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Protein Page:
SUMO3 (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
SUMO3 Ubiquitin-like protein which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. Covalently attached to a number of proteins. Interacts with USP25 (via ts SIM domain); the interaction sumoylates USP25 and inhibits its ubiquitin hydrolyzing activity. Interacts with SAE2 and UBE2I. Expressed predominantly in liver. Belongs to the ubiquitin family. SUMO subfamily. Note: This description may include information from UniProtKB.
Protein type: Ubiquitin-like modifier
Cellular Component: kinetochore; nucleoplasm; PML body; cytoplasm
Molecular Function: protein binding
Biological Process: cellular protein metabolic process; protein sumoylation; post-translational protein modification
Reference #:  P55854 (UniProtKB)
Alt. Names/Synonyms: Small ubiquitin-related modifier 3; SMT3 homolog 1; SMT3 suppressor of mif two 3 homolog 1; SMT3 suppressor of mif two 3 homolog 3 (S. cerevisiae); SMT3A; SMT3H1; SUMO-2; SUMO-3; SUMO3; Ubiquitin-like protein SMT3A
Gene Symbols: SUMO3
Molecular weight: 11,637 Da
Basal Isoelectric point: 5.32  Predict pI for various phosphorylation states
CST Pathways:  IL6 Signaling  |  NF-kB Signaling  |  Protein Acetylation
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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SUMO3

Protein Structure Not Found.


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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 1 S2-p ______MsEEKPKEG
0 2 K11-ac EKPKEGVkTENDHIN
0 4 K11-ub EKPKEGVkTENDHIN
4 2 K11-sm EKPKEGVkTENDHIN
0 1 K20-ub ENDHINLkVAGQDGs
0 6 S27-p kVAGQDGsVVQFkIk
1 28 K32-ub DGsVVQFkIkRHtPL
0 8 K34-ub sVVQFkIkRHtPLSk
0 3 T37-p QFkIkRHtPLSkLMk
0 2 K41-ac kRHtPLSkLMkAYCE
1 0 K41-sm kRHtPLSkLMkAYCE
0 47 K41-ub kRHtPLSkLMkAYCE
0 2 K44-ac tPLSkLMkAYCERQG
0 47 K44-ub tPLSkLMkAYCERQG
0 6 S53-p YCERQGLsMRQIRFR
  mouse

 
S2 ______MSEEKPKEG
K11 EKPKEGVKTENDHIN
K11-ub EKPKEGVkTENDHIN
K11 EKPKEGVKTENDHIN
K20 ENDHINLKVAGQDGs
S27-p KVAGQDGsVVQFkIk
K32-ub DGsVVQFkIkRHtPL
K34-ub sVVQFkIkRHtPLSk
T37-p QFkIkRHtPLSkLMk
K41 kRHtPLSKLMkAYCE
K41 kRHtPLSKLMkAYCE
K41-ub kRHtPLSkLMkAYCE
K44 tPLSkLMKAYCERQG
K44-ub tPLSkLMkAYCERQG
S53 YCERQGLSMRQIRFR
  rat

 
S2 ______MSEEKPKEG
K11 EKPKEGVKTENDHIN
K11 EKPKEGVKTENDHIN
K11 EKPKEGVKTENDHIN
K20 ENDHINLKVAGQDGS
S27 KVAGQDGSVVQFKIK
K32 DGSVVQFKIKRHTPL
K34 SVVQFKIKRHTPLSk
T37 QFKIKRHTPLSkLMk
K41 KRHTPLSKLMkAYCE
K41 KRHTPLSKLMkAYCE
K41-ub KRHTPLSkLMkAYCE
K44-ac TPLSkLMkAYCERQG
K44-ub TPLSkLMkAYCERQG
S53 YCERQGLSMRQIRFR
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