USP13

Protein-coding gene in the species Homo sapiens
USP13
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2L80, 2LBC

Identifiers
AliasesUSP13, ISOT3, IsoT-3, ubiquitin specific peptidase 13 (isopeptidase T-3), ubiquitin specific peptidase 13
External IDsOMIM: 603591; MGI: 1919857; HomoloGene: 68372; GeneCards: USP13; OMA:USP13 - orthologs
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for USP13
Genomic location for USP13
Band3q26.33Start179,653,032 bp[1]
End179,804,366 bp[1]
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)[2]
Chromosome 3 (mouse)
Genomic location for USP13
Genomic location for USP13
Band3|3 A3Start32,871,695 bp[2]
End32,992,220 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Skeletal muscle tissue of biceps brachii

  • glutes

  • thoracic diaphragm

  • deltoid muscle

  • vastus lateralis muscle

  • tibialis anterior muscle

  • triceps brachii muscle

  • Skeletal muscle tissue of rectus abdominis

  • right ventricle

  • myocardium of left ventricle
Top expressed in
  • interventricular septum

  • muscle of thigh

  • triceps brachii muscle

  • temporal muscle

  • sternocleidomastoid muscle

  • digastric muscle

  • soleus muscle

  • myocardium of ventricle

  • gastrocnemius muscle

  • skeletal muscle tissue
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • cysteine-type peptidase activity
  • chaperone binding
  • zinc ion binding
  • BAT3 complex binding
  • metal ion binding
  • ubiquitin-like protein-specific protease activity
  • proteasome binding
  • peptidase activity
  • ubiquitin binding
  • protein binding
  • ubiquitin-like protein ligase binding
  • hydrolase activity
  • ubiquitin protein ligase binding
  • thiol-dependent deubiquitinase
  • cysteine-type endopeptidase activity
Cellular component
  • nucleoplasm
  • cytosol
Biological process
  • regulation of transcription, DNA-templated
  • ubiquitin-dependent protein catabolic process
  • positive regulation of ERAD pathway
  • proteolysis
  • autophagy
  • regulation of autophagy
  • protein K63-linked deubiquitination
  • maintenance of unfolded protein involved in ERAD pathway
  • cell population proliferation
  • melanocyte differentiation
  • protein deubiquitination
  • protein K29-linked deubiquitination
  • protein K6-linked deubiquitination
  • protein stabilization
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

8975

72607

Ensembl

ENSG00000058056

ENSMUSG00000056900

UniProt

Q92995

Q5BKP2

RefSeq (mRNA)

NM_003940

NM_001013024

RefSeq (protein)

NP_003931

NP_001013042

Location (UCSC)Chr 3: 179.65 – 179.8 MbChr 3: 32.87 – 32.99 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Ubiquitin carboxyl-terminal hydrolase 13 is an enzyme that in humans is encoded by the USP13 gene.[5][6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000058056 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000056900 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Puente XS, Sanchez LM, Overall CM, Lopez-Otin C (Jul 2003). "Human and mouse proteases: a comparative genomic approach". Nat Rev Genet. 4 (7): 544–58. doi:10.1038/nrg1111. PMID 12838346. S2CID 2856065.
  6. ^ "Entrez Gene: USP13 ubiquitin specific peptidase 13 (isopeptidase T-3)".

Further reading

  • D'Andrea A, Pellman D (1999). "Deubiquitinating enzymes: a new class of biological regulators". Crit. Rev. Biochem. Mol. Biol. 33 (5): 337–52. doi:10.1080/10409239891204251. PMID 9827704.
  • Timms KM, Ansari-Lari MA, Morris W, et al. (1998). "The genomic organization of Isopeptidase T-3 (ISOT-3), a new member of the ubiquitin specific protease family (UBP)". Gene. 217 (1–2): 101–6. doi:10.1016/S0378-1119(98)00341-2. PMID 9841226.
  • Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
  • McElhinny AS, Kakinuma K, Sorimachi H, et al. (2002). "Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1". J. Cell Biol. 157 (1): 125–36. doi:10.1083/jcb.200108089. PMC 2173255. PMID 11927605.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Colland F, Jacq X, Trouplin V, et al. (2004). "Functional proteomics mapping of a human signaling pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
  • Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to biology: a functional genomics pipeline". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
  • Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
  • Mehrle A, Rosenfelder H, Schupp I, et al. (2006). "The LIFEdb database in 2006". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.


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