G2XKQ0 · SUMO5_HUMAN
- ProteinSmall ubiquitin-related modifier 5
- GeneSUMO1P1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids101 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Regulates the life cycle of promyelocytic leukemia nuclear bodies (PML-NBs). PolySUMO1P1/SUMO5 conjugation on 'Lys-160' of PML facilitates recruitment of PML-NB components, which enlarges PML-NB. SUMO1P1/SUMO5 also increases polySUMO2/3 conjugation of PML, resulting in RNF4-mediated disruption of PML-NBs.
Miscellaneous
Highly conserved among primate species, however is not detected in mice.
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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Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | identical protein binding | |
Molecular Function | protein tag activity | |
Molecular Function | transcription factor binding | |
Molecular Function | ubiquitin-like protein ligase binding | |
Biological Process | PML body organization | |
Biological Process | protein sumoylation |
Keywords
- Biological process
Enzyme and pathway databases
The subsequence KDEDIKLRVIGQDSSEIHFKVKMTTPLKKLKKSYCQRQGVPVNSLRFLFEGQRIADNHTPEELGMEEEDVIEVYQEQIGG, 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 5
- Short namesSUMO-5
- Alternative names
Gene names
- Community suggested namesSUMO1P1
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionG2XKQ0
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Forms prominent non-membrane-bound structures in the nucleus.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 12 | Does not affect nuclear bodies formation. | ||||
Sequence: H → D | ||||||
Mutagenesis | 17-21 | Unable to form nuclear bodies. | ||||
Sequence: IKDED → KEGEY | ||||||
Mutagenesis | 18 | Unable to form nuclear bodies. | ||||
Sequence: K → R | ||||||
Mutagenesis | 95 | Does not affect nuclear bodies formatiom. | ||||
Sequence: I → T | ||||||
Mutagenesis | 96-97 | Lost the ability to conjugate UBE2I. Unable to form nuclear bodies. | ||||
Sequence: GG → AA |
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, cross-link, modified residue (large scale data), propeptide.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000445393 | 1-101 | UniProt | Small ubiquitin-related modifier 5 | |||
Sequence: MSDLEAKPSTEHLGDKIKDEDIKLRVIGQDSSEIHFKVKMTTPLKKLKKSYCQRQGVPVNSLRFLFEGQRIADNHTPEELGMEEEDVIEVYQEQIGGHSTV | |||||||
Cross-link | 18 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1P1/SUMO5) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 31 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 32 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 97 | UniProt | Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) | ||||
Sequence: G | |||||||
Propeptide | PRO_0000445394 | 98-101 | UniProt | ||||
Sequence: HSTV |
Post-translational modification
Cleavage of precursor form is necessary for function.
Autosumoylated at Lys-18.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with CBX4 (PubMed:27211601).
Interacts with PIAS1 (PubMed:27211601).
Found in a complex with SAE2 (PubMed:27211601).
Interacts with UBE2I (PubMed:27211601).
Interacts with SP100 (PubMed:27211601).
Interacts with HIPK2 (PubMed:27211601).
Interacts with DAXX (PubMed:27211601).
Interacts with PML-RARA oncoprotein; PML-RARalpha outcompetes PML for SUMO1P1/SUMO5 conjugation (PubMed:27211601).
Interacts with PIAS1 (PubMed:27211601).
Found in a complex with SAE2 (PubMed:27211601).
Interacts with UBE2I (PubMed:27211601).
Interacts with SP100 (PubMed:27211601).
Interacts with HIPK2 (PubMed:27211601).
Interacts with DAXX (PubMed:27211601).
Interacts with PML-RARA oncoprotein; PML-RARalpha outcompetes PML for SUMO1P1/SUMO5 conjugation (PubMed:27211601).
Binary interactions
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for motif, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 17-21 | Required for PML-NB formation | ||||
Sequence: IKDED | ||||||
Domain | 20-97 | Ubiquitin-like | ||||
Sequence: EDIKLRVIGQDSSEIHFKVKMTTPLKKLKKSYCQRQGVPVNSLRFLFEGQRIADNHTPEELGMEEEDVIEVYQEQIGG |
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)11,526
- Last updated2018-10-10 v2
- Checksum01289B0B66A680FA
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 8 | in Ref. 1; ACM86836 | ||||
Sequence: P → L |
Keywords
- Technical term