UniProt Accession

 UBE2S_HUMAN; Q16763; Q9BTC1 

Genbank Protein ID

 M91670; AB062397; AC020922; BC004236; BC007554; BC065364 

Genbank Nucleotide ID

 AAA58446.1; BAB93484.1; AAH04236.1; AAH07554.1; AAH65364.1 

Protein Name

 Ubiquitin-conjugating enzyme E2 S 

Protein Synonyms/Alias

 E2-EPF; Ubiquitin carrier protein S; Ubiquitin-conjugating enzyme E2-24 kDa; Ubiquitin-conjugating enzyme E2-EPF5; Ubiquitin-protein ligase S 

Gene Name

 UBE2S 

Gene Synonyms/Alias

 E2EPF; OK/SW-cl.73 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
18	HIIRLVYKEVTTLTA	ubiquitination	[1, 2, 3]
32	ADPPDGIKVFPNEED	ubiquitination	[2]
63	AGGLFRMKLLLGKDF	ubiquitination	[4]
68	RMKLLLGKDFPASPP	ubiquitination	[1, 3, 4, 5]
76	DFPASPPKGYFLTKI	ubiquitination	[4]
100	EICVNVLKRDWTAEL	ubiquitination	[1, 3, 4, 5, 6]
117	RHVLLTIKCLLIHPN	ubiquitination	[6]
197	GAEGPMAKKHAGERD	ubiquitination	[1, 2, 3, 6, 7, 8, 9, 10]
198	AEGPMAKKHAGERDK	ubiquitination	[4]

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] 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]
 [3] 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]
 [4] 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]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [7] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [8] 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]
 [9] 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]
 [10] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 

Functional Description

 Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes 'Lys-11'-linked polyubiquitination. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by specifically elongating 'Lys-11'-linked polyubiquitin chains initiated by the E2 enzyme UBE2C/UBCH10 on APC/C substrates, enhancing the degradation of APC/C substrates by the proteasome and promoting mitotic exit. Also acts by elongating ubiquitin chains initiated by the E2 enzyme UBE2D1/UBCH5 in vitro; it is however unclear whether UBE2D1/UBCH5 acts as a E2 enzyme for the APC/C in vivo. Also involved in ubiquitination and subsequent degradation of VHL, resulting in an accumulation of HIF1A. In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, except 'Lys-48'-linked polyubiquitination. 

Sequence Annotation

 ACT_SITE 95 95 Glycyl thioester intermediate.
 MOD_RES 1 1 N-acetylmethionine.  

Keyword

 3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division; Complete proteome; Ligase; Nucleotide-binding; Reference proteome; Ubl conjugation; Ubl conjugation pathway. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 222 AA 

Protein Sequence

Gene Ontology

 GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0051488; P:activation of anaphase-promoting complex activity; IDA:UniProtKB.
 GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0010458; P:exit from mitosis; IDA:UniProtKB.
 GO:0010994; P:free ubiquitin chain polymerization; IDA:UniProtKB.
 GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
 GO:0044314; P:protein K27-linked ubiquitination; IDA:UniProtKB.
 GO:0035519; P:protein K29-linked ubiquitination; IDA:UniProtKB.
 GO:0085020; P:protein K6-linked ubiquitination; IDA:UniProtKB.
 GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB. 

Interpro

 IPR000608; UBQ-conjugat_E2.
 IPR023313; UBQ-conjugating_AS.
 IPR016135; UBQ-conjugating_enzyme/RWD. 

Pfam

 PF00179; UQ_con 

SMART

  

PROSITE

 PS00183; UBIQUITIN_CONJUGAT_1
 PS50127; UBIQUITIN_CONJUGAT_2 

PRINTS