Reviewed,
UniProtKB/Swiss-Prot P55854 (SUMO3_HUMAN)
Last modified
June 16, 2009.
Version 80.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Small ubiquitin-related modifier 3 Short name=SUMO-3 Alternative name(s): Ubiquitin-like protein SMT3A SMT3 homolog 1 SUMO-2 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 103 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 which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. |
| Subunit structure | Interacts with SAE2 and UBE2I. Covalently attached to a number of proteins By similarity. |
| Subcellular location | |
| Tissue specificity | Expressed predominantly in liver. Ref.11 |
| Post-translational modification | Polymeric chains can be formed through Lys-11 cross-linking. Cleavage of precursor form by SENP1, SENP2 or SENP5 is necessary for function. |
| Sequence similarities | Belongs to the ubiquitin family. SUMO subfamily. Contains 1 ubiquitin-like domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Ubl conjugation pathway |
| Cellular component | Cytoplasm |
| Coding sequence diversity | Polymorphism |
| PTM | Isopeptide bond Ubl conjugation |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological process | modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell kinetochore Ref.1Traceable author statement. Source: ProtInc |
| Molecular function | protein binding Inferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| SAE1 | Q9UBE0 | 1 | EBI-474067,EBI-743154 | |
| SP100 | P23497 | 1 | EBI-474067,EBI-751145 | |
| UBE2I | P63279 | 1 | EBI-474067,EBI-80168 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 92 | 92 | Small ubiquitin-related modifier 3 | PRO_0000035957 | ||||||||||||||||||||
| Propeptide | 93 – 103 | 11 | PRO_0000035958 | |||||||||||||||||||||
Regions | ||||||||||||||||||||||||
| Domain | 15 – 92 | 78 | Ubiquitin-like | |||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||
| Cross-link | 11 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.7 | ||||||||||||||||||||||
| Cross-link | 92 | Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) | ||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||
| Natural variant | 38 | 1 | P → S: dbSNP rs1051311. Ref.1 | VAR_052692 | ||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||
| Mutagenesis | 11 | 1 | K → R: Abolishes the formation of poly(SUMO) chains. Ref.7 | |||||||||||||||||||||
| Sequence conflict | 32 | 1 | K → E in BAD96311. Ref.4 | |||||||||||||||||||||
| Sequence conflict | 76 | 1 | E → R in CAA67896. Ref.1 | |||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||
| Beta strand | 16 – 22 | 7 | ||||||||||||||||||||||
| Beta strand | 28 – 34 | 7 | ||||||||||||||||||||||
| Helix | 40 – 50 | 11 | ||||||||||||||||||||||
| Helix | 54 – 56 | 3 | ||||||||||||||||||||||
| Beta strand | 57 – 61 | 5 | ||||||||||||||||||||||
| Turn | 72 – 76 | 5 | ||||||||||||||||||||||
| Beta strand | 82 – 87 | 6 | ||||||||||||||||||||||
| Beta strand | 90 – 92 | 3 | ||||||||||||||||||||||
Sequences
References
| « Hide 'large scale' references | |
| [1] | "SMT3A, a human homologue of the S. cerevisiae SMT3 gene, maps to chromosome 21qter and defines a novel gene family." Lapenta V., Chiurazzi P., van der Spek P.J., Pizzuti A., Hanaoka F., Brahe C. Genomics 40:362-367(1997) [PubMed: 9119407] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-38. Tissue: Brain. |
| [2] | "Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [3] | "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [4] | Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Coronary artery. |
| [5] | "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: Bone marrow and Kidney. |
| [6] | "Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3." Saitoh H., Hinchey J. J. Biol. Chem. 275:6252-6258(2000) [PubMed: 10692421] [Abstract] Cited for: IDENTIFICATION. |
| [7] | "Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9." Tatham M.H., Jaffray E., Vaughan O.A., Desterro J.M.P., Botting C.H., Naismith J.H., Hay R.T. J. Biol. Chem. 276:35368-35374(2001) [PubMed: 11451954] [Abstract] Cited for: SUMOYLATION AT LYS-11, MUTAGENESIS OF LYS-11. |
| [8] | "Molecular features of human ubiquitin-like SUMO genes and their encoded proteins." Su H.-L., Li S.S.-L. Gene 296:65-73(2002) [PubMed: 12383504] [Abstract] Cited for: SUBCELLULAR LOCATION. |
| [9] | "Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation." Tatham M.H., Kim S., Yu B., Jaffray E., Song J., Zheng J., Rodriguez M.S., Hay R.T., Chen Y. Biochemistry 42:9959-9969(2003) [PubMed: 12924945] [Abstract] Cited for: INTERACTION WITH UBE2I. |
| [10] | "A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex." Reverter D., Lima C.D. Structure 12:1519-1531(2004) [PubMed: 15296745] [Abstract] Cited for: CLEAVAGE. |
| [11] | "Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1." Xu Z., Au S.W.N. Biochem. J. 386:325-330(2005) [PubMed: 15487983] [Abstract] Cited for: CLEAVAGE, TISSUE SPECIFICITY. |
| [12] | "Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3." Gong L., Yeh E.T.H. J. Biol. Chem. 281:15869-15877(2006) [PubMed: 16608850] [Abstract] Cited for: CLEAVAGE. |
| [13] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [14] | "Solution structure of human SUMO-3 C47S and its binding surface for Ubc9." Ding H., Xu Y., Chen Q., Dai H., Tang Y., Wu J., Shi Y. Biochemistry 44:2790-2799(2005) [PubMed: 15723523] [Abstract] Cited for: STRUCTURE BY NMR OF 14-92. |
| [15] | "The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing." Shen L.N., Dong C., Liu H., Naismith J.H., Hay R.T. Biochem. J. 397:279-288(2006) [PubMed: 16553580] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH SENP1, CLEAVAGE. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| X99584 mRNA. Translation: CAA67896.1. BT007008 mRNA. Translation: AAP35654.1. CR542173 mRNA. Translation: CAG46970.1. CR542188 mRNA. Translation: CAG46985.1. AK222591 mRNA. Translation: BAD96311.1. BC000036 mRNA. Translation: AAH00036.1. BC008420 mRNA. Translation: AAH08420.1. | |||||||||||||||||||
| IPI | IPI00299147. | ||||||||||||||||||
| RefSeq | NP_008867.2. | ||||||||||||||||||
| UniGene | Hs.474005 | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| |||||||||||||||||||
| SMR | P55854. Positions 1-93. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| IntAct | P55854. 33 interactions. | ||||||||||||||||||
PTM databases | |||||||||||||||||||
| PhosphoSite | P55854. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PRIDE | P55854. | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENSG00000184900. Homo sapiens. [Contig view] | ||||||||||||||||||
| GeneID | 6612. | ||||||||||||||||||
| KEGG | hsa:6612. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| GeneCards | GC21M045049. | ||||||||||||||||||
| H-InvDB | HIX0016173. | ||||||||||||||||||
| HGNC | HGNC:11124. SUMO3. | ||||||||||||||||||
| MIM | 602231. gene. | ||||||||||||||||||
| PharmGKB | PA35973. | ||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| HOGENOM | P55854. | ||||||||||||||||||
| HOVERGEN | P55854. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| ArrayExpress | P55854. | ||||||||||||||||||
| Bgee | P55854. | ||||||||||||||||||
| CleanEx | HS_SUMO3. | ||||||||||||||||||
| GermOnline | ENSG00000184900. Homo sapiens. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR000626. Ubiquitin. IPR019955. Ubiquitin_supergroup. [Graphical view] | ||||||||||||||||||
| 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 Resources | |||||||||||||||||||
| NextBio | 25743. | ||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||
Entry information
| Entry name | SUMO3_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P55854 Secondary accession number(s): Q53HI9, Q6FGD4, Q9BWR4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 21 Human chromosome 21: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


