Q2EF74 · SUMO1_ICTTR
- ProteinSmall ubiquitin-related modifier 1
- GeneSUMO1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids101 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
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. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins (By similarity).
May be involved in modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3
May be involved in modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3
Miscellaneous
Massive conjugation to proteins occurs in brain, kidney and liver during hibernation torpor.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 36 | Interaction with PIAS2 | ||||
Sequence: F |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nuclear membrane | |
Cellular Component | nuclear speck | |
Cellular Component | nuclear stress granule | |
Cellular Component | plasma membrane | |
Cellular Component | PML body | |
Molecular Function | potassium channel regulator activity | |
Molecular Function | protein tag activity | |
Molecular Function | transcription factor binding | |
Molecular Function | ubiquitin protein ligase binding | |
Biological Process | cellular response to cadmium ion | |
Biological Process | cellular response to heat | |
Biological Process | negative regulation of action potential | |
Biological Process | negative regulation of delayed rectifier potassium channel activity | |
Biological Process | protein sumoylation | |
Biological Process | roof of mouth development |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameSmall ubiquitin-related modifier 1
- Short namesSUMO-1
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Sciuromorpha > Sciuridae > Xerinae > Marmotini > Ictidomys
Accessions
- Primary accessionQ2EF74
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Recruited by BCL11A into the nuclear body (By similarity).
In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body (By similarity).
In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body (By similarity).
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Modified residue | 2 | Phosphoserine | ||||
Sequence: S | ||||||
Chain | PRO_0000250517 | 2-97 | Small ubiquitin-related modifier 1 | |||
Sequence: SDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGG | ||||||
Cross-link | 7 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | ||||||
Cross-link | 7 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Modified residue | 9 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 16 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 17 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 23 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 25 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) | ||||
Sequence: K | ||||||
Modified residue | 32 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 37 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 39 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 45 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 46 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 97 | Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) | ||||
Sequence: G | ||||||
Propeptide | PRO_0000250518 | 98-101 | ||||
Sequence: HSNV |
Post-translational modification
Cleavage of precursor form by SENP1 or SENP2 is necessary for function.
Polymeric SUMO1 chains undergo polyubiquitination by RNF4.
Keywords
- PTM
Interaction
Subunit
Covalently attached to KCNB1; UBE2I increases cross-linking with KCNB1 and PIAS1 decreases cross-links with KCNB1 (By similarity).
Interacts with SAE2, RANBP2, PIAS1 and PIAS2 (By similarity).
Interacts with PRKN (By similarity).
Covalently attached to a number of proteins such as IKFZ1, PML, RANGAP1, HIPK2, SP100, p53, p73-alpha, MDM2, JUN, DNMT3B and TDG (By similarity).
Also interacts with HIF1A, HIPK2, HIPK3, CHD3, EXOSC9, RAD51 and RAD52 (By similarity).
Interacts with USP25 (via ts SIM domain); the interaction weakly sumoylates USP25 (By similarity).
Interacts with SIMC1, CASP8AP2, RNF111 and SOBP (via SIM domains) (By similarity).
Interacts with BHLHE40/DEC1 (By similarity).
Interacts with RWDD3 (By similarity).
Interacts with UBE2I/UBC9 and this interaction is enhanced in the presence of RWDD3 (By similarity).
Interacts with MTA1 (By similarity).
Interacts with SENP2 (By similarity).
Interacts with HINT1 (By similarity).
Interacts with SAE2, RANBP2, PIAS1 and PIAS2 (By similarity).
Interacts with PRKN (By similarity).
Covalently attached to a number of proteins such as IKFZ1, PML, RANGAP1, HIPK2, SP100, p53, p73-alpha, MDM2, JUN, DNMT3B and TDG (By similarity).
Also interacts with HIF1A, HIPK2, HIPK3, CHD3, EXOSC9, RAD51 and RAD52 (By similarity).
Interacts with USP25 (via ts SIM domain); the interaction weakly sumoylates USP25 (By similarity).
Interacts with SIMC1, CASP8AP2, RNF111 and SOBP (via SIM domains) (By similarity).
Interacts with BHLHE40/DEC1 (By similarity).
Interacts with RWDD3 (By similarity).
Interacts with UBE2I/UBC9 and this interaction is enhanced in the presence of RWDD3 (By similarity).
Interacts with MTA1 (By similarity).
Interacts with SENP2 (By similarity).
Interacts with HINT1 (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 20-97 | Ubiquitin-like | ||||
Sequence: EYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGG |
Sequence similarities
Belongs to the ubiquitin family. SUMO subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length101
- Mass (Da)11,570
- Last updated2006-03-21 v1
- Checksum89AB77D2D054FB33
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DQ385870 EMBL· GenBank· DDBJ | ABD39322.1 EMBL· GenBank· DDBJ | mRNA |