Q8R5H1 (UBP15_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 98.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Ubiquitin carboxyl-terminal hydrolase 15 EC=3.4.19.12 Alternative name(s): Deubiquitinating enzyme 15 Ubiquitin thioesterase 15 Ubiquitin-specific-processing protease 15 | ||||
| Gene names |
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| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 981 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Hydrolase that removes conjugated ubiquitin from target proteins and regulates various pathways such as the TGF-beta receptor signaling and NF-kappa-B pathways. Acts as a key regulator of TGF-beta receptor signaling pathway, but the precise mechanism is still unclear: according to a report, acts by promoting deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or SMAD3), thereby alleviating inhibition of R-SMADs and promoting activation of TGF-beta target genes. According to another reports, regulates the TGF-beta receptor signaling pathway by mediating deubiquitination and stabilization of TGFBR1, leading to an enhanced TGF-beta signal. Able to mediate deubiquitination of monoubiquitinated substrates as well as 'Lys-48'-linked polyubiquitin chains, protecting them against proteasomal degradation. Acts as an associated component of COP9 signalosome complex (CSN) and regulates different pathways via this association: regulates NF-kappa-B by mediating deubiquitination of NFKBIA and deubiquitinates substrates bound to VCP By similarity. |
| Catalytic activity | Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). |
| Subunit structure | Identified in a complex with the COP9 signalosome complex (CSN). Interacts with SMAD1, SMAD2 and SMAD3; the interaction is direct. Forms a complex with SMURF2 and SMAD7. Interacts with TGFBR1 By similarity. |
| Subcellular location | |
| Tissue specificity | Widely expressed with highest levels in testis, heart and liver. Ref.1 |
| Post-translational modification | Phosphorylated. Phosphorylation protects against ubiquitination and subsequent degradation by the proteasome By similarity. Ubiquitinated, leading to degradation by the proteasome By similarity. |
| Sequence similarities | Belongs to the peptidase C19 family. Contains 1 DUSP domain. |
| Sequence caution | The sequence BAC65583.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence EDL24441.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. |
Ontologies
Alternative products
| This entry describes 5 isoforms produced by alternative splicing. [Align] [Select] Note: Experimental confirmation may be lacking for some isoforms. | ||||||
| Isoform 1 (identifier: Q8R5H1-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q8R5H1-2) The sequence of this isoform differs from the canonical sequence as follows: 18-25: TLLKTSLR → DAWLKPRSG 228-256: Missing. | ||||||
| Isoform 3 (identifier: Q8R5H1-3) The sequence of this isoform differs from the canonical sequence as follows: 229-981: Missing. | ||||||
| Isoform 4 (identifier: Q8R5H1-4) The sequence of this isoform differs from the canonical sequence as follows: 209-227: LVIEQKNEDGTWPRGPSTP → PRCIQFFNFTKDLSFISIK 228-981: Missing. | ||||||
| Isoform 5 (identifier: Q8R5H1-5) The sequence of this isoform differs from the canonical sequence as follows: 228-256: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 981 | 980 | Ubiquitin carboxyl-terminal hydrolase 15 | PRO_0000080642 | |||||
Regions | |||||||||
| Domain | 7 – 118 | 112 | DUSP | ||||||
Sites | |||||||||
| Active site | 298 | 1 | Nucleophile By similarity UniProtKB Q9Y4E8 | ||||||
| Active site | 891 | 1 | Proton acceptor By similarity UniProtKB Q9Y4E8 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||
| Modified residue | 229 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 242 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 961 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 965 | 1 | Phosphoserine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 18 – 25 | 8 | TLLKTSLR → DAWLKPRSG in isoform 2. Ref.1 | VSP_005262 | |||||
| Alternative sequence | 209 – 227 | 19 | LVIEQ…GPSTP → PRCIQFFNFTKDLSFISIK in isoform 4. | VSP_005265 | |||||
| Alternative sequence | 228 – 981 | 754 | Missing in isoform 4. | VSP_005266 | |||||
| Alternative sequence | 228 – 256 | 29 | Missing in isoform 2 and isoform 5. Ref.1 | VSP_005263 | |||||
| Alternative sequence | 229 – 981 | 753 | Missing in isoform 3. | VSP_005264 | |||||
Experimental info | |||||||||
| Sequence conflict | 130 | 1 | E → G in BAE40593. Ref.3 | ||||||
| Sequence conflict | 158 | 1 | I → M in BAE36413. Ref.3 | ||||||
| Sequence conflict | 184 | 1 | M → V in AAH50042. Ref.5 | ||||||
| Sequence conflict | 662 | 1 | D → G in AAH50042. Ref.5 | ||||||
| Sequence conflict | 800 | 1 | K → E in AAH50042. Ref.5 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Isolation and characterization of the mouse ubiquitin-specific protease Usp15." Angelats C., Wang X.-W., Jermiin L.S., Copeland N.G., Jenkins N.A., Baker R.T. Mamm. Genome 14:31-46(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY. Strain: C57BL/6. |
| [2] | "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H. DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). Tissue: Brain. |
| [3] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 5). Strain: C57BL/6J. Tissue: Amnion, Corpora quadrigemina, Testis and Thymus. |
| [4] | Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Trophoblast stem cell. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF468037 mRNA. Translation: AAL77418.1. AK046332 mRNA. Translation: BAC32683.1. AK083303 mRNA. Translation: BAC38854.1. AK133852 mRNA. Translation: BAE21887.1. AK145749 mRNA. Translation: BAE26626.1. AK161469 mRNA. Translation: BAE36413.1. AK168755 mRNA. Translation: BAE40593.1. AK122301 mRNA. Translation: BAC65583.1. Different initiation. CH466578 Genomic DNA. Translation: EDL24441.1. Different initiation. BC050042 mRNA. Translation: AAH50042.1. |
| IPI | IPI00154012. IPI00222152. IPI00222154. IPI00403342. |
| RefSeq | NP_081880.2. NM_027604.3. |
| UniGene | Mm.244209. Mm.470032. |
3D structure databases | |
| ProteinModelPortal | Q8R5H1. |
| SMR | Q8R5H1. Positions 2-222, 285-470, 786-934. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | C19.022. |
PTM databases | |
| PhosphoSite | Q8R5H1. |
Proteomic databases | |
| PaxDb | Q8R5H1. |
| PRIDE | Q8R5H1. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000020334; ENSMUSP00000020334; ENSMUSG00000020124. |
| GeneID | 14479. |
| KEGG | mmu:14479. |
| UCSC | uc007hgn.1. mouse. uc007hgt.1. mouse. uc011xpf.1. mouse. |
Organism-specific databases | |
| CTD | 9958. |
| MGI | MGI:101857. Usp15. |
| Rouge | Search... |
Phylogenomic databases | |
| eggNOG | COG5560. |
| GeneTree | ENSGT00670000097750. |
| HOGENOM | HOG000264375. |
| HOVERGEN | HBG000864. |
| InParanoid | Q8R5H1. |
| KO | K11835. |
| OMA | RMDPLAK. |
| OrthoDB | EOG4DNF3R. |
Gene expression databases | |
| ArrayExpress | Q8R5H1. |
| Bgee | Q8R5H1. |
| CleanEx | MM_USP15. |
| Genevestigator | Q8R5H1. |
| GermOnline | ENSMUSG00000020124. Mus musculus. |
Family and domain databases | |
| InterPro | IPR006615. Pept_C19_DUSP. IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b. [Graphical view] |
| Pfam | PF06337. DUSP. 1 hit. PF00443. UCH. 1 hit. [Graphical view] |
| SMART | SM00695. DUSP. 1 hit. [Graphical view] |
| SUPFAM | SSF55205. RNA3'_cycl/enolpyr_transf_A/B. 1 hit. |
| 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 | |
| ChiTaRS | USP15. mouse. |
| NextBio | 286150. |
| SOURCE | Search... |
Entry information
| Entry name | UBP15_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q8R5H1 Secondary accession number(s): Q3TGF5 Q80UK9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
