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{{Infobox_gene}}
'''Ubiquitin thioesterase OTUB1''' also known as '''otubain-1''' is an [[enzyme]] that in humans is encoded by the ''OTUB1'' [[gene]].<ref name="pmid12704427">{{cite journal | vauthors = Balakirev MY, Tcherniuk SO, Jaquinod M, Chroboczek J | title = Otubains: a new family of cysteine proteases in the ubiquitin pathway | journal = EMBO Rep | volume = 4 | issue = 5 | pages = 517–22 |date=Apr 2003 | pmid = 12704427 | pmc = 1319179 | doi = 10.1038/sj.embor.embor824 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: OTUB1 OTU domain, ubiquitin aldehyde binding 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55611| accessdate = }}</ref> 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 lysine<sup>48</sup> -linked polyubiquitin but not lysine<sup>63</sup> -linked polyubiquitin.<ref name="pmid18954305"/>  It interacts with another [[deubiquitinating enzyme|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.<ref name="entrez" />
== Interactions ==
OTUB1 has been shown to [[Protein-protein interaction|interact]] with [[RNF128]]<ref name="pmid14661020">{{cite journal | vauthors = Soares L, Seroogy C, Skrenta H, Anandasabapathy N, Lovelace P, Chung CD, Engleman E, Fathman CG | title = Two isoforms of otubain 1 regulate T cell anergy via GRAIL | journal = Nat. Immunol. | volume = 5 | issue = 1 | pages = 45–54 |date=January 2004 | pmid = 14661020 | doi = 10.1038/ni1017 | url = | issn = }}</ref> and [[GNB2L1]].<ref name="pmid18954305">{{cite journal | vauthors = Edelmann MJ, Iphöfer A, Akutsu M, Altun M, di Gleria K, Kramer HB, Fiebiger E, Dhe-Paganon S, Kessler BM | title = Structural basis and specificity of human otubain 1-mediated deubiquitination | journal = Biochem. J. | volume = 418 | issue = 2 | pages = 379–90 |date=March 2009 | pmid = 18954305 | doi = 10.1042/BJ20081318 | url = | issn = }}</ref>
== References ==
{{reflist}}
== Further reading ==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8  }}
*{{cite journal  |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  }}
*{{cite journal  | vauthors=Makarova KS, Aravind L, Koonin EV |title=A novel superfamily of predicted cysteine proteases from eukaryotes, viruses and Chlamydia pneumoniae. |journal=Trends Biochem. Sci. |volume=25 |issue= 2 |pages= 50–2 |year= 2000 |pmid= 10664582 |doi=10.1016/S0968-0004(99)01530-3  }}
*{{cite journal  |vauthors=Zhang QH, Ye M, Wu XY, etal |title=Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. |journal=Genome Res. |volume=10 |issue= 10 |pages= 1546–60 |year= 2001 |pmid= 11042152 |doi=10.1101/gr.140200  | pmc=310934  }}
*{{cite journal  |vauthors=Borodovsky A, Ovaa H, Kolli N, etal |title=Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family. |journal=Chem. Biol. |volume=9 |issue= 10 |pages= 1149–59 |year= 2003 |pmid= 12401499 |doi=10.1016/S1074-5521(02)00248-X  }}
*{{cite journal  |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 }}
*{{cite journal  |vauthors=Soares L, Seroogy C, Skrenta H, etal |title=Two isoforms of otubain 1 regulate T cell anergy via GRAIL. |journal=Nat. Immunol. |volume=5 |issue= 1 |pages= 45–54 |year= 2004 |pmid= 14661020 |doi= 10.1038/ni1017 }}
*{{cite journal  |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  |vauthors=Colland F, Jacq X, Trouplin V, etal |title=Functional proteomics mapping of a human signaling pathway. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1324–32 |year= 2004 |pmid= 15231748 |doi= 10.1101/gr.2334104  | pmc=442148 }}
*{{cite journal  |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 }}
*{{cite journal  |vauthors=Rual JF, Venkatesan K, Hao T, etal |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal  |vauthors=Juris SJ, Shah K, Shokat K, etal |title=Identification of otubain 1 as a novel substrate for the Yersinia protein kinase using chemical genetics and mass spectrometry. |journal=FEBS Lett. |volume=580 |issue= 1 |pages= 179–83 |year= 2006 |pmid= 16364312 |doi= 10.1016/j.febslet.2005.11.071 }}
}}
{{refend}}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = OTU domain, ubiquitin aldehyde binding 1
| HGNCid = 23077
| Symbol = OTUB1
| AltSymbols =; FLJ20113; FLJ40710; HSPC263; MGC111158; MGC4584; OTB1; OTU1
| OMIM = 608337
| ECnumber = 
| Homologene = 9772
| MGIid = 2147616
| GeneAtlas_image1 = PBB_GE_OTUB1_201245_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_OTUB1_201246_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_OTUB1_38710_at_tn.png
| Function = {{GNF_GO|id=GO:0008234 |text = cysteine-type peptidase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}} {{GNF_GO|id=GO:0006955 |text = immune response}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 55611
    | Hs_Ensembl = ENSG00000167770
    | Hs_RefseqProtein = NP_060140
    | Hs_RefseqmRNA = NM_017670
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 63510461
    | Hs_GenLoc_end = 63522463
    | Hs_Uniprot = Q96FW1
    | Mm_EntrezGene = 107260
    | Mm_Ensembl = ENSMUSG00000024767
    | Mm_RefseqmRNA = XM_986327
    | Mm_RefseqProtein = XP_991421
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 19
    | Mm_GenLoc_start = 7265250
    | Mm_GenLoc_end = 7273328
    | Mm_Uniprot = Q7TQI3
  }}
}}
'''OTU domain, ubiquitin aldehyde binding 1''', also known as '''OTUB1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: OTUB1 OTU domain, ubiquitin aldehyde binding 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55611| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The product of this gene 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 but not from ubiquitinated substrates. 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. Alternative splicing results in multiple transcript variants.<ref name="entrez">{{cite web | title = Entrez Gene: OTUB1 OTU domain, ubiquitin aldehyde binding 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55611| accessdate = }}</ref>
}}
==References==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
*{{cite journal  | author=Makarova KS, Aravind L, Koonin EV |title=A novel superfamily of predicted cysteine proteases from eukaryotes, viruses and Chlamydia pneumoniae. |journal=Trends Biochem. Sci. |volume=25 |issue= 2 |pages= 50-2 |year= 2000 |pmid= 10664582 |doi=  }}
*{{cite journal  | author=Zhang QH, Ye M, Wu XY, ''et al.'' |title=Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. |journal=Genome Res. |volume=10 |issue= 10 |pages= 1546-60 |year= 2001 |pmid= 11042152 |doi=  }}
*{{cite journal  | author=Borodovsky A, Ovaa H, Kolli N, ''et al.'' |title=Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family. |journal=Chem. Biol. |volume=9 |issue= 10 |pages= 1149-59 |year= 2003 |pmid= 12401499 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Balakirev MY, Tcherniuk SO, Jaquinod M, Chroboczek J |title=Otubains: a new family of cysteine proteases in the ubiquitin pathway. |journal=EMBO Rep. |volume=4 |issue= 5 |pages= 517-22 |year= 2004 |pmid= 12704427 |doi= 10.1038/sj.embor.embor824 }}
*{{cite journal  | author=Soares L, Seroogy C, Skrenta H, ''et al.'' |title=Two isoforms of otubain 1 regulate T cell anergy via GRAIL. |journal=Nat. Immunol. |volume=5 |issue= 1 |pages= 45-54 |year= 2004 |pmid= 14661020 |doi= 10.1038/ni1017 }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Colland F, Jacq X, Trouplin V, ''et al.'' |title=Functional proteomics mapping of a human signaling pathway. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1324-32 |year= 2004 |pmid= 15231748 |doi= 10.1101/gr.2334104 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal  | author=Juris SJ, Shah K, Shokat K, ''et al.'' |title=Identification of otubain 1 as a novel substrate for the Yersinia protein kinase using chemical genetics and mass spectrometry. |journal=FEBS Lett. |volume=580 |issue= 1 |pages= 179-83 |year= 2006 |pmid= 16364312 |doi= 10.1016/j.febslet.2005.11.071 }}
}}
{{refend}}


{{protein-stub}}
{{gene-11-stub}}
{{WikiDoc Sources}}

Latest revision as of 00:42, 7 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

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RefSeq (protein)

n/a

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Location (UCSC)n/an/a
PubMed searchn/an/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.[1][2] 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.[3] 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.[2]

Interactions

OTUB1 has been shown to interact with RNF128[4] and GNB2L1.[3]

References

  1. ↑ 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.
  2. ↑ 2.0 2.1 "Entrez Gene: OTUB1 OTU domain, ubiquitin aldehyde binding 1".
  3. ↑ 3.0 3.1 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.
  4. ↑ 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.

Further reading



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