dbPAF Protein Information
Tag | Content | ||||||||
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dbPAF ID | dbPAF-0016670 | ||||||||
Uniprot Accession | Q12440; APC2_YEAST; D6VYC2; Q2VQX4; Q7LGV7; | ||||||||
Genbank Protein ID | NP_013228.1; | ||||||||
Genbank Nucleotide ID | NM_001182014.1; | ||||||||
Protein Name | Anaphase-promoting complex subunit 2 | ||||||||
Protein Synonyms/Alias | |||||||||
Gene Name | APC2 | ||||||||
Gene Synonyms/Alias | RSI1;YLR127C;L3105;L3108; | ||||||||
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c)(Baker's yeast) | ||||||||
NCBI Taxa ID | 559292 | ||||||||
Functional Description (View all) |
Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication. | ||||||||
Phosphorylation Sites |
dbPAF PTMs: 1
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Sequence (Fasta) | MSFQITPTRD LKVITDELQT LSSYIFHTNI VDDLNSLLTW MSPNDAKSNH QLRPPSLRIK 60 NIIKVLFPNN ATTSPYSMIN TSQANNSIVN EGNTNKELQL QLFSTLKEFY IFQVRYHFFL 120 HFNNINYLKD IQRWENYYEF PLRYVPIFDV NVNDWALELN SLRHYLLNRN IKFKNNLRTR 180 LDKLIMDDDF DLADNLIQWL KSANGSLSST ELIVNALYSK INKFCEDNMS RVWNKRFMIM 240 ETFNKFINQY WSQFSKLVGC PEDDHELTTT VFNCFESNFL RIRTNEIFDI CVLAYPDSKV 300 TLLELRKIMK DFKDYTNIVT TFLSDFKKYI LNPSVTTVDA LLRYVKTIKA FLVLDPTGRC 360 LHSITTFVKP YFQERKHLVN VLLYAMLDLP EEELKEKINF NVDMKALLSL VDTLHDSDIN 420 QDTNITKRDK NKKSPFLWNL KVKGKRELNK DLPIRHAMLY EHILNYYIAW VPEPNDMIPG 480 NIKSSYIKTN LFEVLLDLFE SREFFISEFR NLLTDRLFTL KFYTLDEKWT RCLKLIREKI 540 VKFTETSHSN YITNGILGLL ETTAPAADAD QSNLNSIDVM LWDIKCSEEL CRKMHEVAGL 600 DPIIFPKFIS LLYWKYNCDT QGSNDLAFHL PIDLERELQK YSDIYSQLKP GRKLQLCKDK 660 GKVEIQLAFK DGRKLVLDVS LEQCSVINQF DSPNDEPICL SLEQLSESLN IAPPRLTHLL 720 DFWIQKGVLL KENGTYSVIE HSEMDFDQAQ KTAPMEIENS NYELHNDSEI ERKYELTLQR 780 SLPFIEGMLT NLGAMKLHKI HSFLKITVPK DWGYNRITLQ QLEGYLNTLA DEGRLKYIAN 840 GSYEIVKNGH KNS 854 |
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Keyword | KW-0002--3D-structure |
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Interpro | IPR014786--APC_su2_C |
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PROSITE | PS50069--CULLIN_2 |
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Pfam | |||||||||
Gene Ontology | GO:0005680--C:anaphase-promoting complex |