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OTUD1_MOUSE
ID   OTUD1_MOUSE             Reviewed;         454 AA.
AC   Q9CUB6; A2ATK4;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=OTU domain-containing protein 1;
DE            EC=3.4.19.12;
GN   Name=Otud1;
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 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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 232-454.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen;
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).
CC   -!- FUNCTION: Deubiquitinating enzyme that specifically hydrolyzes 'Lys-
CC       63'-linked polyubiquitin to monoubiquitin. {ECO:0000250}.
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;
CC   -!- DOMAIN: The UIM repeat increases the specificity and efficiency of the
CC       enzyme toward 'Lys-63'-linked polyubiquitin. {ECO:0000250}.
CC   -!- DOMAIN: Specificity is not given by the S1' ubiquitin-binding site
CC       within the OTU domain (composed of the Cys-, His- and Variable-loops).
CC       {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB30530.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AL928877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK016972; BAB30530.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS50508.1; -.
DR   RefSeq; NP_081991.1; NM_027715.1.
DR   AlphaFoldDB; Q9CUB6; -.
DR   SMR; Q9CUB6; -.
DR   STRING; 10090.ENSMUSP00000100617; -.
DR   MEROPS; C85.004; -.
DR   iPTMnet; Q9CUB6; -.
DR   PhosphoSitePlus; Q9CUB6; -.
DR   EPD; Q9CUB6; -.
DR   jPOST; Q9CUB6; -.
DR   MaxQB; Q9CUB6; -.
DR   PaxDb; Q9CUB6; -.
DR   PRIDE; Q9CUB6; -.
DR   ProteomicsDB; 294405; -.
DR   Antibodypedia; 51774; 82 antibodies from 14 providers.
DR   Ensembl; ENSMUST00000052168; ENSMUSP00000100617; ENSMUSG00000043415.
DR   GeneID; 71198; -.
DR   KEGG; mmu:71198; -.
DR   UCSC; uc008imj.2; mouse.
DR   CTD; 220213; -.
DR   MGI; MGI:1918448; Otud1.
DR   VEuPathDB; HostDB:ENSMUSG00000043415; -.
DR   eggNOG; KOG2605; Eukaryota.
DR   GeneTree; ENSGT00510000049635; -.
DR   HOGENOM; CLU_044163_0_0_1; -.
DR   InParanoid; Q9CUB6; -.
DR   OMA; RGGDRCD; -.
DR   OrthoDB; 955020at2759; -.
DR   PhylomeDB; Q9CUB6; -.
DR   TreeFam; TF338508; -.
DR   BioGRID-ORCS; 71198; 1 hit in 74 CRISPR screens.
DR   ChiTaRS; Otud1; mouse.
DR   PRO; PR:Q9CUB6; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q9CUB6; protein.
DR   Bgee; ENSMUSG00000043415; Expressed in ascending aorta and 203 other tissues.
DR   Genevisible; Q9CUB6; MM.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR   GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR   GO; GO:0070536; P:protein K63-linked 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   Hydrolase; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN           1..454
FT                   /note="OTU domain-containing protein 1"
FT                   /id="PRO_0000271019"
FT   DOMAIN          282..411
FT                   /note="OTU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT   DOMAIN          430..449
FT                   /note="UIM"
FT                   /evidence="ECO:0000305"
FT   REGION          36..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          116..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..293
FT                   /note="Cys-loop"
FT                   /evidence="ECO:0000250"
FT   REGION          342..352
FT                   /note="His-loop"
FT                   /evidence="ECO:0000250"
FT   REGION          399..404
FT                   /note="Variable-loop"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        193..207
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        290
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        293
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        404
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   454 AA;  48823 MW;  BAF1702C35D1EF89 CRC64;
     MQLYSSVCTH YPAGTPGPTA AAPPATAAAA FKVSLQSASP AAAAPEPDTG ERPPAAATEP
     REAAAAAAMP AFSACFERSG SAAAPPGACS KPPLPPHFTS TAHIAVRALG AERLLLPPPS
     APSPPRRGSS AWLLEELLRP DEPAAPNAVR DAPDRNFRLS EHRQALAASQ HRAPAPAPVG
     PEPGAGPGSG PWGEERRAER SSRGWDRASG RSDASGSDAL RRQDPEAEAH PVPAPARSSG
     EPAQNGEGEA VGTSRADPRD EKLALYLAEV ERQDKYLRQR NKYRFHIIPD GNCLYRAVSK
     TVYGDQSLHR ELREQTVHYI ADHLDHFSPL IEGDVGEFII AAAQDGAWAG YPELLAMGQM
     LNVNIHLTTG GRLESPTVST MIHYLGPEDS LRPSIWLSWL SNGHYDAVFD HSYPNPEYDN
     WCKQTQIQKK RDEELAKSMA ISLSKMYIEQ NACS
 
 
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