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USP1  -  ubiquitin specific peptidase 1

Homo sapiens

Synonyms: Deubiquitinating enzyme 1, Ubiquitin carboxyl-terminal hydrolase 1, Ubiquitin thioesterase 1, Ubiquitin-specific-processing protease 1, hUBP
 
 
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Disease relevance of USP1

 

Psychiatry related information on USP1

 

High impact information on USP1

 

Chemical compound and disease context of USP1

 

Biological context of USP1

 

Anatomical context of USP1

 

Associations of USP1 with chemical compounds

 

Physical interactions of USP1

 

Regulatory relationships of USP1

 

Other interactions of USP1

 

Analytical, diagnostic and therapeutic context of USP1

  • Chromosomal mapping by fluorescence in situ hybridization and radiation hybrid analyses localized the USP1 gene to the p31.3-p32.1 band of chromosome 1 [2].
  • The EcRE1 at -342 was necessary but not sufficient for the activational response but was the only one of the three putative EcREs to bind the EcR-B1-USP-1 complex in gel mobility shift assays and was responsible for the silencing action of EcR-B1-USP-1 in the absence of hormone [20].
  • Sequence analysis reveals that this protein is conserved between human and mouse and contains the signature motifs of the ubiquitin-specific processing protease family [32].

References

  1. The deubiquitinating enzyme USP1 regulates the Fanconi anemia pathway. Nijman, S.M., Huang, T.T., Dirac, A.M., Brummelkamp, T.R., Kerkhoven, R.M., D'Andrea, A.D., Bernards, R. Mol. Cell (2005) [Pubmed]
  2. Identification and chromosomal assignment of USP1, a novel gene encoding a human ubiquitin-specific protease. Fujiwara, T., Saito, A., Suzuki, M., Shinomiya, H., Suzuki, T., Takahashi, E., Tanigami, A., Ichiyama, A., Chung, C.H., Nakamura, Y., Tanaka, K. Genomics (1998) [Pubmed]
  3. A deubiquitinating enzyme encoded by HSV-1 belongs to a family of cysteine proteases that is conserved across the family Herpesviridae. Kattenhorn, L.M., Korbel, G.A., Kessler, B.M., Spooner, E., Ploegh, H.L. Mol. Cell (2005) [Pubmed]
  4. The papain-like protease from the severe acute respiratory syndrome coronavirus is a deubiquitinating enzyme. Lindner, H.A., Fotouhi-Ardakani, N., Lytvyn, V., Lachance, P., Sulea, T., Ménard, R. J. Virol. (2005) [Pubmed]
  5. The role of protein ubiquitination in neurodegenerative disease. Mayer, R.J., Lowe, J., Landon, M., McDermott, H., László, L. Acta. Biol. Hung. (1991) [Pubmed]
  6. CYLD in ubiquitin signaling and tumor pathogenesis. Ikeda, F., Dikic, I. Cell (2006) [Pubmed]
  7. A role for the deubiquitinating enzyme USP28 in control of the DNA-damage response. Zhang, D., Zaugg, K., Mak, T.W., Elledge, S.J. Cell (2006) [Pubmed]
  8. Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde. Hu, M., Li, P., Li, M., Li, W., Yao, T., Wu, J.W., Gu, W., Cohen, R.E., Shi, Y. Cell (2002) [Pubmed]
  9. The neuron-specific protein PGP 9.5 is a ubiquitin carboxyl-terminal hydrolase. Wilkinson, K.D., Lee, K.M., Deshpande, S., Duerksen-Hughes, P., Boss, J.M., Pohl, J. Science (1989) [Pubmed]
  10. Reversible monoubiquitination of PCNA: A novel slant on regulating translesion DNA synthesis. Friedberg, E.C. Mol. Cell (2006) [Pubmed]
  11. Regulation of monoubiquitinated PCNA by DUB autocleavage. Huang, T.T., Nijman, S.M., Mirchandani, K.D., Galardy, P.J., Cohn, M.A., Haas, W., Gygi, S.P., Ploegh, H.L., Bernards, R., D'Andrea, A.D. Nat. Cell Biol. (2006) [Pubmed]
  12. The deubiquitinating enzyme DUB-2 prolongs cytokine-induced signal transducers and activators of transcription activation and suppresses apoptosis following cytokine withdrawal. Migone, T.S., Humbert, M., Rascle, A., Sanden, D., D'Andrea, A., Johnston, J.A. Blood (2001) [Pubmed]
  13. Caspase-dependent deubiquitination of monoubiquitinated nucleosomal histone H2A induced by diverse apoptogenic stimuli. Mimnaugh, E.G., Kayastha, G., McGovern, N.B., Hwang, S.G., Marcu, M.G., Trepel, J., Cai, S.Y., Marchesi, V.T., Neckers, L. Cell Death Differ. (2001) [Pubmed]
  14. Up-regulation of Expression of the Ubiquitin Carboxyl-Terminal Hydrolase L1 Gene in Human Airway Epithelium of Cigarette Smokers. Carolan, B.J., Heguy, A., Harvey, B.G., Leopold, P.L., Ferris, B., Crystal, R.G. Cancer Res. (2006) [Pubmed]
  15. AMSH is an endosome-associated ubiquitin isopeptidase. McCullough, J., Clague, M.J., Urbé, S. J. Cell Biol. (2004) [Pubmed]
  16. Ubiquitin carboxyl-terminal hydrolase (PGP 9.5) is selectively present in ubiquitinated inclusion bodies characteristic of human neurodegenerative diseases. Lowe, J., McDermott, H., Landon, M., Mayer, R.J., Wilkinson, K.D. J. Pathol. (1990) [Pubmed]
  17. Identification of proteins differentially expressed in quiescent and proliferatively senescent fibroblast cultures. DiPaolo, B.R., Pignolo, R.J., Cristofalo, V.J. Exp. Cell Res. (1995) [Pubmed]
  18. USP19 is a ubiquitin-specific protease regulated in rat skeletal muscle during catabolic states. Combaret, L., Adegoke, O.A., Bedard, N., Baracos, V., Attaix, D., Wing, S.S. Am. J. Physiol. Endocrinol. Metab. (2005) [Pubmed]
  19. Ubiquitin C-terminal hydrolase-L1 (PGP9.5) expression in human neural cell lines following induction of neuronal differentiation and exposure to cytokines, neurotrophic factors or heat stress. Satoh, J.I., Kuroda, Y. Neuropathol. Appl. Neurobiol. (2001) [Pubmed]
  20. Activation of a delayed-early gene encoding MHR3 by the ecdysone receptor heterodimer EcR-B1-USP-1 but not by EcR-B1-USP-2. Lan, Q., Hiruma, K., Hu, X., Jindra, M., Riddiford, L.M. Mol. Cell. Biol. (1999) [Pubmed]
  21. The ubiquitin-specific protease Usp4 regulates the cell surface level of the A2A receptor. Milojevic, T., Reiterer, V., Stefan, E., Korkhov, V.M., Dorostkar, M.M., Ducza, E., Ogris, E., Boehm, S., Freissmuth, M., Nanoff, C. Mol. Pharmacol. (2006) [Pubmed]
  22. Synthesis and characterization of ubiquitin ethyl ester, a new substrate for ubiquitin carboxyl-terminal hydrolase. Wilkinson, K.D., Cox, M.J., Mayer, A.N., Frey, T. Biochemistry (1986) [Pubmed]
  23. Clathrin anchors deubiquitinating enzymes, AMSH and AMSH-like protein, on early endosomes. Nakamura, M., Tanaka, N., Kitamura, N., Komada, M. Genes Cells (2006) [Pubmed]
  24. Further characterization of the putative human isopeptidase T catalytic site. Lacombe, T., Gabriel, J.M. FEBS Lett. (2002) [Pubmed]
  25. The deubiquitinating enzyme UCH37 interacts with Smads and regulates TGF-beta signalling. Wicks, S.J., Haros, K., Maillard, M., Song, L., Cohen, R.E., Dijke, P.T., Chantry, A. Oncogene (2005) [Pubmed]
  26. The finger domain of the human deubiquitinating enzyme HAUSP is a zinc ribbon. Krishna, S.S., Grishin, N.V. Cell Cycle (2004) [Pubmed]
  27. CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members. Trompouki, E., Hatzivassiliou, E., Tsichritzis, T., Farmer, H., Ashworth, A., Mosialos, G. Nature (2003) [Pubmed]
  28. Molecular findings in familial Parkinson disease in Spain. Hoenicka, J., Vidal, L., Morales, B., Ampuero, I., Jiménez-Jiménez, F.J., Berciano, J., del Ser, T., Jiménez, A., Ruíz, P.G., de Yébenes, J.G. Arch. Neurol. (2002) [Pubmed]
  29. The zinc finger of the CSN-associated deubiquitinating enzyme USP15 is essential to rescue the E3 ligase Rbx1. Hetfeld, B.K., Helfrich, A., Kapelari, B., Scheel, H., Hofmann, K., Guterman, A., Glickman, M., Schade, R., Kloetzel, P.M., Dubiel, W. Curr. Biol. (2005) [Pubmed]
  30. The RS447 human megasatellite tandem repetitive sequence encodes a novel deubiquitinating enzyme with a functional promoter. Saitoh, Y., Miyamoto, N., Okada, T., Gondo, Y., Showguchi-Miyata, J., Hadano, S., Ikeda, J.E. Genomics (2000) [Pubmed]
  31. Selective upregulation of the ubiquitin-proteasome proteolytic pathway proteins, proteasome zeta chain and isopeptidase T in fetal Down syndrome. Engidawork, E., Juranville, J.F., Fountoulakis, M., Dierssen, M., Lubec, G. J. Neural Transm. Suppl. (2001) [Pubmed]
  32. Ubiquitination of a novel deubiquitinating enzyme requires direct binding to von Hippel-Lindau tumor suppressor protein. Li, Z., Na, X., Wang, D., Schoen, S.R., Messing, E.M., Wu, G. J. Biol. Chem. (2002) [Pubmed]
 
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