UniProt Accession

 ANC2_HUMAN; Q9UJX6; Q5VSG1; Q96DG5; Q96GG4; Q9P2E1 

Genbank Protein ID

 AF191337; AL929554; BC032503; BC001579; BC009487; AB037827 

Genbank Nucleotide ID

 AAF05751.1; CAH72881.1; AAH32503.1; AAH01579.1; AAH09487.2; BAA92644.1 

Protein Name

 Anaphase-promoting complex subunit 2 

Protein Synonyms/Alias

 APC2; Cyclosome subunit 2 

Gene Name

 ANAPC2 

Gene Synonyms/Alias

 APC2; KIAA1406 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
134	RSLELLEKWTRLGLL	ubiquitination	[1, 2]
190	VYMQSKRKGEGGTDP	ubiquitination	[3, 4, 5, 6, 7]
228	CAGCSSDKQQCWCRQ	ubiquitination	[4, 6, 7, 8]
546	IRNVELLKLRFGEAP	ubiquitination	[6]
562	HFCEVMLKDMADSRR	ubiquitination	[4, 6]
625	ALEAYCKKYEQLKAM	ubiquitination	[6]
630	CKKYEQLKAMRTLSW	ubiquitination	[6]
686	EELSKAVKMPVALLR	ubiquitination	[6]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [6] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [8] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 

Functional Description

 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. 

Sequence Annotation

 MOD_RES 218 218 Phosphoserine.
 MOD_RES 314 314 Phosphoserine.
 MOD_RES 470 470 Phosphoserine.
 MOD_RES 534 534 Phosphoserine.
 MOD_RES 810 810 Phosphotyrosine (By similarity).  

Keyword

 Alternative splicing; Cell cycle; Cell division; Complete proteome; Differentiation; Mitosis; Neurogenesis; Phosphoprotein; Reference proteome; Ubl conjugation pathway. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 822 AA 

Protein Sequence

Gene Ontology

 GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0004842; F:ubiquitin-protein ligase activity; TAS:ProtInc.
 GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
 GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0008054; P:cyclin catabolic process; TAS:ProtInc.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0007094; P:mitotic spindle assembly checkpoint; TAS:Reactome.
 GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
 GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
 GO:0090129; P:positive regulation of synapse maturation; ISS:UniProtKB.
 GO:0031915; P:positive regulation of synaptic plasticity; ISS:UniProtKB.
 GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
 GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
 GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ProtInc. 

Interpro

 IPR014786; APC_su2_C.
 IPR016158; Cullin_homology.
 IPR001373; Cullin_N.
 IPR011991; WHTH_DNA-bd_dom. 

Pfam

 PF08672; APC2
 PF00888; Cullin 

SMART

 SM01013; APC2
 SM00182; CULLIN 

PROSITE

 PS01256; CULLIN_1
 PS50069; CULLIN_2 

PRINTS