CPLM-009702

Genbank Nucleotide ID

Small ubiquitin-related modifier 1

Protein Synonyms/Alias

SUMO-1; GAP-modifying protein 1; GMP1; SMT3 homolog 3; Sentrin; Ubiquitin-homology domain protein PIC1; Ubiquitin-like protein SMT3C; Smt3C; Ubiquitin-like protein UBL1

SMT3C; SMT3H3; UBL1; OK/SW-cl.43

Homo sapiens (Human)

Position	Peptide	Type	References
7	*MSDQEAKPSTEDLG	sumoylation	[1, 2, 3]
23	KKEGEYIKLKVIGQD	acetylation	[4]
25	EGEYIKLKVIGQDSS	sumoylation	[1]
25	EGEYIKLKVIGQDSS	ubiquitination	[5, 6, 7, 8, 9]
37	DSSEIHFKVKMTTHL	acetylation	[10]
37	DSSEIHFKVKMTTHL	ubiquitination	[5, 6, 7, 9]
39	SEIHFKVKMTTHLKK	acetylation	[10]
45	VKMTTHLKKLKESYC	acetylation	[10]
46	KMTTHLKKLKESYCQ	acetylation	[10]
48	TTHLKKLKESYCQRQ	acetylation	[10]
48	TTHLKKLKESYCQRQ	ubiquitination	[6]

[1] In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification.
Blomster HA, Imanishi SY, Siimes J, Kastu J, Morrice NA, Eriksson JE, Sistonen L.
J Biol Chem. 2010 Jun 18;285(25):19324-9. [PMID: 20388717]
[2] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634]
[3] 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]
[4] 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]
[5] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
[6] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[7] 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]
[8] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
[9] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[10] Functional mimicry of the acetylated C-terminal tail of p53 by a SUMO-1 acetylated domain, SAD.
Cheema A, Knights CD, Rao M, Catania J, Perez R, Simons B, Dakshanamurthy S, Kolukula VK, Tilli M, Furth PA, Albanese C, Avantaggiati ML.
J Cell Physiol. 2010 Nov;225(2):371-84. [PMID: 20458745]

Functional Description

Ubiquitin-like protein that can be covalently attached to proteins as a monomer or 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 E3 ligases 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. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development.

DOMAIN 20 97 Ubiquitin-like.
MOD_RES 2 2 N-acetylserine.
MOD_RES 2 2 Phosphoserine.
MOD_RES 9 9 Phosphoserine.
CROSSLNK 7 7 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 25 25 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 97 97 Glycyl lysine isopeptide (Gly-Lys)

3D-structure; Acetylation; Alternative splicing; Chromosomal rearrangement; Complete proteome; Cytoplasm; Isopeptide bond; Membrane; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation; Ubl conjugation pathway.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0030425; C:dendrite; IEA:Compara.
GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO:0005643; C:nuclear pore; TAS:ProtInc.
GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO:0016605; C:PML body; IDA:UniProtKB.
GO:0045202; C:synapse; IEA:Compara.
GO:0019789; F:SUMO ligase activity; IEA:Compara.
GO:0006281; P:DNA repair; TAS:ProtInc.
GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO:0043392; P:negative regulation of DNA binding; IMP:UniProtKB.
GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IMP:UniProtKB.
GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
GO:0060021; P:palate development; ISS:UniProtKB.
GO:0030578; P:PML body organization; IEA:Compara.
GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO:0031334; P:positive regulation of protein complex assembly; IDA:BHF-UCL.
GO:0090204; P:protein localization to nuclear pore; IEA:Compara.
GO:0016925; P:protein sumoylation; IDA:UniProtKB.
GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO:0032880; P:regulation of protein localization; TAS:UniProtKB.

IPR000626; Ubiquitin.
IPR019955; Ubiquitin_supergroup.

PS50053; UBIQUITIN_2