Full text data of USP11
USP11
(UHX1)
[Confidence: low (only semi-automatic identification from reviews)]
Ubiquitin carboxyl-terminal hydrolase 11; 3.4.19.12 (Deubiquitinating enzyme 11; Ubiquitin thioesterase 11; Ubiquitin-specific-processing protease 11)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ubiquitin carboxyl-terminal hydrolase 11; 3.4.19.12 (Deubiquitinating enzyme 11; Ubiquitin thioesterase 11; Ubiquitin-specific-processing protease 11)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P51784
ID UBP11_HUMAN Reviewed; 963 AA.
AC P51784; B2RTX1; Q8IUG6; Q9BWE1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-JUL-2009, sequence version 3.
DT 22-JAN-2014, entry version 136.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 11;
DE EC=3.4.19.12;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA 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.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA 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.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA 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.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA 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.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., 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
RT project: 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.,
RA Hagiwara E., Aoki A., Ishigatsubo Y.;
RT "Structural and functional characterization of the USP11
RT deubiquitinating enzyme, which interacts with the RanGTP-associated
RT 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
RT the X 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, AND 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
RT cellular 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
RT alpha (TNFalpha).";
RL J. Biol. Chem. 282:33943-33948(2007).
RN [7]
RP FUNCTION, AND INTERACTION WITH HUMAN PAPILLOMA VIRUS 16E7.
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 MASS
RP SPECTROMETRY.
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 MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 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.,
RA Burlingame S., Zhang H., Rednam S.P., Lu X., Zhang T., Fu S., Cao G.,
RA 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, 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.,
RA Cortez D.;
RT "Sensitivity to poly(ADP-ribose) polymerase (PARP) inhibition
RT identifies ubiquitin-specific peptidase 11 (USP11) as a regulator of
RT DNA double-strand break repair.";
RL J. Biol. Chem. 285:14565-14571(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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.,
RA Buerckstuemmer T., 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Protease that can remove conjugated ubiquitin from
CC target proteins and polyubiquitin chains. Inhibits the degradation
CC of target proteins by the proteasome. Plays a role in the
CC regulation of pathways leading to NF-kappa-B activation. Plays a
CC role in the regulation of DNA repair after double-stranded DNA
CC breaks.
CC -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC thioester, amide, peptide and isopeptide bonds formed by the C-
CC terminal Gly of ubiquitin (a 76-residue protein attached to
CC proteins as an intracellular targeting signal).
CC -!- SUBUNIT: Interacts with RANBP9/RANBPM. Interacts with BRCA2,
CC CHUK/IKKA and NFKBIA. Interacts with papilloma virus protein 16E7.
CC -!- INTERACTION:
CC P35226:BMI1; NbExp=7; IntAct=EBI-306876, EBI-2341576;
CC Q9HC52:CBX8; NbExp=5; IntAct=EBI-306876, EBI-712912;
CC P03129:E7 (xeno); NbExp=6; IntAct=EBI-306876, EBI-866453;
CC Q9DLK6:NP (xeno); NbExp=3; IntAct=EBI-306876, EBI-8433218;
CC P15659:PA (xeno); NbExp=2; IntAct=EBI-306876, EBI-8431752;
CC P35227:PCGF2; NbExp=5; IntAct=EBI-306876, EBI-2129767;
CC Q06587:RING1; NbExp=4; IntAct=EBI-306876, EBI-752313;
CC Q99496:RNF2; NbExp=4; IntAct=EBI-306876, EBI-722416;
CC P04608:tat (xeno); NbExp=3; IntAct=EBI-306876, EBI-6164389;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly
CC nuclear. Associates with chromatin.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC -!- SIMILARITY: Contains 1 DUSP domain.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-44 is the initiator.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50450.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAC50450.1; Type=Frameshift; Positions=65, 117, 134, 146;
CC Sequence=BAC20463.1; Type=Erroneous initiation;
CC Sequence=CAD20056.1; Type=Erroneous gene model prediction;
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DR EMBL; AL096791; CAD20056.1; ALT_SEQ; 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_005272674.1.
DR UniGene; Hs.171501; -.
DR ProteinModelPortal; P51784; -.
DR SMR; P51784; 96-284, 305-491, 779-931.
DR DIP; DIP-27567N; -.
DR IntAct; P51784; 79.
DR MINT; MINT-1147600; -.
DR STRING; 9606.ENSP00000218348; -.
DR MEROPS; C19.014; -.
DR PhosphoSite; P51784; -.
DR DMDM; 251757432; -.
DR PaxDb; P51784; -.
DR PRIDE; P51784; -.
DR Ensembl; ENST00000218348; ENSP00000218348; ENSG00000102226.
DR GeneID; 8237; -.
DR KEGG; hsa:8237; -.
DR UCSC; uc004dhp.3; human.
DR CTD; 8237; -.
DR GeneCards; GC0XP047093; -.
DR HGNC; HGNC:12609; USP11.
DR HPA; HPA003103; -.
DR HPA; HPA037536; -.
DR MIM; 300050; gene.
DR neXtProt; NX_P51784; -.
DR PharmGKB; PA37235; -.
DR eggNOG; COG5560; -.
DR HOGENOM; HOG000264375; -.
DR HOVERGEN; HBG000864; -.
DR InParanoid; P51784; -.
DR KO; K11835; -.
DR OMA; GQPGICG; -.
DR PhylomeDB; P51784; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; USP11; human.
DR GeneWiki; USP11; -.
DR GenomeRNAi; 8237; -.
DR NextBio; 30985; -.
DR PRO; PR:P51784; -.
DR ArrayExpress; P51784; -.
DR Bgee; P51784; -.
DR CleanEx; HS_USP11; -.
DR Genevestigator; P51784; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:ProtInc.
DR GO; GO:0004843; F:deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:InterPro.
DR GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR InterPro; IPR001394; Peptidase_C19/C67.
DR InterPro; IPR028135; Ub_USP-typ.
DR InterPro; IPR028134; USP.
DR PANTHER; PTHR24006:SF34; PTHR24006:SF34; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF14836; Ubiquitin_3; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS00972; UCH_2_1; 1.
DR PROSITE; PS00973; UCH_2_2; 1.
DR PROSITE; PS50235; UCH_2_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Hydrolase; Nucleus;
KW Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1 963 Ubiquitin carboxyl-terminal hydrolase 11.
FT /FTId=PRO_0000080632.
FT DOMAIN 76 184 DUSP.
FT ACT_SITE 318 318 Nucleophile.
FT ACT_SITE 888 888 Proton acceptor (By similarity).
FT MOD_RES 245 245 N6-acetyllysine.
FT MOD_RES 648 648 Phosphoserine.
FT MOD_RES 948 948 Phosphoserine.
FT MUTAGEN 318 318 C->S: Loss of deubiquitinase activity.
FT CONFLICT 52 52 A -> AT (in Ref. 3; BAC20463).
FT CONFLICT 58 58 V -> M (in Ref. 4; AAC50450).
FT CONFLICT 62 62 A -> R (in Ref. 4; AAC50450).
FT CONFLICT 82 83 WR -> CG (in Ref. 4; AAC50450).
FT CONFLICT 160 160 A -> R (in Ref. 3; BAC20463).
FT CONFLICT 161 161 A -> R (in Ref. 3; BAC20463 and 4;
FT AAC50450).
FT CONFLICT 489 489 P -> L (in Ref. 2; AAH00350).
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
//
ID UBP11_HUMAN Reviewed; 963 AA.
AC P51784; B2RTX1; Q8IUG6; Q9BWE1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-JUL-2009, sequence version 3.
DT 22-JAN-2014, entry version 136.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 11;
DE EC=3.4.19.12;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA 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.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA 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.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA 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.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA 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.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., 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
RT project: 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.,
RA Hagiwara E., Aoki A., Ishigatsubo Y.;
RT "Structural and functional characterization of the USP11
RT deubiquitinating enzyme, which interacts with the RanGTP-associated
RT 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
RT the X 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, AND 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
RT cellular 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
RT alpha (TNFalpha).";
RL J. Biol. Chem. 282:33943-33948(2007).
RN [7]
RP FUNCTION, AND INTERACTION WITH HUMAN PAPILLOMA VIRUS 16E7.
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 MASS
RP SPECTROMETRY.
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 MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 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.,
RA Burlingame S., Zhang H., Rednam S.P., Lu X., Zhang T., Fu S., Cao G.,
RA 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, 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.,
RA Cortez D.;
RT "Sensitivity to poly(ADP-ribose) polymerase (PARP) inhibition
RT identifies ubiquitin-specific peptidase 11 (USP11) as a regulator of
RT DNA double-strand break repair.";
RL J. Biol. Chem. 285:14565-14571(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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.,
RA Buerckstuemmer T., 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Protease that can remove conjugated ubiquitin from
CC target proteins and polyubiquitin chains. Inhibits the degradation
CC of target proteins by the proteasome. Plays a role in the
CC regulation of pathways leading to NF-kappa-B activation. Plays a
CC role in the regulation of DNA repair after double-stranded DNA
CC breaks.
CC -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC thioester, amide, peptide and isopeptide bonds formed by the C-
CC terminal Gly of ubiquitin (a 76-residue protein attached to
CC proteins as an intracellular targeting signal).
CC -!- SUBUNIT: Interacts with RANBP9/RANBPM. Interacts with BRCA2,
CC CHUK/IKKA and NFKBIA. Interacts with papilloma virus protein 16E7.
CC -!- INTERACTION:
CC P35226:BMI1; NbExp=7; IntAct=EBI-306876, EBI-2341576;
CC Q9HC52:CBX8; NbExp=5; IntAct=EBI-306876, EBI-712912;
CC P03129:E7 (xeno); NbExp=6; IntAct=EBI-306876, EBI-866453;
CC Q9DLK6:NP (xeno); NbExp=3; IntAct=EBI-306876, EBI-8433218;
CC P15659:PA (xeno); NbExp=2; IntAct=EBI-306876, EBI-8431752;
CC P35227:PCGF2; NbExp=5; IntAct=EBI-306876, EBI-2129767;
CC Q06587:RING1; NbExp=4; IntAct=EBI-306876, EBI-752313;
CC Q99496:RNF2; NbExp=4; IntAct=EBI-306876, EBI-722416;
CC P04608:tat (xeno); NbExp=3; IntAct=EBI-306876, EBI-6164389;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly
CC nuclear. Associates with chromatin.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC -!- SIMILARITY: Contains 1 DUSP domain.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-44 is the initiator.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50450.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAC50450.1; Type=Frameshift; Positions=65, 117, 134, 146;
CC Sequence=BAC20463.1; Type=Erroneous initiation;
CC Sequence=CAD20056.1; Type=Erroneous gene model prediction;
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DR EMBL; AL096791; CAD20056.1; ALT_SEQ; 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_005272674.1.
DR UniGene; Hs.171501; -.
DR ProteinModelPortal; P51784; -.
DR SMR; P51784; 96-284, 305-491, 779-931.
DR DIP; DIP-27567N; -.
DR IntAct; P51784; 79.
DR MINT; MINT-1147600; -.
DR STRING; 9606.ENSP00000218348; -.
DR MEROPS; C19.014; -.
DR PhosphoSite; P51784; -.
DR DMDM; 251757432; -.
DR PaxDb; P51784; -.
DR PRIDE; P51784; -.
DR Ensembl; ENST00000218348; ENSP00000218348; ENSG00000102226.
DR GeneID; 8237; -.
DR KEGG; hsa:8237; -.
DR UCSC; uc004dhp.3; human.
DR CTD; 8237; -.
DR GeneCards; GC0XP047093; -.
DR HGNC; HGNC:12609; USP11.
DR HPA; HPA003103; -.
DR HPA; HPA037536; -.
DR MIM; 300050; gene.
DR neXtProt; NX_P51784; -.
DR PharmGKB; PA37235; -.
DR eggNOG; COG5560; -.
DR HOGENOM; HOG000264375; -.
DR HOVERGEN; HBG000864; -.
DR InParanoid; P51784; -.
DR KO; K11835; -.
DR OMA; GQPGICG; -.
DR PhylomeDB; P51784; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; USP11; human.
DR GeneWiki; USP11; -.
DR GenomeRNAi; 8237; -.
DR NextBio; 30985; -.
DR PRO; PR:P51784; -.
DR ArrayExpress; P51784; -.
DR Bgee; P51784; -.
DR CleanEx; HS_USP11; -.
DR Genevestigator; P51784; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:ProtInc.
DR GO; GO:0004843; F:deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:InterPro.
DR GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR InterPro; IPR001394; Peptidase_C19/C67.
DR InterPro; IPR028135; Ub_USP-typ.
DR InterPro; IPR028134; USP.
DR PANTHER; PTHR24006:SF34; PTHR24006:SF34; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF14836; Ubiquitin_3; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS00972; UCH_2_1; 1.
DR PROSITE; PS00973; UCH_2_2; 1.
DR PROSITE; PS50235; UCH_2_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Hydrolase; Nucleus;
KW Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1 963 Ubiquitin carboxyl-terminal hydrolase 11.
FT /FTId=PRO_0000080632.
FT DOMAIN 76 184 DUSP.
FT ACT_SITE 318 318 Nucleophile.
FT ACT_SITE 888 888 Proton acceptor (By similarity).
FT MOD_RES 245 245 N6-acetyllysine.
FT MOD_RES 648 648 Phosphoserine.
FT MOD_RES 948 948 Phosphoserine.
FT MUTAGEN 318 318 C->S: Loss of deubiquitinase activity.
FT CONFLICT 52 52 A -> AT (in Ref. 3; BAC20463).
FT CONFLICT 58 58 V -> M (in Ref. 4; AAC50450).
FT CONFLICT 62 62 A -> R (in Ref. 4; AAC50450).
FT CONFLICT 82 83 WR -> CG (in Ref. 4; AAC50450).
FT CONFLICT 160 160 A -> R (in Ref. 3; BAC20463).
FT CONFLICT 161 161 A -> R (in Ref. 3; BAC20463 and 4;
FT AAC50450).
FT CONFLICT 489 489 P -> L (in Ref. 2; AAH00350).
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
//
MIM
300050
*RECORD*
*FIELD* NO
300050
*FIELD* TI
*300050 UBIQUITIN-SPECIFIC PROTEASE 11; USP11
;;UBIQUITIN CARBOXYL-TERMINAL HYDROLASE, X-LINKED; UHX1
read more*FIELD* TX
CLONING
Swanson et al. (1996) used a differential hybridization screen to
isolate a novel cDNA, designated UHX1, from a human retina library. The
cDNA encodes a protein of 690 amino acids that shows strong homology to
the proteins encoded by a variety of ubiquitin hydrolases (p values
ranging between 2.4e-265 and 1.4e-13).
GENE FUNCTION
Swanson et al. (1996) reviewed the role of ubiquitination in protein
degradation and presented evidence that disturbances in protein
processing and turnover can lead to retinal degeneration. They noted
that there are at least 4 X-linked retinal diseases that map to a region
within or overlapping the UHX1 interval (see MAPPING). They cited
evidence indicating that ubiquitin hydrolases play a role in oncogenesis
(oncogenes and tumor suppressor gene products are degraded in
ubiquitin-dependent pathways) and that the region of loss of
heterozygosity in ovarian cancer lies within the mapping interval
defined for UHX1.
MAPPING
Swanson et al. (1996) mapped the structural gene encoding this cDNA,
which they designated UHX1, to Xp21.2-p11.2 by somatic cell
hybridization. By genomic sequence analysis, Stoddart et al. (1999)
mapped the UHX1 gene to Xp11.3.
*FIELD* RF
1. Stoddart, K. L.; Jermak, C.; Nagaraja, R.; Schlessinger, D.; Bech-Hansen,
N. T.: Physical map covering a 2 Mb region in human Xp11.3 distal
to DX6849. Gene 227: 111-116, 1999.
2. Swanson, D. A.; Freund, C. L.; Ploder, L.; McInnes, R. R.; Valle,
D.: A ubiquitin C-terminal hydrolase gene on the proximal short arm
of the X chromosome: implications for X-linked retinal disorders. Hum.
Molec. Genet. 5: 533-538, 1996.
*FIELD* CN
Carol A. Bocchini - updated: 8/3/1999
*FIELD* CD
Moyra Smith: 4/30/1996
*FIELD* ED
carol: 01/16/2014
terry: 8/3/1999
carol: 8/3/1999
alopez: 2/5/1999
carol: 5/12/1996
carol: 5/3/1996
*RECORD*
*FIELD* NO
300050
*FIELD* TI
*300050 UBIQUITIN-SPECIFIC PROTEASE 11; USP11
;;UBIQUITIN CARBOXYL-TERMINAL HYDROLASE, X-LINKED; UHX1
read more*FIELD* TX
CLONING
Swanson et al. (1996) used a differential hybridization screen to
isolate a novel cDNA, designated UHX1, from a human retina library. The
cDNA encodes a protein of 690 amino acids that shows strong homology to
the proteins encoded by a variety of ubiquitin hydrolases (p values
ranging between 2.4e-265 and 1.4e-13).
GENE FUNCTION
Swanson et al. (1996) reviewed the role of ubiquitination in protein
degradation and presented evidence that disturbances in protein
processing and turnover can lead to retinal degeneration. They noted
that there are at least 4 X-linked retinal diseases that map to a region
within or overlapping the UHX1 interval (see MAPPING). They cited
evidence indicating that ubiquitin hydrolases play a role in oncogenesis
(oncogenes and tumor suppressor gene products are degraded in
ubiquitin-dependent pathways) and that the region of loss of
heterozygosity in ovarian cancer lies within the mapping interval
defined for UHX1.
MAPPING
Swanson et al. (1996) mapped the structural gene encoding this cDNA,
which they designated UHX1, to Xp21.2-p11.2 by somatic cell
hybridization. By genomic sequence analysis, Stoddart et al. (1999)
mapped the UHX1 gene to Xp11.3.
*FIELD* RF
1. Stoddart, K. L.; Jermak, C.; Nagaraja, R.; Schlessinger, D.; Bech-Hansen,
N. T.: Physical map covering a 2 Mb region in human Xp11.3 distal
to DX6849. Gene 227: 111-116, 1999.
2. Swanson, D. A.; Freund, C. L.; Ploder, L.; McInnes, R. R.; Valle,
D.: A ubiquitin C-terminal hydrolase gene on the proximal short arm
of the X chromosome: implications for X-linked retinal disorders. Hum.
Molec. Genet. 5: 533-538, 1996.
*FIELD* CN
Carol A. Bocchini - updated: 8/3/1999
*FIELD* CD
Moyra Smith: 4/30/1996
*FIELD* ED
carol: 01/16/2014
terry: 8/3/1999
carol: 8/3/1999
alopez: 2/5/1999
carol: 5/12/1996
carol: 5/3/1996