Reviewed,
UniProtKB/Swiss-Prot P51784 (UBP11_HUMAN)
Last modified
June 16, 2009.
Version 88.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Ubiquitin carboxyl-terminal hydrolase 11 EC=3.1.2.15 Alternative name(s): Ubiquitin thioesterase 11 Ubiquitin-specific-processing protease 11 Deubiquitinating enzyme 11 | ||||
| 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 | 920 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | Ubiquitin C-terminal thioester + H2O = ubiquitin + a thiol. Ref.1 |
| Subunit structure | Interacts with RANBP9/RANBPM. Ref.1 |
| Subcellular location | |
| Sequence similarities | Belongs to the peptidase C19 family. Contains 1 DUSP domain. |
| Sequence caution | The sequence AAC50450.1 differs from that shown. Reason: Frameshift at positions 22, 74, 91 and 103. The sequence CAD20056.1 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Ubl conjugation pathway |
| Cellular component | Nucleus |
| Molecular function | Hydrolase Protease Thiol protease |
| PTM | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | cysteine-type endopeptidase activity Traceable author statement. Source: ProtInc protein bindingInferred from physical interaction. Source: IntAct ubiquitin thiolesterase activityInferred from electronic annotation. Source: EC ubiquitin-specific protease activity Ref.4Traceable author statement. Source: ProtInc |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| E7 | P03129 | 5 | EBI-306876,EBI-866453 | From a different organism. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 920 | 920 | Ubiquitin carboxyl-terminal hydrolase 11 | PRO_0000080632 | |||||
Regions | |||||||||
| Domain | 33 – 141 | 109 | DUSP | ||||||
Sites | |||||||||
| Active site | 275 | 1 | By similarity | ||||||
| Active site | 837 | 1 | By similarity | ||||||
| Active site | 845 | 1 | By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 905 | 1 | Phosphoserine Ref.5 | ||||||
| Modified residue | 910 | 1 | Phosphoserine Ref.5 | ||||||
Experimental info | |||||||||
| Sequence conflict | 9 | 1 | A → AT in BAC20463. Ref.1 | ||||||
| Sequence conflict | 15 | 1 | V → M Ref.4 | ||||||
| Sequence conflict | 19 | 1 | A → R Ref.4 | ||||||
| Sequence conflict | 39 – 40 | 2 | WR → CG Ref.4 | ||||||
| Sequence conflict | 117 | 1 | A → R Ref.1 | ||||||
| Sequence conflict | 118 | 1 | A → R Ref.1 | ||||||
| Sequence conflict | 118 | 1 | A → R Ref.4 | ||||||
| Sequence conflict | 446 | 1 | P → L in AAH00350. Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Structural and functional characterization of the USP11 deubiquitinating enzyme, which interacts with the RanGTP-associated protein RanBPM." Ideguchi H., Ueda A., Tanaka M., Yang J., Tsuji T., Ohno S., Hagiwara E., Aoki A., Ishigatsubo Y. Biochem. J. 367:87-95(2002) [PubMed: 12084015] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH RANBP9. Tissue: Fetal brain. |
| [2] | "The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. Bentley D.R.Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [3] | "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: Muscle. |
| [4] | "A ubiquitin C-terminal hydrolase gene on the proximal short arm of the X chromosome: implications for X-linked retinal disorders." Swanson D.A., Freund C.L., Ploder L., McInnes R.R., Valle D. Hum. Mol. Genet. 5:533-538(1996) [PubMed: 8845848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-920. Tissue: Retina. |
| [5] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-905 AND SER-910, MASS SPECTROMETRY. |
| [6] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AB073597 mRNA. Translation: BAC20463.1. AL096791 Genomic DNA. Translation: CAD20056.1. Sequence problems. BC000350 mRNA. Translation: AAH00350.4. Different initiation. U44839 mRNA. Translation: AAC50450.1. Frameshift. | |
| IPI | IPI00184533. |
| UniGene | Hs.171501 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1NB8 based on UniProtKB Q93009. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP:27567N. |
| IntAct | P51784. 5 interactions. |
Protein family/group databases | |
| MEROPS | C19.014. |
PTM databases | |
| PhosphoSite | P51784. |
Proteomic databases | |
| PRIDE | P51784. |
Genome annotation databases | |
| Ensembl | ENSG00000102226. Homo sapiens. [Contig view] |
Organism-specific databases | |
| GeneCards | GC0XP046977. |
| H-InvDB | HIX0016760. |
| HGNC | HGNC:12609. USP11. |
| MIM | 300050. gene. |
| PharmGKB | PA27521. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOVERGEN | P51784. |
Enzyme and pathway databases | |
| BRENDA | 3.1.2.15. 247. |
Gene expression databases | |
| ArrayExpress | P51784. |
| Bgee | P51784. |
| CleanEx | HS_USP11. |
| GermOnline | ENSG00000102226. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR006615. Pept_C19_DUSP. IPR010460. Pept_C19_N_2. IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. [Graphical view] |
| Pfam | PF06337. DUF1055. 1 hit. PF00443. UCH. 1 hit. [Graphical view] |
| SMART | SM00695. DUSP. 1 hit. [Graphical view] |
| PROSITE | PS51283. DUSP. 1 hit. PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| SOURCE | Search... |
Entry information
| Entry name | UBP11_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P51784 Secondary accession number(s): Q8IUG6, Q9BWE1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome X Human chromosome X: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


