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Protein Page:
UBC9 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
UBC9 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. Interacts with HIPK1, HIPK2, PPM1J, RASD2 and TCF3 Interacts with NR2C1; the interaction promotes its sumoylation. Forms a tight complex with RANGAP1 and RANBP2. Interacts with SIAH1 and PARP. Interacts with various transcription factors such as TFAP2A, TFAP2B, TFAP2C, AR, ETS1 and SOX4. Interacts with RWDD3; the interaction enhances the sumoylation of a number of proteins such as HIF1A and I-kappa-B. Interacts with DNMT1. Interacts with FOXL2. Forms a complex with SENP6 and UBE2I in response to UV irradiation. Interacts with human herpesvirus 6 IE2. Interacts with human adenovirus early E1A protein; this interaction interferes with polysumoylation (Probable). Interacts with DNM1l (via its GTPase and B domains); the interaction promotes sumoylation of DNM1L, mainly in its B domain. Interacts with PML-RARA oncoprotein (via the coiled-colied domain); the interaction is required for sumoylation of the PML- RARA oncoprotein. Interacts with IPO13. Interacts with NFATC2IP; this inhibits formation of poly-SUMO chains. Expressed in heart, skeletal muscle, pancreas, kidney, liver, lung, placenta and brain. Also expressed in testis and thymus. Belongs to the ubiquitin-conjugating enzyme family. Note: This description may include information from UniProtKB.
Protein type: Nuclear receptor co-regulator; EC 6.3.2.19; Ubiquitin conjugating system; Ubiquitin ligase; SUMO conjugating system; EC 6.3.2.-; Ligase
Cellular Component: nucleoplasm; PML body; dendrite; cytoplasm; fibrillar center; synapse; synaptonemal complex; nucleus
Molecular Function: protein C-terminus binding; protein binding; enzyme binding; ubiquitin-protein ligase activity; bHLH transcription factor binding; SUMO ligase activity; HLH domain binding; transcription factor binding; ATP binding
Biological Process: ubiquitin-dependent protein catabolic process; mitosis; proteasomal ubiquitin-dependent protein catabolic process; viral reproduction; positive regulation of steroid hormone receptor signaling pathway; protein ubiquitination; protein modification process; negative regulation of transcription from RNA polymerase II promoter; post-translational protein modification; chromosome segregation; cellular protein metabolic process; protein sumoylation; positive regulation of transcription factor activity; regulation of receptor activity; negative regulation of transcription, DNA-dependent
Reference #:  P63279 (UniProtKB)
Alt. Names/Synonyms: C358B7.1; p18; SUMO-1-protein ligase; SUMO-conjugating enzyme UBC9; SUMO-protein ligase; UBC9; UBCE9; UBE2I; Ubiquitin carrier protein 9; Ubiquitin carrier protein I; ubiquitin conjugating enzyme 9; Ubiquitin-conjugating enzyme E2 I; ubiquitin-conjugating enzyme E2I (homologous to yeast UBC9); ubiquitin-conjugating enzyme E2I (UBC9 homolog, yeast); ubiquitin-conjugating enzyme UbcE2A; ubiquitin-like protein SUMO-1 conjugating enzyme; ubiquitin-protein ligase E2I; Ubiquitin-protein ligase I
Gene Symbols: UBE2I
Molecular weight: 18,007 Da
Basal Isoelectric point: 8.87  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

UBC9

Protein Structure Not Found.


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Sites Implicated In
enzymatic activity, induced: S71‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 S2-p ______MsGIALSRL
3 0 K14-sm SRLAQERkAWRkDHP
0 6 K18-ub QERkAWRkDHPFGFV
0 1 T35-p PTKNPDGtMNLMNWE
1 1 K49-sm ECAIPGKkGTPWEGG
0 6 K49-ub ECAIPGKkGTPWEGG
0 1 K59-ub PWEGGLFkLRMLFkD
1 2 K65-ac FkLRMLFkDDYPssP
0 2 K65-ub FkLRMLFkDDYPssP
0 1 K65-sc FkLRMLFkDDYPssP
0 5 S70-p LFkDDYPssPPKCKF
2 9 S71-p FkDDYPssPPKCKFE
1 0 K146-sm QNRVEYEkRVRAQAk
3 0 K153-sm kRVRAQAkKFAPS__
  mouse

 
S2 ______MSGIALSRL
K14 SRLAQERKAWRkDHP
K18-ub QERKAWRkDHPFGFV
T35 PTKNPDGTMNLMNWE
K49 ECAIPGKKGTPWEGG
K49 ECAIPGKKGTPWEGG
K59 PWEGGLFKLRMLFkD
K65-ac FKLRMLFkDDYPSSP
K65 FKLRMLFKDDYPSSP
K65 FKLRMLFKDDYPSSP
S70 LFkDDYPSSPPKCKF
S71 FkDDYPSSPPKCKFE
K146 QNRVEYEKRVRAQAK
K153 KRVRAQAKKFAPS__
  rat

 
S2 ______MSGIALSRL
K14 SRLAQERKAWRKDHP
K18 QERKAWRKDHPFGFV
T35 PTKNPDGTMNLMNWE
K49 ECAIPGKKGTPWEGG
K49 ECAIPGKKGTPWEGG
K59 PWEGGLFKLRMLFkD
K65-ac FKLRMLFkDDYPSSP
K65 FKLRMLFKDDYPSSP
K65 FKLRMLFKDDYPSSP
S70 LFkDDYPSSPPKCKF
S71 FkDDYPSSPPKCKFE
K146 QNRVEYEKRVRAQAK
K153 KRVRAQAKKFAPS__
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