OTUB1

OTUB1
Available structures
PDB	Human UniProt search: PDBe RCSB
List of PDB id codes
	2ZFY, 3VON, 4DDG, 4DDI, 4DHZ, 4I6L, 4LDT
Identifiers
Aliases	OTUB1, OTB1, OTU1, HSPC263, OTU deubiquitinase, ubiquitin aldehyde binding 1
External IDs	OMIM: 608337 HomoloGene: 134542 GeneCards: OTUB1
Gene location (Human)
Chr.	Chromosome 11 (human)[1]
End	64,001,811 bp[1]
RNA expression pattern
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	• cysteine-type peptidase activity; • NEDD8-specific protease activity; • thiol-dependent ubiquitinyl hydrolase activity; • peptidase activity; • ubiquitin binding; • GO:0001948 protein binding; • thiol-dependent ubiquitin-specific protease activity; • hydrolase activity; • ubiquitin protein ligase binding;
Cellular component	• cytoplasm; • extracellular exosome; • cell nucleus; • nucleoplasm; • cytosol;
Biological process	• adaptive immune response; • protein K48-linked deubiquitination; • immune system process; • proteolysis; • cellular response to DNA damage stimulus; • negative regulation of double-strand break repair; • negative regulation of histone H2A K63-linked ubiquitination; • cellular response to interleukin-1; • DNA repair; • protein deubiquitination;
	Sources:Amigo / QuickGO
Orthologs
	55611
	n/a
	ENSG00000167770
	n/a
	Q96FW1
	n/a
	NM_017670
	n/a
	NP_060140
	n/a
	Wikidata
View/Edit Human

Ubiquitin thioesterase OTUB1 also known as otubain-1 is an enzyme that in humans is encoded by the OTUB1 gene.[3][4] Alternative splicing results in multiple transcript variants.

Function

Otubain-1 is a member of the OTU (ovarian tumor) superfamily of predicted cysteine proteases. The encoded protein is a highly specific ubiquitin iso-peptidase, and cleaves ubiquitin from branched poly-ubiquitin chains, being specific for lysine⁴⁸ -linked polyubiquitin but not lysine⁶³ -linked polyubiquitin.[5] It interacts with another ubiquitin protease and an E3 ubiquitin ligase that inhibits cytokine gene transcription in the immune system. It is proposed to function in specific ubiquitin-dependent pathways, possibly by providing an editing function for polyubiquitin chain growth.[4]

Interactions

OTUB1 has been shown to interact with RNF128[6] and GNB2L1.[5]

References

GRCh38: Ensembl release 89: ENSG00000167770 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Balakirev MY, Tcherniuk SO, Jaquinod M, Chroboczek J (Apr 2003). "Otubains: a new family of cysteine proteases in the ubiquitin pathway". EMBO Rep. 4 (5): 517–22. doi:10.1038/sj.embor.embor824. PMC 1319179. PMID 12704427.
"Entrez Gene: OTUB1 OTU domain, ubiquitin aldehyde binding 1".
Edelmann MJ, Iphöfer A, Akutsu M, Altun M, di Gleria K, Kramer HB, Fiebiger E, Dhe-Paganon S, Kessler BM (March 2009). "Structural basis and specificity of human otubain 1-mediated deubiquitination". Biochem. J. 418 (2): 379–90. doi:10.1042/BJ20081318. PMID 18954305.
Soares L, Seroogy C, Skrenta H, Anandasabapathy N, Lovelace P, Chung CD, Engleman E, Fathman CG (January 2004). "Two isoforms of otubain 1 regulate T cell anergy via GRAIL". Nat. Immunol. 5 (1): 45–54. doi:10.1038/ni1017. PMID 14661020.

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Makarova KS, Aravind L, Koonin EV (2000). "A novel superfamily of predicted cysteine proteases from eukaryotes, viruses and Chlamydia pneumoniae". Trends Biochem. Sci. 25 (2): 50–2. doi:10.1016/S0968-0004(99)01530-3. PMID 10664582.
Zhang QH, Ye M, Wu XY, et al. (2001). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.
Borodovsky A, Ovaa H, Kolli N, et al. (2003). "Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family". Chem. Biol. 9 (10): 1149–59. doi:10.1016/S1074-5521(02)00248-X. PMID 12401499.
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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Soares L, Seroogy C, Skrenta H, et al. (2004). "Two isoforms of otubain 1 regulate T cell anergy via GRAIL". Nat. Immunol. 5 (1): 45–54. doi:10.1038/ni1017. PMID 14661020.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
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.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Juris SJ, Shah K, Shokat K, et al. (2006). "Identification of otubain 1 as a novel substrate for the Yersinia protein kinase using chemical genetics and mass spectrometry". FEBS Lett. 580 (1): 179–83. doi:10.1016/j.febslet.2005.11.071. PMID 16364312.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000167770 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid12704427-3] Balakirev MY, Tcherniuk SO, Jaquinod M, Chroboczek J (Apr 2003). "Otubains: a new family of cysteine proteases in the ubiquitin pathway". EMBO Rep. 4 (5): 517–22. doi:10.1038/sj.embor.embor824. PMC 1319179. PMID 12704427.

[entrez-4] "Entrez Gene: OTUB1 OTU domain, ubiquitin aldehyde binding 1".

[pmid18954305-5] Edelmann MJ, Iphöfer A, Akutsu M, Altun M, di Gleria K, Kramer HB, Fiebiger E, Dhe-Paganon S, Kessler BM (March 2009). "Structural basis and specificity of human otubain 1-mediated deubiquitination". Biochem. J. 418 (2): 379–90. doi:10.1042/BJ20081318. PMID 18954305.

[pmid14661020-6] Soares L, Seroogy C, Skrenta H, Anandasabapathy N, Lovelace P, Chung CD, Engleman E, Fathman CG (January 2004). "Two isoforms of otubain 1 regulate T cell anergy via GRAIL". Nat. Immunol. 5 (1): 45–54. doi:10.1038/ni1017. PMID 14661020.

OTUB1

Function

Interactions

References

Further reading