Q5I0H3 (SUMO1_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 53.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Small ubiquitin-related modifier 1 Short name=SUMO-1 | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 101 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| 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. 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 By similarity. |
| Subunit structure | Interacts with SAE2, UBE2I, RANBP2, PIAS1 and PIAS2. Covalently attached to a number of proteins such as IKFZ1, PML, RANGAP1, HIPK2, SP100, p53, p73-alpha, MDM2, JUN and DNMT3B. Also interacts with HIF1A, HIPK2, HIPK3, CHD3, PIAS1, EXOSC9, TDG, RAD51 and RAD52. Interacts with USP25 (via ts SIM domain); the interaction weakly sumoylates USP25 By similarity. Interacts with PARK2. Ref.2 |
| Subcellular location | Nucleus membrane By similarity. Nucleus speckle By similarity. Cytoplasm By similarity. Note: Recruited by BCL11A into the nuclear body By similarity. |
| Post-translational modification | Cleavage of precursor form by SENP1 or SENP2 is necessary for function By similarity. Polymeric SUMO1 chains undergo polyubiquitination by RNF4 By similarity. |
| Sequence similarities | Belongs to the ubiquitin family. SUMO subfamily. Contains 1 ubiquitin-like domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Ubl conjugation pathway |
| Cellular component | Cytoplasm Membrane Nucleus |
| PTM | Acetylation Isopeptide bond Phosphoprotein Ubl conjugation |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | palate development Inferred from sequence or structural similarity. Source: UniProtKB |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell dendriteInferred from direct assay. Source: RGD nuclear membraneInferred from electronic annotation. Source: UniProtKB-SubCell nuclear speckInferred from electronic annotation. Source: UniProtKB-SubCell synapseInferred from direct assay. Source: RGD |
| Molecular function | ubiquitin protein ligase binding Inferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 97 | 96 | Small ubiquitin-related modifier 1 | PRO_0000267610 | |||||
| Propeptide | 98 – 101 | 4 | By similarity | PRO_0000267611 | |||||
Regions | |||||||||
| Domain | 20 – 97 | 78 | Ubiquitin-like | ||||||
Sites | |||||||||
| Site | 36 | 1 | Interaction with PIAS2 By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylserine By similarity | ||||||
| Modified residue | 2 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 9 | 1 | Phosphoserine By similarity | ||||||
| Cross-link | 7 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity | |||||||
| Cross-link | 25 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity | |||||||
| Cross-link | 97 | Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) By similarity | |||||||
Sequences
References
| « Hide 'large scale' references | |
| [1] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver. |
| [2] | "Functional modulation of parkin through physical interaction with SUMO-1." Um J.W., Chung K.C. J. Neurosci. Res. 84:1543-1554(2006) [PubMed: 16955485] [Abstract] Cited for: INTERACTION WITH PARK2. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC088322 mRNA. Translation: AAH88322.1. |
| IPI | IPI00358028. |
| RefSeq | NP_001009672.1. NM_001009672.1. |
| UniGene | Rn.1221. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1A5R based on UniProtKB P63165. |
| ProteinModelPortal | Q5I0H3. |
| SMR | Q5I0H3. Positions 1-101. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-46501N. |
| MINT | MINT-4651872. |
| STRING | Q5I0H3. |
Proteomic databases | |
| PRIDE | Q5I0H3. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSRNOT00000022047; ENSRNOP00000022048; ENSRNOG00000016133. |
| GeneID | 301442. |
| KEGG | rno:301442. |
| UCSC | NM_001009672. rat. |
Organism-specific databases | |
| CTD | 7341. |
| RGD | 1306919. Sumo1. |
Phylogenomic databases | |
| eggNOG | maNOG20287. |
| GeneTree | ENSGT00390000018808. |
| HOVERGEN | HBG053025. |
| InParanoid | Q5I0H3. |
| OrthoDB | EOG42JNSX. |
| PhylomeDB | Q5I0H3. |
Gene expression databases | |
| ArrayExpress | Q5I0H3. |
| Genevestigator | Q5I0H3. |
| GermOnline | ENSRNOG00000016133. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR000626. Ubiquitin. IPR019955. Ubiquitin_supergroup. [Graphical view] |
| KO | K12160. |
| Pfam | PF00240. ubiquitin. 1 hit. [Graphical view] |
| SMART | SM00213. UBQ. 1 hit. [Graphical view] |
| PROSITE | PS50053. UBIQUITIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 648746. |
Entry information
| Entry name | SUMO1_RAT | ||||||||
| Accession | Primary (citable) accession number: Q5I0H3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with