P63165 · SUMO1_HUMAN
- ProteinSmall ubiquitin-related modifier 1
- GeneSUMO1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids101 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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. Covalently attached to ZFHX3 (PubMed:24651376).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 36 | Interaction with PIAS2 | ||||
Sequence: F |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
The subsequence EGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGG, which contains the Rad60-SLD domain, shows transcriptional repressor activity in a high-throughput recruitment assay.
Names & Taxonomy
Protein names
- Recommended nameSmall ubiquitin-related modifier 1
- Short namesSUMO-1
- Alternative names
Gene names
- Community suggested namesSUMO1
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP63165
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
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 (PubMed:24651376).
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Non-syndromic orofacial cleft 10 (OFC10)
- Note
- DescriptionA birth defect consisting of cleft lips with or without cleft palate. Cleft lips are associated with cleft palate in two-third of cases. A cleft lip can occur on one or both sides and range in severity from a simple notch in the upper lip to a complete opening in the lip extending into the floor of the nostril and involving the upper gum.
- See alsoMIM:613705
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 36 | Abolishes binding to PIAS2. | ||||
Sequence: F → A | ||||||
Mutagenesis | 97 | Abolishes sumoylation of ZBED1. | ||||
Sequence: G → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 68 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, modified residue (large scale data), chain, cross-link, propeptide.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylserine | ||||
Sequence: S | |||||||
Modified residue | 2 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Chain | PRO_0000035939 | 2-97 | UniProt | Small ubiquitin-related modifier 1 | |||
Sequence: SDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGG | |||||||
Cross-link | 7 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | |||||||
Cross-link | 7 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 9 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 9 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 10 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 16 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 17 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 23 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 25 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 31 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 32 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 32 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 37 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 39 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 45 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 46 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 97 | UniProt | Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) | ||||
Sequence: G | |||||||
Propeptide | PRO_0000035940 | 98-101 | UniProt | ||||
Sequence: HSTV |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with SAE2, RANBP2, PIAS1 and PIAS2 (PubMed:10961991, PubMed:15608651, PubMed:15660128, PubMed:15931224, PubMed:16204249).
Interacts with PRKN (PubMed:16955485).
Covalently attached to a number of proteins such as IKFZ1, PML, RANGAP1, HIPK2, SP100, p53, p73-alpha, MDM2, JUN, DNMT3B and TDG (PubMed:10961991, PubMed:15931224, PubMed:15959518, PubMed:17099698).
Also interacts with HIF1A, HIPK2, HIPK3, CHD3, EXOSC9, RAD51 and RAD52 (PubMed:10961991, PubMed:12565818).
Interacts with USP25 (via ts SIM domain); the interaction weakly sumoylates USP25 (PubMed:18538659).
Interacts with SIMC1, CASP8AP2, RNF111 and SOBP (via SIM domains) (PubMed:23086935).
Interacts with BHLHE40/DEC1 (PubMed:21829689).
Interacts with RWDD3 (PubMed:17956732).
Interacts with UBE2I/UBC9 and this interaction is enhanced in the presence of RWDD3 (PubMed:12924945, PubMed:17956732).
Interacts with MTA1 (PubMed:21965678).
Interacts with SENP2 (PubMed:15296745).
Interacts with HINT1 (By similarity).
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 16-25 | (Microbial infection) Interaction with Tula hantavirus | ||||
Sequence: KKEGEYIKLK | ||||||
Domain | 20-97 | Ubiquitin-like | ||||
Sequence: EYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGG | ||||||
Region | 37-40 | (Microbial infection) Interaction with Tula hantavirus | ||||
Sequence: KVKM |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
P63165-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length101
- Mass (Da)11,557
- Last updated2004-09-27 v1
- Checksum89BE97D2D054FB33
P63165-2
- Name2
- Differences from canonical
- 4-28: Missing
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_046756 | 4-28 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 75 | in Ref. 13; AAH66306 | ||||
Sequence: H → N |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X99586 EMBL· GenBank· DDBJ | CAA67898.1 EMBL· GenBank· DDBJ | mRNA | ||
U61397 EMBL· GenBank· DDBJ | AAB40388.1 EMBL· GenBank· DDBJ | mRNA | ||
U38784 EMBL· GenBank· DDBJ | AAC50733.1 EMBL· GenBank· DDBJ | mRNA | ||
U67122 EMBL· GenBank· DDBJ | AAC50996.1 EMBL· GenBank· DDBJ | mRNA | ||
U72722 EMBL· GenBank· DDBJ | AAB40390.1 EMBL· GenBank· DDBJ | mRNA | ||
U83117 EMBL· GenBank· DDBJ | AAB39999.1 EMBL· GenBank· DDBJ | mRNA | ||
AB062294 EMBL· GenBank· DDBJ | BAB93477.1 EMBL· GenBank· DDBJ | mRNA | ||
BT006632 EMBL· GenBank· DDBJ | AAP35278.1 EMBL· GenBank· DDBJ | mRNA | ||
CR542147 EMBL· GenBank· DDBJ | CAG46944.1 EMBL· GenBank· DDBJ | mRNA | ||
CR542156 EMBL· GenBank· DDBJ | CAG46953.1 EMBL· GenBank· DDBJ | mRNA | ||
AK311840 EMBL· GenBank· DDBJ | BAG34782.1 EMBL· GenBank· DDBJ | mRNA | ||
AC079354 EMBL· GenBank· DDBJ | AAY24035.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471063 EMBL· GenBank· DDBJ | EAW70304.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471063 EMBL· GenBank· DDBJ | EAW70307.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC006462 EMBL· GenBank· DDBJ | AAH06462.1 EMBL· GenBank· DDBJ | mRNA | ||
BC053528 EMBL· GenBank· DDBJ | AAH53528.1 EMBL· GenBank· DDBJ | mRNA | ||
BC066306 EMBL· GenBank· DDBJ | AAH66306.1 EMBL· GenBank· DDBJ | mRNA |