USP5

Protein-coding gene in the species Homo sapiens
USP5
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2DAG, 2DAK, 2G43, 2G45, 3IHP

Identifiers
AliasesUSP5, ISOT, ubiquitin specific peptidase 5
External IDsOMIM: 601447; MGI: 1347343; HomoloGene: 55758; GeneCards: USP5; OMA:USP5 - orthologs
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for USP5
Genomic location for USP5
Band12p13.31Start6,852,128 bp[1]
End6,866,632 bp[1]
Gene location (Mouse)
Chromosome 6 (mouse)
Chr.Chromosome 6 (mouse)[2]
Chromosome 6 (mouse)
Genomic location for USP5
Genomic location for USP5
Band6 F2|6 59.17 cMStart124,791,982 bp[2]
End124,806,447 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • prefrontal cortex

  • left testis

  • right testis

  • right frontal lobe

  • right adrenal gland

  • right adrenal cortex

  • Brodmann area 9

  • left adrenal gland

  • lateral nuclear group of thalamus

  • gastrocnemius muscle
Top expressed in
  • spermatocyte

  • dentate gyrus of hippocampal formation granule cell

  • superior frontal gyrus

  • primary visual cortex

  • perirhinal cortex

  • entorhinal cortex

  • ventricular zone

  • otic vesicle

  • lip

  • medulla oblongata
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • peptidase activity
  • cysteine-type peptidase activity
  • cysteine-type endopeptidase activity
  • zinc ion binding
  • ubiquitin binding
  • protein binding
  • hydrolase activity
  • metal ion binding
  • thiol-dependent deubiquitinase
Cellular component
  • lysosome
  • cytosol
Biological process
  • protein K48-linked deubiquitination
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process
  • ubiquitin-dependent protein catabolic process
  • proteolysis
  • protein deubiquitination
  • protein ubiquitination
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

8078

22225

Ensembl

ENSG00000111667

ENSMUSG00000038429

UniProt

P45974

P56399

RefSeq (mRNA)

NM_001098536
NM_003481

NM_013700
NM_001326594

RefSeq (protein)
NP_001092006
NP_003472
NP_001369517
NP_001369518
NP_001369519

NP_001369520

NP_001313523
NP_038728

Location (UCSC)Chr 12: 6.85 – 6.87 MbChr 6: 124.79 – 124.81 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Ubiquitin specific peptidase 5 is an enzyme that in humans is encoded by the USP5 gene.[5][6][7]

Interactions

USP5 has been shown to interact with TADA3L.[8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000111667 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000038429 – 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, Sánchez LM, Overall CM, López-Otín C (Jul 2003). "Human and mouse proteases: a comparative genomic approach". Nature Reviews Genetics. 4 (7): 544–58. doi:10.1038/nrg1111. PMID 12838346. S2CID 2856065.
  6. ^ Ansari-Lari MA, Muzny DM, Lu J, Lu F, Lilley CE, Spanos S, Malley T, Gibbs RA (Apr 1996). "A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13". Genome Research. 6 (4): 314–26. doi:10.1101/gr.6.4.314. PMID 8723724.
  7. ^ "Entrez Gene: USP5 ubiquitin specific peptidase 5 (isopeptidase T)".
  8. ^ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

Further reading

  • D'Andrea A, Pellman D (1999). "Deubiquitinating enzymes: a new class of biological regulators". Critical Reviews in Biochemistry and Molecular Biology. 33 (5): 337–52. doi:10.1080/10409239891204251. PMID 9827704.
  • Falquet L, Paquet N, Frutiger S, Hughes GJ, Hoang-Van K, Jaton JC (Dec 1995). "cDNA cloning of a human 100 kDa de-ubiquitinating enzyme: the 100 kDa human de-ubiquitinase belongs to the ubiquitin C-terminal hydrolase family 2 (UCH2)". FEBS Letters. 376 (3): 233–7. doi:10.1016/0014-5793(95)01287-7. PMID 7498549. S2CID 19521632.
  • Wilkinson KD, Tashayev VL, O'Connor LB, Larsen CN, Kasperek E, Pickart CM (Nov 1995). "Metabolism of the polyubiquitin degradation signal: structure, mechanism, and role of isopeptidase T". Biochemistry. 34 (44): 14535–46. doi:10.1021/bi00044a032. PMID 7578059.
  • Falquet L, Paquet N, Frutiger S, Hughes GJ, Hoang-Van K, Jaton JC (Feb 1995). "A human de-ubiquitinating enzyme with both isopeptidase and peptidase activities in vitro". FEBS Letters. 359 (1): 73–7. doi:10.1016/0014-5793(94)01451-6. PMID 7851534. S2CID 39667023.
  • Ansari-Lari MA, Shen Y, Muzny DM, Lee W, Gibbs RA (Mar 1997). "Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination". Genome Research. 7 (3): 268–80. doi:10.1101/gr.7.3.268. PMID 9074930.
  • Suzuki Y, Tsunoda T, Sese J, Taira H, Mizushima-Sugano J, Hata H, Ota T, Isogai T, Tanaka T, Nakamura Y, Suyama A, Sakaki Y, Morishita S, Okubo K, Sugano S (May 2001). "Identification and characterization of the potential promoter regions of 1031 kinds of human genes". Genome Research. 11 (5): 677–84. doi:10.1101/gr.gr-1640r. PMC 311086. PMID 11337467.
  • Engidawork E, Juranville JF, Fountoulakis M, Dierssen M, Lubec G (2001). "Selective upregulation of the ubiquitin-proteasome proteolytic pathway proteins, proteasome zeta chain and isopeptidase T in fetal Down syndrome". Protein Expression in Down Syndrome Brain. pp. 117–30. doi:10.1007/978-3-7091-6262-0_10. ISBN 978-3-211-83704-7. PMID 11771738. {{cite book}}: |journal= ignored (help)
  • Gabriel JM, Lacombe T, Carobbio S, Paquet N, Bisig R, Cox JA, Jaton JC (Nov 2002). "Zinc is required for the catalytic activity of the human deubiquitinating isopeptidase T". Biochemistry. 41 (46): 13755–66. doi:10.1021/bi026096m. PMID 12427038.
  • Lacombe T, Gabriel JM (Nov 2002). "Further characterization of the putative human isopeptidase T catalytic site". FEBS Letters. 531 (3): 469–74. doi:10.1016/S0014-5793(02)03586-X. PMID 12435595. S2CID 26832850.
  • Anderson NL, Polanski M, Pieper R, Gatlin T, Tirumalai RS, Conrads TP, Veenstra TD, Adkins JN, Pounds JG, Fagan R, Lobley A (Apr 2004). "The human plasma proteome: a nonredundant list developed by combination of four separate sources". Molecular & Cellular Proteomics. 3 (4): 311–26. doi:10.1074/mcp.M300127-MCP200. PMID 14718574.
  • Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ, Li Y, Xu C, Fang R, Guegler K, Rao MS, Mandalam R, Lebkowski J, Stanton LW (Jun 2004). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nature Biotechnology. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197. S2CID 27764390.
  • Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (Jul 2004). "Functional proteomics mapping of a human signaling pathway". Genome Research. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • Reyes-Turcu FE, Horton JR, Mullally JE, Heroux A, Cheng X, Wilkinson KD (Mar 2006). "The ubiquitin binding domain ZnF UBP recognizes the C-terminal diglycine motif of unanchored ubiquitin". Cell. 124 (6): 1197–208. doi:10.1016/j.cell.2006.02.038. PMID 16564012. S2CID 1312137.
  • v
  • t
  • e
  • 2dag: Solution Structure of the First UBA Domain in the Human Ubiquitin Specific Protease 5 (Isopeptidase 5)
    2dag: Solution Structure of the First UBA Domain in the Human Ubiquitin Specific Protease 5 (Isopeptidase 5)
  • 2dak: Solution Structure of the Second UBA Domain in the Human Ubiquitin Specific Protease 5 (Isopeptidase 5)
    2dak: Solution Structure of the Second UBA Domain in the Human Ubiquitin Specific Protease 5 (Isopeptidase 5)
  • 2g45: Co-crystal structure of znf ubp domain from the deubiquitinating enzyme isopeptidase T (isot) in complex with ubiquitin
    2g45: Co-crystal structure of znf ubp domain from the deubiquitinating enzyme isopeptidase T (isot) in complex with ubiquitin


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