Full text data of OTUD6B
OTUD6B
(DUBA5)
[Confidence: low (only semi-automatic identification from reviews)]
OTU domain-containing protein 6B; 3.4.19.12 (DUBA-5)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
OTU domain-containing protein 6B; 3.4.19.12 (DUBA-5)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q8N6M0
ID OTU6B_HUMAN Reviewed; 293 AA.
AC Q8N6M0; A8K6I1; Q9NTA4; Q9Y387;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2002, sequence version 1.
DT 22-JAN-2014, entry version 79.
DE RecName: Full=OTU domain-containing protein 6B;
DE EC=3.4.19.12;
DE AltName: Full=DUBA-5;
GN Name=OTUD6B; Synonyms=DUBA5; ORFNames=CGI-77;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 67-293, AND VARIANT GLN-283.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP IDENTIFICATION.
RX PubMed=23827681; DOI=10.1016/j.cell.2013.05.046;
RA Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M.,
RA Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F.,
RA Freund S.M., Ovaa H., Komander D.;
RT "OTU deubiquitinases reveal mechanisms of linkage specificity and
RT enable ubiquitin chain restriction analysis.";
RL Cell 154:169-184(2013).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC thioester, amide, peptide and isopeptide bonds formed by the C-
CC terminal Gly of ubiquitin (a 76-residue protein attached to
CC proteins as an intracellular targeting signal).
CC -!- MISCELLANEOUS: No deubiquitinase activity has been detected when
CC tested (PubMed:23827681). May require some post-translational
CC modification to be active.
CC -!- SIMILARITY: Contains 1 OTU domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF151836; AAD34073.1; -; mRNA.
DR EMBL; AK291646; BAF84335.1; -; mRNA.
DR EMBL; AC087439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029760; AAH29760.1; -; mRNA.
DR EMBL; AL137441; CAB70738.1; -; mRNA.
DR PIR; T46264; T46264.
DR RefSeq; NP_057107.3; NM_016023.3.
DR UniGene; Hs.30532; -.
DR ProteinModelPortal; Q8N6M0; -.
DR IntAct; Q8N6M0; 5.
DR STRING; 9606.ENSP00000285420; -.
DR PhosphoSite; Q8N6M0; -.
DR DMDM; 74729149; -.
DR PaxDb; Q8N6M0; -.
DR PRIDE; Q8N6M0; -.
DR DNASU; 51633; -.
DR Ensembl; ENST00000285420; ENSP00000285420; ENSG00000155100.
DR Ensembl; ENST00000404789; ENSP00000384190; ENSG00000155100.
DR GeneID; 51633; -.
DR KEGG; hsa:51633; -.
DR UCSC; uc003yeu.4; human.
DR CTD; 51633; -.
DR GeneCards; GC08P092082; -.
DR H-InvDB; HIX0201303; -.
DR HGNC; HGNC:24281; OTUD6B.
DR HPA; HPA024046; -.
DR HPA; HPA024503; -.
DR HPA; HPA024772; -.
DR MIM; 612021; gene.
DR neXtProt; NX_Q8N6M0; -.
DR PharmGKB; PA142671219; -.
DR eggNOG; COG5539; -.
DR HOGENOM; HOG000192906; -.
DR HOVERGEN; HBG080227; -.
DR InParanoid; Q8N6M0; -.
DR OrthoDB; EOG7WT42W; -.
DR GeneWiki; OTUD6B; -.
DR GenomeRNAi; 51633; -.
DR NextBio; 55561; -.
DR PRO; PR:Q8N6M0; -.
DR ArrayExpress; Q8N6M0; -.
DR Bgee; Q8N6M0; -.
DR CleanEx; HS_OTUD6B; -.
DR Genevestigator; Q8N6M0; -.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR003323; OTU.
DR Pfam; PF02338; OTU; 1.
DR PROSITE; PS50802; OTU; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Hydrolase; Polymorphism; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1 293 OTU domain-containing protein 6B.
FT /FTId=PRO_0000076279.
FT DOMAIN 147 284 OTU.
FT REGION 152 158 Cys-loop (By similarity).
FT REGION 219 229 Variable-loop (By similarity).
FT REGION 267 277 His-loop (By similarity).
FT ACT_SITE 155 155 By similarity.
FT ACT_SITE 158 158 Nucleophile (By similarity).
FT ACT_SITE 277 277 By similarity.
FT MOD_RES 1 1 N-acetylmethionine.
FT VARIANT 283 283 R -> Q (in dbSNP:rs3210518).
FT /FTId=VAR_034144.
FT CONFLICT 285 293 VNIVTENCS -> GKHSY (in Ref. 1; AAD34073).
SQ SEQUENCE 293 AA; 33813 MW; 468DB88E2637D869 CRC64;
MEAVLTEELD EEEQLLRRHR KEKKELQAKI QGMKNAVPKN DKKRRKQLTE DVAKLEKEME
QKHREELEQL KLTTKENKID SVAVNISNLV LENQPPRISK AQKRREKKAA LEKEREERIA
EAEIENLTGA RHMESEKLAQ ILAARQLEIK QIPSDGHCMY KAIEDQLKEK DCALTVVALR
SQTAEYMQSH VEDFLPFLTN PNTGDMYTPE EFQKYCEDIV NTAAWGGQLE LRALSHILQT
PIEIIQADSP PIIVGEEYSK KPLILVYMRH AYGLGEHYNS VTRLVNIVTE NCS
//
ID OTU6B_HUMAN Reviewed; 293 AA.
AC Q8N6M0; A8K6I1; Q9NTA4; Q9Y387;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2002, sequence version 1.
DT 22-JAN-2014, entry version 79.
DE RecName: Full=OTU domain-containing protein 6B;
DE EC=3.4.19.12;
DE AltName: Full=DUBA-5;
GN Name=OTUD6B; Synonyms=DUBA5; ORFNames=CGI-77;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 67-293, AND VARIANT GLN-283.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP IDENTIFICATION.
RX PubMed=23827681; DOI=10.1016/j.cell.2013.05.046;
RA Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M.,
RA Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F.,
RA Freund S.M., Ovaa H., Komander D.;
RT "OTU deubiquitinases reveal mechanisms of linkage specificity and
RT enable ubiquitin chain restriction analysis.";
RL Cell 154:169-184(2013).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC thioester, amide, peptide and isopeptide bonds formed by the C-
CC terminal Gly of ubiquitin (a 76-residue protein attached to
CC proteins as an intracellular targeting signal).
CC -!- MISCELLANEOUS: No deubiquitinase activity has been detected when
CC tested (PubMed:23827681). May require some post-translational
CC modification to be active.
CC -!- SIMILARITY: Contains 1 OTU domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF151836; AAD34073.1; -; mRNA.
DR EMBL; AK291646; BAF84335.1; -; mRNA.
DR EMBL; AC087439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029760; AAH29760.1; -; mRNA.
DR EMBL; AL137441; CAB70738.1; -; mRNA.
DR PIR; T46264; T46264.
DR RefSeq; NP_057107.3; NM_016023.3.
DR UniGene; Hs.30532; -.
DR ProteinModelPortal; Q8N6M0; -.
DR IntAct; Q8N6M0; 5.
DR STRING; 9606.ENSP00000285420; -.
DR PhosphoSite; Q8N6M0; -.
DR DMDM; 74729149; -.
DR PaxDb; Q8N6M0; -.
DR PRIDE; Q8N6M0; -.
DR DNASU; 51633; -.
DR Ensembl; ENST00000285420; ENSP00000285420; ENSG00000155100.
DR Ensembl; ENST00000404789; ENSP00000384190; ENSG00000155100.
DR GeneID; 51633; -.
DR KEGG; hsa:51633; -.
DR UCSC; uc003yeu.4; human.
DR CTD; 51633; -.
DR GeneCards; GC08P092082; -.
DR H-InvDB; HIX0201303; -.
DR HGNC; HGNC:24281; OTUD6B.
DR HPA; HPA024046; -.
DR HPA; HPA024503; -.
DR HPA; HPA024772; -.
DR MIM; 612021; gene.
DR neXtProt; NX_Q8N6M0; -.
DR PharmGKB; PA142671219; -.
DR eggNOG; COG5539; -.
DR HOGENOM; HOG000192906; -.
DR HOVERGEN; HBG080227; -.
DR InParanoid; Q8N6M0; -.
DR OrthoDB; EOG7WT42W; -.
DR GeneWiki; OTUD6B; -.
DR GenomeRNAi; 51633; -.
DR NextBio; 55561; -.
DR PRO; PR:Q8N6M0; -.
DR ArrayExpress; Q8N6M0; -.
DR Bgee; Q8N6M0; -.
DR CleanEx; HS_OTUD6B; -.
DR Genevestigator; Q8N6M0; -.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR003323; OTU.
DR Pfam; PF02338; OTU; 1.
DR PROSITE; PS50802; OTU; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Hydrolase; Polymorphism; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1 293 OTU domain-containing protein 6B.
FT /FTId=PRO_0000076279.
FT DOMAIN 147 284 OTU.
FT REGION 152 158 Cys-loop (By similarity).
FT REGION 219 229 Variable-loop (By similarity).
FT REGION 267 277 His-loop (By similarity).
FT ACT_SITE 155 155 By similarity.
FT ACT_SITE 158 158 Nucleophile (By similarity).
FT ACT_SITE 277 277 By similarity.
FT MOD_RES 1 1 N-acetylmethionine.
FT VARIANT 283 283 R -> Q (in dbSNP:rs3210518).
FT /FTId=VAR_034144.
FT CONFLICT 285 293 VNIVTENCS -> GKHSY (in Ref. 1; AAD34073).
SQ SEQUENCE 293 AA; 33813 MW; 468DB88E2637D869 CRC64;
MEAVLTEELD EEEQLLRRHR KEKKELQAKI QGMKNAVPKN DKKRRKQLTE DVAKLEKEME
QKHREELEQL KLTTKENKID SVAVNISNLV LENQPPRISK AQKRREKKAA LEKEREERIA
EAEIENLTGA RHMESEKLAQ ILAARQLEIK QIPSDGHCMY KAIEDQLKEK DCALTVVALR
SQTAEYMQSH VEDFLPFLTN PNTGDMYTPE EFQKYCEDIV NTAAWGGQLE LRALSHILQT
PIEIIQADSP PIIVGEEYSK KPLILVYMRH AYGLGEHYNS VTRLVNIVTE NCS
//
MIM
612021
*RECORD*
*FIELD* NO
612021
*FIELD* TI
*612021 OTU DOMAIN-CONTAINING PROTEIN 6B; OTUD6B
;;DUBA5
*FIELD* TX
DESCRIPTION
Deubiquitinating enzymes (DUBs; see 603478) are proteases that
read morespecifically cleave ubiquitin (191339) linkages, negating the action of
ubiquitin ligases. DUBA5 belongs to a DUB subfamily characterized by an
ovarian tumor (OTU) domain.
CLONING
Kayagaki et al. (2007) identified ovarian tumor domain (OTU)-containing
protein 6B (OTUD6B) in a small interfering RNA (siRNA)-based screen for
OTU deubiquitinating enzyme (DUB) family members. The 3,166-basepair
mRNA contains an open reading frame (ORF) predicting a 293-amino acid
protein.
MAPPING
The OTUD6B gene maps to chromosome 8q21.3 (Kayagaki et al., 2007).
*FIELD* RF
1. Kayagaki, N.; Phung, Q.; Chan, S.; Chaudhari, R.; Quan, C.; O'Rourke,
K. M.; Eby, M.; Pietras, E.; Cheng, G.; Bazan, J. F.; Zhang, Z.; Arnott,
D.; Dixit, V. M.: DUBA: a deubiquitinase that regulates type I interferon
production. Science 318: 1628-1632, 2007.
*FIELD* CD
Ada Hamosh: 5/6/2008
*FIELD* ED
alopez: 05/07/2008
alopez: 5/6/2008
*RECORD*
*FIELD* NO
612021
*FIELD* TI
*612021 OTU DOMAIN-CONTAINING PROTEIN 6B; OTUD6B
;;DUBA5
*FIELD* TX
DESCRIPTION
Deubiquitinating enzymes (DUBs; see 603478) are proteases that
read morespecifically cleave ubiquitin (191339) linkages, negating the action of
ubiquitin ligases. DUBA5 belongs to a DUB subfamily characterized by an
ovarian tumor (OTU) domain.
CLONING
Kayagaki et al. (2007) identified ovarian tumor domain (OTU)-containing
protein 6B (OTUD6B) in a small interfering RNA (siRNA)-based screen for
OTU deubiquitinating enzyme (DUB) family members. The 3,166-basepair
mRNA contains an open reading frame (ORF) predicting a 293-amino acid
protein.
MAPPING
The OTUD6B gene maps to chromosome 8q21.3 (Kayagaki et al., 2007).
*FIELD* RF
1. Kayagaki, N.; Phung, Q.; Chan, S.; Chaudhari, R.; Quan, C.; O'Rourke,
K. M.; Eby, M.; Pietras, E.; Cheng, G.; Bazan, J. F.; Zhang, Z.; Arnott,
D.; Dixit, V. M.: DUBA: a deubiquitinase that regulates type I interferon
production. Science 318: 1628-1632, 2007.
*FIELD* CD
Ada Hamosh: 5/6/2008
*FIELD* ED
alopez: 05/07/2008
alopez: 5/6/2008