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Ubiquitin carboxyl-terminal hydrolase 7 (EC 3.4.19.12) (Deubiquitinating enzyme 7) (Herpesvirus-associated ubiquitin-specific protease) (Ubiquitin thioesterase 7) (Ubiquitin-specific-processing protease 7)

 UBP7_HUMAN              Reviewed;        1102 AA.
Q93009; A6NMY8; B7Z815; H0Y3G8;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
04-NOV-2008, sequence version 2.
27-SEP-2017, entry version 193.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 7;
EC=3.4.19.12 {ECO:0000269|PubMed:11923872, ECO:0000269|PubMed:12507430, ECO:0000269|PubMed:14506283, ECO:0000269|PubMed:15053880, ECO:0000269|PubMed:16964248, ECO:0000269|PubMed:18716620, ECO:0000269|PubMed:21745816};
AltName: Full=Deubiquitinating enzyme 7;
AltName: Full=Herpesvirus-associated ubiquitin-specific protease;
AltName: Full=Ubiquitin thioesterase 7;
AltName: Full=Ubiquitin-specific-processing protease 7;
Name=USP7; Synonyms=HAUSP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE,
CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
HERPESVIRUS 1 TRANS-ACTING TRANSCRIPTIONAL PROTEIN ICP0/VMW110.
TISSUE=Mammary cancer;
PubMed=9034339; DOI=10.1093/emboj/16.3.566;
Everett R.D., Meredith M., Orr A., Cross A., Kathoria M.,
Parkinson J.;
"A novel ubiquitin-specific protease is dynamically associated with
the PML nuclear domain and binds to a herpesvirus regulatory
protein.";
EMBO J. 16:566-577(1997).
[2]
ERRATUM.
PubMed=9130697; DOI=10.1093/emboj/16.7.1519;
Everett R.D., Meredith M., Orr A., Cross A., Kathoria M.,
Parkinson J.;
EMBO J. 16:1519-1530(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 705-1102 (ISOFORM 1), SUBCELLULAR
LOCATION, AND INTERACTION WITH ATXN1.
PubMed=12093161; DOI=10.1006/mcne.2002.1103;
Hong S., Kim S.J., Ka S., Choi I., Kang S.;
"USP7, a ubiquitin-specific protease, interacts with ataxin-1, the
SCA1 gene product.";
Mol. Cell. Neurosci. 20:298-306(2002).
[7]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH TP53, MUTAGENESIS OF
CYS-223, AND ACTIVE SITE.
PubMed=11923872; DOI=10.1038/nature737;
Li M., Chen D., Shiloh A., Luo J., Nikolaev A.Y., Qin J., Gu W.;
"Deubiquitination of p53 by HAUSP is an important pathway for p53
stabilization.";
Nature 416:648-653(2002).
[8]
FUNCTION (MICROBIAL INFECTION), SUBUNIT, BIOPHYSICOCHEMICAL
PROPERTIES, ENZYME REGULATION, INTERACTION WITH HERPESVIRUS 1
TRANS-ACTING TRANSCRIPTIONAL PROTEIN ICP0/VMW110 AND EBV EBNA1
(MICROBIAL INFECTION), AND REGION.
PubMed=14506283; DOI=10.1074/jbc.M307200200;
Holowaty M.N., Sheng Y., Nguyen T., Arrowsmith C., Frappier L.;
"Protein interaction domains of the ubiquitin-specific protease,
USP7/HAUSP.";
J. Biol. Chem. 278:47753-47761(2003).
[9]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH MDM2, MUTAGENESIS OF
CYS-223, AND ACTIVE SITE.
PubMed=15053880; DOI=10.1016/S1097-2765(04)00157-1;
Li M., Brooks C.L., Kon N., Gu W.;
"A dynamic role of HAUSP in the p53-Mdm2 pathway.";
Mol. Cell 13:879-886(2004).
[10]
FUNCTION (MICROBIAL INFECTION), UBIQUITINATION, AND INTERACTION WITH
HERPESVIRUS 1 TRANS-ACTING TRANSCRIPTIONAL PROTEIN ICP0/VMW110
(MICROBIAL INFECTION).
PubMed=16160161; DOI=10.1128/JVI.79.19.12342-12354.2005;
Boutell C., Canning M., Orr A., Everett R.D.;
"Reciprocal activities between herpes simplex virus type 1 regulatory
protein ICP0, a ubiquitin E3 ligase, and ubiquitin-specific protease
USP7.";
J. Virol. 79:12342-12354(2005).
[11]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH DAXX AND MDM2, INTERACTION
WITH DAXX, AND SUBCELLULAR LOCATION.
PubMed=16845383; DOI=10.1038/ncb1442;
Tang J., Qu L.K., Zhang J., Wang W., Michaelson J.S., Degenhardt Y.Y.,
El-Deiry W.S., Yang X.;
"Critical role for Daxx in regulating Mdm2.";
Nat. Cell Biol. 8:855-862(2006).
[12]
FUNCTION, INTERACTION WITH FOXO4, MUTAGENESIS OF CYS-223, AND
CATALYTIC ACTIVITY.
PubMed=16964248; DOI=10.1038/ncb1469;
van der Horst A., de Vries-Smits A.M., Brenkman A.B., van Triest M.H.,
van den Broek N., Colland F., Maurice M.M., Burgering B.M.;
"FOXO4 transcriptional activity is regulated by monoubiquitination and
USP7/HAUSP.";
Nat. Cell Biol. 8:1064-1073(2006).
[13]
SUBUNIT, PHOSPHORYLATION AT SER-18 AND SER-963, UBIQUITINATION AT
LYS-869, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=17651432; DOI=10.1111/j.1742-4658.2007.05952.x;
Fernandez-Montalvan A., Bouwmeester T., Joberty G., Mader R.,
Mahnke M., Pierrat B., Schlaeppi J.M., Worpenberg S., Gerhartz B.;
"Biochemical characterization of USP7 reveals post-translational
modification sites and structural requirements for substrate
processing and subcellular localization.";
FEBS J. 274:4256-4270(2007).
[14]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH DAXX; RASSF1 AND MDM2, AND
INTERACTION WITH DAXX AND MDM2.
PubMed=18566590; DOI=10.1038/emboj.2008.115;
Song M.S., Song S.J., Kim S.Y., Oh H.J., Lim D.S.;
"The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by
disrupting the MDM2-DAXX-HAUSP complex.";
EMBO J. 27:1863-1874(2008).
[15]
RETRACTION, AND CAUTION.
PubMed=18768758; DOI=10.1091/mbc.E08-01-0067;
Zweitzig D.R., Shcherbik N., Haines D.S.;
"AAA ATPase p97 and adaptor UBXD1 suppress MDM2 ubiquitination and
degradation and promote constitutive p53 turnover.";
Mol. Biol. Cell 19:5029-5029(2008).
[16]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PTEN, MUTAGENESIS OF
CYS-223, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=18716620; DOI=10.1038/nature07290;
Song M.S., Salmena L., Carracedo A., Egia A., Lo-Coco F.,
Teruya-Feldstein J., Pandolfi P.P.;
"The deubiquitinylation and localization of PTEN are regulated by a
HAUSP-PML network.";
Nature 455:813-817(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-963, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HERPESVIRUS 1
TRANS-ACTING TRANSCRIPTIONAL PROTEIN ICP0/VMW110 (MICROBIAL
INFECTION), SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY,
AND ALTERNATIVE SPLICING (ISOFORM 2).
PubMed=18590780; DOI=10.1016/j.virusres.2008.05.017;
Antrobus R., Boutell C.;
"Identification of a novel higher molecular weight isoform of
USP7/HAUSP that interacts with the Herpes simplex virus type-1
immediate early protein ICP0.";
Virus Res. 137:64-71(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-869; LYS-1084 AND LYS-1096,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[21]
FUNCTION.
PubMed=20153724; DOI=10.1016/j.bbrc.2010.02.051;
Tang J., Qu L., Pang M., Yang X.;
"Daxx is reciprocally regulated by Mdm2 and Hausp.";
Biochem. Biophys. Res. Commun. 393:542-545(2010).
[22]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH THE PRC1-LIKE
COMPLEX.
PubMed=20601937; DOI=10.1038/emboj.2010.129;
Maertens G.N., El Messaoudi-Aubert S., Elderkin S., Hiom K.,
Peters G.;
"Ubiquitin-specific proteases 7 and 11 modulate Polycomb regulation of
the INK4a tumour suppressor.";
EMBO J. 29:2553-2565(2010).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[25]
INTERACTION WITH TSPYL5.
PubMed=21170034; DOI=10.1038/ncb2142;
Epping M.T., Meijer L.A., Krijgsman O., Bos J.L., Pandolfi P.P.,
Bernards R.;
"TSPYL5 suppresses p53 levels and function by physical interaction
with USP7.";
Nat. Cell Biol. 13:102-108(2011).
[26]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH DNMT1 AND UHRF1,
MUTAGENESIS OF CYS-223, AND ACTIVE SITE.
PubMed=21745816; DOI=10.1093/nar/gkr528;
Felle M., Joppien S., Nemeth A., Diermeier S., Thalhammer V.,
Dobner T., Kremmer E., Kappler R., Langst G.;
"The USP7/Dnmt1 complex stimulates the DNA methylation activity of
Dnmt1 and regulates the stability of UHRF1.";
Nucleic Acids Res. 39:8355-8365(2011).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[28]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH UHRF1, MUTAGENESIS OF
CYS-223, AND ACTIVE SITE.
PubMed=22411829; DOI=10.1073/pnas.1116349109;
Ma H., Chen H., Guo X., Wang Z., Sowa M.E., Zheng L., Hu S., Zeng P.,
Guo R., Diao J., Lan F., Harper J.W., Shi Y.G., Xu Y., Shi Y.;
"M phase phosphorylation of the epigenetic regulator UHRF1 regulates
its physical association with the deubiquitylase USP7 and stability.";
Proc. Natl. Acad. Sci. U.S.A. 109:4828-4833(2012).
[29]
FUNCTION, AND LINKAGE SPECIFICITY.
PubMed=22689415; DOI=10.1002/cbic.201200261;
Iphofer A., Kummer A., Nimtz M., Ritter A., Arnold T., Frank R.,
van den Heuvel J., Kessler B.M., Jansch L., Franke R.;
"Profiling ubiquitin linkage specificities of deubiquitinating enzymes
with branched ubiquitin isopeptide probes.";
ChemBioChem 13:1416-1420(2012).
[30]
INTERACTION WITH MEX3C.
PubMed=22863774; DOI=10.1038/emboj.2012.218;
Cano F., Bye H., Duncan L.M., Buchet-Poyau K., Billaud M., Wills M.R.,
Lehner P.J.;
"The RNA-binding E3 ubiquitin ligase MEX-3C links ubiquitination with
MHC-I mRNA degradation.";
EMBO J. 31:3596-3606(2012).
[31]
FUNCTION, AND INTERACTION WITH UVSSA.
PubMed=22466611; DOI=10.1038/ng.2230;
Schwertman P., Lagarou A., Dekkers D.H., Raams A., van der Hoek A.C.,
Laffeber C., Hoeijmakers J.H., Demmers J.A., Fousteri M.,
Vermeulen W., Marteijn J.A.;
"UV-sensitive syndrome protein UVSSA recruits USP7 to regulate
transcription-coupled repair.";
Nat. Genet. 44:598-602(2012).
[32]
FUNCTION, AND INTERACTION WITH UVSSA.
PubMed=22466612; DOI=10.1038/ng.2228;
Zhang X., Horibata K., Saijo M., Ishigami C., Ukai A., Kanno S.I.,
Tahara H., Neilan E.G., Honma M., Nohmi T., Yasui A., Tanaka K.;
"Mutations in UVSSA cause UV-sensitive syndrome and destabilize ERCC6
in transcription-coupled DNA repair.";
Nat. Genet. 44:593-597(2012).
[33]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION,
INTERACTION WITH FOXP3, AND INDUCTION.
PubMed=23973222; DOI=10.1016/j.immuni.2013.05.018;
van Loosdregt J., Fleskens V., Fu J., Brenkman A.B., Bekker C.P.,
Pals C.E., Meerding J., Berkers C.R., Barbi J., Grone A., Sijts A.J.,
Maurice M.M., Kalkhoven E., Prakken B.J., Ovaa H., Pan F., Zaiss D.M.,
Coffer P.J.;
"Stabilization of the transcription factor Foxp3 by the deubiquitinase
USP7 increases Treg-cell-suppressive capacity.";
Immunity 39:259-271(2013).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[36]
INTERACTION WITH RNF220.
PubMed=25266658; DOI=10.1128/MCB.00731-14;
Ma P., Yang X., Kong Q., Li C., Yang S., Li Y., Mao B.;
"The ubiquitin ligase RNF220 enhances canonical Wnt signaling through
USP7-mediated deubiquitination of beta-catenin.";
Mol. Cell. Biol. 34:4355-4366(2014).
[37]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH ABRAXAS2 AND TP53, AND
SUBCELLULAR LOCATION.
PubMed=25283148; DOI=10.1038/ncomms6059;
Zhang J., Cao M., Dong J., Li C., Xu W., Zhan Y., Wang X., Yu M.,
Ge C., Ge Z., Yang X.;
"ABRO1 suppresses tumourigenesis and regulates the DNA damage response
by stabilizing p53.";
Nat. Commun. 5:5059-5059(2014).
[38]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-869, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[39]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-869 AND LYS-882, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[40]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 208-560 IN COMPLEX WITH
UBIQUITIN, CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF CYS-223;
HIS-456 AND HIS-464, AND INTERACTION WITH TP53.
PubMed=12507430; DOI=10.1016/S0092-8674(02)01199-6;
Hu M., Li P., Li M., Li W., Yao T., Wu J.-W., Gu W., Cohen R.E.,
Shi Y.;
"Crystal structure of a UBP-family deubiquitinating enzyme in
isolation and in complex with ubiquitin aldehyde.";
Cell 111:1041-1054(2002).
[41]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 54-205 IN COMPLEX WITH EBNA1,
AND INTERACTION WITH EBV EBNA1.
PubMed=15808506; DOI=10.1016/j.molcel.2005.02.029;
Saridakis V., Sheng Y., Sarkari F., Holowaty M.N., Shire K.,
Nguyen T., Zhang R.G., Liao J., Lee W., Edwards A.M., Arrowsmith C.H.,
Frappier L.;
"Structure of the p53 binding domain of HAUSP/USP7 bound to Epstein-
Barr nuclear antigen 1 implications for EBV-mediated
immortalization.";
Mol. Cell 18:25-36(2005).
[42]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 43-560 IN COMPLEX WITH TP53
AND MDM2, AND INTERACTION WITH TP53 AND MDM2.
PubMed=16402859; DOI=10.1371/journal.pbio.0040027;
Hu M., Gu L., Li M., Jeffrey P.D., Gu W., Shi Y.;
"Structural basis of competitive recognition of p53 and MDM2 by
HAUSP/USP7: implications for the regulation of the p53-MDM2 pathway.";
PLoS Biol. 4:228-239(2006).
[43]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 54-205 IN COMPLEX WITH TP53
AND MDM2, INTERACTION WITH TP53 AND MDM2, AND MUTAGENESIS OF ASP-164
AND TRP-165.
PubMed=16474402; DOI=10.1038/nsmb1067;
Sheng Y., Saridakis V., Sarkari F., Duan S., Wu T., Arrowsmith C.H.,
Frappier L.;
"Molecular recognition of p53 and MDM2 by USP7/HAUSP.";
Nat. Struct. Mol. Biol. 13:285-291(2006).
-!- FUNCTION: Hydrolase that deubiquitinates target proteins such as
FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN and DAXX
(PubMed:11923872, PubMed:15053880, PubMed:16964248,
PubMed:18716620, PubMed:25283148). Together with DAXX, prevents
MDM2 self-ubiquitination and enhances the E3 ligase activity of
MDM2 towards p53/TP53, thereby promoting p53/TP53 ubiquitination
and proteasomal degradation (PubMed:15053880, PubMed:16845383,
PubMed:18566590, PubMed:20153724). Deubiquitinates p53/TP53,
preventing degradation of p53/TP53, and enhances p53/TP53-
dependent transcription regulation, cell growth repression and
apoptosis (PubMed:25283148). Deubiquitinates p53/TP53 and MDM2 and
strongly stabilizes p53/TP53 even in the presence of excess MDM2,
and also induces p53/TP53-dependent cell growth repression and
apoptosis (PubMed:11923872). Deubiquitination of FOXO4 in presence
of hydrogen peroxide is not dependent on p53/TP53 and inhibits
FOXO4-induced transcriptional activity (PubMed:16964248). In
association with DAXX, is involved in the deubiquitination and
translocation of PTEN from the nucleus to the cytoplasm, both
processes that are counteracted by PML (PubMed:18716620). Involved
in cell proliferation during early embryonic development. Involved
in transcription-coupled nucleotide excision repair (TC-NER) in
response to UV damage: recruited to DNA damage sites following
interaction with KIAA1530/UVSSA and promotes deubiquitination of
ERCC6, preventing UV-induced degradation of ERCC6
(PubMed:22466611, PubMed:22466612). Involved in maintenance of DNA
methylation via its interaction with UHRF1 and DNMT1: acts by
mediating deubiquitination of UHRF1 and DNMT1, preventing their
degradation and promoting DNA methylation by DNMT1
(PubMed:21745816, PubMed:22411829). Acts as a chromatin regulator
via its association with the Polycomb group (PcG) multiprotein
PRC1-like complex; may act by deubiquitinating components of the
PRC1-like complex (PubMed:20601937). Able to mediate
deubiquitination of histone H2B; it is however unsure whether this
activity takes place in vivo (PubMed:20601937). Exhibits a
preference towards 'Lys-48'-linked ubiquitin chains
(PubMed:22689415). Increases regulatory T-cells (Treg) suppressive
capacity by deubiquitinating and stabilizing the transcription
factor FOXP3 which is crucial for Treg cell function
(PubMed:23973222). {ECO:0000269|PubMed:11923872,
ECO:0000269|PubMed:15053880, ECO:0000269|PubMed:16845383,
ECO:0000269|PubMed:16964248, ECO:0000269|PubMed:18566590,
ECO:0000269|PubMed:18716620, ECO:0000269|PubMed:20153724,
ECO:0000269|PubMed:20601937, ECO:0000269|PubMed:21745816,
ECO:0000269|PubMed:22411829, ECO:0000269|PubMed:22466611,
ECO:0000269|PubMed:22466612, ECO:0000269|PubMed:22689415,
ECO:0000269|PubMed:23973222, ECO:0000269|PubMed:25283148}.
-!- FUNCTION: (Microbial infection) Contributes to the overall
stabilization and trans-activation capability of the herpesvirus 1
trans-acting transcriptional protein ICP0/VMW110 during HSV-1
infection. {ECO:0000269|PubMed:14506283,
ECO:0000269|PubMed:16160161, ECO:0000269|PubMed:18590780}.
-!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
thioester, amide, peptide and isopeptide bonds formed by the C-
terminal Gly of ubiquitin (a 76-residue protein attached to
proteins as an intracellular targeting signal).
{ECO:0000269|PubMed:11923872, ECO:0000269|PubMed:12507430,
ECO:0000269|PubMed:14506283, ECO:0000269|PubMed:15053880,
ECO:0000269|PubMed:16964248, ECO:0000269|PubMed:18716620,
ECO:0000269|PubMed:21745816}.
-!- ENZYME REGULATION: Inhibited by N-ethyl-maleimide (NEM) and
divalent cations. Tolerates high concentrations of NaCl but is
inhibited at concentrations of 195 mM and higher.
{ECO:0000269|PubMed:14506283}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Active from pH 7.0 to 9.5. {ECO:0000269|PubMed:14506283};
-!- SUBUNIT: Monomer. Homodimer. Part of a complex with DAXX, MDM2,
RASSF1 and USP7 (PubMed:18566590). Part of a complex with DAXX,
MDM2 and USP7 (PubMed:16845383). Interacts with MDM2; the
interaction is independent of p53/TP53. Interacts with DAXX; the
interaction is direct and independent of MDM2 and p53/TP53
(PubMed:16845383). Interacts with FOXO4; the interaction is
enhanced in presence of hydrogen peroxide and occurs independently
of p53/TP53 (PubMed:16964248). Interacts with p53/TP53; the
interaction is enhanced in response to DNA damage
(PubMed:25283148). Interacts with TSPYL5; this impairs interaction
with p53/TP53 (PubMed:21170034). Interacts with PTEN; the
interaction is direct (PubMed:18716620). Interacts with ATXN1 and
the strength of interaction is influenced by the length of the
poly-Gln region in ATXN1. A weaker interaction seen with mutants
having longer poly-Gln regions (PubMed:12093161). Interacts with
KIAA1530/UVSSA (PubMed:22466611, PubMed:22466612). Interacts with
ABRAXAS2; the interaction is direct (PubMed:25283148). Identified
in a complex with TP53/p53 and ABRAXAS2 (PubMed:25283148).
Interacts with MEX3C and antagonizes its ability to degrade mRNA
(PubMed:22863774). Interacts with DNMT1 and UHRF1
(PubMed:21745816). Interacts with FOXP3 (PubMed:23973222).
Interacts (via MATH domain) with RNF220 (PubMed:25266658).
Associated component of the Polycomb group (PcG) multiprotein
PRC1-like complex (PubMed:20601937). Interacts with EPOP (By
similarity). {ECO:0000250|UniProtKB:Q6A4J8,
ECO:0000269|PubMed:11923872, ECO:0000269|PubMed:12093161,
ECO:0000269|PubMed:12507430, ECO:0000269|PubMed:14506283,
ECO:0000269|PubMed:15053880, ECO:0000269|PubMed:15808506,
ECO:0000269|PubMed:16402859, ECO:0000269|PubMed:16474402,
ECO:0000269|PubMed:16845383, ECO:0000269|PubMed:16964248,
ECO:0000269|PubMed:17651432, ECO:0000269|PubMed:18566590,
ECO:0000269|PubMed:18716620, ECO:0000269|PubMed:20601937,
ECO:0000269|PubMed:21170034, ECO:0000269|PubMed:21745816,
ECO:0000269|PubMed:22411829, ECO:0000269|PubMed:22466611,
ECO:0000269|PubMed:22466612, ECO:0000269|PubMed:22863774,
ECO:0000269|PubMed:23973222, ECO:0000269|PubMed:25266658,
ECO:0000269|PubMed:25283148}.
-!- SUBUNIT: (Microbial infection) Isoform 1 and isoform 2 interact
with herpesvirus 1 trans-acting transcriptional protein
ICP0/VMW110 (PubMed:9034339, PubMed:14506283, PubMed:16160161,
PubMed:18590780). Interacts with Epstein-Barr virus EBNA1
(PubMed:14506283). EBNA1 shows a 10-fold higher affinity than
p53/TP53 and can compete with it for USP7 binding
(PubMed:14506283). Binding to ICP0/VMW110 may modulate the
substrate specificity or activity of USP7 to stabilize viral
proteins. {ECO:0000269|PubMed:14506283,
ECO:0000269|PubMed:16160161, ECO:0000269|PubMed:18590780,
ECO:0000269|PubMed:9034339}.
-!- INTERACTION:
Q6W2J9:BCOR; NbExp=3; IntAct=EBI-302474, EBI-950027;
P35226:BMI1; NbExp=7; IntAct=EBI-302474, EBI-2341576;
Q9HC52:CBX8; NbExp=7; IntAct=EBI-302474, EBI-712912;
Q9UER7:DAXX; NbExp=13; IntAct=EBI-302474, EBI-77321;
P03211:EBNA1 (xeno); NbExp=7; IntAct=EBI-302474, EBI-996522;
P08393:ICP0 (xeno); NbExp=3; IntAct=EBI-302474, EBI-6148881;
Q77UV9:KIE-2 (xeno); NbExp=2; IntAct=EBI-302474, EBI-2608731;
P21145:MAL; NbExp=3; IntAct=EBI-302474, EBI-3932027;
Q00987:MDM2; NbExp=18; IntAct=EBI-302474, EBI-389668;
O15151:MDM4; NbExp=15; IntAct=EBI-302474, EBI-398437;
O35618:Mdm4 (xeno); NbExp=4; IntAct=EBI-302474, EBI-2603376;
Q5U5Q3:MEX3C; NbExp=3; IntAct=EBI-302474, EBI-2864451;
Q99836:MYD88; NbExp=3; IntAct=EBI-302474, EBI-447677;
P35227:PCGF2; NbExp=5; IntAct=EBI-302474, EBI-2129767;
P06400:RB1; NbExp=8; IntAct=EBI-302474, EBI-491274;
Q06587:RING1; NbExp=5; IntAct=EBI-302474, EBI-752313;
Q99496:RNF2; NbExp=5; IntAct=EBI-302474, EBI-722416;
P84022:SMAD3; NbExp=2; IntAct=EBI-302474, EBI-347161;
Q99426:TBCB; NbExp=2; IntAct=EBI-302474, EBI-764356;
P04637:TP53; NbExp=21; IntAct=EBI-302474, EBI-366083;
Q86VY4:TSPYL5; NbExp=4; IntAct=EBI-302474, EBI-3436472;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23973222,
ECO:0000269|PubMed:25283148}. Cytoplasm
{ECO:0000269|PubMed:25283148}. Nucleus, PML body
{ECO:0000269|PubMed:9034339}. Chromosome
{ECO:0000269|PubMed:20601937}. Note=Present in a minority of ND10
nuclear bodies. Association with ICP0/VMW110 at early times of
infection leads to an increased proportion of USP7-containing
ND10. Colocalizes with ATXN1 in the nucleus. Colocalized with DAXX
in speckled structures. Colocalized with PML and PTEN in
promyelocytic leukemia protein (PML) nuclear bodies.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q93009-1; Sequence=Displayed;
Name=2; Synonyms=USP7 beta;
IsoId=Q93009-2; Sequence=Not described;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q93009-3; Sequence=VSP_054884;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Overexpressed in prostate
cancer. {ECO:0000269|PubMed:18716620}.
-!- INDUCTION: Up-regulated in regulatory T-cells (Treg).
{ECO:0000269|PubMed:23973222}.
-!- DOMAIN: The C-terminus plays a role in its oligomerization.
{ECO:0000250}.
-!- PTM: Isoform 1: Phosphorylated. Isoform 1 is phosphorylated at
positions Ser-18 and Ser-963. Isoform 2: Not phosphorylated.
{ECO:0000269|PubMed:17651432}.
-!- PTM: Isoform 1: Polyneddylated. Isoform 2: Not Polyneddylated.
-!- PTM: Isoform 1 and isoform 2: Not sumoylated.
-!- PTM: Isoform 1 and isoform 2: Polyubiquitinated by herpesvirus 1
trans-acting transcriptional protein ICP0/VMW110; leading to its
subsequent proteasomal degradation. Isoform 1: Ubiquitinated at
Lys-869. {ECO:0000269|PubMed:16160161,
ECO:0000269|PubMed:17651432}.
-!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
-!- CAUTION: Was reported to interact with UBXN6 but the corresponding
article has been retracted (PubMed:18768758).
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/USP7ID42773ch16p13.html";
-----------------------------------------------------------------------
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EMBL; Z72499; CAA96580.1; -; mRNA.
EMBL; AK302771; BAH13801.1; -; mRNA.
EMBL; AC022167; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471112; EAW85194.1; -; Genomic_DNA.
CCDS; CCDS32385.1; -. [Q93009-1]
CCDS; CCDS66941.1; -. [Q93009-3]
RefSeq; NP_001308787.1; NM_001321858.1.
RefSeq; NP_003461.2; NM_003470.2. [Q93009-1]
UniGene; Hs.386939; -.
PDB; 1NB8; X-ray; 2.30 A; A/B=208-560.
PDB; 1NBF; X-ray; 2.30 A; A/B/E=208-560.
PDB; 1YY6; X-ray; 1.70 A; A=54-204.
PDB; 1YZE; X-ray; 2.00 A; A/B/C=54-205.
PDB; 2F1W; X-ray; 1.65 A; A=53-206.
PDB; 2F1X; X-ray; 2.30 A; A/B=53-200.
PDB; 2F1Y; X-ray; 1.70 A; A=53-198.
PDB; 2F1Z; X-ray; 3.20 A; A/B=43-560.
PDB; 2FOJ; X-ray; 1.60 A; A=54-205.
PDB; 2FOO; X-ray; 2.20 A; A=54-205.
PDB; 2FOP; X-ray; 2.10 A; A=54-205.
PDB; 2KVR; NMR; -; A=537-664.
PDB; 2XXN; X-ray; 1.60 A; A=63-205.
PDB; 2YLM; X-ray; 2.70 A; A=560-1084.
PDB; 3MQR; X-ray; 1.80 A; A=54-205.
PDB; 3MQS; X-ray; 2.40 A; C=54-205.
PDB; 4JJQ; X-ray; 1.95 A; A=54-205.
PDB; 4KG9; X-ray; 1.70 A; A=54-205.
PDB; 4M5W; X-ray; 2.24 A; A=207-560.
PDB; 4M5X; X-ray; 2.19 A; A/B=207-560.
PDB; 4PYZ; X-ray; 2.84 A; A/B=537-793.
PDB; 4WPH; X-ray; 2.92 A; A/B=535-888.
PDB; 4WPI; X-ray; 3.40 A; A/B=535-888.
PDB; 4YOC; X-ray; 2.92 A; C=560-1102.
PDB; 4YSI; X-ray; 1.02 A; A=63-205.
PDB; 4Z96; X-ray; 2.85 A; A=560-1083.
PDB; 4Z97; X-ray; 3.00 A; A=560-1083.
PDB; 5C56; X-ray; 2.69 A; A=560-1102.
PDB; 5C6D; X-ray; 2.29 A; A/B=561-881.
PDB; 5FWI; X-ray; 3.40 A; C=207-882.
PDB; 5GG4; X-ray; 3.11 A; A/B/C/D=560-890.
PDB; 5J7T; X-ray; 3.20 A; A=211-881.
PDB; 5JTJ; X-ray; 3.32 A; A=209-554, A=1084-1102.
PDB; 5JTV; X-ray; 3.31 A; A/C/E/G=207-554, A/C/E/G=882-1102.
PDBsum; 1NB8; -.
PDBsum; 1NBF; -.
PDBsum; 1YY6; -.
PDBsum; 1YZE; -.
PDBsum; 2F1W; -.
PDBsum; 2F1X; -.
PDBsum; 2F1Y; -.
PDBsum; 2F1Z; -.
PDBsum; 2FOJ; -.
PDBsum; 2FOO; -.
PDBsum; 2FOP; -.
PDBsum; 2KVR; -.
PDBsum; 2XXN; -.
PDBsum; 2YLM; -.
PDBsum; 3MQR; -.
PDBsum; 3MQS; -.
PDBsum; 4JJQ; -.
PDBsum; 4KG9; -.
PDBsum; 4M5W; -.
PDBsum; 4M5X; -.
PDBsum; 4PYZ; -.
PDBsum; 4WPH; -.
PDBsum; 4WPI; -.
PDBsum; 4YOC; -.
PDBsum; 4YSI; -.
PDBsum; 4Z96; -.
PDBsum; 4Z97; -.
PDBsum; 5C56; -.
PDBsum; 5C6D; -.
PDBsum; 5FWI; -.
PDBsum; 5GG4; -.
PDBsum; 5J7T; -.
PDBsum; 5JTJ; -.
PDBsum; 5JTV; -.
DisProt; DP00941; -.
ProteinModelPortal; Q93009; -.
SMR; Q93009; -.
BioGrid; 113622; 341.
CORUM; Q93009; -.
DIP; DIP-29053N; -.
ELM; Q93009; -.
IntAct; Q93009; 152.
MINT; MINT-234628; -.
STRING; 9606.ENSP00000343535; -.
BindingDB; Q93009; -.
ChEMBL; CHEMBL2157850; -.
MEROPS; C19.016; -.
iPTMnet; Q93009; -.
PhosphoSitePlus; Q93009; -.
BioMuta; USP7; -.
DMDM; 212276477; -.
EPD; Q93009; -.
PaxDb; Q93009; -.
PeptideAtlas; Q93009; -.
PRIDE; Q93009; -.
DNASU; 7874; -.
Ensembl; ENST00000344836; ENSP00000343535; ENSG00000187555. [Q93009-1]
Ensembl; ENST00000381886; ENSP00000371310; ENSG00000187555. [Q93009-3]
GeneID; 7874; -.
KEGG; hsa:7874; -.
UCSC; uc002czk.4; human. [Q93009-1]
CTD; 7874; -.
DisGeNET; 7874; -.
EuPathDB; HostDB:ENSG00000187555.14; -.
GeneCards; USP7; -.
H-InvDB; HIX0038590; -.
HGNC; HGNC:12630; USP7.
HPA; CAB008108; -.
HPA; HPA015641; -.
MIM; 602519; gene.
neXtProt; NX_Q93009; -.
OpenTargets; ENSG00000187555; -.
PharmGKB; PA37255; -.
eggNOG; KOG1863; Eukaryota.
eggNOG; COG5077; LUCA.
GeneTree; ENSGT00760000119158; -.
HOGENOM; HOG000160240; -.
HOVERGEN; HBG018029; -.
InParanoid; Q93009; -.
KO; K11838; -.
OMA; MCERAGF; -.
OrthoDB; EOG091G01BK; -.
PhylomeDB; Q93009; -.
TreeFam; TF105667; -.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
Reactome; R-HSA-6782135; Dual incision in TC-NER.
Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
Reactome; R-HSA-8948747; Regulation of PTEN localization.
SignaLink; Q93009; -.
SIGNOR; Q93009; -.
ChiTaRS; USP7; human.
EvolutionaryTrace; Q93009; -.
GeneWiki; USP7; -.
GenomeRNAi; 7874; -.
PRO; PR:Q93009; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000187555; -.
CleanEx; HS_USP7; -.
ExpressionAtlas; Q93009; baseline and differential.
Genevisible; Q93009; HS.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IMP:UniProtKB.
GO; GO:0002039; F:p53 binding; IDA:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:UniProtKB.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0035616; P:histone H2B conserved C-terminal lysine deubiquitination; ISS:UniProtKB.
GO; GO:0010216; P:maintenance of DNA methylation; IMP:UniProtKB.
GO; GO:0035520; P:monoubiquitinated protein deubiquitination; IDA:MGI.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
GO; GO:0051090; P:regulation of sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
GO; GO:1904353; P:regulation of telomere capping; TAS:BHF-UCL.
GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IMP:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 2.60.210.10; -; 1.
InterPro; IPR002083; MATH/TRAF_dom.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR008974; TRAF-like.
InterPro; IPR024729; USP7_ICP0-binding_dom.
InterPro; IPR029346; USP_C.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
Pfam; PF00917; MATH; 1.
Pfam; PF00443; UCH; 1.
Pfam; PF14533; USP7_C2; 1.
Pfam; PF12436; USP7_ICP0_bdg; 1.
SMART; SM00061; MATH; 1.
SUPFAM; SSF49599; SSF49599; 1.
PROSITE; PS50144; MATH; 1.
PROSITE; PS00972; USP_1; 1.
PROSITE; PS00973; USP_2; 1.
PROSITE; PS50235; USP_3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Chromosome;
Complete proteome; Cytoplasm; Developmental protein;
Direct protein sequencing; DNA damage; DNA repair;
Host-virus interaction; Hydrolase; Isopeptide bond; Nucleus;
Phosphoprotein; Protease; Reference proteome; Thiol protease;
Ubl conjugation; Ubl conjugation pathway.
CHAIN 1 1102 Ubiquitin carboxyl-terminal hydrolase 7.
/FTId=PRO_0000080626.
DOMAIN 68 195 MATH. {ECO:0000255|PROSITE-
ProRule:PRU00129}.
DOMAIN 214 521 USP.
REGION 1 208 Interaction with TSPYL5.
{ECO:0000269|PubMed:21170034}.
REGION 53 208 Interaction with p53/TP53, MDM2 and
EBNA1. {ECO:0000269|PubMed:14506283}.
REGION 70 205 Necessary for nuclear localization.
REGION 622 801 Interaction with ICP0/VMW110.
{ECO:0000269|PubMed:16160161}.
COMPBIAS 4 10 Poly-Gln.
ACT_SITE 223 223 Nucleophile.
{ECO:0000269|PubMed:12507430,
ECO:0000305|PubMed:11923872,
ECO:0000305|PubMed:15053880,
ECO:0000305|PubMed:16964248,
ECO:0000305|PubMed:18716620,
ECO:0000305|PubMed:21745816,
ECO:0000305|PubMed:22411829}.
ACT_SITE 464 464 Proton acceptor.
{ECO:0000305|PubMed:12507430}.
MOD_RES 18 18 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:17651432}.
MOD_RES 49 49 Phosphoserine.
{ECO:0000250|UniProtKB:Q6A4J8}.
MOD_RES 869 869 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 963 963 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:17651432}.
MOD_RES 1084 1084 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1096 1096 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
CROSSLNK 869 869 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:28112733}.
CROSSLNK 869 869 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate. {ECO:0000269|PubMed:17651432}.
CROSSLNK 882 882 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 25 MNHQQQQQQQKAGEQQLSEPEDMEM -> MAGNHRLGL
(in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054884.
MUTAGEN 164 164 D->A: Decreased binding to p53/TP53 and
MDM2. {ECO:0000269|PubMed:16474402}.
MUTAGEN 165 165 W->A: Loss of binding to p53/TP53 and
MDM2. {ECO:0000269|PubMed:16474402}.
MUTAGEN 223 223 C->A: Complete loss of activity.
Localized in the nucleus and does not
inhibit FOXO4-dependent transcriptional
activity. {ECO:0000269|PubMed:11923872,
ECO:0000269|PubMed:12507430,
ECO:0000269|PubMed:15053880,
ECO:0000269|PubMed:16964248,
ECO:0000269|PubMed:18716620,
ECO:0000269|PubMed:21745816,
ECO:0000269|PubMed:22411829}.
MUTAGEN 223 223 C->S: No effect on p53/TP53 and PTEN
binding but is defective in
deubiquitinating p53/TP53 and PTEN.
{ECO:0000269|PubMed:11923872,
ECO:0000269|PubMed:12507430,
ECO:0000269|PubMed:15053880,
ECO:0000269|PubMed:16964248,
ECO:0000269|PubMed:18716620,
ECO:0000269|PubMed:21745816,
ECO:0000269|PubMed:22411829}.
MUTAGEN 456 456 H->A: Complete loss of activity.
{ECO:0000269|PubMed:12507430}.
MUTAGEN 464 464 H->A: Complete loss of activity.
{ECO:0000269|PubMed:12507430}.
CONFLICT 201 201 H -> I (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 205 205 W -> P (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 207 207 S -> Q (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 1045 1045 M -> T (in Ref. 1; CAA96580).
{ECO:0000305}.
CONFLICT 1066 1066 Q -> T (in Ref. 1; AA sequence).
{ECO:0000305}.
STRAND 67 77 {ECO:0000244|PDB:4YSI}.
HELIX 78 80 {ECO:0000244|PDB:4YSI}.
STRAND 90 92 {ECO:0000244|PDB:4YSI}.
STRAND 95 105 {ECO:0000244|PDB:4YSI}.
STRAND 106 110 {ECO:0000244|PDB:2F1X}.
STRAND 113 122 {ECO:0000244|PDB:4YSI}.
STRAND 131 140 {ECO:0000244|PDB:4YSI}.
HELIX 146 148 {ECO:0000244|PDB:4YSI}.
STRAND 150 159 {ECO:0000244|PDB:4YSI}.
HELIX 160 162 {ECO:0000244|PDB:2F1Z}.
STRAND 164 172 {ECO:0000244|PDB:4YSI}.
HELIX 173 176 {ECO:0000244|PDB:4YSI}.
TURN 179 181 {ECO:0000244|PDB:4YSI}.
STRAND 182 185 {ECO:0000244|PDB:2XXN}.
STRAND 188 197 {ECO:0000244|PDB:4YSI}.
STRAND 201 203 {ECO:0000244|PDB:4YSI}.
TURN 209 211 {ECO:0000244|PDB:4M5W}.
TURN 221 224 {ECO:0000244|PDB:1NB8}.
HELIX 225 233 {ECO:0000244|PDB:4M5X}.
HELIX 236 244 {ECO:0000244|PDB:4M5X}.
STRAND 248 250 {ECO:0000244|PDB:5J7T}.
TURN 252 254 {ECO:0000244|PDB:4M5X}.
HELIX 256 269 {ECO:0000244|PDB:4M5X}.
HELIX 277 283 {ECO:0000244|PDB:4M5X}.
TURN 288 293 {ECO:0000244|PDB:4M5X}.
HELIX 296 311 {ECO:0000244|PDB:4M5X}.
TURN 315 318 {ECO:0000244|PDB:4M5X}.
HELIX 319 324 {ECO:0000244|PDB:4M5X}.
STRAND 326 338 {ECO:0000244|PDB:4M5X}.
STRAND 340 352 {ECO:0000244|PDB:4M5X}.
HELIX 360 367 {ECO:0000244|PDB:4M5X}.
STRAND 371 373 {ECO:0000244|PDB:4M5X}.
HELIX 375 377 {ECO:0000244|PDB:4M5X}.
HELIX 382 384 {ECO:0000244|PDB:4M5X}.
STRAND 385 387 {ECO:0000244|PDB:5J7T}.
STRAND 389 397 {ECO:0000244|PDB:4M5X}.
STRAND 400 406 {ECO:0000244|PDB:4M5X}.
STRAND 409 412 {ECO:0000244|PDB:1NBF}.
TURN 413 415 {ECO:0000244|PDB:4M5X}.
STRAND 417 420 {ECO:0000244|PDB:1NBF}.
STRAND 429 432 {ECO:0000244|PDB:4M5X}.
HELIX 434 436 {ECO:0000244|PDB:4M5X}.
STRAND 437 439 {ECO:0000244|PDB:4M5X}.
STRAND 442 444 {ECO:0000244|PDB:4M5W}.
STRAND 447 458 {ECO:0000244|PDB:4M5X}.
STRAND 460 462 {ECO:0000244|PDB:4M5X}.
STRAND 464 469 {ECO:0000244|PDB:4M5X}.
STRAND 473 475 {ECO:0000244|PDB:4M5X}.
STRAND 477 481 {ECO:0000244|PDB:4M5X}.
STRAND 484 488 {ECO:0000244|PDB:4M5X}.
HELIX 490 493 {ECO:0000244|PDB:4M5X}.
HELIX 495 497 {ECO:0000244|PDB:4M5X}.
TURN 504 506 {ECO:0000244|PDB:5J7T}.
TURN 507 510 {ECO:0000244|PDB:1NBF}.
STRAND 511 520 {ECO:0000244|PDB:4M5X}.
HELIX 521 523 {ECO:0000244|PDB:4M5X}.
HELIX 524 527 {ECO:0000244|PDB:4M5X}.
HELIX 533 535 {ECO:0000244|PDB:4M5X}.
HELIX 538 551 {ECO:0000244|PDB:4M5X}.
HELIX 561 563 {ECO:0000244|PDB:5C56}.
STRAND 564 570 {ECO:0000244|PDB:5C6D}.
HELIX 572 574 {ECO:0000244|PDB:5C6D}.
TURN 575 577 {ECO:0000244|PDB:5C6D}.
STRAND 580 584 {ECO:0000244|PDB:5C6D}.
STRAND 588 597 {ECO:0000244|PDB:5C6D}.
HELIX 602 613 {ECO:0000244|PDB:5C6D}.
HELIX 617 619 {ECO:0000244|PDB:5C6D}.
STRAND 620 628 {ECO:0000244|PDB:5C6D}.
TURN 629 631 {ECO:0000244|PDB:5C56}.
STRAND 633 635 {ECO:0000244|PDB:5C6D}.
HELIX 640 643 {ECO:0000244|PDB:2YLM}.
STRAND 645 647 {ECO:0000244|PDB:5C6D}.
HELIX 648 651 {ECO:0000244|PDB:5C6D}.
TURN 652 654 {ECO:0000244|PDB:5C6D}.
STRAND 656 664 {ECO:0000244|PDB:5C6D}.
HELIX 668 671 {ECO:0000244|PDB:5C56}.
TURN 681 683 {ECO:0000244|PDB:5C6D}.
STRAND 684 693 {ECO:0000244|PDB:5C6D}.
TURN 694 697 {ECO:0000244|PDB:5C6D}.
STRAND 698 708 {ECO:0000244|PDB:5C6D}.
HELIX 714 716 {ECO:0000244|PDB:5C6D}.
HELIX 717 724 {ECO:0000244|PDB:5C6D}.
STRAND 732 739 {ECO:0000244|PDB:5C6D}.
STRAND 742 745 {ECO:0000244|PDB:5C6D}.
STRAND 749 752 {ECO:0000244|PDB:2YLM}.
HELIX 753 756 {ECO:0000244|PDB:5C6D}.
STRAND 757 759 {ECO:0000244|PDB:5C56}.
STRAND 764 770 {ECO:0000244|PDB:5C6D}.
HELIX 773 777 {ECO:0000244|PDB:5C6D}.
STRAND 778 780 {ECO:0000244|PDB:5C6D}.
HELIX 783 792 {ECO:0000244|PDB:5C6D}.
STRAND 793 800 {ECO:0000244|PDB:5C6D}.
STRAND 803 805 {ECO:0000244|PDB:4Z96}.
STRAND 809 814 {ECO:0000244|PDB:5C6D}.
HELIX 819 829 {ECO:0000244|PDB:5C6D}.
HELIX 834 836 {ECO:0000244|PDB:5C6D}.
STRAND 837 840 {ECO:0000244|PDB:5C6D}.
STRAND 846 848 {ECO:0000244|PDB:5C6D}.
HELIX 861 865 {ECO:0000244|PDB:5C6D}.
STRAND 866 868 {ECO:0000244|PDB:5J7T}.
STRAND 870 872 {ECO:0000244|PDB:5C6D}.
STRAND 875 880 {ECO:0000244|PDB:5C6D}.
HELIX 885 890 {ECO:0000244|PDB:5C56}.
STRAND 894 899 {ECO:0000244|PDB:5C56}.
STRAND 905 910 {ECO:0000244|PDB:5C56}.
HELIX 918 928 {ECO:0000244|PDB:5C56}.
STRAND 933 935 {ECO:0000244|PDB:4YOC}.
STRAND 939 945 {ECO:0000244|PDB:5C56}.
STRAND 948 953 {ECO:0000244|PDB:5C56}.
HELIX 959 961 {ECO:0000244|PDB:5C56}.
STRAND 969 974 {ECO:0000244|PDB:5C56}.
HELIX 977 979 {ECO:0000244|PDB:5C56}.
TURN 984 986 {ECO:0000244|PDB:5C56}.
STRAND 987 998 {ECO:0000244|PDB:5C56}.
STRAND 1003 1014 {ECO:0000244|PDB:5C56}.
HELIX 1017 1027 {ECO:0000244|PDB:5C56}.
HELIX 1032 1035 {ECO:0000244|PDB:5C56}.
STRAND 1039 1044 {ECO:0000244|PDB:5C56}.
STRAND 1047 1050 {ECO:0000244|PDB:5C56}.
TURN 1053 1055 {ECO:0000244|PDB:5C56}.
HELIX 1060 1062 {ECO:0000244|PDB:5C56}.
STRAND 1070 1072 {ECO:0000244|PDB:2YLM}.
STRAND 1076 1080 {ECO:0000244|PDB:5C56}.
SEQUENCE 1102 AA; 128302 MW; F1A5A5C421396E45 CRC64;
MNHQQQQQQQ KAGEQQLSEP EDMEMEAGDT DDPPRITQNP VINGNVALSD GHNTAEEDME
DDTSWRSEAT FQFTVERFSR LSESVLSPPC FVRNLPWKIM VMPRFYPDRP HQKSVGFFLQ
CNAESDSTSW SCHAQAVLKI INYRDDEKSF SRRISHLFFH KENDWGFSNF MAWSEVTDPE
KGFIDDDKVT FEVFVQADAP HGVAWDSKKH TGYVGLKNQG ATCYMNSLLQ TLFFTNQLRK
AVYMMPTEGD DSSKSVPLAL QRVFYELQHS DKPVGTKKLT KSFGWETLDS FMQHDVQELC
RVLLDNVENK MKGTCVEGTI PKLFRGKMVS YIQCKEVDYR SDRREDYYDI QLSIKGKKNI
FESFVDYVAV EQLDGDNKYD AGEHGLQEAE KGVKFLTLPP VLHLQLMRFM YDPQTDQNIK
INDRFEFPEQ LPLDEFLQKT DPKDPANYIL HAVLVHSGDN HGGHYVVYLN PKGDGKWCKF
DDDVVSRCTK EEAIEHNYGG HDDDLSVRHC TNAYMLVYIR ESKLSEVLQA VTDHDIPQQL
VERLQEEKRI EAQKRKERQE AHLYMQVQIV AEDQFCGHQG NDMYDEEKVK YTVFKVLKNS
SLAEFVQSLS QTMGFPQDQI RLWPMQARSN GTKRPAMLDN EADGNKTMIE LSDNENPWTI
FLETVDPELA ASGATLPKFD KDHDVMLFLK MYDPKTRSLN YCGHIYTPIS CKIRDLLPVM
CDRAGFIQDT SLILYEEVKP NLTERIQDYD VSLDKALDEL MDGDIIVFQK DDPENDNSEL
PTAKEYFRDL YHRVDVIFCD KTIPNDPGFV VTLSNRMNYF QVAKTVAQRL NTDPMLLQFF
KSQGYRDGPG NPLRHNYEGT LRDLLQFFKP RQPKKLYYQQ LKMKITDFEN RRSFKCIWLN
SQFREEEITL YPDKHGCVRD LLEECKKAVE LGEKASGKLR LLEIVSYKII GVHQEDELLE
CLSPATSRTF RIEEIPLDQV DIDKENEMLV TVAHFHKEVF GTFGIPFLLR IHQGEHFREV
MKRIQSLLDI QEKEFEKFKF AIVMMGRHQY INEDEYEVNL KDFEPQPGNM SHPRPWLGLD
HFNKAPKRSR YTYLEKAIKI HN


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