Reviewed,
UniProtKB/Swiss-Prot P61956 (SUMO2_HUMAN)
Last modified
November 25, 2008.
Version 62.
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 2 Short name=SUMO-2 Alternative name(s): Ubiquitin-like protein SMT3B SMT3 homolog 2 Sentrin-2 HSMT3 SUMO-3 | ||||
| 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 | 95 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 | Homotrimer Potential. Crystal packing analysis suggests a possible trimeric assembly, of which the biological significance remains to be determined. Interacts with SAE2 and UBE2I. Covalently attached to a number of proteins. Interacts with PELP1. |
| Subcellular location | Nucleus. Note= Nuclear bodies. |
| Tissue specificity | Broadly expressed. |
| Post-translational modification | Polymeric chains can be formed through Lys-11 cross-linking. Cleavage of precursor form by SENP1 or SENP2 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 | Nucleus |
| Coding sequence diversity | Polymorphism |
| PTM | Ubl conjugation |
| Technical term | 3D-structure |
Gene Ontology (GO) | |
| Biological process | protein modification process Inferred from electronic annotation. Source: InterPro ubiquitin-dependent protein catabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | nucleus Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | protein binding Inferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||
Molecule processing | |||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 93 | 93 | Small ubiquitin-related modifier 2 | PRO_0000035949 | |||||||||||||||||||
| Propeptide | 94 – 95 | 2 | PRO_0000035950 | ||||||||||||||||||||
Regions | |||||||||||||||||||||||
| Domain | 16 – 95 | 80 | Ubiquitin-like | ||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||
| Cross-link | 11 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | |||||||||||||||||||||
| Cross-link | 93 | Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) | |||||||||||||||||||||
Natural variations | |||||||||||||||||||||||
| Natural variant | 16 | 1 | D → N: dbSNP rs17850328. | VAR_047508 | |||||||||||||||||||
Experimental info | |||||||||||||||||||||||
| Mutagenesis | 11 | 1 | K → R: Abolishes the formation of poly(SUMO) chains | ||||||||||||||||||||
| Sequence conflict | 55 | 1 | M → V in AC005000. Ref.3 | ||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||
| Beta strand | 18 – 23 | 6 | |||||||||||||||||||||
| Beta strand | 27 – 34 | 8 | |||||||||||||||||||||
| Helix | 41 – 51 | 11 | |||||||||||||||||||||
| Turn | 55 – 57 | 3 | |||||||||||||||||||||
| Beta strand | 59 – 62 | 4 | |||||||||||||||||||||
| Turn | 73 – 77 | 5 | |||||||||||||||||||||
| Beta strand | 82 – 87 | 6 | |||||||||||||||||||||
Sequences
References
| « Hide 'large scale' references | |
| [1] | "Cloning and expression of human homolog HSMT3 to yeast SMT3 suppressor of MIF2 mutations in a centromere protein gene." Mannen H., Tseng H.M., Cho C.L., Li S.S.-L. Biochem. Biophys. Res. Commun. 222:178-180(1996) [PubMed: 8630065] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain. |
| [2] | "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]. Tissue: Brain. |
| [3] | "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. Nusbaum C.Nature 440:1045-1049(2006) [PubMed: 16625196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [4] | "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], VARIANT ASN-16. Tissue: Blood vessel, Bone, Bone marrow, Brain, Lung and Testis. |
| [5] | "Characterization of a second member of the sentrin family of ubiquitin-like proteins." Kamitani T., Kito K., Nguyen H.P., Fukuda-Kamitani T., Yeh E.T.H. J. Biol. Chem. 273:11349-11353(1998) [PubMed: 9556629] [Abstract] Cited for: FUNCTION, PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. |
| [6] | "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. |
| [7] | "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. |
| [8] | "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. |
| [9] | "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. |
| [10] | "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. |
| [11] | "NXP-2 association with SUMO-2 depends on lysines required for transcriptional repression." Rosendorff A., Sakakibara S., Lu S., Kieff E., Xuan Y., DiBacco A., Shi Y., Shi Y., Gill G. Proc. Natl. Acad. Sci. U.S.A. 103:5308-5313(2006) [PubMed: 16567619] [Abstract] Cited for: INTERACTION WITH PELP1. |
| [12] | "Crystal structures of the human SUMO-2 protein at 1.6 A and 1.2 A resolution: implication on the functional differences of SUMO proteins." Huang W.-C., Ko T.-P., Li S.S.-L., Wang A.H.-J. Eur. J. Biochem. 271:4114-4122(2004) [PubMed: 15479240] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 9-93, SUBUNIT. |
| [13] | "Solution structure of human SUMO-2 (SMT3B), a ubiquitin-like protein." RIKEN structural genomics initiative (RSGI) Submitted (AUG-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1-93. |
| [14] | "Crystal structure of SUMO-3-modified thymine-DNA glycosylase." Baba D., Maita N., Jee J.-G., Uchimura Y., Saitoh H., Sugasawa K., Hanaoka F., Tochio H., Hiroaki H., Shirakawa M. J. Mol. Biol. 359:137-147(2006) [PubMed: 16626738] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-93 CONJUGATED TO TDG. |
| [15] | "Solution structure of human small ubiquitin-like modifier protein isoform 2 (SUMO-2)." Chang C.K., Wang Y.H., Chung T.L., Chang C.F., Li S.S.L., Huang T.H. Submitted (OCT-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1-95. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| L76416 mRNA. Translation: AAD45399.1. X99585 mRNA. Translation: CAA67897.1. AC005000 Genomic DNA. No translation available. BC008450 mRNA. Translation: AAH08450.1. BC016775 mRNA. Translation: AAH16775.1. BC022340 mRNA. Translation: AAH22340.1. BC062713 mRNA. Translation: AAH62713.1. BC068465 mRNA. Translation: AAH68465.1. BC070159 mRNA. Translation: AAH70159.1. BC071645 mRNA. Translation: AAH71645.1. BC071646 mRNA. Translation: AAH71646.1. BC107853 mRNA. Translation: AAI07854.1. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PIR | JC4760. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| RefSeq | NP_001005849.1. NP_008868.3. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| UniGene | Hs.380973 Hs.546298 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| IntAct | P61956. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PTM databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PhosphoSite | P61956. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| GeneID | 6613. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| KEGG | hsa:6613. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| H-InvDB | HIX0014166. HIX0034144. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| HGNC | HGNC:11125. SUMO2. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| HPA | CAB012180. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| MIM | 603042. gene. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PharmGKB | PA134914683. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| GeneCards | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| HOGENOM | P61956. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| HOVERGEN | P61956. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| CleanEx | HS_SUMO2. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| GermOnline | ENSG00000188612. Homo sapiens. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| InterPro | IPR000626. Ubiquitin. [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 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| LinkHub | P61956. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| NextBio | 25747. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Entry information
| Entry name | SUMO2_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P61956 Secondary accession number(s): P55855 Q96HK1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 17 Human chromosome 17: 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


