UBP11_HUMAN
ID UBP11_HUMAN Reviewed; 963 AA.
AC P51784; B2RTX1; Q8IUG6; Q9BWE1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 11;
DE EC=3.4.19.12 {ECO:0000269|PubMed:12084015, ECO:0000269|PubMed:24724799, ECO:0000269|PubMed:28992046};
DE AltName: Full=Deubiquitinating enzyme 11;
DE AltName: Full=Ubiquitin thioesterase 11;
DE AltName: Full=Ubiquitin-specific-processing protease 11;
GN Name=USP11; Synonyms=UHX1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 41-963, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH RANBP9.
RC TISSUE=Fetal brain;
RX PubMed=12084015; DOI=10.1042/bj20011851;
RA Ideguchi H., Ueda A., Tanaka M., Yang J., Tsuji T., Ohno S., Hagiwara E.,
RA Aoki A., Ishigatsubo Y.;
RT "Structural and functional characterization of the USP11 deubiquitinating
RT enzyme, which interacts with the RanGTP-associated protein RanBPM.";
RL Biochem. J. 367:87-95(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 52-963.
RC TISSUE=Retina;
RX PubMed=8845848; DOI=10.1093/hmg/5.4.533;
RA Swanson D.A., Freund C.L., Ploder L., McInnes R.R., Valle D.;
RT "A ubiquitin C-terminal hydrolase gene on the proximal short arm of the X
RT chromosome: implications for X-linked retinal disorders.";
RL Hum. Mol. Genet. 5:533-538(1996).
RN [5]
RP FUNCTION, INTERACTION WITH BRCA2, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP CYS-318, ACTIVE SITE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15314155; DOI=10.1128/mcb.24.17.7444-7455.2004;
RA Schoenfeld A.R., Apgar S., Dolios G., Wang R., Aaronson S.A.;
RT "BRCA2 is ubiquitinated in vivo and interacts with USP11, a
RT deubiquitinating enzyme that exhibits prosurvival function in the cellular
RT response to DNA damage.";
RL Mol. Cell. Biol. 24:7444-7455(2004).
RN [6]
RP FUNCTION, AND INTERACTION WITH CHUK.
RX PubMed=17897950; DOI=10.1074/jbc.m706282200;
RA Yamaguchi T., Kimura J., Miki Y., Yoshida K.;
RT "The deubiquitinating enzyme USP11 controls an IkappaB kinase alpha
RT (IKKalpha)-p53 signaling pathway in response to tumor necrosis factor alpha
RT (TNFalpha).";
RL J. Biol. Chem. 282:33943-33948(2007).
RN [7]
RP FUNCTION, AND INTERACTION WITH HUMAN PAPILLOMA VIRUS 16E7 (MICROBIAL
RP INFECTION).
RX PubMed=18408009; DOI=10.1074/jbc.m708278200;
RA Lin C.H., Chang H.S., Yu W.C.;
RT "USP11 stabilizes HPV-16E7 and further modulates the E7 biological
RT activity.";
RL J. Biol. Chem. 283:15681-15688(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-948, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-245, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP FUNCTION, INTERACTION WITH NFKBIA, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19874889; DOI=10.1016/j.cellsig.2009.10.008;
RA Sun W., Tan X., Shi Y., Xu G., Mao R., Gu X., Fan Y., Yu Y., Burlingame S.,
RA Zhang H., Rednam S.P., Lu X., Zhang T., Fu S., Cao G., Qin J., Yang J.;
RT "USP11 negatively regulates TNFalpha-induced NF-kappaB activation by
RT targeting on IkappaBalpha.";
RL Cell. Signal. 22:386-394(2010).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH THE PRC1-LIKE COMPLEX.
RX PubMed=20601937; DOI=10.1038/emboj.2010.129;
RA Maertens G.N., El Messaoudi-Aubert S., Elderkin S., Hiom K., Peters G.;
RT "Ubiquitin-specific proteases 7 and 11 modulate Polycomb regulation of the
RT INK4a tumour suppressor.";
RL EMBO J. 29:2553-2565(2010).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20233726; DOI=10.1074/jbc.m110.104745;
RA Wiltshire T.D., Lovejoy C.A., Wang T., Xia F., O'Connor M.J., Cortez D.;
RT "Sensitivity to poly(ADP-ribose) polymerase (PARP) inhibition identifies
RT ubiquitin-specific peptidase 11 (USP11) as a regulator of DNA double-strand
RT break repair.";
RL J. Biol. Chem. 285:14565-14571(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-948, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-318,
RP AND ACTIVE SITE.
RX PubMed=28992046; DOI=10.1093/jmcb/mjx034;
RA Wang D., Zhao J., Li S., Wei J., Nan L., Mallampalli R.K.,
RA Weathington N.M., Ma H., Zhao Y.;
RT "Phosphorylated E2F1 is stabilized by nuclear USP11 to drive Peg10 gene
RT expression and activate lung epithelial cells.";
RL J. Mol. Cell Biol. 10:60-73(2018).
RN [20]
RP INTERACTION WITH SPRY3; RAE1; MYCBP2 AND KCTD6.
RX PubMed=29293652; DOI=10.1371/journal.pone.0190513;
RA Stockum A., Snijders A.P., Maertens G.N.;
RT "USP11 deubiquitinates RAE1 and plays a key role in bipolar spindle
RT formation.";
RL PLoS ONE 13:e0190513-e0190513(2018).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 67-288, FUNCTION, CATALYTIC
RP ACTIVITY, AND SUBUNIT.
RX PubMed=24724799; DOI=10.1021/bi500116x;
RA Harper S., Gratton H.E., Cornaciu I., Oberer M., Scott D.J., Emsley J.,
RA Dreveny I.;
RT "Structure and catalytic regulatory function of ubiquitin specific protease
RT 11 N-terminal and ubiquitin-like domains.";
RL Biochemistry 53:2966-2978(2014).
CC -!- FUNCTION: Protease that can remove conjugated ubiquitin from target
CC proteins and polyubiquitin chains (PubMed:12084015, PubMed:15314155,
CC PubMed:17897950, PubMed:19874889, PubMed:20233726, PubMed:28992046,
CC PubMed:24724799). Inhibits the degradation of target proteins by the
CC proteasome (PubMed:12084015). 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)
CC (PubMed:24724799). Plays a role in the regulation of pathways leading
CC to NF-kappa-B activation (PubMed:17897950, PubMed:19874889). Plays a
CC role in the regulation of DNA repair after double-stranded DNA breaks
CC (PubMed:15314155, PubMed:20233726). Acts as a chromatin regulator via
CC its association with the Polycomb group (PcG) multiprotein PRC1-like
CC complex; may act by deubiquitinating components of the PRC1-like
CC complex (PubMed:20601937). Promotes cell proliferation by
CC deubiquitinating phosphorylated E2F1 (PubMed:28992046).
CC {ECO:0000269|PubMed:15314155, ECO:0000269|PubMed:17897950,
CC ECO:0000269|PubMed:18408009, ECO:0000269|PubMed:19874889,
CC ECO:0000269|PubMed:20233726, ECO:0000269|PubMed:24724799,
CC ECO:0000269|PubMed:28992046}.
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:0000269|PubMed:12084015,
CC ECO:0000269|PubMed:24724799, ECO:0000269|PubMed:28992046};
CC -!- SUBUNIT: Monomer (PubMed:24724799). Associated component of the
CC Polycomb group (PcG) multiprotein PRC1-like complex (PubMed:20601937).
CC Interacts with RANBP9/RANBPM (PubMed:12084015). Interacts with BRCA2
CC (PubMed:15314155). Interacts with CHUK/IKKA (PubMed:17897950).
CC Interacts with NFKBIA (PubMed:19874889). Interacts with SPRY3, RAE1,
CC MYCBP2/PAM, and KCTD6 (PubMed:29293652). {ECO:0000269|PubMed:12084015,
CC ECO:0000269|PubMed:15314155, ECO:0000269|PubMed:17897950,
CC ECO:0000269|PubMed:19874889, ECO:0000269|PubMed:20601937,
CC ECO:0000269|PubMed:24724799, ECO:0000269|PubMed:29293652}.
CC -!- SUBUNIT: (Microbial infection) Interacts with papilloma virus protein
CC 16E7 (PubMed:18408009). {ECO:0000269|PubMed:18408009}.
CC -!- INTERACTION:
CC P51784; P35226: BMI1; NbExp=7; IntAct=EBI-306876, EBI-2341576;
CC P51784; Q9HC52: CBX8; NbExp=5; IntAct=EBI-306876, EBI-712912;
CC P51784; Q9NUI1: DECR2; NbExp=3; IntAct=EBI-306876, EBI-3937367;
CC P51784; Q86YC2: PALB2; NbExp=2; IntAct=EBI-306876, EBI-1222653;
CC P51784; P35227: PCGF2; NbExp=5; IntAct=EBI-306876, EBI-2129767;
CC P51784; Q06587: RING1; NbExp=4; IntAct=EBI-306876, EBI-752313;
CC P51784; Q99496: RNF2; NbExp=4; IntAct=EBI-306876, EBI-722416;
CC P51784; P03129: E7; Xeno; NbExp=6; IntAct=EBI-306876, EBI-866453;
CC P51784; Q9DLK6: NP; Xeno; NbExp=3; IntAct=EBI-306876, EBI-8433218;
CC P51784; P15659: PA; Xeno; NbExp=2; IntAct=EBI-306876, EBI-8431752;
CC P51784; P04608: tat; Xeno; NbExp=3; IntAct=EBI-306876, EBI-6164389;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12084015,
CC ECO:0000269|PubMed:15314155, ECO:0000269|PubMed:20233726,
CC ECO:0000269|PubMed:28992046}. Cytoplasm {ECO:0000269|PubMed:15314155,
CC ECO:0000269|PubMed:28992046}. Chromosome {ECO:0000269|PubMed:20233726,
CC ECO:0000269|PubMed:20601937}. Note=Predominantly nuclear
CC (PubMed:12084015, PubMed:15314155). Associates with chromatin
CC (PubMed:20601937, PubMed:20233726). {ECO:0000269|PubMed:12084015,
CC ECO:0000269|PubMed:15314155, ECO:0000269|PubMed:20233726,
CC ECO:0000269|PubMed:20601937}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-44 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50450.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC50450.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC20463.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL096791; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC140849; AAI40850.1; -; mRNA.
DR EMBL; BC000350; AAH00350.4; -; mRNA.
DR EMBL; AB073597; BAC20463.1; ALT_INIT; mRNA.
DR EMBL; U44839; AAC50450.1; ALT_SEQ; mRNA.
DR RefSeq; NP_004642.2; NM_004651.3.
DR RefSeq; XP_005272731.1; XM_005272674.3.
DR RefSeq; XP_011542290.1; XM_011543988.1.
DR PDB; 4MEL; X-ray; 2.90 A; A/B=67-288.
DR PDB; 5OK6; X-ray; 1.30 A; A/B=67-288.
DR PDBsum; 4MEL; -.
DR PDBsum; 5OK6; -.
DR AlphaFoldDB; P51784; -.
DR SMR; P51784; -.
DR BioGRID; 113866; 383.
DR DIP; DIP-27567N; -.
DR IntAct; P51784; 135.
DR MINT; P51784; -.
DR STRING; 9606.ENSP00000218348; -.
DR BindingDB; P51784; -.
DR ChEMBL; CHEMBL4630820; -.
DR MEROPS; C19.014; -.
DR GlyGen; P51784; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P51784; -.
DR MetOSite; P51784; -.
DR PhosphoSitePlus; P51784; -.
DR BioMuta; USP11; -.
DR DMDM; 251757432; -.
DR EPD; P51784; -.
DR jPOST; P51784; -.
DR MassIVE; P51784; -.
DR MaxQB; P51784; -.
DR PaxDb; P51784; -.
DR PeptideAtlas; P51784; -.
DR PRIDE; P51784; -.
DR ProteomicsDB; 56381; -.
DR Antibodypedia; 25411; 307 antibodies from 37 providers.
DR DNASU; 8237; -.
DR Ensembl; ENST00000218348.7; ENSP00000218348.3; ENSG00000102226.10.
DR GeneID; 8237; -.
DR UCSC; uc064yux.1; human.
DR CTD; 8237; -.
DR DisGeNET; 8237; -.
DR GeneCards; USP11; -.
DR HGNC; HGNC:12609; USP11.
DR HPA; ENSG00000102226; Low tissue specificity.
DR MIM; 300050; gene.
DR neXtProt; NX_P51784; -.
DR OpenTargets; ENSG00000102226; -.
DR PharmGKB; PA37235; -.
DR VEuPathDB; HostDB:ENSG00000102226; -.
DR eggNOG; KOG1870; Eukaryota.
DR GeneTree; ENSGT00940000160485; -.
DR InParanoid; P51784; -.
DR OrthoDB; 1283205at2759; -.
DR PhylomeDB; P51784; -.
DR TreeFam; TF106276; -.
DR PathwayCommons; P51784; -.
DR Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR SignaLink; P51784; -.
DR BioGRID-ORCS; 8237; 8 hits in 755 CRISPR screens.
DR ChiTaRS; USP11; human.
DR GeneWiki; USP11; -.
DR GenomeRNAi; 8237; -.
DR Pharos; P51784; Tbio.
DR PRO; PR:P51784; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P51784; protein.
DR Bgee; ENSG00000102226; Expressed in right frontal lobe and 204 other tissues.
DR ExpressionAtlas; P51784; baseline and differential.
DR Genevisible; P51784; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:ARUK-UCL.
DR GO; GO:0016579; P:protein deubiquitination; IDA: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; IPR029346; USP_C.
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 Pfam; PF14533; USP7_C2; 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 3D-structure; Acetylation; Chromosome; Cytoplasm; Host-virus interaction;
KW Hydrolase; Nucleus; Phosphoprotein; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..963
FT /note="Ubiquitin carboxyl-terminal hydrolase 11"
FT /id="PRO_0000080632"
FT DOMAIN 76..184
FT /note="DUSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 309..930
FT /note="USP"
FT REGION 64..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..666
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 318
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:15314155,
FT ECO:0000305|PubMed:28992046"
FT ACT_SITE 888
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 245
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 733
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5D006"
FT MOD_RES 948
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MUTAGEN 318
FT /note="C->S: Loss of deubiquitinase activity."
FT /evidence="ECO:0000269|PubMed:15314155,
FT ECO:0000269|PubMed:28992046"
FT CONFLICT 52
FT /note="A -> AT (in Ref. 3; BAC20463)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="V -> M (in Ref. 4; AAC50450)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="A -> R (in Ref. 4; AAC50450)"
FT /evidence="ECO:0000305"
FT CONFLICT 82..83
FT /note="WR -> CG (in Ref. 4; AAC50450)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="A -> R (in Ref. 3; BAC20463)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="A -> R (in Ref. 3; BAC20463 and 4; AAC50450)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="P -> L (in Ref. 2; AAH00350)"
FT /evidence="ECO:0000305"
FT HELIX 78..86
FT /evidence="ECO:0007829|PDB:5OK6"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:5OK6"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:5OK6"
FT HELIX 107..117
FT /evidence="ECO:0007829|PDB:5OK6"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:4MEL"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:5OK6"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:5OK6"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:5OK6"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:5OK6"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:5OK6"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:5OK6"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:5OK6"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:5OK6"
FT STRAND 206..215
FT /evidence="ECO:0007829|PDB:5OK6"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:5OK6"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:5OK6"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:5OK6"
FT TURN 261..265
FT /evidence="ECO:0007829|PDB:5OK6"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:5OK6"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:5OK6"
SQ SEQUENCE 963 AA; 109817 MW; 876FDC41945AFD9B CRC64;
MAVAPRLFGG LCFRFRDQNP EVAVEGRLPI SHSCVGCRRE RTAMATVAAN PAAAAAAVAA
AAAVTEDREP QHEELPGLDS QWRQIENGES GRERPLRAGE SWFLVEKHWY KQWEAYVQGG
DQDSSTFPGC INNATLFQDE INWRLKEGLV EGEDYVLLPA AAWHYLVSWY GLEHGQPPIE
RKVIELPNIQ KVEVYPVELL LVRHNDLGKS HTVQFSHTDS IGLVLRTARE RFLVEPQEDT
RLWAKNSEGS LDRLYDTHIT VLDAALETGQ LIIMETRKKD GTWPSAQLHV MNNNMSEEDE
DFKGQPGICG LTNLGNTCFM NSALQCLSNV PQLTEYFLNN CYLEELNFRN PLGMKGEIAE
AYADLVKQAW SGHHRSIVPH VFKNKVGHFA SQFLGYQQHD SQELLSFLLD GLHEDLNRVK
KKEYVELCDA AGRPDQEVAQ EAWQNHKRRN DSVIVDTFHG LFKSTLVCPD CGNVSVTFDP
FCYLSVPLPI SHKRVLEVFF IPMDPRRKPE QHRLVVPKKG KISDLCVALS KHTGISPERM
MVADVFSHRF YKLYQLEEPL SSILDRDDIF VYEVSGRIEA IEGSREDIVV PVYLRERTPA
RDYNNSYYGL MLFGHPLLVS VPRDRFTWEG LYNVLMYRLS RYVTKPNSDD EDDGDEKEDD
EEDKDDVPGP STGGSLRDPE PEQAGPSSGV TNRCPFLLDN CLGTSQWPPR RRRKQLFTLQ
TVNSNGTSDR TTSPEEVHAQ PYIAIDWEPE MKKRYYDEVE AEGYVKHDCV GYVMKKAPVR
LQECIELFTT VETLEKENPW YCPSCKQHQL ATKKLDLWML PEILIIHLKR FSYTKFSREK
LDTLVEFPIR DLDFSEFVIQ PQNESNPELY KYDLIAVSNH YGGMRDGHYT TFACNKDSGQ
WHYFDDNSVS PVNENQIESK AAYVLFYQRQ DVARRLLSPA GSSGAPASPA CSSPPSSEFM
DVN
