UniProt Accession

 UBC9_HUMAN; P63279; D3DU69; P50550; Q15698; Q59GX1; Q86VB3 

Genbank Protein ID

 X96427; U45328; D45050; U29092; U31933; U31882; U66867; U66818; U38785; AJ002385; BT006932; AB208988; AE006466; AL031714; CH471112; CH471112; CH471112; CH471112; CH471112; BC000427; BC004429; BC051289 

Genbank Nucleotide ID

 CAA65287.1; AAA86662.1; BAA08091.1; AAC51361.1; AAB02181.1; AAC50603.1; AAC50716.1; AAC50715.1; AAB09410.1; CAA05359.1; AAP35578.1; BAD92225.1; AAK61274.1; CAB45853.1; EAW85673.1; EAW85676.1; EAW85677.1; EAW85678.1; EAW85679.1; AAH00427.1; AAH04429.1; AAH51289.3 

Protein Name

 SUMO-conjugating enzyme UBC9 

Protein Synonyms/Alias

 SUMO-protein ligase; Ubiquitin carrier protein 9; Ubiquitin carrier protein I; Ubiquitin-conjugating enzyme E2 I; Ubiquitin-protein ligase I; p18 

Gene Name

 UBE2I 

Gene Synonyms/Alias

 UBC9; UBCE9 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
14	SRLAQERKAWRKDHP	sumoylation	[1]
18	QERKAWRKDHPFGFV	ubiquitination	[2, 3, 4]
49	ECAIPGKKGTPWEGG	sumoylation	[1, 5]
49	ECAIPGKKGTPWEGG	ubiquitination	[4]
59	PWEGGLFKLRMLFKD	ubiquitination	[3]
65	FKLRMLFKDDYPSSP	acetylation	[6, 7]
65	FKLRMLFKDDYPSSP	ubiquitination	[3, 4]
153	KRVRAQAKKFAPS**	sumoylation	[1, 8]

Reference

 [1] Rhes, a physiologic regulator of sumoylation, enhances cross-sumoylation between the basic sumoylation enzymes E1 and Ubc9.
 Subramaniam S, Mealer RG, Sixt KM, Barrow RK, Usiello A, Snyder SH.
 J Biol Chem. 2010 Jul 2;285(27):20428-32. [PMID: 20424159]
 [2] Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry.
 Meierhofer D, Wang X, Huang L, Kaiser P.
 J Proteome Res. 2008 Oct;7(10):4566-76. [PMID: 18781797]
 [3] 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]
 [4] 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]
 [5] Targeted identification of SUMOylation sites in human proteins using affinity enrichment and paralog-specific reporter ions.
 Lamoliatte F, Bonneil E, Durette C, Caron-Lizotte O, Wildemann D, Zerweck J, Wenschuh H, Thibault P.
 Mol Cell Proteomics. 2013 Jun 7;. [PMID: 23750026]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [7] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation.
 Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C.
 Sci Signal. 2011 Jul 26;4(183):ra48. [PMID: 21791702]
 [8] In vitro modification of human centromere protein CENP-C fragments by small ubiquitin-like modifier (SUMO) protein: definitive identification of the modification sites by tandem mass spectrometry analysis of the isopeptides.
 Chung TL, Hsiao HH, Yeh YY, Shia HL, Chen YL, Liang PH, Wang AH, Khoo KH, Shoei-Lung Li S.
 J Biol Chem. 2004 Sep 17;279(38):39653-62. [PMID: 15272016] 

Functional Description

 Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3 and SUMO4 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2 or CBX4. Can catalyze the formation of poly- SUMO chains. Necessary for sumoylation of FOXL2 and KAT5. Essential for nuclear architecture and chromosome segregation. Sumoylates p53/TP53 at 'Lys-386'. 

Sequence Annotation

 REGION 13 18 Interaction with SUMO1.
 ACT_SITE 93 93 Glycyl thioester intermediate.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 65 65 N6-acetyllysine.
 MOD_RES 71 71 Phosphoserine; by CDK1.
 CROSSLNK 18 18 Glycyl lysine isopeptide (Lys-Gly)  

Keyword

 3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division; Chromosome partition; Complete proteome; Cytoplasm; Host-virus interaction; Isopeptide bond; Ligase; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation; Ubl conjugation pathway. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 158 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0030425; C:dendrite; IEA:Compara.
 GO:0001650; C:fibrillar center; IEA:Compara.
 GO:0016605; C:PML body; IDA:UniProtKB.
 GO:0045202; C:synapse; IEA:Compara.
 GO:0000795; C:synaptonemal complex; TAS:ProtInc.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0019789; F:SUMO ligase activity; IEA:Compara.
 GO:0004842; F:ubiquitin-protein ligase activity; TAS:BHF-UCL.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
 GO:0033145; P:positive regulation of intracellular steroid hormone receptor signaling pathway; IEA:Compara.
 GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IEA:Compara.
 GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; IEA:Compara.
 GO:0016925; P:protein sumoylation; IDA:BHF-UCL.
 GO:0010469; P:regulation of receptor activity; IEA:Compara.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:ProtInc.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 

Interpro

 IPR027230; Ubc9.
 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