Home

SUMO2 (human)

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 Cellular Component: nucleus Molecular Function: protein binding; ubiquitin protein ligase binding Biological Process: protein sumoylation; positive regulation of proteasomal ubiquitin-dependent protein catabolic process 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:  Jak/Stat/IL-6 Signaling  |  NF-kB Signaling  |  Protein Acetylation Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below SUMO2 1WM2 - A=12-89 (human) 1WM3 - A=17-88 (human) 1WZ0 - A=1-93 (human) 1Z5Q - B=15-93 (human) 2AWT - A=1-95 (human) 2CKH - B=15-93 (human) 2D07 - B=1-93 (human) 2IO0 - B=15-95 (human) 2IO3 - B=15-93 (human) 2IYD - B=15-95 (human) 2RPQ - A=1-93 (human) 3UIN - B=14-93 (human) 3UIO - B=14-93 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1WM2 1WM3 1WZ0 1Z5Q 2AWT 2CKH 2D07 2IO0 2IO3 2IYD 2RPQ 3UIN 3UIO  |  Phospho3D  |  DISEASE  |  Source  |  InnateDB  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	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

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-a	___MADEkPkEGVkT
0	3		K5-u	___MADEkPkEGVkT
1	1		K5-s	___MADEkPkEGVkT
0	2		K7-u	_MADEkPkEGVkTEN
1	0		K7-s	_MADEkPkEGVkTEN
0	6		K11-a	EkPkEGVkTENNDHI
0	85		K11-u	EkPkEGVkTENNDHI
5	3		K11-s	EkPkEGVkTENNDHI
0	18		K21-u	NNDHINLkVAGQDGs
0	3		S28-p	kVAGQDGsVVQFkIk
1	27		K33-u	DGsVVQFkIkRHtPL
0	8		K35-u	sVVQFkIkRHtPLSk
0	3		T38-p	QFkIkRHtPLSkLMk
0	2		K42-a	kRHtPLSkLMkAYCE
0	47		K42-u	kRHtPLSkLMkAYCE
2	0		K42-s	kRHtPLSkLMkAYCE
0	2		K45-a	tPLSkLMkAYCERQG
0	47		K45-u	tPLSkLMkAYCERQG
0	6		S54-p	YCERQGLsMRQIRFR

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

	rat
K5	___MADEKPKEGVkT
K5	___MADEKPKEGVkT
K5	___MADEKPKEGVkT
K7	_MADEKPKEGVkTEN
K7	_MADEKPKEGVkTEN
K11	EKPKEGVKTENNDHI
K11-u	EKPKEGVkTENNDHI
K11	EKPKEGVKTENNDHI
K21	NNDHINLKVAGQDGS
S28	KVAGQDGSVVQFKIK
K33	DGSVVQFKIKRHTPL
K35	SVVQFKIKRHTPLSk
T38	QFKIKRHTPLSkLMk
K42	KRHTPLSKLMkAYCE
K42-u	KRHTPLSkLMkAYCE
K42	KRHTPLSKLMkAYCE
K45-a	TPLSkLMkAYCERQG
K45-u	TPLSkLMkAYCERQG
S54	YCERQGLSMRQIRFR

Home  |  Curator Login With enhanced literature mining using Linguamatics I2E Produced by 3rd Millennium  |  Design by Digizyme ©2003-2013 Cell Signaling Technology, Inc.