UBP11_MOUSE
ID UBP11_MOUSE Reviewed; 921 AA.
AC Q99K46; B1AXB2; Q3TLG5;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 11;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:P51784};
DE AltName: Full=Deubiquitinating enzyme 11;
DE AltName: Full=Ubiquitin thioesterase 11;
DE AltName: Full=Ubiquitin-specific-processing protease 11;
GN Name=Usp11;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-367.
RC TISSUE=Mammary gland;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 125-921.
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;
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: Protease that can remove conjugated ubiquitin from target
CC proteins and polyubiquitin chains. Inhibits the degradation of target
CC proteins by the proteasome. Cleaves preferentially 'Lys-6' and 'Lys-
CC 63'-linked ubiquitin chains. Has lower activity with 'Lys-11' and 'Lys-
CC 33'-linked ubiquitin chains, and extremely low activity with 'Lys-27',
CC 'Lys-29' and 'Lys-48'-linked ubiquitin chains (in vitro). Plays a role
CC in the regulation of pathways leading to NF-kappa-B activation. Plays a
CC role in the regulation of DNA repair after double-stranded DNA breaks.
CC Acts as a chromatin regulator via its association with the Polycomb
CC group (PcG) multiprotein PRC1-like complex; may act by deubiquitinating
CC components of the PRC1-like complex. Promotes cell proliferation by
CC deubiquitinating phosphorylated E2F1. {ECO:0000250|UniProtKB:P51784}.
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:P51784};
CC -!- SUBUNIT: Monomer (By similarity). Associated component of the Polycomb
CC group (PcG) multiprotein PRC1-like complex (By similarity). Interacts
CC with RANBP9/RANBPM (By similarity). Interacts with BRCA2 (By
CC similarity). Interacts with CHUK/IKKA (By similarity). Interacts with
CC NFKBIA (By similarity). Interacts with SPRY3, RAE1, MYCBP2/PAM, and
CC KCTD6 (By similarity). {ECO:0000250|UniProtKB:P51784}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51784}. Cytoplasm
CC {ECO:0000250|UniProtKB:P51784}. Chromosome
CC {ECO:0000250|UniProtKB:P51784}. Note=Predominantly nuclear. Associates
CC with chromatin. {ECO:0000250|UniProtKB:P51784}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH05470.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK166523; BAE38827.1; -; mRNA.
DR EMBL; AL807240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466625; EDL00740.1; -; Genomic_DNA.
DR EMBL; BC005470; AAH05470.1; ALT_INIT; mRNA.
DR CCDS; CCDS53015.1; -.
DR RefSeq; NP_663603.3; NM_145628.4.
DR AlphaFoldDB; Q99K46; -.
DR SMR; Q99K46; -.
DR BioGRID; 231786; 2.
DR IntAct; Q99K46; 1.
DR STRING; 10090.ENSMUSP00000033383; -.
DR MEROPS; C19.014; -.
DR iPTMnet; Q99K46; -.
DR PhosphoSitePlus; Q99K46; -.
DR EPD; Q99K46; -.
DR MaxQB; Q99K46; -.
DR PaxDb; Q99K46; -.
DR PeptideAtlas; Q99K46; -.
DR PRIDE; Q99K46; -.
DR ProteomicsDB; 298408; -.
DR Antibodypedia; 25411; 307 antibodies from 37 providers.
DR DNASU; 236733; -.
DR Ensembl; ENSMUST00000033383; ENSMUSP00000033383; ENSMUSG00000031066.
DR GeneID; 236733; -.
DR KEGG; mmu:236733; -.
DR UCSC; uc009stq.3; mouse.
DR CTD; 8237; -.
DR MGI; MGI:2384312; Usp11.
DR VEuPathDB; HostDB:ENSMUSG00000031066; -.
DR eggNOG; KOG1870; Eukaryota.
DR GeneTree; ENSGT00940000160485; -.
DR HOGENOM; CLU_001060_7_1_1; -.
DR InParanoid; Q99K46; -.
DR OMA; TGQLVIM; -.
DR OrthoDB; 1283205at2759; -.
DR PhylomeDB; Q99K46; -.
DR TreeFam; TF106276; -.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 236733; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Usp11; mouse.
DR PRO; PR:Q99K46; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q99K46; protein.
DR Bgee; ENSMUSG00000031066; Expressed in dorsomedial nucleus of hypothalamus and 211 other tissues.
DR Genevisible; Q99K46; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:MGI.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.30.2230.10; -; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR028135; Ub_USP-typ.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF14836; Ubiquitin_3; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF143791; SSF143791; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS51283; DUSP; 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 Acetylation; Chromosome; Cytoplasm; Hydrolase; Nucleus; Phosphoprotein;
KW Protease; Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..921
FT /note="Ubiquitin carboxyl-terminal hydrolase 11"
FT /id="PRO_0000080633"
FT DOMAIN 28..133
FT /note="DUSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 257..889
FT /note="USP"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..622
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 266
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 847
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 194
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51784"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51784"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5D006"
FT MOD_RES 906
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51784"
FT CONFLICT 863
FT /note="F -> L (in Ref. 4; AAH05470)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 921 AA; 105384 MW; 269E4A3267B9EE1D CRC64;
MAAVAADPAA AAVPASAEDR DTQPEAMPDL DEQWRQIGNG RERPLRAGES WFLVEKHWYK
QWEVYVKGGD QDASTFPGCI NNAGLFEDQI SWHLRERLLE GDDYVLLPAP AWNYMVSWYG
LMDGQPPIER KVIELPGIRK VEVYPLELLL VQHSDMETAL TIQFSYTDSV ELVLQTAREQ
FLVEPQEDTR LWTKNSEGSL DRLCNTQITL LDACLETGQL VIMETRNKDG TWPSAQLCGM
NNIPDEDEDF QGQPGICGLT NLGNTCFMNS ALQCLSNVPQ LTEYFLNNRY LEELNFRNPL
GMKGELAEAY ADLVKQTWSG YHRSIVPNVF KNKVGHFASQ FLGYQQHDSQ ELLSFLLDGL
HEDLNRVKKK EYVELCNGAG RPDLEVAQEA WQNHKRRNDS VIVDTFHGLF KSTLVCPDCG
NVSVTFDPFC YLSVPLPVCS RRVLEVFFVP MDPRRKPEQH RVVVPKKGNI SDLCVALSTH
TSVAPDKMIV ADVFSHRFYK LYQLEDPLSG ILDRDDIFVY EVTGRIEPVE GSRDDIVVPV
YLRERTPSRD YNNSYYGLIL FGHPLLVSVP RDRFSWEGLY NILMYRLSRY VTKPTSDEDD
GDEKVDEDED EDVEDDSSSE EEKEEMSAPT VNDGTREAEQ EQAGTSSGVT ERCPSLLDNS
LRASQWPPRR RRKQLFTLQT VNSNGTSDRT TSPEEMQTQP YIAMDWEPDM KRRYYDEVEA
EGYVKHDCVG YMLKKSPVQL KECIKLFTTV ETLEKENPWY CSSCKQHQLA TKKLDLWMLP
EVLIIHLKRF SFSKISREKL DTLVQFPIRD LDFSEFVIKP KNESSPDLYK YDLIAVSNHY
GGMRDGHYTT FACNKDSGQW HYFDDNSVSP VNENQIESKA AYVLFYQRQD VGRRQSQTSS
SDTPASPVSS STPNSDIMDI N
