OTU6B_MOUSE
ID OTU6B_MOUSE Reviewed; 294 AA.
AC Q8K2H2; A2AP24; Q3T9X5; Q3U1R9;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Deubiquitinase OTUD6B {ECO:0000305};
DE AltName: Full=OTU domain-containing protein 6B {ECO:0000312|MGI:MGI:1919451};
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q8N6M0};
GN Name=Otud6b {ECO:0000312|MGI:MGI:1919451};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Liver, Mammary gland, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Embryo, and Mammary tumor;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP TISSUE SPECIFICITY, AND INDUCTION BY CYTOKINES.
RX PubMed=21267069; DOI=10.1371/journal.pone.0014514;
RA Xu Z., Zheng Y., Zhu Y., Kong X., Hu L.;
RT "Evidence for OTUD-6B participation in B lymphocytes cell cycle after
RT cytokine stimulation.";
RL PLoS ONE 6:E14514-E14514(2011).
RN [7]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=28343629; DOI=10.1016/j.ajhg.2017.03.001;
RG EuroEPINOMICS RES Consortium Autosomal Recessive working group, S. Hande Caglayan;
RA Santiago-Sim T., Burrage L.C., Ebstein F., Tokita M.J., Miller M., Bi W.,
RA Braxton A.A., Rosenfeld J.A., Shahrour M., Lehmann A., Cogne B., Kuery S.,
RA Besnard T., Isidor B., Bezieau S., Hazart I., Nagakura H., Immken L.L.,
RA Littlejohn R.O., Roeder E., Kara B., Hardies K., Weckhuysen S., May P.,
RA Lemke J.R., Elpeleg O., Abu-Libdeh B., James K.N., Silhavy J.L., Issa M.Y.,
RA Zaki M.S., Gleeson J.G., Seavitt J.R., Dickinson M.E., Ljungberg M.C.,
RA Wells S., Johnson S.J., Teboul L., Eng C.M., Yang Y., Kloetzel P.M.,
RA Heaney J.D., Walkiewicz M.A.;
RT "Biallelic variants in OTUD6B cause an intellectual disability syndrome
RT associated with seizures and dysmorphic features.";
RL Am. J. Hum. Genet. 100:676-688(2017).
CC -!- FUNCTION: Deubiquitinating enzyme that may play a role in the
CC ubiquitin-dependent regulation of protein synthesis, downstream of
CC mTORC1 (By similarity). May associate with the protein synthesis
CC initiation complex and modify its ubiquitination to repress translation
CC (By similarity). May also repress DNA synthesis and modify different
CC cellular targets thereby regulating cell growth and proliferation (By
CC similarity). May also play a role in proteasome assembly and function
CC (By similarity). {ECO:0000250|UniProtKB:Q8N6M0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q8N6M0};
CC -!- SUBUNIT: Interacts with the eukaryotic translation initiation factor 4F
CC complex. {ECO:0000250|UniProtKB:Q8N6M0}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expression is observed in
CC several organ systems including the cardiovascular, digestive, central
CC and peripheral nervous and musculoskeletal systems.
CC {ECO:0000269|PubMed:21267069, ECO:0000269|PubMed:28343629}.
CC -!- INDUCTION: Up-regulated by cytokines but followed by a rapid decline in
CC B lymphocytes. {ECO:0000269|PubMed:21267069}.
CC -!- DISRUPTION PHENOTYPE: Mice are sub-viable and die between embryonic day
CC 18.5 and shortly after birth. They show intrauterine growth retardation
CC and a high percentage of ventricular septal cardiac defects.
CC {ECO:0000269|PubMed:28343629}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK155761; BAE33424.1; -; mRNA.
DR EMBL; AK169134; BAE40913.1; -; mRNA.
DR EMBL; AK166445; BAE38781.1; -; mRNA.
DR EMBL; AK172229; BAE42895.1; -; mRNA.
DR EMBL; AK172338; BAE42955.1; -; mRNA.
DR EMBL; AL831792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466538; EDL05608.1; -; Genomic_DNA.
DR EMBL; BC031474; AAH31474.1; -; mRNA.
DR EMBL; BC087552; AAH87552.1; -; mRNA.
DR CCDS; CCDS17980.3; -.
DR RefSeq; NP_690025.2; NM_152812.3.
DR AlphaFoldDB; Q8K2H2; -.
DR SMR; Q8K2H2; -.
DR BioGRID; 215215; 7.
DR STRING; 10090.ENSMUSP00000113553; -.
DR MEROPS; C85.009; -.
DR iPTMnet; Q8K2H2; -.
DR PhosphoSitePlus; Q8K2H2; -.
DR EPD; Q8K2H2; -.
DR MaxQB; Q8K2H2; -.
DR PaxDb; Q8K2H2; -.
DR PeptideAtlas; Q8K2H2; -.
DR PRIDE; Q8K2H2; -.
DR ProteomicsDB; 294403; -.
DR Antibodypedia; 12759; 160 antibodies from 24 providers.
DR DNASU; 72201; -.
DR Ensembl; ENSMUST00000117268; ENSMUSP00000113553; ENSMUSG00000040550.
DR GeneID; 72201; -.
DR KEGG; mmu:72201; -.
DR CTD; 51633; -.
DR MGI; MGI:1919451; Otud6b.
DR VEuPathDB; HostDB:ENSMUSG00000040550; -.
DR eggNOG; KOG2606; Eukaryota.
DR GeneTree; ENSGT00390000012840; -.
DR InParanoid; Q8K2H2; -.
DR OrthoDB; 1541668at2759; -.
DR TreeFam; TF315010; -.
DR BioGRID-ORCS; 72201; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Otud6b; mouse.
DR PRO; PR:Q8K2H2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8K2H2; protein.
DR Bgee; ENSMUSG00000040550; Expressed in ectoplacental cone and 97 other tissues.
DR ExpressionAtlas; Q8K2H2; baseline and differential.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; ISO:MGI.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; ISO:MGI.
DR GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR GO; GO:0045727; P:positive regulation of translation; ISO:MGI.
DR GO; GO:0043248; P:proteasome assembly; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR Pfam; PF02338; OTU; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50802; OTU; 1.
PE 1: Evidence at protein level;
KW Acetylation; Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..294
FT /note="Deubiquitinase OTUD6B"
FT /id="PRO_0000076280"
FT DOMAIN 148..285
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT REGION 153..159
FT /note="Cys-loop"
FT /evidence="ECO:0000250"
FT REGION 220..230
FT /note="Variable-loop"
FT /evidence="ECO:0000250"
FT REGION 268..278
FT /note="His-loop"
FT /evidence="ECO:0000250"
FT ACT_SITE 156
FT /evidence="ECO:0000250"
FT ACT_SITE 159
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8N6M0"
FT ACT_SITE 278
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6M0"
FT CONFLICT 53
FT /note="A -> T (in Ref. 1; BAE33424)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="T -> S (in Ref. 1; BAE42955/BAE42895/BAE38781 and 3;
FT EDL05608)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 294 AA; 33758 MW; 024FB22EF139F517 CRC64;
MEEVVAEELD DEEQLVRRHR KEKKELQAKI QGMKNAVPKN DKKRRKQLTE DVAKLEREME
QKHREELEQL KQLTFKDSKI DSVAVNISNL VLENQPPRIS KAQKRREKKA ALEKEREERI
AEAEIENLSG ARHLESEKLA QILAARELEI KQIPSDGHCM YGALEDQLRE QDCALTVASL
RRQTAEYMQT HSDDFLPFLT NPSTGDMYTP EEFGKYCDDI VNTAAWGGQL ELRALSHILQ
TPIEILQADA PPIIVGEEYP RNPLVLVYMR HAYGLGEHYN SVTRLVNSAT ENCS
