OTUB1

OTUB1
Available structures
PDB	Ortholog 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; MGI: 2147616; HomoloGene: 134542; GeneCards: OTUB1; OMA:OTUB1 - orthologs
Gene location (Human)
Chr.	Chromosome 11 (human)
End	64,001,811 bp
Gene location (Mouse)
Chr.	Chromosome 19 (mouse)
End	7,183,681 bp
RNA expression pattern
	Top expressed in
	right frontal lobe; ; prefrontal cortex; ; right hemisphere of cerebellum; ; Brodmann area 10; ; cingulate gyrus; ; anterior cingulate cortex; ; granulocyte; ; pancreatic ductal cell; ; mucosa of ileum; ; Brodmann area 9;
	Top expressed in
	dentate gyrus of hippocampal formation granule cell; ; superior frontal gyrus; ; yolk sac; ; ventricular zone; ; neural layer of retina; ; morula; ; tail of embryo; ; lip; ; primary visual cortex; ; spermatocyte;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	cysteine-type peptidase activity ; NEDD8-specific protease activity ; thiol-dependent deubiquitinase ; peptidase activity ; ubiquitin binding ; protein binding ; hydrolase activity ; ubiquitin protein ligase binding ;
Cellular component	cytoplasm ; extracellular exosome ; 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
	107260
	ENSG00000167770
	ENSMUSG00000024767
	Q96FW1
	Q7TQI3
	NM_017670
	NM_134150
	NP_060140
	NP_598911
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated October 03, 2024

Ubiquitin thioesterase OTUB1 also known as otubain-1 is an enzyme that in humans is encoded by the OTUB1 gene.^[5]^[6] 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.^[7] 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.^[6]

Interactions

OTUB1 has been shown to interact with RNF128 ^[8] and GNB2L1.^[7]

Related Research Articles

Deubiquitinating enzymes (DUBs), also known as deubiquitinating peptidases, deubiquitinating isopeptidases, deubiquitinases, ubiquitin proteases, ubiquitin hydrolases, or ubiquitin isopeptidases, are a large group of proteases that cleave ubiquitin from proteins. Ubiquitin is attached to proteins in order to regulate the degradation of proteins via the proteasome and lysosome; coordinate the cellular localisation of proteins; activate and inactivate proteins; and modulate protein-protein interactions. DUBs can reverse these effects by cleaving the peptide or isopeptide bond between ubiquitin and its substrate protein. In humans there are nearly 100 DUB genes, which can be classified into two main classes: cysteine proteases and metalloproteases. The cysteine proteases comprise ubiquitin-specific proteases (USPs), ubiquitin C-terminal hydrolases (UCHs), Machado-Josephin domain proteases (MJDs) and ovarian tumour proteases (OTU). The metalloprotease group contains only the Jab1/Mov34/Mpr1 Pad1 N-terminal+ (MPN+) (JAMM) domain proteases.

40S ribosomal protein S27a is a protein that in humans is encoded by the RPS27A gene.

60S ribosomal protein L40 (RPL40) is a protein that in humans is encoded by the UBA52 gene.

Ras GTPase-activating protein-binding protein 1 is an enzyme that in humans is encoded by the G3BP1 gene.

Ubiquitin-conjugating enzyme E2 N is a protein that in humans is encoded by the UBE2N gene.

Bleomycin hydrolase is an enzyme that in humans is encoded by the BLMH gene.

NEDD8-activating enzyme E1 catalytic subunit is a protein that in humans is encoded by the UBA3 gene.

Ubiquitin carboxyl-terminal hydrolase 8 is an enzyme that in humans is encoded by the USP8 gene.

E3 ubiquitin-protein ligase RNF216 is an enzyme that in humans is encoded by the RNF216 gene.

Ubiquitin specific protease 4 (USP4) is an enzyme that cleaves ubiquitin from a number of protein substrates. Prior to the standardization of nomenclature USP4 was known as UNP, and was one of the first deubiquitinating enzymes to be identified in mammals. In the mouse and human the USP4 protein is encoded by a gene containing 22 exons.

RING finger protein 31 is a protein that in humans is encoded by the RNF31 gene.

Ubiquitin specific processing protease 37 is an enzyme that in humans, is encoded by the USP37 gene.

Ubiquitin-conjugating enzyme E2 J1 is a protein that in humans is encoded by the UBE2J1 gene.

NEDD8-conjugating enzyme Ubc12 is a protein that in humans is encoded by the UBE2M gene.

Ubiquitin carboxyl-terminal hydrolase 2 is an enzyme that in humans is encoded by the USP2 gene.

Ubiquitin carboxyl-terminal hydrolase 20 is an enzyme that in humans is encoded by the USP20 gene.

Sentrin-specific protease 8 is an enzyme that in humans is encoded by the SENP8 gene.

Ubiquitin-fold modifier 1, also known as UFM1, is a protein which in humans is encoded by the UFM1 gene.

Ubiquitin-conjugating enzyme E2 R2 is a protein that in humans is encoded by the UBE2R2 gene.

Ubiquitin carboxyl-terminal hydrolase 51 is an enzyme that in humans is encoded by the USP51 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000167770 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000024767 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse 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.
1 2 "Entrez Gene: OTUB1 OTU domain, ubiquitin aldehyde binding 1".
1 2 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" (PDF). 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. S2CID 27005972.

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. Bibcode:2002PNAS...9916899M. 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. S2CID 27005972.
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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
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. Bibcode:2006FEBSL.580..179J. doi: 10.1016/j.febslet.2005.11.071 . PMID 16364312. S2CID 24766989.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000167770 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000024767 – 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.

[pmid12704427-5] 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-6] 1 2 "Entrez Gene: OTUB1 OTU domain, ubiquitin aldehyde binding 1".

[pmid18954305-7] 1 2 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" (PDF). Biochem. J. 418 (2): 379–90. doi:10.1042/BJ20081318. PMID 18954305.

[pmid14661020-8] 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. S2CID 27005972.

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OTUB1

Contents

Function

Interactions

Related Research Articles

References

Further reading