UniProt Accession

 CCNA2_HUMAN; P20248; A8K7B6; Q2M3U6; Q4W5P4; Q6LER8 

Genbank Protein ID

 X51688; X68303; CR407692; AF518006; AK291931; AC079341; CH471056; BC104783; BC104787 

Genbank Nucleotide ID

 CAA35986.1; CAA48375.1; CAG28620.1; AAM54042.1; BAF84620.1; AAY40969.1; EAX05246.1; AAI04784.1; AAI04788.1 

Protein Name

 Cyclin-A2 

Protein Synonyms/Alias

 Cyclin-A 

Gene Name

 CCNA2 

Gene Synonyms/Alias

 CCN1; CCNA 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
37	QENINPEKAAPVQQP	ubiquitination	[1, 2]
54	RAALAVLKSGNPRGL	acetylation	[3, 4, 5]
54	RAALAVLKSGNPRGL	ubiquitination	[1, 2, 6, 7]
68	LAQQQRPKTRRVAPL	acetylation	[3, 4, 5]
95	PPWKANSKQPAFTIH	acetylation	[3, 4]
112	EAEKEAQKKPAESQK	acetylation	[3, 4]

Reference

 [1] 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]
 [2] 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]
 [3] Degradation of cyclin A is regulated by acetylation.
 Mateo F, Vidal-Laliena M, Canela N, Busino L, Martinez-Balbas MA, Pagano M, Agell N, Bachs O.
 Oncogene. 2009 Jul 23;28(29):2654-66. [PMID: 19483727]
 [4] Acetylation of cyclin A: a new cell cycle regulatory mechanism.
 Mateo F, Vidal-Laliena M, Pujol MJ, Bachs O.
 Biochem Soc Trans. 2010 Feb;38(Pt 1):83-6. [PMID: 20074040]
 [5] The ATAC acetyl transferase complex controls mitotic progression by targeting non-histone substrates.
 Orpinell M, Fournier M, Riss A, Nagy Z, Krebs AR, Frontini M, Tora L.
 EMBO J. 2010 Jul 21;29(14):2381-94. [PMID: 20562830]
 [6] 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]
 [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] 

Functional Description

 Essential for the control of the cell cycle at the G1/S (start) and the G2/M (mitosis) transitions. 

Sequence Annotation

 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 5 5 Phosphoserine.
 MOD_RES 55 55 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Cell cycle; Cell division; Complete proteome; Cyclin; Cytoplasm; Mitosis; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 432 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0001939; C:female pronucleus; IEA:Compara.
 GO:0001940; C:male pronucleus; IEA:Compara.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0007095; P:mitotic G2 DNA damage checkpoint; TAS:ProtInc.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IEA:Compara.
 GO:0007265; P:Ras protein signal transduction; IEP:BHF-UCL.
 GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:InterPro. 

Interpro

 IPR013763; Cyclin-like.
 IPR014400; Cyclin_A/B/D/E.
 IPR004367; Cyclin_C-dom.
 IPR006671; Cyclin_N. 

Pfam

 PF02984; Cyclin_C
 PF00134; Cyclin_N 

SMART

 SM00385; CYCLIN 

PROSITE

 PS00292; CYCLINS 

PRINTS