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   24-JAN-2024, entry version 164.
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; 3.
DR   IntAct; Q99K46; 1.
DR   STRING; 10090.ENSMUSP00000033383; -.
DR   MEROPS; C19.014; -.
DR   GlyGen; Q99K46; 4 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; Q99K46; -.
DR   PhosphoSitePlus; Q99K46; -.
DR   SwissPalm; Q99K46; -.
DR   EPD; Q99K46; -.
DR   MaxQB; Q99K46; -.
DR   PaxDb; 10090-ENSMUSP00000033383; -.
DR   PeptideAtlas; Q99K46; -.
DR   ProteomicsDB; 298408; -.
DR   Pumba; Q99K46; -.
DR   Antibodypedia; 25411; 351 antibodies from 37 providers.
DR   DNASU; 236733; -.
DR   Ensembl; ENSMUST00000033383.3; ENSMUSP00000033383.3; ENSMUSG00000031066.11.
DR   GeneID; 236733; -.
DR   KEGG; mmu:236733; -.
DR   UCSC; uc009stq.3; mouse.
DR   AGR; MGI:2384312; -.
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; 5474185at2759; -.
DR   PhylomeDB; Q99K46; -.
DR   TreeFam; TF106276; -.
DR   Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR   BioGRID-ORCS; 236733; 0 hits in 78 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 214 other cell types or tissues.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02674; Peptidase_C19R; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   Gene3D; 3.30.2230.10; DUSP-like; 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   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF29; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 11; 1.
DR   Pfam; PF06337; DUSP; 1.
DR   Pfam; PF14836; Ubiquitin_3; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00695; DUSP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 1.
DR   PROSITE; PS51283; DUSP; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   Genevisible; Q99K46; MM.
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
//