CPLM-009703

Genbank Nucleotide ID

Small ubiquitin-related modifier 1

Protein Synonyms/Alias

SUMO-1; SMT3 homolog 3; Ubiquitin-homology domain protein PIC1; Ubiquitin-like protein SMT3C; Smt3C

Mus musculus (Mouse)

Position	Peptide	Type	References
37	DSSEIHFKVKMTTHL	acetylation	[1]
37	DSSEIHFKVKMTTHL	ubiquitination	[2]

[1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]
[2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]

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 (By similarity).
MOD_RES 2 2 Phosphoserine.
MOD_RES 9 9 Phosphoserine (By similarity).
CROSSLNK 7 7 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 25 25 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 97 97 Glycyl lysine isopeptide (Gly-Lys)

Acetylation; Complete proteome; Cytoplasm; Isopeptide bond; Membrane; Nucleus; Phosphoprotein; Reference proteome; Stress response; 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:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO:0016605; C:PML body; ISS:UniProtKB.
GO:0045202; C:synapse; IEA:Compara.
GO:0019789; F:SUMO ligase activity; IDA:MGI.
GO:0031625; F:ubiquitin protein ligase binding; ISS:UniProtKB.
GO:0043392; P:negative regulation of DNA binding; IEA:Compara.
GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IEA:Compara.
GO:0045892; P:negative regulation of transcription, DNA-dependent; IEA:Compara.
GO:0060021; P:palate development; IMP:UniProtKB.
GO:0030578; P:PML body organization; IMP:MGI.
GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Compara.
GO:0031334; P:positive regulation of protein complex assembly; IEA:Compara.
GO:0090204; P:protein localization to nuclear pore; IMP:MGI.
GO:0016925; P:protein sumoylation; ISS:UniProtKB.
GO:0006355; P:regulation of transcription, DNA-dependent; IDA:MGI.
GO:0006950; P:response to stress; IEA:UniProtKB-KW.

IPR000626; Ubiquitin.
IPR019955; Ubiquitin_supergroup.

PS50053; UBIQUITIN_2