| UniProt ID | APC1_YEAST | |
|---|---|---|
| UniProt AC | P53886 | |
| Protein Name | Anaphase-promoting complex subunit 1 | |
| Gene Name | APC1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1748 | |
| Subcellular Localization | Nucleus . Cytoplasm . Cytoplasm, cytoskeleton, spindle pole . | |
| Protein Description | 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.. | |
| Protein Sequence | MTSKPSTRNDYLPRETHNGEYTGDSPEWQLQINITNKIGGINGDIWLSRDGRSVKWCIEDQCLRQFTYNQKIIKAGYIDFEKTPDCFVVVLSDIAHVYMLKNGGSTTVCFPFQIGNAFWYANGVILERETSASFMDGGYDLKPIEFDLKHKYITLTDPMAPFGLISITNTFKGGINSASGNKTDILQDFQLVLFPSDKDKCIAVFLDRNSKVLRFYYSRILSSDQSRKGELTISSTKKTGLDAAGNSQKSGGISKDLRKFSHLTRRSTSINSNSHDFNAAERVLSGNVGNASGRTDIFALPSSCSRRSLSATLDRMGNNIAPTNRAAPSGFFDSSSANTATHSNITPVSQPMQQQQQEYLNQTATSSKDIVLTEISSLKLPDDIIFTSRRLSSILSKLKFLSLRFERREGLLIFHEPTHFCKIWLIDLLPDVLDSIPFKIYGNSPQNMIRLENLKLKEPSRIQAMYIHELLESCLILVSEGQNKEEYKACLYDPFVKITSPSKNISEELTKQNSLPSLQKLFPYPETSFTKLCFEAVKYITSPAFNISFIFLWQSAYSILLSRANDDVVGGLKMEHDAFSLVLSLLILPIPSSSAQEYQEYKEIYERDLFQHLKQDSEITSSVLPRIVIGLHLIREEYSLNVLCRNEHALLGQFLRFATAAMGWPDLWQSYYVPKMDSESKTFLHPREQNSTFFHPLDEPPSITKSLYSITENSSIPLCPFISFSRLVATDTQVELRITPRSFKILGLYELVHSPNFLPDYVLGILSSFKVDKDELQTYPLGILVPLQNILKILEDKLSEVRDNLELLDRADLQRCSAIINSIRSDSKEVLKRGQRDSYMLCKVPLAKNRSSLSKKPSDIYSILSEIVKSASQVPLDGSAMRMSNIQDDEDIDEGRSLKLNAGLIFSEDKRFTHVVSLLAYYRPTKTQFFTTKTEYAQILAQKKYFAKIMALRTCTNGVGWGAVAYATEKPISTQKWVIQPLNLISVFPDDTKITVKAPEDIAHDIVEWGQFHAGVSSGLRISKKATGITGSWIAFNKPKELDAYHGGFLLGLGLNGHLKNLEEWHIYNYLSPRNTHISIGLLLGMSSSMKGSMDSKLIKVISVHLVAFLPSGSSDLNIDLKLQTAGIIGMGMLYLNSRHKRMSDSIFAQLVSLLNVNDEMVADEEYRLAAGISLGLINLGAGQTKLRKWDSSLLGLGDDLPEDVYDSSDVEQNVMYEDLTTKLLEIVTSTYDVENDWIPENSQIGAVIAIMFLFLKSNNFGISNMLKVDLKEILKANINTRPELLMYREWASNMILWEFIGDDLSFIMKDVDIGVKFSELNTDLLPIYYTMAGRILAMGIRFASTGNLKIRNILLSLVDKFLPLYQYPGKQNLDFRLTISVINVLTNVIVVSLSMVMCASGDLEVLRRVKYLHEVASGPYSDLFQEIPSSKSDVSGVTQVTSNTNTPGNSDRERVDETAASLDDERSSNGSDISDPTAYLEDKKDIDDHYGKFISTNLALGFLFLGSGQYALNTSTLESIAFLSMSVLPTYTTPHPLQELKHFWSMAVEPRCLVIKDISTGDAVNNVPIELVVEEDVEKEEVIREISTPCLLPDFSKIKSIRVKMHGYFPLEVNFTKDYSASDFFSGGTIIYIQRKSESVFENKASFRNVEDIHVALKRKAAESKNYSRLNLKNEQGNTTSSQLVESLGIQDLTMVELDTLLSAGNNTALTDSESYNLGLLCSDKNSGDILDCQLELWYKSFGPHDE | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 152 | Phosphorylation | EFDLKHKYITLTDPM EEECCCCEEEECCCC | 10.00 | 20377248 | |
| 154 | Phosphorylation | DLKHKYITLTDPMAP ECCCCEEEECCCCCC | 22.10 | 20377248 | |
| 156 | Phosphorylation | KHKYITLTDPMAPFG CCCEEEECCCCCCCE | 29.43 | 20377248 | |
| 168 | Phosphorylation | PFGLISITNTFKGGI CCEEEEEECEECCCC | 22.78 | 20377248 | |
| 170 | Phosphorylation | GLISITNTFKGGINS EEEEEECEECCCCCC | 20.34 | 20377248 | |
| 216 | Phosphorylation | NSKVLRFYYSRILSS CCCCHHHHHHHHCCC | 8.29 | 28889911 | |
| 217 | Phosphorylation | SKVLRFYYSRILSSD CCCHHHHHHHHCCCC | 6.69 | 28889911 | |
| 218 | Phosphorylation | KVLRFYYSRILSSDQ CCHHHHHHHHCCCCC | 11.06 | 28889911 | |
| 222 | Phosphorylation | FYYSRILSSDQSRKG HHHHHHCCCCCCCCC | 29.51 | 30377154 | |
| 268 | Phosphorylation | SHLTRRSTSINSNSH HHHHCCCCCCCCCCC | 31.64 | 28889911 | |
| 269 | Phosphorylation | HLTRRSTSINSNSHD HHHCCCCCCCCCCCC | 22.48 | 25752575 | |
| 272 | Phosphorylation | RRSTSINSNSHDFNA CCCCCCCCCCCCCCH | 37.73 | 19779198 | |
| 274 | Phosphorylation | STSINSNSHDFNAAE CCCCCCCCCCCCHHH | 25.01 | 19779198 | |
| 285 | Phosphorylation | NAAERVLSGNVGNAS CHHHHHHCCCCCCCC | 26.01 | 23749301 | |
| 292 | Phosphorylation | SGNVGNASGRTDIFA CCCCCCCCCCCCEEE | 32.57 | 25005228 | |
| 305 | Phosphorylation | FALPSSCSRRSLSAT EECCCCCCHHHHHHH | 32.45 | 28889911 | |
| 308 | Phosphorylation | PSSCSRRSLSATLDR CCCCCHHHHHHHHHH | 26.09 | 23749301 | |
| 310 | Phosphorylation | SCSRRSLSATLDRMG CCCHHHHHHHHHHCC | 22.06 | 22369663 | |
| 441 | Phosphorylation | DSIPFKIYGNSPQNM HHCCEEECCCCCCCC | 15.73 | 19779198 | |
| 444 | Phosphorylation | PFKIYGNSPQNMIRL CEEECCCCCCCCEEE | 24.41 | 19779198 | |
| 506 | Phosphorylation | TSPSKNISEELTKQN CCCCCCCCHHHHHHC | 34.12 | 27017623 | |
| 510 | Phosphorylation | KNISEELTKQNSLPS CCCCHHHHHHCCCCC | 33.59 | 27017623 | |
| 670 | Phosphorylation | GWPDLWQSYYVPKMD CCCHHHHHHEECCCC | 13.57 | 30377154 | |
| 817 | Phosphorylation | RADLQRCSAIINSIR HHHHHHHHHHHHHHC | 25.37 | 28889911 | |
| 870 | Phosphorylation | ILSEIVKSASQVPLD HHHHHHHHCCCCCCC | 23.43 | 28889911 | |
| 897 | Phosphorylation | EDIDEGRSLKLNAGL CCCCCHHCEEECCEE | 40.49 | 28889911 | |
| 913 | Phosphorylation | FSEDKRFTHVVSLLA ECCCCCHHHHHHHHH | 20.14 | 30377154 | |
| 921 | Phosphorylation | HVVSLLAYYRPTKTQ HHHHHHHHHCCCCCE | 10.44 | 30377154 | |
| 922 | Phosphorylation | VVSLLAYYRPTKTQF HHHHHHHHCCCCCEE | 12.43 | 30377154 | |
| 1076 | Phosphorylation | NYLSPRNTHISIGLL CCCCCCCCEECHHHH | 23.13 | 27017623 | |
| 1087 | Phosphorylation | IGLLLGMSSSMKGSM HHHHHCCCCCCCCCC | 19.91 | 27017623 | |
| 1436 | Phosphorylation | PSSKSDVSGVTQVTS CCCCCCCCCCEEEEC | 32.32 | 23749301 | |
| 1439 | Phosphorylation | KSDVSGVTQVTSNTN CCCCCCCEEEECCCC | 22.35 | 22369663 | |
| 1442 | Phosphorylation | VSGVTQVTSNTNTPG CCCCEEEECCCCCCC | 13.36 | 22369663 | |
| 1443 | Phosphorylation | SGVTQVTSNTNTPGN CCCEEEECCCCCCCC | 42.68 | 22369663 | |
| 1445 | Phosphorylation | VTQVTSNTNTPGNSD CEEEECCCCCCCCCC | 39.99 | 22369663 | |
| 1447 | Phosphorylation | QVTSNTNTPGNSDRE EEECCCCCCCCCCHH | 30.45 | 22369663 | |
| 1451 | Phosphorylation | NTNTPGNSDRERVDE CCCCCCCCCHHHHHH | 43.91 | 22369663 | |
| 1462 | Phosphorylation | RVDETAASLDDERSS HHHHHHHCCCCCHHC | 29.84 | 23749301 | |
| 1468 | Phosphorylation | ASLDDERSSNGSDIS HCCCCCHHCCCCCCC | 26.55 | 28889911 | |
| 1472 | Phosphorylation | DERSSNGSDISDPTA CCHHCCCCCCCCCCH | 35.70 | 28889911 | |
| 1620 | Phosphorylation | EVNFTKDYSASDFFS EEECCCCCCHHHHCC | 14.00 | 27017623 | |
| 1621 | Phosphorylation | VNFTKDYSASDFFSG EECCCCCCHHHHCCC | 31.28 | 27017623 | |
| 1633 | Phosphorylation | FSGGTIIYIQRKSES CCCCEEEEEEECCHH | 6.27 | 27017623 | |
| 1668 | Phosphorylation | KAAESKNYSRLNLKN HHHHCCCCCCCCCCC | 10.02 | 21440633 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of APC1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of APC1_YEAST !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of APC1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, AND MASSSPECTROMETRY. | |
