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Protein Page:
UBC9 (human)
rdtyret
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
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: EC 6.3.2.-; EC 6.3.2.19; Ubiquitin ligase; Nuclear receptor co-regulator; Ubiquitin conjugating system; SUMO conjugating system; Ligase
Chromosomal Location of Human Ortholog: 16p13.3
Cellular Component: cytoplasm; cytosol; nuclear envelope; nucleoplasm; nucleus; PML body; synaptonemal complex
Molecular Function: ATP binding; enzyme binding; HLH domain binding; ligase activity; protein binding; SUMO ligase activity; transcription factor binding; ubiquitin protein ligase binding
Biological Process: cell division; cellular protein metabolic process; chromosome segregation; DNA repair; double-strand break repair; double-strand break repair via homologous recombination; mitosis; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent; nucleotide-excision repair; positive regulation of I-kappaB kinase/NF-kappaB cascade; post-translational protein modification; protein modification process; protein sumoylation; ubiquitin-dependent protein catabolic process; viral reproduction
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  
Click here to view other types of protein modifications

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 LTP 

LTP: 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.


 HTP 

HTP: 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
1 1 T35‑p PTKNPDGtMNLMNWE
1 1 K49‑sm ECAIPGKkGTPWEGG
0 7 K49‑ub ECAIPGKkGTPWEGG
0 1 K59‑ub PWEGGLFkLRMLFkD
1 4 K65‑ac FkLRMLFkDDYPssP
0 2 K65‑ub FkLRMLFkDDYPssP
0 1 K65‑sc FkLRMLFkDDYPssP
0 5 S70‑p LFkDDYPssPPKCKF
3 10 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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