UBP26_MOUSE
ID UBP26_MOUSE Reviewed; 835 AA.
AC Q99MX1; Q05A11;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 26;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 26;
DE AltName: Full=Ubiquitin thioesterase 26;
DE AltName: Full=Ubiquitin-specific-processing protease 26;
GN Name=Usp26;
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 [MRNA].
RC TISSUE=Testis;
RX PubMed=11279525; DOI=10.1038/86927;
RA Wang P.J., McCarrey J.R., Yang F., Page D.C.;
RT "An abundance of X-linked genes expressed in spermatogonia.";
RL Nat. Genet. 27:422-426(2001).
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 MRNA].
RC TISSUE=Brain;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Involved in the ubiquitin-dependent proteolytic pathway in
CC conjunction with the 26S proteasome. Deubiquitinates the androgen
CC receptor and regulates the androgen receptor signaling pathway.
CC {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 -!- SUBUNIT: Interacts with AR. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; AF285570; AAK31949.1; -; mRNA.
DR EMBL; AL662931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC125454; AAI25455.1; -; mRNA.
DR EMBL; BC132154; AAI32155.1; -; mRNA.
DR CCDS; CCDS30122.1; -.
DR RefSeq; NP_113565.2; NM_031388.2.
DR RefSeq; XP_017174134.1; XM_017318645.1.
DR AlphaFoldDB; Q99MX1; -.
DR SMR; Q99MX1; -.
DR BioGRID; 219948; 5.
DR STRING; 10090.ENSMUSP00000110519; -.
DR MEROPS; C19.045; -.
DR PhosphoSitePlus; Q99MX1; -.
DR PaxDb; Q99MX1; -.
DR PRIDE; Q99MX1; -.
DR ProteomicsDB; 298458; -.
DR DNASU; 83563; -.
DR Ensembl; ENSMUST00000069509; ENSMUSP00000069140; ENSMUSG00000055780.
DR Ensembl; ENSMUST00000114869; ENSMUSP00000110519; ENSMUSG00000055780.
DR GeneID; 83563; -.
DR KEGG; mmu:83563; -.
DR UCSC; uc009tec.1; mouse.
DR CTD; 83844; -.
DR MGI; MGI:1933247; Usp26.
DR VEuPathDB; HostDB:ENSMUSG00000055780; -.
DR eggNOG; KOG1868; Eukaryota.
DR GeneTree; ENSGT00940000161929; -.
DR HOGENOM; CLU_012557_0_0_1; -.
DR InParanoid; Q99MX1; -.
DR OMA; DAYDFER; -.
DR OrthoDB; 129045at2759; -.
DR PhylomeDB; Q99MX1; -.
DR TreeFam; TF323032; -.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 83563; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q99MX1; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q99MX1; protein.
DR Bgee; ENSMUSG00000055780; Expressed in spermatid and 6 other tissues.
DR Genevisible; Q99MX1; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; ISO:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd13312; PH_USP37_like; 1.
DR Gene3D; 2.30.29.180; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR032069; USP37-like_PH.
DR InterPro; IPR038093; USP37-like_PH_sf.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF16674; UCH_N; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Nucleus; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..835
FT /note="Ubiquitin carboxyl-terminal hydrolase 26"
FT /id="PRO_0000080656"
FT DOMAIN 286..816
FT /note="USP"
FT REGION 102..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..747
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 295
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 771
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT CONFLICT 746
FT /note="L -> F (in Ref. 1; AAK31949)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 835 AA; 95452 MW; E66CCCE3B3042998 CRC64;
MEPILINAQV QMWSAKAGMS KSRNALIETC VGKREVKLIL YFSTGKIKTL QLHDNIKSVV
LQTYGEDQNY LHLTFKNNDF LFVEKLTTTD ARRLKRFLDK TSQGSIRPAR SDERCGEPST
SAQELNGSGS SCETNSECFE SPKESEMCMF RELSLLPSSS TFLHNVGLLE NQFIKRKRFF
SDLAKNEKQS NLKDSIRDFE ANLVVCISNE KGKERNVREV DISKPGFGFP FETNYPEDSG
VDVRDLNDLI TKLFSPVLLE THCIENGLEW HEYMKTYLLY PEKLWQGLPN VGNTCYINVV
LQSLCSIPLF INDLFNQGFP WIKAPKDDFN MLLMQLLVLK DIYNARFRQK LLIGITKALP
IFGEIFAVDR QNDAHEFLSL CLVQLKETFQ RVTMMWQSEN DSGDFYLLKD IFADYATINK
MPVCPVTNNF EFELLSSIFC KACGLTLFKG EPSRYLSINI PQGGKDMSIQ STLDLFFSAE
ELEHRCEKCL YNKSVSFHRF GRLPRVIIVH LKRYHFNESW VMKKDERPIL VSKYLRLSCH
CSKSTKPPPP LRPGEHVKNL DLLKPLEVLG SEILKLPFNS VRTSRSKGFE TINITSNRES
EAQSGKRVSE VLSGKVQQEN SGKGDTAHIV GSELTKETEK LKKHEEEHRP SDLDSGSIRE
AQKYQQAEKC NEGRSDKQIS LEALTQSRPK PISQEQTENL GKTTLSHTQD SSQSSQSSSD
SSKSSRCSDD LDKKAKPTRK VDPTKLNKKE DNVYRLVNII NHIGNSPNGG HYINDAFDFK
RQSWFTYSDL HVTRTQEDFV YRGRSSTGYV FFYMHNDIFE ELLAKETQST STSKG
