAVVRAVARIAIHRGCDAFAIYEGYEGLVQGGDMIKQLQWGDVRGWLAEGGTLIGTARCMAFRERPGRLRAAKNLISAGIDSIIVCGGDGSLTGADIFRSDWPGLVKELEDTKAITPEQAKLYRHLTIVGLVGSIDNDMSSTDVTIGAFSSLHRICEAVDSISSTAISHSRAFIVEVMGRHCGWLAVLAALATGADFVFIPERPAEVGKWQDELCNSLSSVRKLGKRKSIVIVAEGAIDSELNHISPEDIKNLLVERLHLDTRVTTLGHVQRGGIPCAYDRMLATLQGVDAVDAVLASTPDTPSPMIAINGNKINRKPLMEAVKLTHEVADAIEKKQFAHAMELRDPEFADYLHTWEGTTFIEDESHFVPKDERMRVAIIHVGAPAGGMNSATRAAVRYCLNRGHTPLAIDNGFSGFLRHDSIHELSWIDVDEWCIRGGSEIGTNRDTPDLDMGFTAFKFQQHKIDALIIIGGFEAFTALSQLESARVNYPSFRIPMAIIPATISNNVPGTEFSLGCDTCLNAVMEYCDTIKQSASASRRRVFVCEVQGGRSGYIATVGGLITGASAIYTPEDGISLDMLRKDIDHLKATFALEAGRNRAGQLILRNECASKVYTTEVIGNIISEEAHKRFSARTAVPGHVQQGGNPTPMDRARAARLAMRAIRFFETCRANDLGNDPSSAVVIGIRGTGVSFSSVADVENNETEIEMRRPKNAWWRDMHNLVNILAGKTFAD
|
2.7.1.11
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03184};
|
canonical glycolysis [GO:0061621]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002]; glycolytic process [GO:0006096]
|
6-phosphofructokinase complex [GO:0005945]; cytoplasm [GO:0005737]; cytoplasmic side of mitochondrial outer membrane [GO:0032473]; cytosol [GO:0005829]; mitochondrion [GO:0005739]
|
6-phosphofructokinase activity [GO:0003872]; AMP binding [GO:0016208]; ATP binding [GO:0005524]; fructose-6-phosphate binding [GO:0070095]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; monosaccharide binding [GO:0048029]
|
PF00365;PF18468;
|
3.40.50.450;3.10.180.10;3.40.50.460;
|
Phosphofructokinase type A (PFKA) family, ATP-dependent PFK group I subfamily, Eukaryotic two domain clade 'E' sub-subfamily
|
PTM: The N-terminus is blocked.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
|
CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:11015725};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.025 mM for ATP (without effector) {ECO:0000269|PubMed:11015725}; KM=0.027 mM for ATP (with 2.6 uM fructose 2,6-bisphosphate) {ECO:0000269|PubMed:11015725}; KM=0.63 mM for fructose 6-phosphate (without effector) {ECO:0000269|PubMed:11015725}; KM=0.31 mM for fructose 6-phosphate (with 1 mM AMP) {ECO:0000269|PubMed:11015725}; KM=0.17 mM for fructose 6-phosphate (with 2.6 uM fructose 2,6-bisphosphate) {ECO:0000269|PubMed:11015725};
|
PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_03184}.
| null | null |
FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. May also have a role in cell cycle regulation. {ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:11015725, ECO:0000269|PubMed:12237855}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O42976
|
YGZ7_SCHPO
|
MKEENGFAGFLNTAVNRLSGVLNDTAPTKSQSLKNGVNNEGNRGFSLFRNPRFMSDEKLSSEASSHSTLGQQQARDGRQSPSKEAPFGEGELKLENFENQENEADEAENEETSYSEQNHTENTEEIAEESRPLERTHSGSNHHEASSTGHLNLPPLENTLSQGSAITAPSRKVSITSSNGVSARLSGYAFANSKRNRDFHRIFKVLPPEDHLIDDYGCALQRDIFLHGRMYLSESHICFNSSIFGWVTNIVIPVTEIVSVEKKSTAVVFPNAIQITTLHARYIFASFISRDTTYQLIIAIWKNTHPFLTTLANGHGVMDASGNHHSGSSNQSINADSSAGSEGVDEGTSTEANDESSEDDDEDNNTDEANEDAQSNVSDESPKGEGSSHSDNVVLSDGNSVKKMNEDGADTSLLSVSEVTSHPPTEWTGSPLAHVLCSDVVNLSVSTVFNLLCGSDTTWIINFFKSEKLTEIKIGKWEKIDDKWNRKVQYIKPVAPPYRQTSCYITDTIQHLDINNYIEILSTTSTPDVPSGTSFVVKTLYALSWAHSSKTKLNISYSVEWSKSSWLKGPIEKGAQEGQASYVKDLLTAFENYKVSPKGRRKKITKHTKKKNKHASETSVAPEKVDNSSIEQSSSFLTKLYTFPFTIITWLMHPTHLLLVVMFSMLVLQWWYMQQILHAELPSTSSRSDSSRDLDFDHIPMDDTAFKLWITSRLDSVERDRDFVYENSDPNLEHGKIKIATDYMERRLKKLKERLRKLEASGYI
| null | null |
intermembrane sterol transfer [GO:0120011]; intracellular sterol transport [GO:0032366]; sterol transport [GO:0015918]
|
cortical endoplasmic reticulum [GO:0032541]; cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-plasma membrane contact site [GO:0140268]; mitochondria-associated endoplasmic reticulum membrane [GO:0044233]; mitochondrion [GO:0005739]; nucleus-vacuole junction [GO:0071561]; perinuclear endoplasmic reticulum membrane [GO:1990578]; plasma membrane [GO:0005886]; vacuole-mitochondrion membrane contact site [GO:1990816]
|
cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; lipid binding [GO:0008289]; sterol binding [GO:0032934]; sterol transfer activity [GO:0120015]
|
PF02893;PF16016;
|
2.30.29.30;
|
YSP2 family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Localizes to cytoplasmic punctate structures. {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
| null | null | null | null | null | null |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O42995
|
MIS19_SCHPO
|
MDLMPLEKARAIEIAFDNVFHNTKIPDNLQQFDAILKRLERRRFIPTENQKPRVYETELLVLRFREFGVKDNHNHPINLHSLRSKSLIRAQGKKLDLHNRVFLRRNVRAVKM
| null | null |
attachment of mitotic spindle microtubules to kinetochore [GO:0051315]; cell division [GO:0051301]; mitotic sister chromatid segregation [GO:0000070]; protein localization to chromosome, centromeric region [GO:0071459]
|
CENP-A recruiting complex [GO:0098654]; chromosome, centromeric core domain [GO:0034506]; kinetochore [GO:0000776]; nucleoplasm [GO:0005654]
| null | null | null | null | null |
SUBCELLULAR LOCATION: Chromosome, centromere {ECO:0000269|PubMed:24774534, ECO:0000269|PubMed:24789708, ECO:0000269|PubMed:25375240}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:25375240}. Note=Localizes at the centromeres during interphase, but not in mitosis (PubMed:24774534, PubMed:25375240). {ECO:0000269|PubMed:24774534, ECO:0000269|PubMed:25375240}.
| null | null | null | null | null |
FUNCTION: Component of the CENP-A recruiting complex that ensures the integrity of mitotic spindles through maintenance of kinetochore factors mis6/CENP-I and cnp1/CENP-A (PubMed:24774534, PubMed:24789708, PubMed:25375240). Links mis16 and mis18 to recruit CENP-A through interacting with non-sense-mediated mRNA decay (NMD) factors and the SWI/SNF complex (PubMed:24774534). Links also mis18 with the CCAN/mis6/ctf19 complex to promote CENP-A assembly (PubMed:24789708). {ECO:0000269|PubMed:24774534, ECO:0000269|PubMed:24789708, ECO:0000269|PubMed:25375240}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O42998
|
SIP1_SCHPO
|
MSLASLPLEKLTKVADVDKRETIYIDLLNYEKQLRNLNKNTREDSLQTNLNPLLSLIKKYGNFIAYPTRKLLSNCIIALLKGLEGYHQHRVLLYFVDSIHEKKDYIEIINVLSVLTSCLEEYGNQINQQETFIRFFFKYSKTNLSYGVRSIALDGLSKCIETSIQSTNEDLIKEIWKCIKSNLNTSSTNVLLSALRCAYYILGSSRLRNSELEWFKSFLFKKSSIDNSLLHSSLGRCFSALASAQADKSIEAAANAVPSTPADDENNEEVENRSTTRRFDETESFRHALRILVENYHSKHAKYESSKAVLVFAVKHLFLMQRPSFVSLNYTTIVDIILLHQSHSTSKEWLSSLEQYHCTYLFRDVIGRRFLDQSSELQGIEILLKRVLEPYLKDQSKISEIAVKTAMASTADILSRSKGSATALYSQLLDTTLQILYLGKDSLKNEVAWLLRCLLSVMPSPLMPTLLALFNRLELEFKHLRSKPKEVSPKLNVGIFNNLTLSLMSIYVAAEENPLYVASSIFSKLFNFSLDLIKSSSKLDLLAAQAQIKTGWRLLSAYVSFGPSFTRMQLSQLLILWKNALSRVPSKIHSQNFMETNADMFNRFEALQCLLSFLEYNKILFTPDVRKRVIIFLNNCLKFYKAFSLTKRLEITMPIPASDYSHLELRSLLLARIFQCFFELSQLSGMSLDDQELLSTTVSTIAELSSLQGYDTADEIVQAKAFTSPRVIPGIGSRFYAQPEEEFQTTMDDILPCYICESSSDSLSVISRSNSAKLPYVPPSLTSLIDNAIQLFASMFCHQPPKVMESTLEIMVASVTNLKSGRDILRYKAVTANTLFSIYGFLSAFDNKKVTLPDKVVSLMIELLENLTAVNDPKLIPYISKSYAFLAYLYQSKPTSVLDTIIKRAAESGDPNCRAVLILAVGHILKKVGSGVPQTTLITAYQLLKVFNTDSNDLVRECSIRASSVSLGSIAKTIPSVLTAQTRILLSYMLLPECDIDVQLLKKRNSLFFPSTLFANYLDCLINELGPNLRSDSSTSHFAFDLAHQLLLLSRDTGDNIIHVYKCYQHLYLFTPLETNSDFFIRELCGNIIDLKQPKRREISIEVLYQILLQNHEFSESCYKRHFDRLIWQSLDTTPDNKLLKNILYIWLNDYKDSDIHSWVNILLFLVGIKNTSSSERSNEQDIQNNLDEDTVSLAYGTSENASNPLFQKNYRWQTQFYAATCLKTCISEVMAENKEPAKYLISRISDLVRAAFVLSTSDNFYLKQGGFELLDTIITDFSNVMDPDFDDVSLLDQFQAQISSAFSSAFVDDSSPEIVAMSLNIASNFIGTGLLKTESQAAKILNLLKEALESSLPERAGFEENRHFKYDSKYFLRIATLSAWASLLVHSANVSYLKEFLSSNIRRLSSHWIMALRGYSRLQFGPSLVKDFVADTSFTRVQSINPKILLNIYEKSWLNIAESLTILLSTDANLIYGILSGDELSLSEEDVFFQDNINYASNRYSFNFFLFSVCFQSLLIPSTLQGFRNPVFRIMRIMTEVLTEELCTKVLYDHNVFPEVVDLLVRLILTEDWETKASIVIFVKKLALANPAHNDLKFCETDSVTSMEPTVSESVEMLFQLVKILTLALTVRVPGLRSDPAESATNKKASEFVILCFNAFLDVSNIFPAIVRVDLFATAMHVYEVIMDDQQLLKNSKQELLAALRKLLSTMVEQNDHTCTTLIYTLFEHLLNIYKETINDSDKKEKNETAFMSMVLVLTLAAPILDSEQLVVHDFLEELFSSLKSSEEDFALRTRCVTSLMLVNSKHPSMSALCRFIIYKSVTMLQNGEVLKSGDYVTEFIPALLDMHVHIPEEKKKSFLSMSIPIAAHFSILVEHADARKRIGEKLLKIMAIQPDEAKAIIQQLSPRQKKCVEEILIQNVE
| null | null |
endocytosis [GO:0006897]; intracellular protein transport [GO:0006886]; protein localization [GO:0008104]; retrograde transport, endosome to Golgi [GO:0042147]
|
cytosol [GO:0005829]; endocytic vesicle [GO:0030139]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; nucleus [GO:0005634]
| null |
PF20210;
| null | null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11859360, ECO:0000269|PubMed:16823372}. Cytoplasmic vesicle {ECO:0000269|PubMed:11859360}. Nucleus {ECO:0000269|PubMed:11859360, ECO:0000269|PubMed:16823372}. Golgi apparatus {ECO:0000269|PubMed:16823372}. Note=Localizes to endocytotic vesicles. {ECO:0000269|PubMed:11859360}.
| null | null | null | null | null |
FUNCTION: Required for endocytosis. Also involved in cytokinesis and cell division. {ECO:0000269|PubMed:19243310}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O43001
|
SYJ1_SCHPO
|
MQCLLREKPRSLALVNKDHALMFHSVPQNKNSLSVCVAEFTALSEKPLEGFRKISSHRIYGTLGLIELEGSNFLCVISGASEVARVRDKERVFRIMEVCFYSVNRSNWDHIRQENYSPDIPDGYDTDTQGYDSYKYAAEPFSSLRKLLTNGSFYFSLDFDITTRLQLRTSQTMTEPQYDSMHTQFMWNEFMLRQLIKFRSHLNGDEKSALDGCRFFTCAIRGFASTEQFKLGIQTIRLSLISRLSSLRAGTRFLSRGVDDDGNVANFVETETILDSSKYCVSYCQVRGSIPIFWEQEGVQMFGQKIDITRSLEATRAAFEKHFTSLIEEYGPVHIINLLGTGSGERSLSERLRQHIQLSPEKDLIHLTEFDYHSQIRSFEDANKIRPMIYSDAETFGFYFENNEGQSIVVQDGVFRTNCLDCLDRTNVIQNLVSRVFLEQVMIYTRQNAGYDFWQVHSTIWANNGDALARIYTGTGALKSSFTRKGKLSIAGALNDLSKSVGRMYINNFQDKGRQETIDLLLGRLIDQHPVILYDPIHEYVNHELRKRENEFSEHKNVKIFVASYNLNGCSATTKLENWLFPENTPLADIYVVGFQEIVQLTPQQVISADPAKRREWESCVKRLLNGKCTSGPGYVQLRSGQLVGTALMIFCKESCLPSIKNVEGTVKKTGLGGVSGNKGAVAIRFDYEDTGLCFITSHLAAGYTNYDERDHDYRTIASGLRFRRGRSIFNHDYVVWFGDFNYRISLTYEEVVPCIAQGKLSYLFEYDQLNKQMLTGKVFPFFSELPITFPPTYKFDIGTDIYDTSDKHRVPAWTDRILYRGELVPHSYQSVPLYYSDHRPIYATYEANIVKVDREKKKILFEELYNQRKQEVRDASQTSYTLIDIAGSVAGKPNLIPHLPANGVDKIKQPSSERSKWWFDDGLPAKSIAAPPGPEYRLNPSRPINPFEPTAEPDWISNTKQSFDKKSSLIDSIPALSPAPSSLARSSVSSQRSSTSIIPIKPNKPTKPDHLVAPRVKPLLPPRSGSSSSGVPAPNLTPVNVPPTPPPRKSSASQRSGDLLASSPEESSISWKPLV
|
3.1.3.36
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15316017};
|
phosphatidylinositol dephosphorylation [GO:0046856]; phosphatidylinositol metabolic process [GO:0046488]; protein transport [GO:0015031]
|
cell division site [GO:0032153]; cell tip [GO:0051286]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]
|
calcium ion binding [GO:0005509]; inositol-1,2,4,5,6-pentakisphosphate 5-phosphatase activity [GO:1990651]; inositol-1,2,4,5-tetrakisphosphate 5-phosphatase activity [GO:1990649]; inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity [GO:0052659]; inositol-1,4,5-trisphosphate 5-phosphatase activity [GO:0052658]; inositol-2,4,5,6-tetrakisphosphate 5-phosphatase activity [GO:1990650]; inositol-2,4,5-triphosphate 5-phosphatase activity [GO:1990640]; inositol-4,5,6-triphosphate 5-phosphatase activity [GO:1990648]; inositol-4,5-bisphosphate 5-phosphatase activity [GO:0030487]; phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity [GO:0034485]; phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity [GO:0043813]; phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity [GO:0004439]; SH3 domain binding [GO:0017124]
|
PF03372;PF02383;
|
3.60.10.10;
|
Synaptojanin family; Inositol 1,4,5-trisphosphate 5-phosphatase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Note=Localizes at the cell tip and the barrier septum.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178, ChEBI:CHEBI:58456; EC=3.1.3.36; Evidence={ECO:0000269|PubMed:11348594};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=57.8 uM for Ins(1,4,5)P3 (at pH 7.4 and 30 degrees Celsius) {ECO:0000269|PubMed:15316017}; KM=10.9 uM for Ins(2,4,5)P3 (at pH 7.4 and 30 degrees Celsius) {ECO:0000269|PubMed:15316017}; KM=75.9 uM for Ins(2,4)P2 (at pH 7.4 and 30 degrees Celsius) {ECO:0000269|PubMed:15316017}; KM=5860 uM for p-nitrophenyl phosphate (at pH 7 and 30 degrees Celsius) {ECO:0000269|PubMed:15316017}; KM=182 uM for 3-O-methylfluorescein phosphate (at pH 7 and 30 degrees Celsius) {ECO:0000269|PubMed:15316017}; KM=530 uM for magnesium ions {ECO:0000269|PubMed:15316017}; KM=12 uM for manganese ions {ECO:0000269|PubMed:15316017}; KM=6.39 uM for nickel ions {ECO:0000269|PubMed:15316017}; KM=14.5 uM for cobalt ions {ECO:0000269|PubMed:15316017};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is about 7.4. {ECO:0000269|PubMed:15316017};
| null |
FUNCTION: Controls the cellular levels and subcellular distribution of phosphatidylinositol 3-phosphate and phosphatidylinositol 4,5-bisphosphate. Involved in distinct membrane trafficking and signal transduction pathways. Highly active against a range of soluble and lipid inositol phosphates. Active in dephosphorylating the 5-position of Ins(1,4,5)P3 and Ins(1,3,4,5)P4 and to a lesser extent Ins(1,4,5,6)P4. The enzyme is also active against PI(4,5)P2 presented in sonicated vesicles and Triton mixed micelles, and somewhat less active against PI(3,5)P2 in unilamellar vesicles. Activity against PI(3,5)P2 drops sharply when this substrate is presented in mixed micelles. Also hydrolyzes PIP3 to produce PI(3,4)P2. {ECO:0000269|PubMed:15316017}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O43007
|
C1TM_SCHPO
|
MNVMVSFNQLRNYFLESNSLRPSKWLFQSYGTSSSANILNGKLLARKLQRSVAEEVQALKAKDRNFKPALAIVQVGKREDSNVYVRMKEKAARLVGIDFKYCPFPETIQMPALLHELKKLNDDHTVHGVLVQLPLPKHLNERTVTESITPPKDVDGFGAFNIGLLAKNDATPIHYPCTPKGIMELLKDNKISVAGLNAVVLGRSDIVGNPISYLLRKDNATVTVCHSKTKDLIQHISNADLVIAALGKPEFVRGEWLKPGSVVVDVGINAVQRNGKRVLVGDVHFESASKVASSITPVPGGVGPMTVAMLMENIVNAAKIARTENIYRKIDLNPLELKKPVPSDIEIANSQEPKLISNLAKEMGIYDTELENYGNYKAKVNLAVYERLKHRKDGNYVVVSGITPTPFGEGKSTVVAGLVQAMGHLGKLGIACVRQPSQGPTFGVKGGAAGGGYAQFIPMDDFNLHMTGDIHAVTAANNLLVAALETRMFHENTQSDAALIKRLIPVKNGRRVIPRGLIGRWNRICASHNMDPEDVNNASPELLKEFVRLNVDPDTIECNRVLDVNDRFLRSIEVGKASTEKGHVRKTSFDISVASECMSILALSCDLNDMHSRLSRMVIANDKYGNAITAGDLGVSGALTVLLKDAIKPNLMQTLEGTPAFVHAGPFANISIGASSIIADKIALKLAGTESFDRPEDAGYVVTEAGFASDMGMEKFFNIKCRYSKLVPNTVVLVTTVKALKLHGGGPKLKPGAPIPEEYLVENLDLVKNGCSNMVKHIQNCHKFNIPVVVAINSYKTDSSKEHEIIREAALQAGAVDAVPSDHWAQGGKGAIELAKSVMTACDQSSNSKFRLLYDSETSIEDKVNVIAKEMYGANGVEFSSLAKERINTFIKQGFGNLPICMAKTQYSLSHNPEFRNVPKNFTVPIRDMRLNAGAGFIYPLAAEIQTIPGLPTAPAYLNIDICENGEIVGLS
|
1.5.1.5; 3.5.4.9; 6.3.4.3
| null |
10-formyltetrahydrofolate biosynthetic process [GO:0009257]; folic acid biosynthetic process [GO:0046656]; purine nucleobase biosynthetic process [GO:0009113]; tetrahydrofolate interconversion [GO:0035999]
|
cytosol [GO:0005829]; mitochondrion [GO:0005739]
|
ATP binding [GO:0005524]; formate-tetrahydrofolate ligase activity [GO:0004329]; methenyltetrahydrofolate cyclohydrolase activity [GO:0004477]; methylenetetrahydrofolate dehydrogenase (NADP+) activity [GO:0004488]
|
PF01268;PF00763;PF02882;
|
3.10.410.10;3.40.50.10860;3.40.50.720;3.40.50.300;
|
Tetrahydrofolate dehydrogenase/cyclohydrolase family; Formate--tetrahydrofolate ligase family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
|
CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-methenyltetrahydrofolate + NADPH; Xref=Rhea:RHEA:22812, ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.5; Evidence={ECO:0000250|UniProtKB:P09440}; CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methenyltetrahydrofolate + H2O = (6R)-10-formyltetrahydrofolate + H(+); Xref=Rhea:RHEA:23700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57455, ChEBI:CHEBI:195366; EC=3.5.4.9; Evidence={ECO:0000250|UniProtKB:P09440}; CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6R)-10-formyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:20221, ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57453, ChEBI:CHEBI:195366, ChEBI:CHEBI:456216; EC=6.3.4.3; Evidence={ECO:0000250|UniProtKB:P09440};
| null |
PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
| null | null |
FUNCTION: Mitochondrial isozyme of C-1-tetrahydrofolate synthase. The trifunctional enzyme catalyzes the interconversion of the one-carbon derivatives of tetrahydrofolate (THF) between different oxidation states by the enzymatic activities 10-formyltetrahydrofolate synthetase, 5,lO-methenyltetrahydrofolate cyclohydrolase, and 5,lO-methylenetetrahydrofolate dehydrogenase. {ECO:0000250|UniProtKB:P09440}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O43029
|
FAP1_SCHPO
|
MVKNTSVIIVGAGVFGLSAALELTKRGGYTIKILDRAPPPVIDGSSVDANRIIRSDYADAVYCSMGIDALEEWRTNPLFKEQFYGSGLMFVGRDNVEYRDMSLENLTKMGVSAAKFQTTEELRKLFPKWIGELNDGEAGYANFSSGWANAEQSVKSVVNYLAHAGVSFISGPEGTVEELITEENVVKGVRTTTGAYMAEKLIFATGAWTASLLPNDHTRFLATGQPVAYIKLTPEEYIRFLTNPVYLDFDTGFYIFPPTPDGYLKFARHGYGFTRMQNLKSGKVESVPPKKPLVSPILPKEAELDLRRNLQRTYGEEISQRPFYKTRICYYTDTADAEFVFDYHPDYENLFVCTGGSGHGFKFFPILGKYSIGCMFRELEEPLLKKWRWKKENLEFAALDHSRAGPSRQELS
|
1.5.3.7
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:16233628};
|
L-lysine catabolic process [GO:0019477]
|
cytosol [GO:0005829]; extracellular region [GO:0005576]; nucleus [GO:0005634]
|
flavin adenine dinucleotide binding [GO:0050660]; L-pipecolate oxidase activity [GO:0050031]; proline dehydrogenase activity [GO:0004657]; sarcosine oxidase activity [GO:0008115]
|
PF01266;
|
3.30.9.10;3.50.50.60;
|
MSOX/MTOX family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
|
CATALYTIC ACTIVITY: Reaction=L-pipecolate + O2 = H(+) + H2O2 + L-1-piperideine-6-carboxylate; Xref=Rhea:RHEA:11992, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:58769, ChEBI:CHEBI:61185; EC=1.5.3.7; Evidence={ECO:0000269|PubMed:16233628};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.07 mM for L-pipecolate {ECO:0000269|PubMed:16233628}; KM=33.5 mM for L-proline {ECO:0000269|PubMed:16233628}; Vmax=46.1 umol/min/mg enzyme for L-pipecolate {ECO:0000269|PubMed:16233628}; Vmax=9.45 umol/min/mg enzyme for L-proline {ECO:0000269|PubMed:16233628};
| null | null | null |
FUNCTION: Oxidizes L-pipecolate and L-proline (6,7% of the activity for L-pipecolate). {ECO:0000269|PubMed:16233628}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O43043
|
SCAP_SCHPO
|
MRIFTLGKGRISRGYARQVNPSLFAKYSYCIANNPWYFILVFTLLSITGIYSSLVAYQQSLYDQSLARWSAWYAESINAEANVITKQLYLLGTNTSVFSEDYLSNAYRWETSFHQYLAEYGYPCIRDEKSCVTISPIPKYYGKVDPVAQYSYTKGLPENEREVNKLRNDTIAEGFDSLSAFVITYFLKPEQVDTFHVVLKKFISETPNLYASLLDTSPTTVVARIPDLTVIYRWYLWVGFGVGLFAYLYLSLVRLHDIRAKFGLTATIFIQSGTAYFSTCSLLYFFERTGPICPWPMAYYIIIFMDIENSFRLLRAVIASPQTKRVPSRIMEGFSSTIIASFSSLLKKLLTLFVLSFFVYPLVQEFCLFLACSFVVSFLLHGSFFLAVLSVDIRRLELQDFLDSNSSNRNSKWWVPYLEYVRFMWSPWIIDNLGTVSFHMYVIYLQLQSSTDINGSWRLASPNIRFLITLYHRLGRILRERKLFPLITTGWFGDPTFLEALKEKTMAENLVIALYRPVILDTVNRRDYTNVYNSFHDRRVWRWSTFFSILFAIDFAVGLLVKALLRGWSDHDELSTDTTLHEEKFRIEPVPVHHQLDILKIAVSENYKTFASVGLDRCLVVWDLRQWCTKLVLSKEQMPRTLKAIALDPQGNYVSLFSKDTLFILNVESPCLMLQHSYHCKPNSKLNVFWMPGTHKDDEWKNFELVVVESSGEIQVFSLTIEIEGADIALVEKFQLSSPIIKSISIVSPTANRIACLTESGEVTVYSKKGPVWSPKILSQNKNYLTETKKDIYGIAMADILFLARDSGVDMIDLKNDELLHSFTLPPIKVNTFSVGVSNSRFVNGQFRVSSISFCFTHAVTEKVLYYYYGNECNESYIILNKWDQQPNLVDVHDPDNSLACLTFDELQENIHEVEDASECVMSSDGLYIFGMRRKSSSGICPTADEKNEDNGFTLRNRKLRTGHYNWTSYVPLLDSYMQDMEHKKNTHSGGETQVWEVWMYSQSEKKHRCKSLKMYNSLIIADPGPSLAVSDRCVAIVLGNYVALVGYGSEIFRDFYQIRNSDEMDRILRRKRKNLQRKRSGTIGC
| null | null |
cellular response to hypoxia [GO:0071456]; positive regulation of ergosterol biosynthetic process [GO:0070452]; regulation of cholesterol biosynthetic process [GO:0045540]; SREBP signaling pathway [GO:0032933]; steroid metabolic process [GO:0008202]
|
cytoplasmic side of endoplasmic reticulum membrane [GO:0098554]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; SREBP-SCAP complex [GO:0032936]
|
sterol binding [GO:0032934]
|
PF12349;
|
2.130.10.10;
|
WD repeat SCAP family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P97260}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P97260}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P97260}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P97260}.
| null | null | null | null | null |
FUNCTION: Escort protein required for sre1 processing at low sterol as well as oxygen levels. May regulate export of the scp1/sre1 complex from the ER at low sterol or oxygen levels (PubMed:15797383, PubMed:17595166). 4-methyl sterols bound to scp1 may mask an ER export signal in scp1 leading to retention of the complex in the ER (PubMed:15797383, PubMed:17595166). Release of 4-methyl sterols may trigger a conformational change in the SSD domain of scp1 unmasking the ER export signal leading to recruitment into COPII-coated vesicles, transport to the Golgi complex, proteolytic cleavage of sre1 in the Golgi, release of the transcription factor fragment of sre1 from the membrane, its import into the nucleus and up-regulation of genes required for ergosterol biosynthesis as well as anaerobic growth (By similarity). Binds 4-methyl sterols (PubMed:17595166). {ECO:0000250|UniProtKB:P97260, ECO:0000269|PubMed:15797383, ECO:0000269|PubMed:17595166}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O43052
|
RGA1_SCHPO
|
MSQRDAKKDGLLYTTNGVSPTPPKRIPVPSRQNKIEENSTTKNFPHSRHTSTVAGTEGGSSLSRRHTSAESRKALPNQQQLAQSGLLNKEEQQSLKRSDTSVFPKAVRKVSSSKICASCGQVISGQYVRALGNIYHLECFRCHDCNSLVASKFFPIDDPTLNKQVPLCETDYFRRLDLLCASCGMALRGYYITALNKKFHIEHFTCSLCYTVFGPNDSYYEYEGKVYCHYHYSTLFAARCCGCDGPILRQFVEVYRNGVSQNWHVPCHMIYKFWNVKLCQKTSIETSKKKDSELSQSQLRKREKHLEQKIFHIWHALSYFEEYTASCISDMLLLVSNGEFTKSVICAQKFIRYIEILFKGIDSLETILSSFHAKSMPYVREAKLLCKKLVSIFALLAKCHNSDIRDVAIVQDFLSLFTGLAHYLKLLIRISLTGGLRLEQDHACKHALPQFLQTVEEARFVDQEGYDSSSFDMPLNLANASSDLCYVCHSALEEDCVLLGEIRCHIGCLSCTKCKYNNRENYDWARWNNQTKQIECYLCYTESSNVSNDEPHPSFEYVSRLSQYIYLLRIALVRLYTILMENNDSSQRKPLSVDPKQENVSSTVETAKQAETTASSDSFRKYANTLNDLRHLKSSRNRKATSNETQSSSNSTETSKLSKNVSESGKDKSPHWHSHGGSITGKSIVEQASSPLERRMDAFDENRAFTLDDIPKVISEQRNREHRPNAFRHMPSYTDPSYRKNSGAIYDKNDGTQKGLTPKSEDAPIRYLSDLSNLELLFTKHVAVLILHPLVRDYYSLDELMEMSDLRKGGFWEKFGKAFKGKDAEKKNVKKKGTFGVPLEILVERNNAQSTVGTGVGVKHIPAFIGNTLAAMKRKDMSVVGVFRKNGNIRRLKELSDMLDVSPDSIDYEQETPIQLAALLKKFLRELPDPLLTFKLFGLFITSSKLESEEERMRVLHLTICLLPKGHRDTMEVIFGFLYWVASFSHIDDEVGSKMDIHNLATVITPNILYSKSNDPVDESFLAIEAVHLLIENFEKFCEVPREISLLLDDPTLFYNNAAWTSKELYKRCEEIISQMSLDERNTPKHTASTKRKRQPIRRVTTNLTSDVPSGSEVADTNSLSSTTKDEASPNSDAQPKPQVKPQHAVIRDS
| null | null |
actin cytoskeleton organization [GO:0030036]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of actin filament polymerization [GO:0030833]; regulation of cell wall organization or biogenesis [GO:1903338]; regulation of small GTPase mediated signal transduction [GO:0051056]; signal transduction [GO:0007165]
|
cell cortex of cell tip [GO:0051285]; cell division site [GO:0032153]; cell tip [GO:0051286]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; division septum [GO:0000935]; nucleus [GO:0005634]
|
GTPase activator activity [GO:0005096]; metal ion binding [GO:0046872]
|
PF00412;PF00620;
|
2.10.110.10;1.10.555.10;
| null | null |
SUBCELLULAR LOCATION: Cell tip {ECO:0000269|PubMed:11737264}. Nucleus {ECO:0000269|PubMed:11737264}. Note=Cell poles and cell division site. {ECO:0000269|PubMed:11737264}.
| null | null | null | null | null |
FUNCTION: GTPase-activating protein for Rho1. Involved in the F-actin patch localization, cell morphogenesis, regulation of septation, and cell wall synthesis. {ECO:0000269|PubMed:11737264}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O43058
|
SEP1_SCHPO
|
MNFNSTNPYYFTHEKNLNNASKYSELPIAYQEIPLQSLPPYPKVASKLKGVVAGGKENNIASFQKPSSKATRPYIPSYTRLTYSVPPLPIPPPSEQSLDTIIYRNPSVSSSQSQEPEEFFLPLDDGKKPPYSYAMLIGMSIIRSPDRRLTLSAIYDWISNTFSFYNKSNNGWQNSIRHNLSLNKAFMKIERPRNLPGKGHFWSIRPGHEEQFLKLKLRKPGVNSRPAPPVQDVTSSTKYGSSTGSSGFNTFNTSPHIFNQRHQYLQNYYTASLTNIPTISNVNATNFHPLHSQQPYVDTPGIDAPSDLEAKFSDLGVSSVVSVTSPLQSCTNSPSPPLSSPASSASPSESLRNESLGIKSAKSLGLNKDDAPVEGPPVSHLEKDVETPSVHDSVLGFNDTVTNLGKKGLKDGTTNTLQIPAVRLPSLPSSPTIKNPSGLLLKRSNSIDFPTPPKALCPKLFCFRDDIVADDYTKFSLLSPIRSDMSGISASPNTNLKEHRTRILQMLATPDAKQLSSLTSSDAEFWSVTPLKSSILRNGDASKQVTLSESPKGDSLLDGGSLSYFTNNISSVAGLETPSKLPMSKSFDTFEDDFLDPMDMLSFENHFSDFNSNRKVSPVKREVRRKYISSATTIHSSAAQDDTYLPSPTKRKMPLLRQTSTLF
| null | null |
anatomical structure morphogenesis [GO:0009653]; cell differentiation [GO:0030154]; division septum assembly [GO:0000917]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
|
chromatin [GO:0000785]; M/G1 phase-specific MADS box-forkhead transcription factor complex [GO:0097221]; nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00250;
|
1.10.10.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:9427538}.
| null | null | null | null | null |
FUNCTION: Required for promoter sequence element PCB-driven, M-phase-specific transcription. Acts as a transcriptional activator with a role in the regulation of mitosis. Regulates septation and the periodic transcription of cdc15. {ECO:0000269|PubMed:15509866}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O43060
|
EIF3F_SCHPO
|
MALGTKHVLHLTKPSSRSSPLNIVIEPAVLFSILDHSTRKSENNQRVIGTLLGTRSEDGREIEIKSCFAVPHNESSEQVEVEMEYHRAMYHLHLKANPREVVVGWYATSPDLDAFSALIQNLYASPAEPGTAPLGTYPHPCVHLTVNTDVSSPLAIKTYVSSPVGITERLADSCAFVPTPFTIRDDEAVRSGLKAVAAPKNDPSRLASLFTDLQQLRRSTLELLSMIERVSDYVQNVIDGSSPANVAVGRYLMKCFSLIPCVEGQDFEKIFSSHLQDVLVVVYLANTLRTQVDIASRLNLLP
| null | null |
cytoplasmic translational initiation [GO:0002183]; formation of cytoplasmic translation initiation complex [GO:0001732]; translational initiation [GO:0006413]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; 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]
|
deubiquitinase activity [GO:0101005]; metallopeptidase activity [GO:0008237]; translation initiation factor activity [GO:0003743]; translation initiation factor binding [GO:0031369]
|
PF01398;PF13012;
|
3.40.140.10;
|
EIF-3 subunit F family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03005, ECO:0000269|PubMed:15904532, ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: 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_03005, ECO:0000269|PubMed:15904532}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O43068
|
MDE4_SCHPO
|
MSTISTSTDSKLDNLGLSVTSRRNQILFYLSKALNLAHLLRSDSLQKSFLDALKQSATDSELLHKNLDEIKFLQNEKLNNEKLLEQEQNEANDYRLKVERLEHKISDYVQEINSLNSQLQIQKSNPEKHEDAVSQNRLRGSLDTVSSPSKTHKANKDEKATRLHLIIANLKKALKEKDAEVLNLQSHVSSKESELDRFKIKLETEESNWKVRLQVLESKLATQDRKLRMQKKSTERKSLLVSPRVSSPKLFSPSKQAIMGTRQPNATSGSPLSVTPFLQKTSTSIGLSSSPPQSSPSAQSSQPFSRDKYPHSMTVSPSNARYLKKHLDDTIPSNVSDINHNDHLKIPQSPSSLSPSKIPIRKKRKLKDTVSNCEFTEEDSESSFLLETIQPTKSTLRRSISPLKKRNDEINELKKGFTMKK
| null | null |
attachment of mitotic spindle microtubules to kinetochore [GO:0051315]; cell division [GO:0051301]; meiotic sister chromatid segregation [GO:0045144]; mitotic chromosome centromere condensation [GO:1990893]
|
chromosome, centromeric core domain [GO:0034506]; mitotic spindle [GO:0072686]; mitotic spindle pole body [GO:0044732]; monopolin complex [GO:0033551]; nucleolus [GO:0005730]; nucleus [GO:0005634]
| null |
PF10422;
| null | null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17627824}. Chromosome, centromere {ECO:0000269|PubMed:17627824}. Note=Localizes to the central core of the centromere.
| null | null | null | null | null |
FUNCTION: The monopolin-like pcs1/mde4 complex is essential for accurate chromosome segregation during mitosis and meiosis II. May clamp together microtubule binding sites on the same kinetochore, preventing merotelic attachment of microtubules. {ECO:0000269|PubMed:17627824}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O43069
|
ATG7_SCHPO
|
MFVGKALQFQSFHSSIDATFWHQLSNYKVEKQKLDASPLTIHGKFNTYSRGNISIVFGEAPSNSNIKDCLAEGTLLNANTPQEFTNADVKKIREEIGEVLLNSIKNGVVSERPNELLRFLIFSYADIKAYKYHYWCLFPSFKETPHWIVKDLSPAESLIPSGPILSQIREFLSTADYYQRPFFLLIKSTLDEWTIAPLKELSHCVDKSLQFYLVAEDSVQLAEYPSWPVRNILAFAFIKFKLKVINLFLYRDGINSDTLSKSILIKVEADKDMILEAPLSIVGWERNGKGVLGPRVVNLSTVLDPFVLSESASTLNLSLMRWRLVPQLDLDRIQNSKCLLLGAGTLGCGVARNLLSWGVRHVTFVDYSTVSYSNPVRQSLFTFEDCKRKLPKAECAAQRLKEIYPNMFSTGYNISIPMLGHPIYEAGIEKTMHDYETLENLISTHDAIFLLTDTRESRWLPTVISTAMDKLLINSALGFDSWLVMRHGSVLQKENRLGCYFCNDIFAPSNSLVDRTLDQTCTVTRSGCANIATAIAVELFVSLLQHPNGHAAPVLNEDQTVLGELPHQIRGFLHNFSLMKISGMAYPQCSACSECIINEWNREKWMFVLRAINEPDYVEELCGLREVQALGEIAGTMEEWISDKESVIL
| null | null |
autophagosome assembly [GO:0000045]; cellular response to nitrogen starvation [GO:0006995]; macroautophagy [GO:0016236]; piecemeal microautophagy of the nucleus [GO:0034727]; protein modification by small protein conjugation [GO:0032446]; protein transport [GO:0015031]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; phagophore assembly site [GO:0000407]; phagophore assembly site membrane [GO:0034045]
|
Atg12 activating enzyme activity [GO:0019778]; Atg8 activating enzyme activity [GO:0019779]; ATP hydrolysis activity [GO:0016887]
|
PF16420;PF00899;
|
3.40.50.720;3.40.140.100;3.40.140.70;
|
ATG7 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Preautophagosomal structure membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates atg12 for its conjugation with atg5 and atg8 for its conjugation with phosphatidylethanolamine. Both systems are needed for the atg8 association to Cvt vesicles and autophagosomes membranes. Autophagy is essential for maintenance of amino acid levels and protein synthesis under nitrogen starvation. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Plays a role in the regulation of filamentous growth and chronological longevity (By similarity). Plays a role in meiosis and sporulation. {ECO:0000250, ECO:0000269|PubMed:19778961}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O43070
|
NBS1_SCHPO
|
MWIIEAEGDILKGKSRILFPGTYIVGRNVSDDSSHIQVISKSISKRHARFTILTPSEKDYFTGGPCEFEVKDLDTKFGTKVNEKVVGQNGDSYKEKDLKIQLGKCPFTINAYWRSMCIQFDNPEMLSQWASNLNLLGIPTGLRDSDATTHFVMNRQAGSSITVGTMYAFLKKTVIIDDSYLQYLSTVKESVIEDASLMPDALECFKNIIKNNDQFPSSPEDCINSLEGFSCAMLNTSSESHHLLELLGLRISTFMSLGDIDKELISKTDFVVLNNAVYDSEKISFPEGIFCLTIEQLWKIIIERNSRELISKEIERLKYATASNSTPQKIIQPQRHIQKNIVDDLFSVKKPLPCSPKSKRVKTLENLSIMDFVQPKQMFGKEPEGYLSNQSNNGSAQNKKSGDNSEKTKNSLKSSSKKSANTGSGQGKTKVEYVSYNSVDKGNSSPFKPLELNVVGEKKANAEVDSLPSENVQESEDDKAFEENRRLRNLGSVEYIRIMSSEKSNANSRHTSKYYSGRKNFKKFQKKASQKAPLQAFLSLSEHKKTEVFDQDDTDLEPVPRLMSKVESIPAGASSDKSGKSSISKKSSNSFKELSPKTNNDEDDEFNDLKFHF
| null | null |
DNA double-strand break processing [GO:0000729]; DNA duplex unwinding [GO:0032508]; DNA repair [GO:0006281]; double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724]; double-strand break repair via nonhomologous end joining [GO:0006303]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; mitotic intra-S DNA damage checkpoint signaling [GO:0031573]; protein localization to chromosome, telomeric region [GO:0070198]; telomere maintenance [GO:0000723]; telomere maintenance via recombination [GO:0000722]
|
chromosome, telomeric repeat region [GO:0140445]; Mre11 complex [GO:0030870]; nucleus [GO:0005634]; site of double-strand break [GO:0035861]
|
chromatin-protein adaptor activity [GO:0140463]; damaged DNA binding [GO:0003684]; molecular adaptor activity [GO:0060090]; phosphorylation-dependent protein binding [GO:0140031]
|
PF00498;
|
2.60.200.20;3.40.50.11080;3.40.50.10190;
|
Nibrin family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12944481}. Chromosome {ECO:0000269|PubMed:19804755}. Chromosome, telomere {ECO:0000269|PubMed:12944481, ECO:0000269|PubMed:12944482}. Note=Localizes to DNA double-strand breaks (DSBs); recruited to DNA damage sites. {ECO:0000269|PubMed:19804755}.
| null | null | null | null | null |
FUNCTION: Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed:12944481, PubMed:12944482, PubMed:15964794, PubMed:19804755, PubMed:22705791). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (PubMed:12944481, PubMed:12944482, PubMed:15964794, PubMed:19804755, PubMed:22705791). The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of tel1/atm upon DNA damage (PubMed:15964794, PubMed:19804755). The MRN complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11, to initiate end resection, which is required for single-strand invasion and recombination (By similarity). Within the MRN complex, nbs1 acts as a protein-protein adapter, which specifically recognizes and binds phosphorylated proteins, promoting their recruitment to DNA damage sites (PubMed:19804755, PubMed:22705791). Recruits rad32 and rad50 components of the MRN complex to DSBs in response to DNA damage (By similarity). Promotes the recruitment of tel1/atm to the DNA damage sites, activating tel1/atm function (PubMed:15964794). Mediates the recruitment of phosphorylated ctp1/CtIP to DSBs, leading to cooperation between the MRN complex and ctp1/CtIP to initiate end resection (PubMed:19804755). {ECO:0000250|UniProtKB:O60934, ECO:0000269|PubMed:12944481, ECO:0000269|PubMed:12944482, ECO:0000269|PubMed:15964794, ECO:0000269|PubMed:19804755, ECO:0000269|PubMed:22705791}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O43085
|
DSC1_SCHPO
|
MDRRRWVPSTPVVTLLLLFMLFAPAPRLPSRNGESSEKSIKAEKRAFSEIKNATFLNIPERVEHSLTFPTEIWETRDGLFEEPVGKGDSHLNHTSVMTGNWNILPYPSFGKVSPNVTWHTTLRNIVMSQSGRFSANLYEYVDGNSDGISFVLNLENNNDTSVYHMTFHGDRVKPINVFLGSTDVTPNFGGVDVIPWLLKDSPYKDAPPLDGTEYFPLLQNRSLERIETRLQDAQTVGWSPLVFEEEEVTCSAFVFLHNKNTGLDKETLKAIENEFYHPQGVSTQKMPEVFVSGLVYSPDCNVAFTFSNTKGPRNFVLENHLVRFSSLYIFIVLSQIFVLLRQMRINSPSHVQRLSFLTIAMQAGLDAYIAIFFLSTNAVIEKGYLPFVSVAFLSLVPSVMFTMRYLALILRVQNSNMPPPAPRPVTNNSSNNNTNQSNASNENSPNAPSAANDNTETTTVNPPQEDDQPMTQHERDQRDWSAVCLRFYFIILVVCIASLYSAFWPVIYRFYFISALIFTSYSFWIPQIIQNVKQGTSRSFTWTYILGASVLRLYLPLAIFIDSELILGFPPKYFFALGLVLWMLFQVLVLLVQDTLGPRFFLPKKFFLSSPVYDYHPVIQQDDLEAFMRDANVCPICMQPIELVSTGSTLNPASMMVRRNYMLTPCHHLYHRQCLLQWMETRSICPVCRCHLPAV
|
2.3.2.27
| null |
proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein ubiquitination [GO:0016567]; SREBP signaling pathway [GO:0032933]; ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043162]
|
Dsc E3 ubiquitin ligase complex [GO:0044695]; endomembrane system [GO:0012505]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
|
ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]
|
PF12678;
|
3.30.40.10;
| null | null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
|
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: Catalytic component of the DSC E3 ubiquitin ligase complex which is required for the sre1 transcriptional activator proteolytic cleavage to release the soluble transcription factor from the membrane in low oxygen or sterol conditions (PubMed:21504829, PubMed:27655872). The complex also plays an important role in the multivesicular body (MVB) pathway and functions in a post-endoplasmic reticulum pathway for protein degradation (PubMed:21504829). {ECO:0000269|PubMed:21504829, ECO:0000269|PubMed:27655872}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O43086
|
ELG1_SCHPO
|
MQIVGYLSADSQSNPDLKSENEAKEEKPIGRRHTMSPVPATSENKYFGKSPLSGSRKPRRSRSLHKERSYMRKFFDMDMEESKDFENDQSLLVTLKVSTSLGQKIENILHPKLSNDTNSTAFPPAKSSGEASDTNILVENINSQETVNSSPLVSELHYSNLADSPSNLRNTVTSMHPFFMSKSVKKNSEIKFVSEERGGTKPERLLDPLWPTPDSQSMLEYAGSIEPSVFWFPKKHLEEAILEETSHLSFKEVLSSTTANMITPLAEKNKTEVLQVTPSKLHTFALESLCFSPAPFIQKVLSRLLPSDPNVEMPMIPQILEKGLWVSKYAPSKTQDCCAFSQCLSKIADWLRSCRLTKPESSSVPPSSSISRSSTIHSCTSSKRNEDSLSESDFEPDIIEEEDDSDEFNPSVSRKKAKLTSSQFSNWMLVTGVTGIGKTSCLYAICRELNFEVVEIHPGMRRSGKELLERIGELTQSHIVDKSRLNNTPDILILLEEVDILFQDDRGFWQAVSTLIEKSKRPVVMTCNETDFLPSAFLQEDHIVQFQSISSALLTDYISSVLYADRCIISRNVVESISYRYGSDLRGILMQLNFWSLVNFPSLPSKDKQDDSHEPFIEATISAFDEGVGVYNPRIQTSEDLLQTYSEEQMGDIGLLFMPNLVNWRKVCVPKSEMEEKEAIMEKLIYSHQYADSLSYVDYRFSSQPTIYETYELMNDSASFEDMSLECRDNCANAFQDNLVGFPTISNPFHANAPPEPHELKLQYHSFCFINNLFSKSSLKAISSNDSIVPKALNNRELQLSALASTIGYKLDPDDVYNILSFLSFANSQVTSYTPPNSIDRPNDILILEVAPFVRCMRRYDRIRLNSYKLLLSSKGRSASHISRRGAASILRSAGYNYGRLQYLEGSDRILSTWFSTTLD
| null | null |
DNA recombination [GO:0006310]; mitotic DNA replication [GO:1902969]; telomere maintenance [GO:0000723]; UV-damage excision repair [GO:0070914]
|
chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; cytosol [GO:0005829]; Elg1 RFC-like complex [GO:0031391]; nuclear DNA replication factor C complex [GO:0043599]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA clamp loader activity [GO:0003689]; DNA clamp unloader activity [GO:0061860]
|
PF00004;
|
3.40.50.300;
|
ELG1 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome, telomere {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Involved in the negative control of telomere length and in telomeric silencing through a replication-mediated pathway. May have a role in Okazaki fragment maturation. Required for S-phase progression. An RFC-like complex (elg1-RFC) is formed where elg1 replaces rfc1 in the RFC complex. This complex appears to have a role in DNA replication, replication fork re-start, recombination and repair. {ECO:0000269|PubMed:16040599}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O43091
|
DPS1_SCHPO
|
MIQYVYLKHMRKLWSLGKVRSTVLRFSTTNRNASHLIKNELEQISPGIRQMLNSNSEFLEECSKYYTIAQGKQMRPSLVLLMSKATSLCHGIDRSVVGDKYIDDDDLRSFSTGQILPSQLRLAQITEMIHIASLLHDDVIDHANVRRGSPSSNVAFGNRRSILAGNFILARASTAMARLRNPQVTELLATVIADLVRGEFLQLKNTMDPSSLEIKQSNFDYYIEKSFLKTASLISKSCKASTILGQCSPTVATAAGEYGRCIGTAFQLMDDVLDYTSKDDTLGKAAGADLKLGLATAPVLFAWKKYPELGAMIVNRFNHPSDIQRARSLVECTDAIEQTITWAKEYIKKAKDSLLCLPDSPARKALFALADKVITRKK
|
2.5.1.91
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250};
|
farnesyl diphosphate biosynthetic process, mevalonate pathway [GO:0010142]; isoprenoid biosynthetic process [GO:0008299]; plastoquinone biosynthetic process [GO:0010236]; ubiquinone biosynthetic process [GO:0006744]
|
mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; polyprenyl diphosphate synthase complex [GO:0032476]; transferase complex [GO:1990234]
|
all-trans-decaprenyl-diphosphate synthase activity [GO:0097269]; metal ion binding [GO:0046872]; prenyltransferase activity [GO:0004659]
|
PF00348;
|
1.10.600.10;
|
FPP/GGPP synthase family
| null | null |
CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate = all-trans-decaprenyl diphosphate + 7 diphosphate; Xref=Rhea:RHEA:27802, ChEBI:CHEBI:33019, ChEBI:CHEBI:60721, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.91;
| null |
PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
| null | null |
FUNCTION: Supplies decaprenyl diphosphate, the precursor for the side chain of the isoprenoid quinones ubiquinone-10.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O43099
|
PRX5_ASPFU
|
MSGLKAGDSFPSDVVFSYIPWSEDKGEITACGIPINYNASKEWADKKVILFALPGAFTPVCSARHVPEYIEKLPEIRAKGVDVVAVLAYNDAYVMSAWGKANQVTGDDILFLSDPDARFSKSIGWADEEGRTKRYALVIDHGKITYAALEPAKNHLEFSSAETVLKHL
|
1.11.1.24
| null |
cell redox homeostasis [GO:0045454]; cellular response to oxidative stress [GO:0034599]; hydrogen peroxide catabolic process [GO:0042744]
|
cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; peroxisome [GO:0005777]
|
IgE binding [GO:0019863]; protein homodimerization activity [GO:0042803]; thioredoxin peroxidase activity [GO:0008379]
|
PF08534;
|
3.40.30.10;
|
Peroxiredoxin family, Prx5 subfamily
| null | null |
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:27624005};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=72.29 uM for H(2)O(2) {ECO:0000269|PubMed:27624005}; KM=70.48 uM for tert-butyl hydroperoxide {ECO:0000269|PubMed:27624005}; Note=kcat is 12.53 sec(-1) with H(2)O(2) as substrate and 12.96 sec(-1) with tert-butyl hydroperoxide as substrate. {ECO:0000269|PubMed:27624005};
| 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. Required for virulence. {ECO:0000269|PubMed:27624005}.
|
Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
|
O43100
|
CBF5_EMENI
|
MAKEVDYTIKPEATASNINTEDWPLLLKNYDKLMVRTGHFTPIPAGSSPLKRDLKSYINSGVINLDKPSNPSSHEVVAWMKRILRAEKTGHSGTLDPKVTGCLIVCIDRATRLVKSQQGAGKEYVCVIRLHDKIPGGEAQFKRALETLTGALFQRPPLISAVKRQLRIRTIHESKLYEFDNERHLGVFWVSCEAGTYIRTLCVHLGLLLGVGAHMQELRRVRSGAMSENEGMVTLHDVLDAQWLYDNQRDESYLRKVIKPLESLLTTYKRIVVKDSAVNAVCYGAKLMIPGLLRFEAGIELGEEVVLMTTKGEAIAIGIAQMSTVELSTCDHGVVAKVKRCIMERDLYPRRWGLGPVALEKKKLKSSGKLDKYGRANEATPAKWKSEYKDYSAPDGDSSQQAVDVVAKEEASPKEEPSLEANESKMDIDDAQDDEDKKKRKRHEGETPEERAERKRKKKEKKEKKERRKSKQEKDDSDDSD
|
5.4.99.-
| null |
anisotropic cell growth [GO:0051211]; box H/ACA RNA 3'-end processing [GO:0000495]; conidium formation [GO:0048315]; endocytosis [GO:0006897]; establishment of cell polarity [GO:0030010]; mRNA pseudouridine synthesis [GO:1990481]; rRNA pseudouridine synthesis [GO:0031118]; snRNA pseudouridine synthesis [GO:0031120]
|
box H/ACA snoRNP complex [GO:0031429]; microtubule [GO:0005874]
|
DNA binding [GO:0003677]; pseudouridine synthase activity [GO:0009982]; pseudouridylate synthase activity [GO:0004730]; RNA binding [GO:0003723]; snRNA pseudouridine synthase activity [GO:0106032]
|
PF08068;PF01472;PF16198;PF01509;
|
3.30.2350.10;2.30.130.10;
|
Pseudouridine synthase TruB family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:P33322}.
|
CATALYTIC ACTIVITY: Reaction=uridine in 5S rRNA = pseudouridine in 5S rRNA; Xref=Rhea:RHEA:47036, Rhea:RHEA-COMP:11730, Rhea:RHEA-COMP:11731, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; Evidence={ECO:0000250|UniProtKB:P33322}; CATALYTIC ACTIVITY: Reaction=uridine in snRNA = pseudouridine in snRNA; Xref=Rhea:RHEA:51124, Rhea:RHEA-COMP:12891, Rhea:RHEA-COMP:12892, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; Evidence={ECO:0000250|UniProtKB:P33322}; CATALYTIC ACTIVITY: Reaction=a uridine in mRNA = a pseudouridine in mRNA; Xref=Rhea:RHEA:56644, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:14659, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; Evidence={ECO:0000250|UniProtKB:P33322};
| null | null | null | null |
FUNCTION: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs and play a central role in ribosomal RNA processing. The H/ACA snoRNP complex also mediates pseudouridylation of other types of RNAs. Catalyzes pseudouridylation at position 93 in U2 snRNA. Also catalyzes pseudouridylation of mRNAs; H/ACA-type snoRNAs probably guide pseudouridylation of mRNAs. {ECO:0000250|UniProtKB:P33322}.
|
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
|
O43114
|
ORC5_SCHPO
|
MHLYQLEDELKKNVFCREDQIKKLSCLLFNKDCRVPSIVLYGVASTAKTFLLRTAFDLSKEENVWINLQDCFTVAHFWYRILIKVGVDKDIALKKGINISGFIYLLEQAMSKRDYHTFLVLDQIDDFAEASTILFSQLAQLPIVANIPNLSIIFVLHSHPAQYLGTLSIAVIFFPQYTQAEILEICQKTPPNLDFLDRSGDSVFEDEIELSVWMQYCSFLWSVFGVQCLNDYRSFRSVLDRYWPKFIQPIVEGDIHPADYAQLHKLAKNFLVSDATVTKRLHIINPTEIKNLLDSKSINLSLVSKYLLVSAFLASYNPSRLDAQFFSFSKTSKRRGRKRKQIQDEGVLFSKIPRTAGSKGRSAVKISQLTLGPKPFEVERLIAIYYAISSPVEKVLTADVFVQIATLASLKMILSASKGVLRSLDSPRYIVNVSREYVLKIADSLSFPLDSYLAG
| null | null |
DNA replication initiation [GO:0006270]; mitotic DNA replication initiation [GO:1902975]
|
chromatin [GO:0000785]; DNA replication preinitiation complex [GO:0031261]; nuclear origin of replication recognition complex [GO:0005664]; nuclear pre-replicative complex [GO:0005656]; nuclear replication fork [GO:0043596]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA replication origin binding [GO:0003688]
|
PF13191;PF14630;PF21639;
|
3.40.50.300;
|
ORC5 family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. ORC binds to multiple sites within the ars1 origin of DNA replication in an ATP-independent manner.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O43133
|
TBP_CANAL
|
MDLKLPPTNPTNPQQAKTFMKSIEEDEKNKAEDLDIIKKEDIDEPKQEDTTDGNGGGGIGIVPTLQNIVATVNLDCRLDLKTIALHARNAEYNPKRFAAVIMRIRDPKTTALIFASGKMVVTGAKSEDDSKLASRKYARIIQKLGFNAKFCDFKIQNIVGSTDVKFAIRLEGLAFAHGTFSSYEPELFPGLIYRMVKPKIVLLIFVSGKIVLTGAKKREEIYDAFESIYPVLNEFRKN
| null | null |
DNA-templated transcription initiation [GO:0006352]; transcription initiation at RNA polymerase I promoter [GO:0006361]; transcription initiation at RNA polymerase II promoter [GO:0006367]
|
RNA polymerase I transcription regulator complex [GO:0000120]; transcription factor TFIID complex [GO:0005669]; transcription regulator complex [GO:0005667]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; RNA polymerase II general transcription initiation factor activity [GO:0016251]; RNA polymerase III type 3 promoter sequence-specific DNA binding [GO:0001006]
|
PF00352;
|
3.30.310.10;
|
TBP family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II.
|
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
|
O43143
|
DHX15_HUMAN
|
MSKRHRLDLGEDYPSGKKRAGTDGKDRDRDRDREDRSKDRDRERDRGDREREREKEKEKELRASTNAMLISAGLPPLKASHSAHSTHSAHSTHSTHSAHSTHAGHAGHTSLPQCINPFTNLPHTPRYYDILKKRLQLPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVEYMRSLPGPKRGVACTQPRRVAAMSVAQRVADEMDVMLGQEVGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSDLKVIVMSATLDAGKFQIYFDNCPLLTIPGRTHPVEIFYTPEPERDYLEAAIRTVIQIHMCEEEEGDLLLFLTGQEEIDEACKRIKREVDDLGPEVGDIKIIPLYSTLPPQQQQRIFEPPPPKKQNGAIGRKVVVSTNIAETSLTIDGVVFVIDPGFAKQKVYNPRIRVESLLVTAISKASAQQRAGRAGRTRPGKCFRLYTEKAYKTEMQDNTYPEILRSNLGSVVLQLKKLGIDDLVHFDFMDPPAPETLMRALELLNYLAALNDDGDLTELGSMMAEFPLDPQLAKMVIASCDYNCSNEVLSITAMLSVPQCFVRPTEAKKAADEAKMRFAHIDGDHLTLLNVYHAFKQNHESVQWCYDNFINYRSLMSADNVRQQLSRIMDRFNLPRRSTDFTSRDYYINIRKALVTGYFMQVAHLERTGHYLTVKDNQVVQLHPSTVLDHKPEWVLYNEFVLTTKNYIRTCTDIKPEWLVKIAPQYYDMSNFPQCEAKRQLDRIIAKLQSKEYSQY
|
3.6.4.13
| null |
antiviral innate immune response [GO:0140374]; defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; response to alkaloid [GO:0043279]; response to toxic substance [GO:0009636]; RNA splicing [GO:0008380]
|
nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]; U12-type spliceosomal complex [GO:0005689]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on RNA [GO:0008186]; double-stranded RNA binding [GO:0003725]; helicase activity [GO:0004386]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]
|
PF00270;PF21010;PF04408;PF00271;PF07717;
|
1.20.120.1080;3.40.50.300;
|
DEAD box helicase family, DEAH subfamily, DDX15/PRP43 sub-subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12458796}. Nucleus, nucleolus {ECO:0000269|PubMed:12458796}.
|
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; Evidence={ECO:0000269|PubMed:19432882, ECO:0000269|PubMed:32179686};
| null | null | null | null |
FUNCTION: RNA helicase involved in mRNA processing and antiviral innate immunity (PubMed:19103666, PubMed:19432882, PubMed:24782566, PubMed:24990078, PubMed:32179686, PubMed:34161762). Pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA (PubMed:19103666). In cooperation with TFIP11 seem to be involved in the transition of the U2, U5 and U6 snRNP-containing IL complex to the snRNP-free IS complex leading to efficient debranching and turnover of excised introns (PubMed:19103666). Plays a key role in antiviral innate immunity by promoting both MAVS-dependent signaling and NLRP6 inflammasome (PubMed:24782566, PubMed:24990078, PubMed:34161762). Acts as an RNA virus sensor: recognizes and binds viral double stranded RNA (dsRNA) and activates the MAVS-dependent signaling to produce interferon-beta and interferon lambda-3 (IFNL3) (PubMed:24782566, PubMed:24990078, PubMed:34161762). Involved in intestinal antiviral innate immunity together with NLRP6: recognizes and binds viral dsRNA and promotes activation of the NLRP6 inflammasome in intestinal epithelial cells to restrict infection by enteric viruses (PubMed:34161762). The NLRP6 inflammasome acts by promoting maturation and secretion of IL18 in the extracellular milieu (PubMed:34161762). Also involved in antibacterial innate immunity by promoting Wnt-induced antimicrobial protein expression in Paneth cells (By similarity). {ECO:0000250|UniProtKB:O35286, ECO:0000269|PubMed:19103666, ECO:0000269|PubMed:19432882, ECO:0000269|PubMed:24782566, ECO:0000269|PubMed:24990078, ECO:0000269|PubMed:32179686, ECO:0000269|PubMed:34161762}.
|
Homo sapiens (Human)
|
O43147
|
SGSM2_HUMAN
|
MGSAEDAVKEKLLWNVKKEVKQIMEEAVTRKFVHEDSSHIIALCGAVEACLLHQLRRRAAGFLRSDKMAALFTKVGKTCPVAGEICHKVQELQQQAEGRKPSGVSQEALRRQGSASGKAPALSPQALKHVWVRTALIEKVLDKVVQYLAENCSKYYEKEALLADPVFGPILASLLVGPCALEYTKLKTADHYWTDPSADELVQRHRIRGPPTRQDSPAKRPALGIRKRHSSGSASEDRLAACARECVESLHQNSRTRLLYGKNHVLVQPKEDMEAVPGYLSLHQSAESLTLKWTPNQLMNGTLGDSELEKSVYWDYALVVPFSQVVCIHCHQQKSGGTLVLVSQDGIQRPPLHFPQGGHLLSFLSCLENGLLPRGQLEPPLWTQQGKGKVFPKLRKRSSIRSVDMEEMGTGRATDYVFRIIYPGHRHEHNAGDMIEMQGFGPSLPAWHLEPLCSQGSSCLSCSSSSSPHATPSHCSCIPDRLPLRLLCESMKRQIVSRAFYGWLAHCRHLSTVRTHLSALVHHSVIPPDRPPGASAGLTKDVWSKYQKDKKNYKELELLRQVYYGGIEHEIRKDVWPFLLGHYKFGMSKKEMEQVDAVVAARYQQVLAEWKACEVVVRQREREAHPATRTKFSSGSSIDSHVQRLIHRDSTISNDVFISVDDLEPPEPQDPEDSRPKPEQEAGPGTPGTAVVEQQHSVEFDSPDSGLPSSRNYSVASGIQSSLDEGQSVGFEEEDGGGEEGSSGPGPAAHTLREPQDPSQEKPQAGELEAGEELAAVCAAAYTIELLDTVALNLHRIDKDVQRCDRNYWYFTPPNLERLRDVMCSYVWEHLDVGYVQGMCDLLAPLLVTLDNDQLAYSCFSHLMKRMSQNFPNGGAMDTHFANMRSLIQILDSELFELMHQNGDYTHFYFCYRWFLLDFKRELLYEDVFAVWEVIWAARHISSEHFVLFIALALVEAYREIIRDNNMDFTDIIKFFNERAEHHDAQEILRIARDLVHKVQMLIENK
| null | null |
late endosome to Golgi transport [GO:0034499]; positive regulation of GTPase activity [GO:0043547]
|
cytoplasm [GO:0005737]; melanosome [GO:0042470]
|
GTPase activator activity [GO:0005096]; small GTPase binding [GO:0031267]
|
PF12068;PF00566;PF02759;
|
1.20.58.900;2.30.29.230;1.10.8.270;1.10.472.80;
|
RUTBC family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26620560}. Melanosome {ECO:0000269|PubMed:26620560}. Note=Melanosomal localization is mediated by RAB9A. {ECO:0000269|PubMed:26620560}.
| null | null | null | null | null |
FUNCTION: Possesses GTPase activator activity towards RAB32, RAB33B and RAB38 (PubMed:21808068, PubMed:26620560). Regulates the trafficking of melanogenic enzymes TYR, TYRP1 and DCT/TYRP2 to melanosomes in melanocytes by inactivating RAB32 and RAB38. Inhibits RAB32 and RAB38 activation both directly by promoting their GTPase activity and indirectly by disrupting the RAB9A-HPS4 interaction which is required for RAB32/38 activation (PubMed:26620560). {ECO:0000269|PubMed:21808068, ECO:0000269|PubMed:26620560}.
|
Homo sapiens (Human)
|
O43148
|
MCES_HUMAN
|
MANSAKAEEYEKMSLEQAKASVNSETESSFNINENTTASGTGLSEKTSVCRQVDIARKRKEFEDDLVKESSSCGKDTPSKKRKLDPEIVPEEKDCGDAEGNSKKRKRETEDVPKDKSSTGDGTQNKRKIALEDVPEKQKNLEEGHSSTVAAHYNELQEVGLEKRSQSRIFYLRNFNNWMKSVLIGEFLEKVRQKKKRDITVLDLGCGKGGDLLKWKKGRINKLVCTDIADVSVKQCQQRYEDMKNRRDSEYIFSAEFITADSSKELLIDKFRDPQMCFDICSCQFVCHYSFESYEQADMMLRNACERLSPGGYFIGTTPNSFELIRRLEASETESFGNEIYTVKFQKKGDYPLFGCKYDFNLEGVVDVPEFLVYFPLLNEMAKKYNMKLVYKKTFLEFYEEKIKNNENKMLLKRMQALEPYPANESSKLVSEKVDDYEHAAKYMKNSQVRLPLGTLSKSEWEATSIYLVFAFEKQQ
|
2.1.1.56
| null |
7-methylguanosine mRNA capping [GO:0006370]; cellular response to leukemia inhibitory factor [GO:1990830]
|
fibrillar center [GO:0001650]; mRNA capping enzyme complex [GO:0031533]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; receptor complex [GO:0043235]
|
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:11114884, ECO:0000269|PubMed:15767670}.
|
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:0000255|PROSITE-ProRule:PRU00895, ECO:0000269|PubMed:10347220, ECO:0000269|PubMed:27422871, ECO:0000269|PubMed:9705270, ECO:0000269|PubMed:9790902};
| null | null | null | null |
FUNCTION: Catalytic subunit of the mRNA-capping methyltransferase RNMT:RAMAC complex that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs (PubMed:10347220, PubMed:11114884, PubMed:22099306, PubMed:27422871, PubMed:9705270, PubMed:9790902). Binds RNA containing 5'-terminal GpppC (PubMed:11114884). {ECO:0000269|PubMed:10347220, ECO:0000269|PubMed:11114884, ECO:0000269|PubMed:22099306, ECO:0000269|PubMed:27422871, ECO:0000269|PubMed:9705270, ECO:0000269|PubMed:9790902}.
|
Homo sapiens (Human)
|
O43149
|
ZZEF1_HUMAN
|
MGNAPSHSSEDEAAAAGGEGWGPHQDWAAVSGTTPGPGVAAPALPPAAALLEPARLREAAAALLPTPPCESLVSRHRGALFRWLEERLGRGEESVTLEQFRELLEARGAGCSSEQFEEAFAQFDAEGDGTVDAENMLEALKNSSGANLQGELSHIIRQLQACSLVPGFTDIFSESKEGLDIHSSMILRFLHRNRLSSAVMPYPMLEHCNNMCTMRSSVLKESLDQLVQKEKESPGDLTRSPEMDKLKSVAKCYAYIETSSNSADIDKMTNGETSSYWQSDGSACSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVAVGRNASDLQEVRDVHIPSNVTGYVTLLENANVSQLYVQINIKRCLSDGCDTRIHGLRAVGFQRVKKSGVSVSDASAIWYWSLLTSLVTASMETNPAFVQTVLHNTQKALRHMPPLSLSPGSTDFSTFLSPNVLEEVDSFLIRITSCCSTPEVELTLLAFALARGSVAKVMSSLCTITDHLDTQYDASSLILSMASVRQNLLLKYGKPLQLTLQACDVKGKEDKSGPENLLVEPWTRDGFLTETGKTRASTIFSTGTESAFQVTQIRIMVRRGGIGAQCGLVFAYNSSSDKFCAEEHFKRFEKYDKWKLQELRQFVKSRIGCSSDDLGEDDPIGWFELEEEWDEADVKLQQCRVAKYLMVKFLCTRQESAERLGVQGLTISGYLRPARAEAEQSVTCAHCRKDTEESVCGATLLLRTLQFIQQLAHDLVQQKESGLKYKSFLDFAGLDLQIFWNFYSKLKQNPREECVSAQTLLLQLLQSCFSVLQGDVLAASEEEKAPIQSPKGVEAAKELYTHLCDVVDKVDGDSVPMEILKQEVRNTLLNGAAIFFPNRQTRRNHLFTMMNVTEQEHKQSLQLTFRSLCTYFSDKDPGGLLLLPEKNDLAKMNISEVLAVMDTLVSVAARECELLMLSGAPGEVGSVLFSLFWSVQGSLLSWCYLQLKSTDSGAKDLAVDLIEKYVGQFLASMRAILESLFSQYSGKTIVERLCNSVFSMAARQLVIFLLDFCTLDIPHCVLLREFSVLTELLKKLCSGPEGGLRKLDVETWQQEQPVVLHTWTKESAHNYENNCHEVSVFVSPGATYFEVEFDDRCETEKRYDYLEFTDARGRKTRYDTKVGTDKWPKKVTFKAGPRLQFLFHSDSSHNEWGYKFTVTACGLPDVAVSWGLDLQLLVSRLMGRLASQCMALKSVRQLGSNMVVPQAKMALVLSSPLWKPVFRHQVCPELELEASWPTHPHRNSKEVKNIPDDPCRHFLLDFAQSEPAQNFCGPYSELFKGFIQACRKQAPKTDIVAGSTIDQAVNATFAALVYRTPDLYEKLQKYVNSGGKIALSEEFAQVYSLADGIRIWMLEMKQKSLMSLGNEAEEKHSSEATEVNPESLAKECIEKSLLLLKFLPTGISSKESCEKLETADETSHLQPLNKRQRTSSVVEEHFQASVSPTEAAPPATGDQSPGLGTQPKLPSSSGLPAADVSPATAEEPLSPSTPTRRPPFTRGRLRLLSFRSMEEARLVPTVKEKYPVLKDVMDFIKDQSLSHRSVVKVLSLRKAQAQSILEVLKITQHCAESLGQPHCFHPPFILFLLELLTCQKDFTNYFGHLEGCGADLHKEIRDTYYQLVLFLVKAVKGFSSLNDRSLLPALSCVQTALLHLLDMGWEPNDLAFFVDIQLPDLLMKMSQENISVHDSVISQWSEEDELADAKQNSEWMDECQDGMFEAWYEKIAQEDPEKQRKMHMFIARYCDLLNVDISCDGCDEIAPWHRYRCLQCSDMDLCKTCFLGGVKPEGHGDDHEMVNMEFTCDHCQGLIIGRRMNCNVCDDFDLCYGCYAAKKYSYGHLPTHSITAHPMVTIRISDRQRLIQPYIHNYSWLLFAALALYSAHLASAEDVDGEKLDPQTRSSATTLRSQCMQLVGDCLMKAHQGKGLKALALLGVLPDGDSSLEDQALPVTVPTGASEEQLEKKAVQGAELSEAGNGKRAVHEEIRPVDFKQRNKADKGVSLSKDPSCQTQISDSPADASPPTGLPDAEDSEVSSQKPIEEKAVTPSPEQVFAECSQKRILGLLAAMLPPLKSGPTVPLIDLEHVLPLMFQVVISNAGHLNETYHLTLGLLGQLIIRLLPAEVDAAVIKVLSAKHNLFAAGDSSIVPDGWKTTHLLFSLGAVCLDSRVGLDWACSMAEILRSLNSAPLWRDVIATFTDHCIKQLPFQLKHTNIFTLLVLVGFPQVLCVGTRCVYMDNANEPHNVIILKHFTEKNRAVIVDVKTRKRKTVKDYQLVQKGGGQECGDSRAQLSQYSQHFAFIASHLLQSSMDSHCPEAVEATWVLSLALKGLYKTLKAHGFEEIRATFLQTDLLKLLVKKCSKGTGFSKTWLLRDLEILSIMLYSSKKEINALAEHGDLELDERGDREEEVERPVSSPGDPEQKKLDPLEGLDEPTRICFLMAHDALNAPLHILRAIYELQMKKTDYFFLEVQKRFDGDELTTDERIRSLAQRWQPSKSLRLEEQSAKAVDTDMIILPCLSRPARCDQATAESNPVTQKLISSTESELQQSYAKQRRSKSAALLHKELNCKSKRAVRDYLFRVNEATAVLYARHVLASLLAEWPSHVPVSEDILELSGPAHMTYILDMFMQLEEKHEWEKILQKVLQGCREDMLGTMALAACQFMEEPGMEVQVRESKHPYNNNTNFEDKVHIPGAIYLSIKFDSQCNTEEGCDELAMSSSSDFQQDRHSFSGSQQKWKDFELPGDTLYYRFTSDMSNTEWGYRFTVTAGHLGRFQTGFEILKQMLSEERVVPHLPLAKIWEWLVGVACRQTGHQRLKAIHLLLRIVRCCGHSDLCDLALLKPLWQLFTHMEYGLFEDVTQPGILLPLHRALTELFFVTENRAQELGVLQDYLLALTTDDHLLRCAAQALQNIAAISLAINYPNKATRLWNVEC
| null | null | null | null |
calcium ion binding [GO:0005509]; histone reader activity [GO:0140566]; lysine-acetylated histone binding [GO:0070577]; methylated histone binding [GO:0035064]; zinc ion binding [GO:0008270]
|
PF03256;PF00569;
|
3.30.60.90;1.10.238.10;2.60.120.260;
| null | null | null | null | null | null | null | null |
FUNCTION: Histone H3 reader which may act as a transcriptional coactivator for KLF6 and KLF9 transcription factors. {ECO:0000269|PubMed:33227311}.
|
Homo sapiens (Human)
|
O43150
|
ASAP2_HUMAN
|
MPDQISVSEFVAETHEDYKAPTASSFTTRTAQCRNTVAAIEEALDVDRMVLYKMKKSVKAINSSGLAHVENEEQYTQALEKFGGNCVCRDDPDLGSAFLKFSVFTKELTALFKNLIQNMNNIISFPLDSLLKGDLKGVKGDLKKPFDKAWKDYETKITKIEKEKKEHAKLHGMIRTEISGAEIAEEMEKERRFFQLQMCEYLLKVNEIKIKKGVDLLQNLIKYFHAQCNFFQDGLKAVESLKPSIETLSTDLHTIKQAQDEERRQLIQLRDILKSALQVEQKEDSQIRQSTAYSLHQPQGNKEHGTERNGSLYKKSDGIRKVWQKRKCSVKNGFLTISHGTANRPPAKLNLLTCQVKTNPEEKKCFDLISHDRTYHFQAEDEQECQIWMSVLQNSKEEALNNAFKGDDNTGENNIVQELTKEIISEVQRMTGNDVCCDCGAPDPTWLSTNLGILTCIECSGIHRELGVHYSRMQSLTLDVLGTSELLLAKNIGNAGFNEIMECCLPAEDSVKPNPGSDMNARKDYITAKYIERRYARKKHADNAAKLHSLCEAVKTRDIFGLLQAYADGVDLTEKIPLANGHEPDETALHLAVRSVDRTSLHIVDFLVQNSGNLDKQTGKGSTALHYCCLTDNAECLKLLLRGKASIEIANESGETPLDIAKRLKHEHCEELLTQALSGRFNSHVHVEYEWRLLHEDLDESDDDMDEKLQPSPNRREDRPISFYQLGSNQLQSNAVSLARDAANLAKEKQRAFMPSILQNETYGALLSGSPPPAQPAAPSTTSAPPLPPRNVGKVQTASSANTLWKTNSVSVDGGSRQRSSSDPPAVHPPLPPLRVTSTNPLTPTPPPPVAKTPSVMEALSQPSKPAPPGISQIRPPPLPPQPPSRLPQKKPAPGADKSTPLTNKGQPRGPVDLSATEALGPLSNAMVLQPPAPMPRKSQATKLKPKRVKALYNCVADNPDELTFSEGDVIIVDGEEDQEWWIGHIDGDPGRKGAFPVSFVHFIAD
| null | null | null |
cytosol [GO:0005829]; Golgi cisterna membrane [GO:0032580]; plasma membrane [GO:0005886]
|
GTPase activator activity [GO:0005096]; metal ion binding [GO:0046872]
|
PF12796;PF01412;PF16746;PF00169;PF14604;
|
1.25.40.950;1.25.40.20;1.10.220.150;1.20.1270.60;2.30.29.30;2.30.30.40;
| null |
PTM: Phosphorylated on tyrosine residues by SRC and PTK2B. {ECO:0000269|PubMed:10022920}.
|
SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, Golgi stack membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Note=Colocalizes with F-actin and ARF6 in phagocytic cups.
| null | null | null | null | null |
FUNCTION: Activates the small GTPases ARF1, ARF5 and ARF6. Regulates the formation of post-Golgi vesicles and modulates constitutive secretion. Modulates phagocytosis mediated by Fc gamma receptor and ARF6. Modulates PXN recruitment to focal contacts and cell migration. {ECO:0000269|PubMed:10022920, ECO:0000269|PubMed:10749932, ECO:0000269|PubMed:11304556}.
|
Homo sapiens (Human)
|
O43151
|
TET3_HUMAN
|
MSQFQVPLAVQPDLPGLYDFPQRQVMVGSFPGSGLSMAGSESQLRGGGDGRKKRKRCGTCEPCRRLENCGACTSCTNRRTHQICKLRKCEVLKKKVGLLKEVEIKAGEGAGPWGQGAAVKTGSELSPVDGPVPGQMDSGPVYHGDSRQLSASGVPVNGAREPAGPSLLGTGGPWRVDQKPDWEAAPGPAHTARLEDAHDLVAFSAVAEAVSSYGALSTRLYETFNREMSREAGNNSRGPRPGPEGCSAGSEDLDTLQTALALARHGMKPPNCNCDGPECPDYLEWLEGKIKSVVMEGGEERPRLPGPLPPGEAGLPAPSTRPLLSSEVPQISPQEGLPLSQSALSIAKEKNISLQTAIAIEALTQLSSALPQPSHSTPQASCPLPEALSPPAPFRSPQSYLRAPSWPVVPPEEHSSFAPDSSAFPPATPRTEFPEAWGTDTPPATPRSSWPMPRPSPDPMAELEQLLGSASDYIQSVFKRPEALPTKPKVKVEAPSSSPAPAPSPVLQREAPTPSSEPDTHQKAQTALQQHLHHKRSLFLEQVHDTSFPAPSEPSAPGWWPPPSSPVPRLPDRPPKEKKKKLPTPAGGPVGTEKAAPGIKPSVRKPIQIKKSRPREAQPLFPPVRQIVLEGLRSPASQEVQAHPPAPLPASQGSAVPLPPEPSLALFAPSPSRDSLLPPTQEMRSPSPMTALQPGSTGPLPPADDKLEELIRQFEAEFGDSFGLPGPPSVPIQDPENQQTCLPAPESPFATRSPKQIKIESSGAVTVLSTTCFHSEEGGQEATPTKAENPLTPTLSGFLESPLKYLDTPTKSLLDTPAKRAQAEFPTCDCVEQIVEKDEGPYYTHLGSGPTVASIRELMEERYGEKGKAIRIEKVIYTGKEGKSSRGCPIAKWVIRRHTLEEKLLCLVRHRAGHHCQNAVIVILILAWEGIPRSLGDTLYQELTDTLRKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWSMYFNGCKYARSKTPRKFRLAGDNPKEEEVLRKSFQDLATEVAPLYKRLAPQAYQNQVTNEEIAIDCRLGLKEGRPFAGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRCVGKIPEDEQLHVLPLYKMANTDEFGSEENQNAKVGSGAIQVLTAFPREVRRLPEPAKSCRQRQLEARKAAAEKKKIQKEKLSTPEKIKQEALELAGITSDPGLSLKGGLSQQGLKPSLKVEPQNHFSSFKYSGNAVVESYSVLGNCRPSDPYSMNSVYSYHSYYAQPSLTSVNGFHSKYALPSFSYYGFPSSNPVFPSQFLGPGAWGHSGSSGSFEKKPDLHALHNSLSPAYGGAEFAELPSQAVPTDAHHPTPHHQQPAYPGPKEYLLPKAPLLHSVSRDPSPFAQSSNCYNRSIKQEPVDPLTQAEPVPRDAGKMGKTPLSEVSQNGGPSHLWGQYSGGPSMSPKRTNGVGGSWGVFSSGESPAIVPDKLSSFGASCLAPSHFTDGQWGLFPGEGQQAASHSGGRLRGKPWSPCKFGNSTSALAGPSLTEKPWALGAGDFNSALKGSPGFQDKLWNPMKGEEGRIPAAGASQLDRAWQSFGLPLGSSEKLFGALKSEEKLWDPFSLEEGPAEEPPSKGAVKEEKGGGGAEEEEEELWSDSEHNFLDENIGGVAVAPAHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKQLAERARARQEEAARLGLGQQEAKLYGKKRKWGGTVVAEPQQKEKKGVVPTRQALAVPTDSAVTVSSYAYTKVTGPYSRWI
|
1.14.11.80
|
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q6N021}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q6N021}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q6N021}; Note=The zinc ions have a structural role. {ECO:0000250|UniProtKB:Q6N021};
|
5-methylcytosine catabolic process [GO:0006211]; DNA demethylation [GO:0080111]; epigenetic programing of male pronucleus [GO:0044727]; positive regulation of gene expression via CpG island demethylation [GO:0044029]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein O-linked glycosylation [GO:0006493]
|
chromosome [GO:0005694]; cytoplasm [GO:0005737]; female pronucleus [GO:0001939]; male pronucleus [GO:0001940]; nucleus [GO:0005634]
|
5-methylcytosine dioxygenase activity [GO:0070579]; methyl-CpG binding [GO:0008327]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270]
|
PF12851;PF02008;
| null |
TET family
|
PTM: Monoubiquitinated at Lys-994 by the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex called CRL4(VprBP) or CUL4A-RBX1-DDB1-DCAF1/VPRBP complex; this modification promotes binding to DNA. {ECO:0000269|PubMed:25557551}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8BG87}. Cytoplasm {ECO:0000250|UniProtKB:Q8BG87}. Chromosome {ECO:0000250|UniProtKB:Q8BG87}. Note=At the zygotic stage, localizes in the male pronucleus, while it localizes to the cytoplasm at other preimplantation stages. Binds to the promoter of target genes, close to the transcription start site. {ECO:0000250|UniProtKB:Q8BG87}.
|
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a 5-methyl-2'-deoxycytidine in DNA + O2 = a 5-hydroxymethyl-2'-deoxycytidine in DNA + CO2 + succinate; Xref=Rhea:RHEA:52636, Rhea:RHEA-COMP:11370, Rhea:RHEA-COMP:13315, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:85454, ChEBI:CHEBI:136731; EC=1.14.11.80; Evidence={ECO:0000269|PubMed:31928709}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52637; Evidence={ECO:0000305|PubMed:31928709}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a 5-hydroxymethyl-2'-deoxycytidine in DNA + O2 = a 5-formyl-2'-deoxycytidine in DNA + CO2 + H2O + succinate; Xref=Rhea:RHEA:53828, Rhea:RHEA-COMP:13315, Rhea:RHEA-COMP:13656, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:136731, ChEBI:CHEBI:137731; EC=1.14.11.80; Evidence={ECO:0000250|UniProtKB:Q8BG87}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a 5-formyl-2'-deoxycytidine in DNA + O2 = a 5-carboxyl-2'-deoxycytidine in DNA + CO2 + H(+) + succinate; Xref=Rhea:RHEA:53832, Rhea:RHEA-COMP:13656, Rhea:RHEA-COMP:13657, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:137731, ChEBI:CHEBI:137732; EC=1.14.11.80; Evidence={ECO:0000250|UniProtKB:Q8BG87};
| null | null | null | null |
FUNCTION: Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) and plays a key role in epigenetic chromatin reprogramming in the zygote following fertilization (PubMed:31928709). Also mediates subsequent conversion of 5hmC into 5-formylcytosine (5fC), and conversion of 5fC to 5-carboxylcytosine (5caC). Conversion of 5mC into 5hmC, 5fC and 5caC probably constitutes the first step in cytosine demethylation (By similarity). Selectively binds to the promoter region of target genes and contributes to regulate the expression of numerous developmental genes (PubMed:23217707). In zygotes, DNA demethylation occurs selectively in the paternal pronucleus before the first cell division, while the adjacent maternal pronucleus and certain paternally-imprinted loci are protected from this process. Participates in DNA demethylation in the paternal pronucleus by mediating conversion of 5mC into 5hmC, 5fC and 5caC. Does not mediate DNA demethylation of maternal pronucleus because of the presence of DPPA3/PGC7 on maternal chromatin that prevents TET3-binding to chromatin (By similarity). In addition to its role in DNA demethylation, also involved in the recruitment of the O-GlcNAc transferase OGT to CpG-rich transcription start sites of active genes, thereby promoting histone H2B GlcNAcylation by OGT (PubMed:23353889). Binds preferentially to DNA containing cytidine-phosphate-guanosine (CpG) dinucleotides over CpH (H=A, T, and C), hemimethylated-CpG and hemimethylated-hydroxymethyl-CpG (PubMed:29276034). {ECO:0000250|UniProtKB:Q8BG87, ECO:0000269|PubMed:23217707, ECO:0000269|PubMed:23353889, ECO:0000269|PubMed:29276034, ECO:0000269|PubMed:31928709}.
|
Homo sapiens (Human)
|
O43155
|
FLRT2_HUMAN
|
MGLQTTKWPSHGAFFLKSWLIISLGLYSQVSKLLACPSVCRCDRNFVYCNERSLTSVPLGIPEGVTVLYLHNNQINNAGFPAELHNVQSVHTVYLYGNQLDEFPMNLPKNVRVLHLQENNIQTISRAALAQLLKLEELHLDDNSISTVGVEDGAFREAISLKLLFLSKNHLSSVPVGLPVDLQELRVDENRIAVISDMAFQNLTSLERLIVDGNLLTNKGIAEGTFSHLTKLKEFSIVRNSLSHPPPDLPGTHLIRLYLQDNQINHIPLTAFSNLRKLERLDISNNQLRMLTQGVFDNLSNLKQLTARNNPWFCDCSIKWVTEWLKYIPSSLNVRGFMCQGPEQVRGMAVRELNMNLLSCPTTTPGLPLFTPAPSTASPTTQPPTLSIPNPSRSYTPPTPTTSKLPTIPDWDGRERVTPPISERIQLSIHFVNDTSIQVSWLSLFTVMAYKLTWVKMGHSLVGGIVQERIVSGEKQHLSLVNLEPRSTYRICLVPLDAFNYRAVEDTICSEATTHASYLNNGSNTASSHEQTTSHSMGSPFLLAGLIGGAVIFVLVVLLSVFCWHMHKKGRYTSQKWKYNRGRRKDDYCEAGTKKDNSILEMTETSFQIVSLNNDQLLKGDFRLQPIYTPNGGINYTDCHIPNNMRYCNSSVPDLEHCHT
| null | null |
axon guidance [GO:0007411]; basement membrane organization [GO:0071711]; cell adhesion involved in heart morphogenesis [GO:0061343]; fibroblast growth factor receptor signaling pathway [GO:0008543]; heart morphogenesis [GO:0003007]; positive regulation of synapse assembly [GO:0051965]; regulation of neuron migration [GO:2001222]
|
cell-cell junction [GO:0005911]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; synapse [GO:0045202]
|
chemorepellent activity [GO:0045499]; fibroblast growth factor receptor binding [GO:0005104]; protein-macromolecule adaptor activity [GO:0030674]
|
PF00041;PF13855;PF01463;
|
2.60.40.10;3.80.10.10;
| null |
PTM: N-glycosylated. {ECO:0000269|PubMed:10644439, ECO:0000269|PubMed:19159218}.; PTM: Proteolytic cleavage in the juxtamembrane region gives rise to a soluble ectodomain. Cleavage is probably effected by a metalloprotease. {ECO:0000250|UniProtKB:Q8BLU0}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8BLU0}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8BLU0}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8BLU0}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q8BLU0}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q8BLU0}. Microsome membrane {ECO:0000250|UniProtKB:Q8BLU0}. Secreted {ECO:0000250|UniProtKB:Q8BLU0}. Synapse, synaptosome {ECO:0000250|UniProtKB:D3ZTV3}. Note=Proteolytic cleavage gives rise to a shedded ectodomain. {ECO:0000250|UniProtKB:Q8BLU0}.
| null | null | null | null | null |
FUNCTION: Functions in cell-cell adhesion, cell migration and axon guidance. Mediates cell-cell adhesion via its interactions with ADGRL3 and probably also other latrophilins that are expressed at the surface of adjacent cells. May play a role in the migration of cortical neurons during brain development via its interaction with UNC5D. Mediates axon growth cone collapse and plays a repulsive role in neuron guidance via its interaction with UNC5D, and possibly also other UNC-5 family members. Plays a role in fibroblast growth factor-mediated signaling cascades. Required for normal organization of the cardiac basement membrane during embryogenesis, and for normal embryonic epicardium and heart morphogenesis. {ECO:0000250|UniProtKB:Q8BLU0}.
|
Homo sapiens (Human)
|
O43156
|
TTI1_HUMAN
|
MAVFDTPEEAFGVLRPVCVQLTKTQTVENVEHLQTRLQAVSDSALQELQQYILFPLRFTLKTPGPKRERLIQSVVECLTFVLSSTCVKEQELLQELFSELSACLYSPSSQKPAAVSEELKLAVIQGLSTLMHSAYGDIILTFYEPSILPRLGFAVSLLLGLAEQEKSKQIKIAALKCLQVLLLQCDCQDHPRSLDELEQKQLGDLFASFLPGISTALTRLITGDFKQGHSIVVSSLKIFYKTVSFIMADEQLKRISKVQAKPAVEHRVAELMVYREADWVKKTGDKLTILIKKIIECVSVHPHWKVRLELVELVEDLLLKCSQSLVECAGPLLKALVGLVNDESPEIQAQCNKVLRHFADQKVVVGNKALADILSESLHSLATSLPRLMNSQDDQGKFSTLSLLLGYLKLLGPKINFVLNSVAHLQRLSKALIQVLELDVADIKIVEERRWNSDDLNASPKTSATQPWNRIQRRYFRFFTDERIFMLLRQVCQLLGYYGNLYLLVDHFMELYHQSVVYRKQAAMILNELVTGAAGLEVEDLHEKHIKTNPEELREIVTSILEEYTSQENWYLVTCLETEEMGEELMMEHPGLQAITSGEHTCQVTSFLAFSKPSPTICSMNSNIWQICIQLEGIGQFAYALGKDFCLLLMSALYPVLEKAGDQTLLISQVATSTMMDVCRACGYDSLQHLINQNSDYLVNGISLNLRHLALHPHTPKVLEVMLRNSDANLLPLVADVVQDVLATLDQFYDKRAASFVSVLHALMAALAQWFPDTGNLGHLQEQSLGEEGSHLNQRPAALEKSTTTAEDIEQFLLNYLKEKDVADGNVSDFDNEEEEQSVPPKVDENDTRPDVEPPLPLQIQIAMDVMERCIHLLSDKNLQIRLKVLDVLDLCVVVLQSHKNQLLPLAHQAWPSLVHRLTRDAPLAVLRAFKVLRTLGSKCGDFLRSRFCKDVLPKLAGSLVTQAPISARAGPVYSHTLAFKLQLAVLQGLGPLCERLDLGEGDLNKVADACLIYLSVKQPVKLQEAARSVFLHLMKVDPDSTWFLLNELYCPVQFTPPHPSLHPVQLHGASGQQNPYTTNVLQLLKELQ
| null | null |
chromatin remodeling [GO:0006338]; positive regulation of DNA damage checkpoint [GO:2000003]; protein stabilization [GO:0050821]; regulation of TOR signaling [GO:0032006]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; TORC1 complex [GO:0031931]; TORC2 complex [GO:0031932]; TTT Hsp90 cochaperone complex [GO:0110078]
| null |
PF21547;
|
1.25.10.10;
|
Tti1 family
|
PTM: Phosphorylated at Ser-828 by CK2 following growth factor deprivation, leading to its subsequent ubiquitination by the SCF(FBXO9) complex. Phosphorylation by CK2 only takes place when TELO2 is bound to mTORC1, not mTORC2; leading to selective ubiquitination of mTORC1-associated protein. {ECO:0000269|PubMed:23263282}.; PTM: Ubiquitinated by the SCF(FBXO9) complex following phosphorylation by CK2 in response to growth factor deprivation, leading to its degradation by the proteasome. Only mTORC1-associated protein is ubiquitinated and degraded, leading to selective inactivation of mTORC1 to restrain cell growth and protein translation, while mTORC2 is activated due to the relief of feedback inhibition by mTORC1. {ECO:0000269|PubMed:23263282}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23263282}.
| null | null | null | null | null |
FUNCTION: Regulator of the DNA damage response (DDR). Part of the TTT complex that is required to stabilize protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins. The TTT complex is involved in the cellular resistance to DNA damage stresses, like ionizing radiation (IR), ultraviolet (UV) and mitomycin C (MMC). Together with the TTT complex and HSP90 may participate in the proper folding of newly synthesized PIKKs. Promotes assembly, stabilizes and maintains the activity of mTORC1 and mTORC2 complexes, which regulate cell growth and survival in response to nutrient and hormonal signals. {ECO:0000269|PubMed:20427287, ECO:0000269|PubMed:20801936, ECO:0000269|PubMed:20810650, ECO:0000269|PubMed:36724785}.
|
Homo sapiens (Human)
|
O43157
|
PLXB1_HUMAN
|
MPALGPALLQALWAGWVLTLQPLPPTAFTPNGTYLQHLARDPTSGTLYLGATNFLFQLSPGLQLEATVSTGPVLDSRDCLPPVMPDECPQAQPTNNPNQLLLVSPGALVVCGSVHQGVCEQRRLGQLEQLLLRPERPGDTQYVAANDPAVSTVGLVAQGLAGEPLLFVGRGYTSRGVGGGIPPITTRALWPPDPQAAFSYEETAKLAVGRLSEYSHHFVSAFARGASAYFLFLRRDLQAQSRAFRAYVSRVCLRDQHYYSYVELPLACEGGRYGLIQAAAVATSREVAHGEVLFAAFSSAAPPTVGRPPSAAAGASGASALCAFPLDEVDRLANRTRDACYTREGRAEDGTEVAYIEYDVNSDCAQLPVDTLDAYPCGSDHTPSPMASRVPLEATPILEWPGIQLTAVAVTMEDGHTIAFLGDSQGQLHRVYLGPGSDGHPYSTQSIQQGSAVSRDLTFDGTFEHLYVMTQSTLLKVPVASCAQHLDCASCLAHRDPYCGWCVLLGRCSRRSECSRGQGPEQWLWSFQPELGCLQVAAMSPANISREETREVFLSVPDLPPLWPGESYSCHFGEHQSPALLTGSGVMCPSPDPSEAPVLPRGADYVSVSVELRFGAVVIAKTSLSFYDCVAVTELRPSAQCQACVSSRWGCNWCVWQHLCTHKASCDAGPMVASHQSPLVSPDPPARGGPSPSPPTAPKALATPAPDTLPVEPGAPSTATASDISPGASPSLLSPWGPWAGSGSISSPGSTGSPLHEEPSPPSPQNGPGTAVPAPTDFRPSATPEDLLASPLSPSEVAAVPPADPGPEALHPTVPLDLPPATVPATTFPGAMGSVKPALDWLTREGGELPEADEWTGGDAPAFSTSTLLSGDGDSAELEGPPAPLILPSSLDYQYDTPGLWELEEATLGASSCPCVESVQGSTLMPVHVEREIRLLGRNLHLFQDGPGDNECVMELEGLEVVVEARVECEPPPDTQCHVTCQQHQLSYEALQPELRVGLFLRRAGRLRVDSAEGLHVVLYDCSVGHGDCSRCQTAMPQYGCVWCEGERPRCVTREACGEAEAVATQCPAPLIHSVEPLTGPVDGGTRVTIRGSNLGQHVQDVLGMVTVAGVPCAVDAQEYEVSSSLVCITGASGEEVAGATAVEVPGRGRGVSEHDFAYQDPKVHSIFPARGPRAGGTRLTLNGSKLLTGRLEDIRVVVGDQPCHLLPEQQSEQLRCETSPRPTPATLPVAVWFGATERRLQRGQFKYTLDPNITSAGPTKSFLSGGREICVRGQNLDVVQTPRIRVTVVSRMLQPSQGLGRRRRVVPETACSLGPSCSSQQFEEPCHVNSSQLITCRTPALPGLPEDPWVRVEFILDNLVFDFATLNPTPFSYEADPTLQPLNPEDPTMPFRHKPGSVFSVEGENLDLAMSKEEVVAMIGDGPCVVKTLTRHHLYCEPPVEQPLPRHHALREAPDSLPEFTVQMGNLRFSLGHVQYDGESPGAFPVAAQVGLGVGTSLLALGVIIIVLMYRRKSKQALRDYKKVQIQLENLESSVRDRCKKEFTDLMTEMTDLTSDLLGSGIPFLDYKVYAERIFFPGHRESPLHRDLGVPESRRPTVEQGLGQLSNLLNSKLFLTKFIHTLESQRTFSARDRAYVASLLTVALHGKLEYFTDILRTLLSDLVAQYVAKNPKLMLRRTETVVEKLLTNWMSICLYTFVRDSVGEPLYMLFRGIKHQVDKGPVDSVTGKAKYTLNDNRLLREDVEYRPLTLNALLAVGPGAGEAQGVPVKVLDCDTISQAKEKMLDQLYKGVPLTQRPDPRTLDVEWRSGVAGHLILSDEDVTSEVQGLWRRLNTLQHYKVPDGATVALVPCLTKHVLRENQDYVPGERTPMLEDVDEGGIRPWHLVKPSDEPEPPRPRRGSLRGGERERAKAIPEIYLTRLLSMKGTLQKFVDDLFQVILSTSRPVPLAVKYFFDLLDEQAQQHGISDQDTIHIWKTNSLPLRFWINIIKNPQFVFDVQTSDNMDAVLLVIAQTFMDACTLADHKLGRDSPINKLLYARDIPRYKRMVERYYADIRQTVPASDQEMNSVLAELSWNYSGDLGARVALHELYKYINKYYDQIITALEEDGTAQKMQLGYRLQQIAAAVENKVTDL
| null | null |
axon extension [GO:0048675]; cell migration [GO:0016477]; inhibitory synapse assembly [GO:1904862]; intracellular signal transduction [GO:0035556]; negative regulation of cell adhesion [GO:0007162]; negative regulation of osteoblast proliferation [GO:0033689]; neuron projection morphogenesis [GO:0048812]; ossification involved in bone maturation [GO:0043931]; positive regulation of axonogenesis [GO:0050772]; positive regulation of GTPase activity [GO:0043547]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of Rho protein signal transduction [GO:0035025]; regulation of cell migration [GO:0030334]; regulation of cell shape [GO:0008360]; regulation of cytoskeleton organization [GO:0051493]; semaphorin-plexin signaling pathway [GO:0071526]; semaphorin-plexin signaling pathway involved in axon guidance [GO:1902287]
|
extracellular region [GO:0005576]; plasma membrane [GO:0005886]; semaphorin receptor complex [GO:0002116]
|
GTPase activating protein binding [GO:0032794]; GTPase activator activity [GO:0005096]; semaphorin receptor activity [GO:0017154]; semaphorin receptor binding [GO:0030215]; transmembrane signaling receptor activity [GO:0004888]
|
PF08337;PF20170;PF01437;PF01403;PF01833;PF18020;PF17960;
|
2.60.40.10;2.130.10.10;
|
Plexin family
|
PTM: Phosphorylated on tyrosine residues by ERBB2 and MET upon SEMA4D binding. {ECO:0000269|PubMed:10520995, ECO:0000269|PubMed:15210733}.; PTM: Proteolytic processing favors heterodimerization with PLXNB2 and SEMA4D binding. {ECO:0000269|PubMed:12533544}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:12533544}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:10520995}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000269|PubMed:10520995}.
| null | null | null | null | null |
FUNCTION: Receptor for SEMA4D (PubMed:19843518, PubMed:20877282, PubMed:21912513). Plays a role in GABAergic synapse development (By similarity). Mediates SEMA4A- and SEMA4D-dependent inhibitory synapse development (By similarity). Plays a role in RHOA activation and subsequent changes of the actin cytoskeleton (PubMed:12196628, PubMed:15210733). Plays a role in axon guidance, invasive growth and cell migration (PubMed:12198496). {ECO:0000250|UniProtKB:Q8CJH3, ECO:0000269|PubMed:12196628, ECO:0000269|PubMed:12198496, ECO:0000269|PubMed:15210733, ECO:0000269|PubMed:19843518, ECO:0000269|PubMed:20877282, ECO:0000269|PubMed:21912513}.
|
Homo sapiens (Human)
|
O43159
|
RRP8_HUMAN
|
MFEEPEWAEAAPVAAGLGPVISRPPPAASSQNKGSKRRQLLATLRALEAASLSQHPPSLCISDSEEEEEERKKKCPKKASFASASAEVGKKGKKKCQKQGPPCSDSEEEVERKKKCHKQALVGSDSAEDEKRKRKCQKHAPINSAQHLDNVDQTGPKAWKGSTTNDPPKQSPGSTSPKPPHTLSRKQWRNRQKNKRRCKNKFQPPQVPDQAPAEAPTEKTEVSPVPRTDSHEARAGALRARMAQRLDGARFRYLNEQLYSGPSSAAQRLFQEDPEAFLLYHRGFQSQVKKWPLQPVDRIARDLRQRPASLVVADFGCGDCRLASSIRNPVHCFDLASLDPRVTVCDMAQVPLEDESVDVAVFCLSLMGTNIRDFLEEANRVLKPGGLLKVAEVSSRFEDVRTFLRAVTKLGFKIVSKDLTNSHFFLFDFQKTGPPLVGPKAQLSGLQLQPCLYKRR
|
2.1.1.-
| null |
cellular response to glucose starvation [GO:0042149]; energy homeostasis [GO:0097009]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; negative regulation of cell cycle [GO:0045786]; negative regulation of DNA-templated transcription [GO:0045892]; rDNA heterochromatin formation [GO:0000183]; regulation of G1 to G0 transition [GO:1903450]; regulation of transcription by glucose [GO:0046015]; ribosomal large subunit biogenesis [GO:0042273]
|
chromatin silencing complex [GO:0005677]; cytosol [GO:0005829]; eNoSc complex [GO:0061773]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; rDNA heterochromatin [GO:0033553]
|
methylated histone binding [GO:0035064]; RNA binding [GO:0003723]; rRNA (adenine) methyltransferase activity [GO:0016433]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]
|
PF05148;
|
1.10.10.2150;3.40.50.150;
|
Methyltransferase superfamily, RRP8 family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11790298, ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:18485871}. Note=Localizes at rDNA locus.
| null | null | null | null | null |
FUNCTION: Essential component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. In the complex, RRP8 binds to H3K9me2 and probably acts as a methyltransferase. Its substrates are however unknown. {ECO:0000269|PubMed:18485871}.
|
Homo sapiens (Human)
|
O43164
|
PJA2_HUMAN
|
MSQYTEKEPAAMDQESGKAVWPKPAGGYQTITGRRYGRRHAYVSFKPCMTRHERSLGRAGDDYEVLELDDVPKENSSGSSPLDQVDSSLPSEPIFEKSETEIPTCGSALNQTTESSQSFVAVHHSEEGRDTLGSSTNLHNHSEGEYIPGACSASSVQNGIALVHTDSYDPDGKHGEDNDHLQLSAEVVEGSRYQESLGNTVFELENREAEAYTGLSPPVPSFNCEVRDEFEELDSVPLVKSSAGDTEFVHQNSQEIQRSSQDEMVSTKQQNNTSQERQTEHSPEDAACGPGHICSEQNTNDREKNHGSSPEQVVRPKVRKLISSSQVDQETGFNRHEAKQRSVQRWREALEVEESGSDDLLIKCEEYDGEHDCMFLDPPYSRVITQRETENNQMTSESGATAGRQEVDNTFWNGCGDYYQLYDKDEDSSECSDGEWSASLPHRFSGTEKDQSSSDESWETLPGKDENEPELQSDSSGPEEENQELSLQEGEQTSLEEGEIPWLQYNEVNESSSDEGNEPANEFAQPAFMLDGNNNLEDDSSVSEDLDVDWSLFDGFADGLGVAEAISYVDPQFLTYMALEERLAQAMETALAHLESLAVDVEVANPPASKESIDGLPETLVLEDHTAIGQEQCCPICCSEYIKDDIATELPCHHFFHKPCVSIWLQKSGTCPVCRRHFPPAVIEASAAPSSEPDPDAPPSNDSIAEAP
|
2.3.2.27
| null |
inflammatory response [GO:0006954]; innate immune response [GO:0045087]; long-term memory [GO:0007616]; positive regulation of JNK cascade [GO:0046330]; positive regulation of p38MAPK cascade [GO:1900745]; positive regulation of toll-like receptor 2 signaling pathway [GO:0034137]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein ubiquitination [GO:0016567]; regulation of macrophage activation [GO:0043030]; regulation of protein kinase A signaling [GO:0010738]
|
centriolar satellite [GO:0034451]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; intermediate filament cytoskeleton [GO:0045111]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]
|
metal ion binding [GO:0046872]; protein kinase A catalytic subunit binding [GO:0034236]; protein kinase A regulatory subunit binding [GO:0034237]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]
|
PF13639;
|
3.30.40.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21423175}. Cell membrane {ECO:0000269|PubMed:21423175}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21423175}; Peripheral membrane protein {ECO:0000269|PubMed:21423175}. Golgi apparatus membrane {ECO:0000269|PubMed:21423175}; Peripheral membrane protein {ECO:0000269|PubMed:21423175}. Synapse {ECO:0000250|UniProtKB:Q63364}. Postsynaptic density {ECO:0000250|UniProtKB:Q63364}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:33934390}. Note=Localizes at the cytoplasmic side of endoplasmic reticulum and Golgi apparatus (PubMed:21423175). Expressed in the postsynaptic density region of synapses (By similarity). Colocalizes with PRKAR2A and PRKAR2B in the cytoplasm and the cell membrane (PubMed:21423175). {ECO:0000250|UniProtKB:Q63364, ECO:0000269|PubMed:21423175}.
|
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:0000269|PubMed:12036302, ECO:0000269|PubMed:21423175};
| null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:12036302, ECO:0000269|PubMed:21423175}.
| null | null |
FUNCTION: Has E2-dependent E3 ubiquitin-protein ligase activity (PubMed:12036302, PubMed:21423175). Responsible for ubiquitination of cAMP-dependent protein kinase type I and type II-alpha/beta regulatory subunits and for targeting them for proteasomal degradation. Essential for PKA-mediated long-term memory processes (PubMed:21423175). Through the ubiquitination of MFHAS1, positively regulates the TLR2 signaling pathway that leads to the activation of the downstream p38 and JNK MAP kinases and promotes the polarization of macrophages toward the pro-inflammatory M1 phenotype (PubMed:28471450). Plays a role in ciliogenesis by ubiquitinating OFD1 (PubMed:33934390). {ECO:0000269|PubMed:12036302, ECO:0000269|PubMed:21423175, ECO:0000269|PubMed:28471450, ECO:0000269|PubMed:33934390}.
|
Homo sapiens (Human)
|
O43166
|
SI1L1_HUMAN
|
MTSLKRSQTERPLATDRASVVGTDGTPKVHTDDFYMRRFRSQNGSLGSSVMAPVGPPRSEGSHHITSTPGVPKMGVRARIADWPPRKENIKESSRSSQEIETSSCLDSLSSKSSPVSQGSSVSLNSNDSAMLKSIQNTLKNKTRPSENMDSRFLMPEAYPSSPRKALRRIRQRSNSDITISELDVDSFDECISPTYKTGPSLHREYGSTSSIDKQGTSGESFFDLLKGYKDDKSDRGPTPTKLSDFLITGGGKGSGFSLDVIDGPISQRENLRLFKEREKPLKRRSKSETGDSSIFRKLRNAKGEELGKSSDLEDNRSEDSVRPWTCPKCFAHYDVQSILFDLNEAIMNRHNVIKRRNTTTGASAAAVASLVSGPLSHSASFSSPMGSTEDLNSKGSLSMDQGDDKSNELVMSCPYFRNEIGGEGERKISLSKSNSGSFSGCESASFESTLSSHCTNAGVAVLEVPKENLVLHLDRVKRYIVEHVDLGAYYYRKFFYQKEHWNYFGADENLGPVAVSIRREKPDEMKENGSPYNYRIIFRTSELMTLRGSVLEDAIPSTAKHSTARGLPLKEVLEHVVPELNVQCLRLAFNTPKVTEQLMKLDEQGLNYQQKVGIMYCKAGQSTEEEMYNNESAGPAFEEFLQLLGERVRLKGFEKYRAQLDTKTDSTGTHSLYTTYKDYEIMFHVSTMLPYTPNNKQQLLRKRHIGNDIVTIVFQEPGAQPFSPKNIRSHFQHVFVIVRVHNPCSDSVCYSVAVTRSRDVPSFGPPIPKGVTFPKSNVFRDFLLAKVINAENAAHKSEKFRAMATRTRQEYLKDLAEKNVTNTPIDPSGKFPFISLASKKKEKSKPYPGAELSSMGAIVWAVRAEDYNKAMELDCLLGISNEFIVLIEQETKSVVFNCSCRDVIGWTSTDTSLKIFYERGECVSVGSFINIEEIKEIVKRLQFVSKGCESVEMTLRRNGLGQLGFHVNYEGIVADVEPYGYAWQAGLRQGSRLVEICKVAVATLSHEQMIDLLRTSVTVKVVIIPPHDDCTPRRSCSETYRMPVMEYKMNEGVSYEFKFPFRNNNKWQRNASKGPHSPQVPSQVQSPMTSRLNAGKGDGKMPPPERAANIPRSISSDGRPLERRLSPGSDIYVTVSSMALARSQCRNSPSNLSSSSDTGSVGGTYRQKSMPEGFGVSRRSPASIDRQNTQSDIGGSGKSTPSWQRSEDSIADQMAYSYRGPQDFNSFVLEQHEYTEPTCHLPAVSKVLPAFRESPSGRLMRQDPVVHLSPNKQGHSDSHYSSHSSSNTLSSNASSAHSDEKWYDGDRTESELNSYNYLQGTSADSGIDTTSYGPSHGSTASLGAATSSPRSGPGKEKVAPLWHSSSEVISMADRTLETESHGLDRKTESSLSLDIHSKSQAGSTPLTRENSTFSINDAASHTSTMSSRHSASPVVFTSARSSPKEELHPAAPSQLAPSFSSSSSSSSGPRSFYPRQGATSKYLIGWKKPEGTINSVGFMDTRKRHQSDGNEIAHTRLRASTRDLRASPKPTSKSTIEEDLKKLIDLESPTPESQKSFKFHALSSPQSPFPSTPTSRRALHRTLSDESIYNSQREHFFTSRASLLDQALPNDVLFSSTYPSLPKSLPLRRPSYTLGMKSLHGEFSASDSSLTDIQETRRQPMPDPGLMPLPDTAADLDWSNLVDAAKAYEVQRASFFAASDENHRPLSAASNSDQLEDQALAQMKPYSSSKDSSPTLASKVDQLEGMLKMLREDLKKEKEDKAHLQAEVQHLREDNLRLQEESQNASDKLKKFTEWVFNTIDMS
| null | null |
actin cytoskeleton organization [GO:0030036]; activation of GTPase activity [GO:0090630]; ephrin receptor signaling pathway [GO:0048013]; regulation of axonogenesis [GO:0050770]; regulation of dendritic spine morphogenesis [GO:0061001]; regulation of GTPase activity [GO:0043087]; regulation of small GTPase mediated signal transduction [GO:0051056]; regulation of synaptic plasticity [GO:0048167]
|
actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; dendritic spine [GO:0043197]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]
|
ephrin receptor binding [GO:0046875]; GTPase activator activity [GO:0005096]
|
PF00595;PF21022;PF02145;PF11881;
|
2.30.42.10;6.10.140.210;3.40.50.11210;
| null |
PTM: Ubiquitinated and degraded by the SCF(BTRC) following phosphorylation by PLK2. {ECO:0000250}.; PTM: Phosphorylated at Ser-1349 by CDK5, creating a docking site for the POLO box domains of PLK2. Subsequently, PLK2 binds and phosphorylates SIPA1L1, leading to ubiquitination and degradation by the proteasome (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Postsynaptic density {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Note=Associated with the actin cytoskeleton. Detected at synapses and dendritic spines of cultured hippocampal neurons (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Stimulates the GTPase activity of RAP2A. Promotes reorganization of the actin cytoskeleton and recruits DLG4 to F-actin. Contributes to the regulation of dendritic spine morphogenesis (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O43167
|
ZBT24_HUMAN
|
MAETSPEPSGQLVVHSDAHSDTVLASFEDQRKKGFLCDITLIVENVHFRAHKALLAASSEYFSMMFAEEGEIGQSIYMLEGMVADTFGILLEFIYTGYLHASEKSTEQILATAQFLKVYDLVKAYTDFQNNHSSPKPTTLNTAGAPVVVISNKKNDPPKRKRGRPKKVNTLQEEKSELAAEEEIQLRVNNSVQNRQNFVVKGDSGVLNEQIAAKEKEESEPTCEPSREEEMPVEKDENYDPKTEDGQASQSRYSKRRIWRSVKLKDYKLVGDQEDHGSAKRICGRRKRPGGPEARCKDCGKVFKYNHFLAIHQRSHTGERPFKCNECGKGFAQKHSLQVHTRMHTGERPYTCTVCSKALTTKHSLLEHMSLHSGQKSFTCDQCGKYFSQNRQLKSHYRVHTGHSLPECKDCHRKFMDVSQLKKHLRTHTGEKPFTCEICGKSFTAKSSLQTHIRIHRGEKPYSCGICGKSFSDSSAKRRHCILHTGKKPFSCPECNLQFARLDNLKAHLKIHSKEKHASDASSISGSSNTEEVRNILQLQPYQLSTSGEQEIQLLVTDSVHNINFMPGPSQGISIVTAESSQNMTADQAANLTLLTQQPEQLQNLILSAQQEQTEHIQSLNMIESQMGPSQTEPVHVITLSKETLEHLHAHQEQTEELHLATSTSDPAQHLQLTQEPGPPPPTHHVPQPTPLGQEQS
| null | null |
hematopoietic progenitor cell differentiation [GO:0002244]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00651;PF00096;
|
3.30.160.60;
|
Krueppel C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: May be involved in BMP2-induced transcription. {ECO:0000250}.
|
Homo sapiens (Human)
|
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