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Protein Page:
SUMO2 (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
SUMO2 Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptide bond 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. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. Homotrimer (Potential). Crystal packing analysis suggests a possible trimeric assembly, of which the biological significance remains to be determined. Interacts with SAE2 and UBE2I. Covalently attached to a number of proteins. Interacts with PELP1. Interacts with USP25; the interaction sumoylates USP25. Broadly expressed. Belongs to the ubiquitin family. SUMO subfamily. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Ubiquitin-like modifier
Chromosomal Location of Human Ortholog: 17q25.1
Cellular Component: nucleoplasm; PML body
Molecular Function: protein binding; ubiquitin protein ligase binding
Biological Process: cellular protein metabolic process; protein sumoylation; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; post-translational protein modification
Reference #:  P61956 (UniProtKB)
Alt. Names/Synonyms: HSMT3; MGC117191; sentrin 2; Sentrin-2; small ubiquitin-like modifier 2; Small ubiquitin-related modifier 2; SMT3 homolog 2; SMT3 suppressor of mif two 3 homolog 2 (S. cerevisiae); SMT3B; SMT3H2; SUMO-2; SUMO-3; SUMO2; SUMO3; Ubiquitin-like protein SMT3B
Gene Symbols: SUMO2
Molecular weight: 10,871 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
Select Structure to View Below

SUMO2

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 2 K5-ac ___MADEkPkEGVkt
0 3 K5-ub ___MADEkPkEGVkt
1 1 K5-sm ___MADEkPkEGVkt
0 2 K7-ub _MADEkPkEGVktEN
1 0 K7-sm _MADEkPkEGVktEN
0 7 K11-ac EkPkEGVktENNDHI
0 85 K11-ub EkPkEGVktENNDHI
6 3 K11-sm EkPkEGVktENNDHI
0 1 T12-p kPkEGVktENNDHIN
0 18 K21-ub NNDHINLkVAGQDGs
0 7 S28-p kVAGQDGsVVQFkIk
1 27 K33-ub DGsVVQFkIkRHtPL
0 8 K35-ub sVVQFkIkRHtPLSk
0 3 T38-p QFkIkRHtPLSkLMk
0 2 K42-ac kRHtPLSkLMkAYCE
0 47 K42-ub kRHtPLSkLMkAYCE
2 0 K42-sm kRHtPLSkLMkAYCE
0 2 K45-ac tPLSkLMkAYCERQG
0 47 K45-ub tPLSkLMkAYCERQG
0 6 S54-p YCERQGLsMRQIRFR
  mouse

 
K5 ___MADEKPKEGVkT
K5 ___MADEKPKEGVkT
K5 ___MADEKPKEGVkT
K7 _MADEKPKEGVkTEN
K7 _MADEKPKEGVkTEN
K11 EKPKEGVKTENNDHI
K11-ub EKPKEGVkTENNDHI
K11 EKPKEGVKTENNDHI
T12 KPKEGVkTENNDHIN
K21-ub NNDHINLkVAGQDGs
S28-p kVAGQDGsVVQFkIk
K33-ub DGsVVQFkIkRHtPL
K35-ub sVVQFkIkRHtPLSk
T38-p QFkIkRHtPLSkLMk
K42 kRHtPLSKLMkAYCE
K42-ub kRHtPLSkLMkAYCE
K42 kRHtPLSKLMkAYCE
K45 tPLSkLMKAYCERQG
K45-ub tPLSkLMkAYCERQG
S54 YCERQGLSMRQIRFR
  rat

 
K5-ac ___MADEkPKEGVkT
K5 ___MADEKPKEGVkT
K5 ___MADEKPKEGVkT
K7 _MADEkPKEGVkTEN
K7 _MADEkPKEGVkTEN
K11-ac EkPKEGVkTENNDHI
K11-ub EkPKEGVkTENNDHI
K11 EkPKEGVKTENNDHI
T12 kPKEGVkTENNDHIN
K21 NNDHINLKVAGQDGS
S28 KVAGQDGSVVQFKIK
K33 DGSVVQFKIKRHTPL
K35 SVVQFKIKRHTPLSk
T38 QFKIKRHTPLSkLMk
K42-ac KRHTPLSkLMkAYCE
K42-ub KRHTPLSkLMkAYCE
K42 KRHTPLSKLMkAYCE
K45-ac TPLSkLMkAYCERQG
K45-ub TPLSkLMkAYCERQG
S54 YCERQGLSMRQIRFR
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