UniProt Accession

 SUMO3_HUMAN; P55854; B2R5X4; Q53HI9; Q6FGD4; Q9BWR4 

Genbank Protein ID

 X99584; BT007008; CR542173; CR542188; AK222591; AK312350; CH471079; BC000036; BC008420 

Genbank Nucleotide ID

 CAA67896.1; AAP35654.1; CAG46970.1; CAG46985.1; BAD96311.1; BAG35271.1; EAX09392.1; AAH00036.1; AAH08420.1 

Protein Name

 Small ubiquitin-related modifier 3 

Protein Synonyms/Alias

 SUMO-3; SMT3 homolog 1; SUMO-2; Ubiquitin-like protein SMT3B; Smt3B 

Gene Name

 SUMO3 

Gene Synonyms/Alias

 SMT3B; SMT3H1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
5	***MSEEKPKEGVKT	sumoylation	[1]
11	EKPKEGVKTENDHIN	acetylation	[2]
11	EKPKEGVKTENDHIN	sumoylation	[1, 3, 4]
11	EKPKEGVKTENDHIN	ubiquitination	[5, 6]
41	KRHTPLSKLMKAYCE	acetylation	[2]
41	KRHTPLSKLMKAYCE	sumoylation	[4]
44	TPLSKLMKAYCERQG	acetylation	[2]

Reference

 [1] Targeted identification of SUMOylation sites in human proteins using affinity enrichment and paralog-specific reporter ions.
 Lamoliatte F, Bonneil E, Durette C, Caron-Lizotte O, Wildemann D, Zerweck J, Wenschuh H, Thibault P.
 Mol Cell Proteomics. 2013 Jun 7;. [PMID: 23750026]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] Positive and negative regulation of APP amyloidogenesis by sumoylation.
 Li Y, Wang H, Wang S, Quon D, Liu YW, Cordell B.
 Proc Natl Acad Sci U S A. 2003 Jan 7;100(1):259-64. [PMID: 12506199]
 [4] A novel proteomics approach to identify SUMOylated proteins and their modification sites in human cells.
 Galisson F, Mahrouche L, Courcelles M, Bonneil E, Meloche S, Chelbi-Alix MK, Thibault P.
 Mol Cell Proteomics. 2011 Feb;10(2):M110.004796. [PMID: 21098080]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 

Functional Description

 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. 

Sequence Annotation

 DOMAIN 15 92 Ubiquitin-like.
 CROSSLNK 11 11 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 92 92 Glycyl lysine isopeptide (Gly-Lys)  

Keyword

 3D-structure; Complete proteome; Cytoplasm; Isopeptide bond; Polymorphism; Reference proteome; Ubl conjugation; Ubl conjugation pathway. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 103 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0000776; C:kinetochore; TAS:ProtInc.
 GO:0005634; C:nucleus; IEA:InterPro.
 GO:0016925; P:protein sumoylation; IDA:UniProtKB. 

Interpro

 IPR022617; SUMO.
 IPR027218; SUMO_chordates.
 IPR000626; Ubiquitin.
 IPR019955; Ubiquitin_supergroup. 

Pfam

 PF11976; Rad60-SLD 

SMART

 SM00213; UBQ 

PROSITE

 PS50053; UBIQUITIN_2 

PRINTS