USP25

Ubiquitin specific peptidase 25 is a protein that in humans is encoded by the USP25 gene. ^[5]

USP25
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2MUX
Identifiers
Aliases	USP25, USP21, ubiquitin specific peptidase 25
External IDs	OMIM: 604736; MGI: 1353655; HomoloGene: 8374; GeneCards: USP25; OMA:USP25 - orthologs
Gene location (Human) Chr. Chromosome 21 (human)[1] Band 21q21.1 Start 15,729,982 bp[1] End 15,880,064 bp[1]
Gene location (Mouse) Chr. Chromosome 16 (mouse)[2] Band 16|16 C3.1 Start 76,810,594 bp[2] End 76,913,668 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in sperm Skeletal muscle tissue of rectus abdominis glutes amniotic fluid muscle of thigh biceps brachii Achilles tendon Skeletal muscle tissue of biceps brachii gastrocnemius muscle vastus lateralis muscle Top expressed in muscle of thigh knee joint ciliary body spermatid blood vastus lateralis muscle granulocyte fetal liver hematopoietic progenitor cell genital tubercle esophagus More reference expression data BioGPS n/a
Gene ontology Molecular function ATPase binding peptidase activity cysteine-type peptidase activity ubiquitin binding protein binding hydrolase activity ubiquitin protein ligase binding thiol-dependent deubiquitinase ubiquitin-like protein-specific protease activity cysteine-type endopeptidase activity Cellular component endoplasmic reticulum nucleus cytoplasm cytosol Biological process protein K63-linked deubiquitination protein K48-linked deubiquitination negative regulation of ERAD pathway ubiquitin-dependent protein catabolic process proteolysis protein deubiquitination regulation of protein stability Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 29761 30940 Ensembl ENSG00000155313 ENSMUSG00000022867 UniProt Q9UHP3 P57080 RefSeq (mRNA) NM_001283041 NM_001283042 NM_013396 NM_001352560 NM_001352561 NM_001388299 NM_001388300 NM_001388301 NM_001388302 NM_013918 RefSeq (protein) NP_001269970 NP_001269971 NP_037528 NP_001339489 NP_001339490 NP_038946 Location (UCSC) Chr 21: 15.73 – 15.88 Mb Chr 16: 76.81 – 76.91 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Function

Ubiquitin is a highly conserved 76-amino acid protein involved in regulation of intracellular protein breakdown, cell cycle regulation, and stress response. Ubiquitin is released from degraded proteins by disassembly of the polyubiquitin chains, which is mediated by ubiquitin-specific proteases (USPs), such as USP25 (Valero et al., 1999 [PubMed 10644437]).[supplied by OMIM, Mar 2008].

References

1. GRCh38: Ensembl release 89: ENSG00000155313 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000022867 – 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. "Entrez Gene: Ubiquitin specific peptidase 25". Retrieved 2017-10-31.

Further reading

• Valero R, Bayés M, Francisca Sánchez-Font M, González-Angulo O, Gonzàlez-Duarte R, Marfany G (2001). "Characterization of alternatively spliced products and tissue-specific isoforms of USP28 and USP25". Genome Biol. 2 (10): RESEARCH0043. doi:10.1186/gb-2001-2-10-research0043. PMC 57798. PMID 11597335.
• Yamada H, Yanagisawa K, Tokumaru S, Taguchi A, Nimura Y, Osada H, Nagino M, Takahashi T (2008). "Detailed characterization of a homozygously deleted region corresponding to a candidate tumor suppressor locus at 21q11-21 in human lung cancer". Genes Chromosomes Cancer. 47 (9): 810–8. doi:10.1002/gcc.20582. PMID 18523997. S2CID 39369334.
• Meulmeester E, Kunze M, Hsiao HH, Urlaub H, Melchior F (2008). "Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25". Mol. Cell. 30 (5): 610–9. doi:10.1016/j.molcel.2008.03.021. hdl:11858/00-001M-0000-0012-DBA8-3. PMID 18538659.
• Denuc A, Bosch-Comas A, Gonzàlez-Duarte R, Marfany G (2009). "The UBA-UIM domains of the USP25 regulate the enzyme ubiquitination state and modulate substrate recognition". PLOS ONE. 4 (5): e5571. Bibcode:2009PLoSO...4.5571D. doi:10.1371/journal.pone.0005571. PMC 2679190. PMID 19440361.
• Törkvist L, Halfvarson J, Ong RT, Lördal M, Sjöqvist U, Bresso F, Björk J, Befrits R, Löfberg R, Blom J, Carlson M, Padyukov L, D'Amato M, Seielstad M, Pettersson S (2010). "Analysis of 39 Crohn's disease risk loci in Swedish inflammatory bowel disease patients". Inflamm. Bowel Dis. 16 (6): 907–9. doi:10.1002/ibd.21105. PMID 19760754.
• Cholay M, Reverdy C, Benarous R, Colland F, Daviet L (2010). "Functional interaction between the ubiquitin-specific protease 25 and the SYK tyrosine kinase". Exp. Cell Res. 316 (4): 667–75. doi:10.1016/j.yexcr.2009.10.023. PMID 19909739.
• Rose JE, Behm FM, Drgon T, Johnson C, Uhl GR (2010). "Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score". Mol. Med. 16 (7–8): 247–53. doi:10.2119/molmed.2009.00159. PMC 2896464. PMID 20379614.
• Kessler BM, Edelmann MJ (2011). "PTMs in conversation: activity and function of deubiquitinating enzymes regulated via post-translational modifications". Cell Biochem. Biophys. 60 (1–2): 21–38. doi:10.1007/s12013-011-9176-6. PMC 3094536. PMID 21480003.
• Blount JR, Burr AA, Denuc A, Marfany G, Todi SV (2012). "Ubiquitin-specific protease 25 functions in Endoplasmic Reticulum-associated degradation". PLOS ONE. 7 (5): e36542. Bibcode:2012PLoSO...736542B. doi:10.1371/journal.pone.0036542. PMC 3348923. PMID 22590560.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.