| UniProt ID | ANC2_MOUSE | |
|---|---|---|
| UniProt AC | Q8BZQ7 | |
| Protein Name | Anaphase-promoting complex subunit 2 | |
| Gene Name | Anapc2 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 837 | |
| Subcellular Localization | ||
| Protein Description | Together with the RING-H2 protein ANAPC11, constitutes the catalytic component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. The CDC20-APC/C complex positively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 drives presynaptic differentiation.. | |
| Protein Sequence | MEAEGVAVAAAAAAAAAAATIIASDDCDSRPGQELLVAWNTVSTGLVPPAALGLASSRTSGAVPPKEEELRAAVEVLRGHGLHSVLEEWFVEVLQNDLQGNIATEFWNAIALRENSVDEPQCLGLLLDAFGLLESRLDPYLHSLELLEKWTRLGLLMGAGAQGLREKVHTMLRGVLFFSTPRTFQEMVQRLYGRFLRVYMQSKRKGEGGTDPELEGELDSRYARRRYYRLLQSPLCAGCGSDKQQCWCRQALEQFNQLSQVLHRLSLLERVCAEAVTTTLHQVTRERMEDRCRGEYERSFLREFHKWIERVVGWLGKVFLQDNPTRPTSPEAGNTLRRWRCHVQRFFYRIYATLRIEELFSIIRDFPDSRPAIEDLKYCLERTDQRQQLLVSLKVALETRLLHPGVNTCDIITLYISAIKALRVLDPSMVILEVACEPIRRYLRTREDTVRQIVAGLTGDSDGTGDLAVELSKTDPACLETGQDSEDDSGEPEDWVPDPVDADPVKSSSKRRSSDIISLLVSIYGSKDLFINEYRSLLADRLLHQFSFSPEREIRNVELLKLRFGEAPMHFCEVMLKDMADSRRINANIREEDEKRPVEEQPPFGVYAVILSSEFWPPFKDEKLEVPEDIRAALDVYCKKYEKLKAMRTLSWKHTLGLVTMDVELADRTLSVAVTPVQAVVLLYFQNQASWTLEELSKVVKMPVALLRRRMSVWLQQGVLREEPPGTFSVIEEERPQDRDNMVLIDSDDESDSGMASQADQKEEELLLFWAYIQAMLTNLESLSLERIYSMLRMFVMTGPALAEIDLQELQGYLQKKVRDQQLIYSAGVYRLPKNSN | |
| 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 |
|---|---|---|---|---|---|
| 43 | Phosphorylation | LVAWNTVSTGLVPPA EEEEEECCCCCCCHH | 18.08 | 24719451 | |
| 205 | Ubiquitination | VYMQSKRKGEGGTDP HHHHHHCCCCCCCCH | 66.12 | - | |
| 233 | Phosphorylation | RYYRLLQSPLCAGCG HHHHHHCCCCCCCCC | 21.58 | - | |
| 325 | Phosphorylation | VFLQDNPTRPTSPEA HHCCCCCCCCCCCCH | 56.38 | 25777480 | |
| 328 | Phosphorylation | QDNPTRPTSPEAGNT CCCCCCCCCCCHHHH | 54.33 | 21149613 | |
| 329 | Phosphorylation | DNPTRPTSPEAGNTL CCCCCCCCCCHHHHH | 24.35 | 25521595 | |
| 335 | Phosphorylation | TSPEAGNTLRRWRCH CCCCHHHHHHHHHHH | 22.26 | 29472430 | |
| 408 | Phosphorylation | LLHPGVNTCDIITLY HCCCCCCHHHHHHHH | 14.78 | 21454597 | |
| 415 | Phosphorylation | TCDIITLYISAIKAL HHHHHHHHHHHHHHH | 5.56 | 21454597 | |
| 474 | Phosphorylation | LAVELSKTDPACLET EEEEECCCCHHHHHC | 43.79 | 27087446 | |
| 481 | Phosphorylation | TDPACLETGQDSEDD CCHHHHHCCCCCCCC | 27.48 | 21149613 | |
| 485 | Phosphorylation | CLETGQDSEDDSGEP HHHCCCCCCCCCCCC | 34.73 | 24925903 | |
| 489 | Phosphorylation | GQDSEDDSGEPEDWV CCCCCCCCCCCCCCC | 58.33 | 21659605 | |
| 513 | Phosphorylation | KSSSKRRSSDIISLL CCCCCCCHHHHHHHH | 36.07 | 26745281 | |
| 514 | Phosphorylation | SSSKRRSSDIISLLV CCCCCCHHHHHHHHH | 30.90 | 26745281 | |
| 518 | Phosphorylation | RRSSDIISLLVSIYG CCHHHHHHHHHHHHC | 18.91 | 25777480 | |
| 522 | Phosphorylation | DIISLLVSIYGSKDL HHHHHHHHHHCCCCH | 15.29 | - | |
| 547 | Phosphorylation | DRLLHQFSFSPEREI HHHHHHCCCCCHHHC | 20.46 | 27600695 | |
| 549 | Phosphorylation | LLHQFSFSPEREIRN HHHHCCCCCHHHCCC | 25.34 | 26824392 | |
| 561 | Ubiquitination | IRNVELLKLRFGEAP CCCEEEEEHHHCCCC | 50.68 | - | |
| 712 | Phosphorylation | ALLRRRMSVWLQQGV HHHHHHHHHHHHCCC | 14.34 | 22817900 | |
| 747 | Phosphorylation | DNMVLIDSDDESDSG CCEEEECCCCCCCCC | 39.71 | 25521595 | |
| 751 | Phosphorylation | LIDSDDESDSGMASQ EECCCCCCCCCCCCC | 44.03 | 22817900 | |
| 753 | Phosphorylation | DSDDESDSGMASQAD CCCCCCCCCCCCCCC | 39.48 | 29550500 | |
| 757 | Phosphorylation | ESDSGMASQADQKEE CCCCCCCCCCCHHHH | 19.60 | 29550500 | |
| 825 | Phosphorylation | VRDQQLIYSAGVYRL HCCCHHHHHEECEEC | 10.89 | 22817900 | |
| 826 | Phosphorylation | RDQQLIYSAGVYRLP CCCHHHHHEECEECC | 16.14 | 22006019 |
| 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 ANC2_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ANC2_MOUSE !! | ||||||
* 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 ANC2_MOUSE !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling."; Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.; J. Immunol. 179:5864-5876(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-825, AND MASSSPECTROMETRY. | |
