Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Ubiquitin carboxyl-terminal hydrolase 15 (EC 3.4.19.12) (Deubiquitinating enzyme 15) (Ubiquitin thioesterase 15) (Ubiquitin-specific-processing protease 15) (Unph-2) (Unph4)

 UBP15_HUMAN             Reviewed;         981 AA.
Q9Y4E8; Q08AL5; Q9H8G9; Q9HCA6; Q9UNP0; Q9Y5B5;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
12-FEB-2003, sequence version 3.
25-OCT-2017, entry version 176.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 15;
EC=3.4.19.12 {ECO:0000269|PubMed:10444327, ECO:0000269|PubMed:16005295, ECO:0000269|PubMed:21947082, ECO:0000269|PubMed:22344298, ECO:0000269|PubMed:24852371, ECO:0000269|PubMed:27368102};
AltName: Full=Deubiquitinating enzyme 15;
AltName: Full=Ubiquitin thioesterase 15;
AltName: Full=Ubiquitin-specific-processing protease 15;
AltName: Full=Unph-2;
AltName: Full=Unph4;
Name=USP15; Synonyms=KIAA0529;
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 2).
TISSUE=Brain;
Kim K.I., Nagase T., Chung C.H.;
"Identification and characterization of a new human deubiquitinating
enzyme Unph4.";
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=9628581; DOI=10.1093/dnares/5.1.31;
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
Ohara O.;
"Prediction of the coding sequences of unidentified human genes. IX.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:31-39(1998).
[3]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Hair follicle dermal papilla;
Kim M.K., Kim Y.H., Seo J.M., Lee H.M., Chung H.J., Sohn M.Y.,
Hwang S.Y., Im S.U., Jung E.J., Lee J.H., Kim J.C.;
"A catalogue of genes in the human dermal papilla cells as identified
by expressed sequence tags.";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Placenta;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
TISSUE=Brain, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 2-21; 475-482 AND 924-932, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Mammary carcinoma;
Bienvenut W.V., Matallanas D., Cooper W.N., Kolch W.;
Submitted (JUL-2007) to UniProtKB.
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 19-981 (ISOFORM 3).
TISSUE=Fetal brain;
Kimura Y., Saya H., Nakao M.;
"Cloning and identification of human Unph-2.";
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[10]
IDENTIFICATION (ISOFORM 2), AND CATALYTIC ACTIVITY.
PubMed=10444327; DOI=10.1006/geno.1999.5879;
Baker R.T., Wang X.-W., Woollatt E., White J.A., Sutherland G.R.;
"Identification, functional characterization, and chromosomal
localization of USP15, a novel human ubiquitin-specific protease
related to the UNP oncoprotein, and a systematic nomenclature for
human ubiquitin-specific proteases.";
Genomics 59:264-274(1999).
[11]
ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
PubMed=12532266; DOI=10.1007/s00335-002-3035-0;
Angelats C., Wang X.-W., Jermiin L.S., Copeland N.G., Jenkins N.A.,
Baker R.T.;
"Isolation and characterization of the mouse ubiquitin-specific
protease Usp15.";
Mamm. Genome 14:31-46(2003).
[12]
FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-812, IDENTIFICATION
IN A COMPLEX WITH THE COP9 SIGNALOSOME, PHOSPHORYLATION, AND
UBIQUITINATION.
PubMed=16005295; DOI=10.1016/j.cub.2005.05.059;
Hetfeld B.K., Helfrich A., Kapelari B., Scheel H., Hofmann K.,
Guterman A., Glickman M., Schade R., Kloetzel P.M., Dubiel W.;
"The zinc finger of the CSN-associated deubiquitinating enzyme USP15
is essential to rescue the E3 ligase Rbx1.";
Curr. Biol. 15:1217-1221(2005).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[14]
FUNCTION.
PubMed=17318178; DOI=10.1038/sj.emboj.7601600;
Schweitzer K., Bozko P.M., Dubiel W., Naumann M.;
"CSN controls NF-kappaB by deubiquitinylation of IkappaBalpha.";
EMBO J. 26:1532-1541(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229; SER-961 AND
SER-965, 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).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND 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).
[17]
FUNCTION.
PubMed=19826004; DOI=10.1074/jbc.M109.037952;
Cayli S., Klug J., Chapiro J., Frohlich S., Krasteva G., Orel L.,
Meinhardt A.;
"COP9 signalosome interacts ATP-dependently with p97/valosin-
containing protein (VCP) and controls the ubiquitination status of
proteins bound to p97/VCP.";
J. Biol. Chem. 284:34944-34953(2009).
[18]
FUNCTION, AND MUTAGENESIS OF CYS-812.
PubMed=19576224; DOI=10.1016/j.jmb.2009.06.066;
Huang X., Langelotz C., Hetfeld-Pechoc B.K., Schwenk W., Dubiel W.;
"The COP9 signalosome mediates beta-catenin degradation by
deneddylation and blocks adenomatous polyposis coli destruction via
USP15.";
J. Mol. Biol. 391:691-702(2009).
[19]
FUNCTION (MICROBIAL INFECTION), MUTAGENESIS OF CYS-298, AND
INTERACTION WITH HUMAN PAPILLOMAVIRUS TYPE 16 PROTEIN E6 (MICROBIAL
INFECTION).
PubMed=19553310; DOI=10.1128/JVI.00605-09;
Vos R.M., Altreuter J., White E.A., Howley P.M.;
"The ubiquitin-specific peptidase USP15 regulates human papillomavirus
type 16 E6 protein stability.";
J. Virol. 83:8885-8892(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229; SER-242; SER-961
AND SER-965, 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).
[22]
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).
[23]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH
SMAD1; SMAD2 AND SMAD3, AND MUTAGENESIS OF CYS-298.
PubMed=21947082; DOI=10.1038/ncb2346;
Inui M., Manfrin A., Mamidi A., Martello G., Morsut L., Soligo S.,
Enzo E., Moro S., Polo S., Dupont S., Cordenonsi M., Piccolo S.;
"USP15 is a deubiquitylating enzyme for receptor-activated SMADs.";
Nat. Cell Biol. 13:1368-1375(2011).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, 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).
[25]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[26]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH TGFBR1; SMAD7 AND
SMURF2, AND MUTAGENESIS OF CYS-298.
PubMed=22344298; DOI=10.1038/nm.2619;
Eichhorn P.J., Rodon L., Gonzalez-Junca A., Dirac A., Gili M.,
Martinez-Saez E., Aura C., Barba I., Peg V., Prat A., Cuartas I.,
Jimenez J., Garcia-Dorado D., Sahuquillo J., Bernards R., Baselga J.,
Seoane J.;
"USP15 stabilizes TGF-beta receptor I and promotes oncogenesis through
the activation of TGF-beta signaling in glioblastoma.";
Nat. Med. 18:429-435(2012).
[27]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-226; SER-229 AND
SER-242, 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).
[29]
FUNCTION, INTERACTION WITH RNF20; RNF40 AND SART3, REGION, AND
SUBCELLULAR LOCATION.
PubMed=24526689; DOI=10.1074/jbc.M114.551754;
Long L., Thelen J.P., Furgason M., Haj-Yahya M., Brik A., Cheng D.,
Peng J., Yao T.;
"The U4/U6 recycling factor SART3 has histone chaperone activity and
associates with USP15 to regulate H2B deubiquitination.";
J. Biol. Chem. 289:8916-8930(2014).
[30]
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).
[31]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-298.
PubMed=27368102; DOI=10.1016/j.cell.2016.05.078;
Jongsma M.L., Berlin I., Wijdeven R.H., Janssen L., Janssen G.M.,
Garstka M.A., Janssen H., Mensink M., van Veelen P.A., Spaapen R.M.,
Neefjes J.;
"An ER-associated pathway defines endosomal architecture for
controlled cargo transport.";
Cell 166:152-166(2016).
[32]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PRKN, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF CYS-298.
PubMed=24852371; DOI=10.1093/hmg/ddu244;
Cornelissen T., Haddad D., Wauters F., Van Humbeeck C.,
Mandemakers W., Koentjoro B., Sue C., Gevaert K., De Strooper B.,
Verstreken P., Vandenberghe W.;
"The deubiquitinase USP15 antagonizes Parkin-mediated mitochondrial
ubiquitination and mitophagy.";
Hum. Mol. Genet. 23:5227-5242(2014).
[33]
STRUCTURE BY NMR OF 1-120.
PubMed=16298993; DOI=10.1074/jbc.M510993200;
de Jong R.N., Ab E., Diercks T., Truffault V., Danieels M.,
Kaptein R., Folkers G.E.;
"Solution structure of the human ubiquitin-specific protease 15 DUSP
domain.";
J. Biol. Chem. 281:5026-5031(2006).
[34]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-222.
PubMed=21848306; DOI=10.1021/bi200726e;
Harper S., Besong T.M., Emsley J., Scott D.J., Dreveny I.;
"Structure of the USP15 N-terminal domains: a beta-hairpin mediates
close association between the DUSP and UBL domains.";
Biochemistry 50:7995-8004(2011).
[35]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-223.
PubMed=22001210; DOI=10.1016/j.febslet.2011.09.040;
Elliott P.R., Liu H., Pastok M.W., Grossmann G.J., Rigden D.J.,
Clague M.J., Urbe S., Barsukov I.L.;
"Structural variability of the ubiquitin specific protease DUSP-UBL
double domains.";
FEBS Lett. 585:3385-3390(2011).
[36]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-133.
Structural genomics consortium (SGC);
"Crystal structure of the human ubiquitin-specific protease 15 DUSP
domain.";
Submitted (APR-2010) to the PDB data bank.
-!- FUNCTION: Hydrolase that removes conjugated ubiquitin from target
proteins and regulates various pathways such as the TGF-beta
receptor signaling, NF-kappa-B and RNF41/NRDP1-PRKN pathways
(PubMed:21947082, PubMed:22344298, PubMed:24852371,
PubMed:16005295, PubMed:17318178, PubMed:19826004,
PubMed:19576224). Acts as a key regulator of TGF-beta receptor
signaling pathway, but the precise mechanism is still unclear:
according to a report, acts by promoting deubiquitination of
monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or SMAD3), thereby
alleviating inhibition of R-SMADs and promoting activation of TGF-
beta target genes (PubMed:21947082). According to another reports,
regulates the TGF-beta receptor signaling pathway by mediating
deubiquitination and stabilization of TGFBR1, leading to an
enhanced TGF-beta signal (PubMed:22344298). Able to mediate
deubiquitination of monoubiquitinated substrates as well as 'Lys-
48'-linked polyubiquitin chains, protecting them against
proteasomal degradation. May also regulate gene expression and/or
DNA repair through the deubiquitination of histone H2B
(PubMed:24526689). Acts as an inhibitor of mitophagy by
counteracting the action of parkin (PRKN): hydrolyzes cleavage of
'Lys-48'- and 'Lys-63'-linked polyubiquitin chains attached by
parkin on target proteins such as MFN2, thereby reducing parkin's
ability to drive mitophagy (PubMed:24852371). Acts as an
associated component of COP9 signalosome complex (CSN) and
regulates different pathways via this association: regulates NF-
kappa-B by mediating deubiquitination of NFKBIA and
deubiquitinates substrates bound to VCP (PubMed:16005295,
PubMed:17318178, PubMed:19826004, PubMed:19576224). Involved in
endosome organization by mediating deubiquitination of SQSTM1:
ubiquitinated SQSTM1 forms a molecular bridge that restrains
cognate vesicles in the perinuclear region and its
deubiquitination releases target vesicles for fast transport into
the cell periphery (PubMed:27368102).
{ECO:0000269|PubMed:16005295, ECO:0000269|PubMed:17318178,
ECO:0000269|PubMed:19576224, ECO:0000269|PubMed:19826004,
ECO:0000269|PubMed:21947082, ECO:0000269|PubMed:22344298,
ECO:0000269|PubMed:24526689, ECO:0000269|PubMed:24852371,
ECO:0000269|PubMed:27368102}.
-!- FUNCTION: (Microbial infection) Protects APC and human
papillomavirus type 16 protein E6 against degradation via the
ubiquitin proteasome pathway. {ECO:0000269|PubMed:19553310}.
-!- 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:10444327, ECO:0000269|PubMed:16005295,
ECO:0000269|PubMed:21947082, ECO:0000269|PubMed:22344298,
ECO:0000269|PubMed:27368102}.
-!- SUBUNIT: A homodimer structure has been reported; however it is
unclear whether the protein form a homodimer in vivo
(PubMed:22001210). Identified in a complex with the COP9
signalosome complex (CSN) (PubMed:16005295). Interacts with SMAD1,
SMAD2 and SMAD3; the interaction is direct (PubMed:21947082).
Forms a complex with SMURF2 and SMAD7 (PubMed:22344298). Interacts
with TGFBR1 (PubMed:22344298). Interacts with SART3; the
interaction is direct (PubMed:24526689). May interact with RNF20
and RNF40 (PubMed:24526689). May interact with PRKN
(PubMed:24852371). {ECO:0000269|PubMed:16005295,
ECO:0000269|PubMed:21947082, ECO:0000269|PubMed:22001210,
ECO:0000269|PubMed:22344298, ECO:0000269|PubMed:24526689,
ECO:0000269|PubMed:24852371}.
-!- SUBUNIT: (Microbial infection) Interacts with human papillomavirus
type 16 protein E6. {ECO:0000269|PubMed:19553310}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-1043104, EBI-1043104;
Q9H257:CARD9; NbExp=3; IntAct=EBI-1043104, EBI-751319;
Q2TAC2:CCDC57; NbExp=3; IntAct=EBI-1043104, EBI-2808286;
Q9Y6D9:MAD1L1; NbExp=3; IntAct=EBI-1043104, EBI-742610;
Q96EA4:SPDL1; NbExp=3; IntAct=EBI-1043104, EBI-715381;
P19474:TRIM21; NbExp=3; IntAct=EBI-1043104, EBI-81290;
Q9BTM9:URM1; NbExp=2; IntAct=EBI-1043104, EBI-714589;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21947082,
ECO:0000269|PubMed:24526689}. Nucleus
{ECO:0000269|PubMed:21947082, ECO:0000269|PubMed:24526689}.
Mitochondrion {ECO:0000269|PubMed:24852371}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q9Y4E8-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y4E8-2; Sequence=VSP_005261;
Name=3;
IsoId=Q9Y4E8-3; Sequence=VSP_005260;
Name=4;
IsoId=Q9Y4E8-4; Sequence=VSP_045165, VSP_045166;
-!- TISSUE SPECIFICITY: Expressed in skeletal muscle, kidney, heart,
placenta, liver, thymus, lung, and ovary, with little or no
expression in other tissues.
-!- PTM: Phosphorylated. Phosphorylation protects against
ubiquitination and subsequent degradation by the proteasome.
{ECO:0000269|PubMed:16005295}.
-!- PTM: Ubiquitinated, leading to degradation by the proteasome.
{ECO:0000269|PubMed:16005295}.
-!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/USP15ID44585ch12q14.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF106069; AAD52099.1; -; mRNA.
EMBL; AB011101; BAA25455.2; -; mRNA.
EMBL; AF153604; AAD41086.1; -; mRNA.
EMBL; AK023703; BAB14648.1; -; mRNA.
EMBL; AK292337; BAF85026.1; -; mRNA.
EMBL; AC048342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC079035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC117370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC020688; AAH20688.1; -; mRNA.
EMBL; BC063454; AAH63454.1; -; mRNA.
EMBL; BC125123; AAI25124.1; -; mRNA.
EMBL; AF013990; AAG28973.1; -; mRNA.
CCDS; CCDS58250.1; -. [Q9Y4E8-4]
CCDS; CCDS58251.1; -. [Q9Y4E8-1]
CCDS; CCDS8963.1; -. [Q9Y4E8-2]
RefSeq; NP_001239007.1; NM_001252078.1. [Q9Y4E8-1]
RefSeq; NP_001239008.1; NM_001252079.1. [Q9Y4E8-4]
RefSeq; NP_006304.1; NM_006313.2. [Q9Y4E8-2]
UniGene; Hs.434951; -.
PDB; 1W6V; NMR; -; A=1-120.
PDB; 3LMN; X-ray; 2.15 A; A/B=1-133.
PDB; 3PPA; X-ray; 2.35 A; A=6-223.
PDB; 3PV1; X-ray; 2.60 A; A/B=1-223.
PDB; 3T9L; X-ray; 1.50 A; A=1-222.
PDB; 4A3O; X-ray; 2.20 A; A/B=4-223.
PDB; 4A3P; X-ray; 1.40 A; A=6-223.
PDB; 5JJW; X-ray; 3.01 A; B=1-223.
PDBsum; 1W6V; -.
PDBsum; 3LMN; -.
PDBsum; 3PPA; -.
PDBsum; 3PV1; -.
PDBsum; 3T9L; -.
PDBsum; 4A3O; -.
PDBsum; 4A3P; -.
PDBsum; 5JJW; -.
ProteinModelPortal; Q9Y4E8; -.
SMR; Q9Y4E8; -.
BioGrid; 115283; 201.
DIP; DIP-50239N; -.
IntAct; Q9Y4E8; 62.
MINT; MINT-4542165; -.
STRING; 9606.ENSP00000258123; -.
MEROPS; C19.022; -.
iPTMnet; Q9Y4E8; -.
PhosphoSitePlus; Q9Y4E8; -.
BioMuta; USP15; -.
DMDM; 28381406; -.
EPD; Q9Y4E8; -.
PaxDb; Q9Y4E8; -.
PeptideAtlas; Q9Y4E8; -.
PRIDE; Q9Y4E8; -.
DNASU; 9958; -.
Ensembl; ENST00000280377; ENSP00000280377; ENSG00000135655. [Q9Y4E8-1]
Ensembl; ENST00000312635; ENSP00000309240; ENSG00000135655. [Q9Y4E8-4]
Ensembl; ENST00000353364; ENSP00000258123; ENSG00000135655. [Q9Y4E8-2]
GeneID; 9958; -.
KEGG; hsa:9958; -.
UCSC; uc001sra.4; human. [Q9Y4E8-1]
CTD; 9958; -.
DisGeNET; 9958; -.
EuPathDB; HostDB:ENSG00000135655.13; -.
GeneCards; USP15; -.
H-InvDB; HIX0010773; -.
HGNC; HGNC:12613; USP15.
HPA; HPA006237; -.
HPA; HPA006428; -.
HPA; HPA071014; -.
MIM; 604731; gene.
neXtProt; NX_Q9Y4E8; -.
OpenTargets; ENSG00000135655; -.
PharmGKB; PA37239; -.
eggNOG; KOG1870; Eukaryota.
eggNOG; COG5560; LUCA.
GeneTree; ENSGT00670000097750; -.
HOGENOM; HOG000264375; -.
HOVERGEN; HBG000864; -.
InParanoid; Q9Y4E8; -.
KO; K21343; -.
OMA; CTEETCK; -.
OrthoDB; EOG091G0157; -.
PhylomeDB; Q9Y4E8; -.
TreeFam; TF106276; -.
Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
ChiTaRS; USP15; human.
EvolutionaryTrace; Q9Y4E8; -.
GeneWiki; USP15; -.
GenomeRNAi; 9958; -.
PRO; PR:Q9Y4E8; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000135655; -.
CleanEx; HS_USP15; -.
ExpressionAtlas; Q9Y4E8; baseline and differential.
Genevisible; Q9Y4E8; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IMP:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046332; F:SMAD 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:0005160; F:transforming growth factor beta receptor binding; IPI:UniProtKB.
GO; GO:0061649; F:ubiquitin modification-dependent histone binding; IDA:UniProtKB.
GO; GO:0030509; P:BMP signaling pathway; IDA:UniProtKB.
GO; GO:0035616; P:histone H2B conserved C-terminal lysine deubiquitination; IDA:UniProtKB.
GO; GO:0035520; P:monoubiquitinated protein deubiquitination; IDA:UniProtKB.
GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IMP:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
Gene3D; 3.30.2230.10; -; 1.
InterPro; IPR035927; DUSP-like_sf.
InterPro; IPR006615; Pept_C19_DUSP.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
InterPro; IPR028135; Ub_USP-typ.
InterPro; IPR029071; Ubiquitin-rel_dom.
InterPro; IPR028134; USP4.
InterPro; IPR029346; USP_C.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
PANTHER; PTHR43913; PTHR43913; 1.
Pfam; PF06337; DUSP; 1.
Pfam; PF14836; Ubiquitin_3; 1.
Pfam; PF00443; UCH; 1.
Pfam; PF14533; USP7_C2; 1.
SMART; SM00695; DUSP; 1.
SUPFAM; SSF143791; SSF143791; 1.
SUPFAM; SSF54236; SSF54236; 1.
SUPFAM; SSF55205; SSF55205; 1.
PROSITE; PS51283; DUSP; 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; Complete proteome;
Cytoplasm; Direct protein sequencing; Hydrolase; Mitochondrion;
Nucleus; Phosphoprotein; Protease; Reference proteome; Thiol protease;
Ubl conjugation; Ubl conjugation pathway.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.8}.
CHAIN 2 981 Ubiquitin carboxyl-terminal hydrolase 15.
/FTId=PRO_0000080641.
DOMAIN 7 118 DUSP. {ECO:0000255|PROSITE-
ProRule:PRU00613}.
DOMAIN 289 933 USP. {ECO:0000255|PROSITE-
ProRule:PRU01035}.
REGION 2 223 Mediates interaction with SART3.
{ECO:0000269|PubMed:24526689}.
ACT_SITE 298 298 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU01035,
ECO:0000305|PubMed:19553310,
ECO:0000305|PubMed:21947082,
ECO:0000305|PubMed:22344298,
ECO:0000305|PubMed:24852371,
ECO:0000305|PubMed:27368102}.
ACT_SITE 891 891 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.8}.
MOD_RES 226 226 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 229 229 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 242 242 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 602 602 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8R5H1}.
MOD_RES 961 961 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 965 965 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
VAR_SEQ 217 256 DGTWPRGPSTPKSPGASNFSTLPKISPSSLSNNYNNMNNR
-> QKNEDGTWPRGPSTP (in isoform 3).
{ECO:0000303|Ref.9}.
/FTId=VSP_005260.
VAR_SEQ 228 256 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9628581,
ECO:0000303|Ref.1}.
/FTId=VSP_005261.
VAR_SEQ 229 235 SPGASNF -> KPLEQSC (in isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_045165.
VAR_SEQ 236 981 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_045166.
MUTAGEN 298 298 C->A: Loss of enzyme activity.
{ECO:0000269|PubMed:19553310,
ECO:0000269|PubMed:21947082,
ECO:0000269|PubMed:22344298,
ECO:0000269|PubMed:24852371,
ECO:0000269|PubMed:27368102}.
MUTAGEN 812 812 C->A: Loss of activity towards
polyubiquitin.
{ECO:0000269|PubMed:16005295,
ECO:0000269|PubMed:19576224}.
CONFLICT 559 559 T -> A (in Ref. 9; AAG28973).
{ECO:0000305}.
CONFLICT 747 747 S -> F (in Ref. 7; AAI25124).
{ECO:0000305}.
CONFLICT 968 968 N -> H (in Ref. 9; AAG28973).
{ECO:0000305}.
STRAND 4 6 {ECO:0000244|PDB:1W6V}.
HELIX 9 19 {ECO:0000244|PDB:4A3P}.
STRAND 29 34 {ECO:0000244|PDB:4A3P}.
HELIX 35 45 {ECO:0000244|PDB:4A3P}.
TURN 46 48 {ECO:0000244|PDB:3T9L}.
TURN 53 56 {ECO:0000244|PDB:4A3P}.
HELIX 58 60 {ECO:0000244|PDB:4A3P}.
HELIX 68 70 {ECO:0000244|PDB:4A3P}.
STRAND 73 76 {ECO:0000244|PDB:3T9L}.
TURN 86 88 {ECO:0000244|PDB:4A3P}.
STRAND 89 93 {ECO:0000244|PDB:4A3P}.
HELIX 94 104 {ECO:0000244|PDB:4A3P}.
STRAND 114 120 {ECO:0000244|PDB:4A3P}.
STRAND 122 124 {ECO:0000244|PDB:5JJW}.
STRAND 127 129 {ECO:0000244|PDB:4A3P}.
STRAND 134 140 {ECO:0000244|PDB:4A3P}.
STRAND 143 152 {ECO:0000244|PDB:4A3P}.
HELIX 158 168 {ECO:0000244|PDB:4A3P}.
STRAND 173 175 {ECO:0000244|PDB:4A3O}.
STRAND 177 184 {ECO:0000244|PDB:4A3P}.
STRAND 187 190 {ECO:0000244|PDB:4A3P}.
HELIX 198 201 {ECO:0000244|PDB:4A3P}.
STRAND 208 213 {ECO:0000244|PDB:4A3P}.
SEQUENCE 981 AA; 112419 MW; E81FEB9DE57F7089 CRC64;
MAEGGAADLD TQRSDIATLL KTSLRKGDTW YLVDSRWFKQ WKKYVGFDSW DKYQMGDQNV
YPGPIDNSGL LKDGDAQSLK EHLIDELDYI LLPTEGWNKL VSWYTLMEGQ EPIARKVVEQ
GMFVKHCKVE VYLTELKLCE NGNMNNVVTR RFSKADTIDT IEKEIRKIFS IPDEKETRLW
NKYMSNTFEP LNKPDSTIQD AGLYQGQVLV IEQKNEDGTW PRGPSTPKSP GASNFSTLPK
ISPSSLSNNY NNMNNRNVKN SNYCLPSYTA YKNYDYSEPG RNNEQPGLCG LSNLGNTCFM
NSAIQCLSNT PPLTEYFLND KYQEELNFDN PLGMRGEIAK SYAELIKQMW SGKFSYVTPR
AFKTQVGRFA PQFSGYQQQD CQELLAFLLD GLHEDLNRIR KKPYIQLKDA DGRPDKVVAE
EAWENHLKRN DSIIVDIFHG LFKSTLVCPE CAKISVTFDP FCYLTLPLPM KKERTLEVYL
VRMDPLTKPM QYKVVVPKIG NILDLCTALS ALSGIPADKM IVTDIYNHRF HRIFAMDENL
SSIMERDDIY VFEININRTE DTEHVIIPVC LREKFRHSSY THHTGSSLFG QPFLMAVPRN
NTEDKLYNLL LLRMCRYVKI STETEETEGS LHCCKDQNIN GNGPNGIHEE GSPSEMETDE
PDDESSQDQE LPSENENSQS EDSVGGDNDS ENGLCTEDTC KGQLTGHKKR LFTFQFNNLG
NTDINYIKDD TRHIRFDDRQ LRLDERSFLA LDWDPDLKKR YFDENAAEDF EKHESVEYKP
PKKPFVKLKD CIELFTTKEK LGAEDPWYCP NCKEHQQATK KLDLWSLPPV LVVHLKRFSY
SRYMRDKLDT LVDFPINDLD MSEFLINPNA GPCRYNLIAV SNHYGGMGGG HYTAFAKNKD
DGKWYYFDDS SVSTASEDQI VSKAAYVLFY QRQDTFSGTG FFPLDRETKG ASAATGIPLE
SDEDSNDNDN DIENENCMHT N


Related products :

Catalog number Product name Quantity
EIAAB44989 Deubiquitinating enzyme 15,Homo sapiens,Human,KIAA0529,Ubiquitin carboxyl-terminal hydrolase 15,Ubiquitin thiolesterase 15,Ubiquitin-specific-processing protease 15,Unph-2,Unph4,USP15
EIAAB45096 Deubiquitinating enzyme 7,HAUSP,Herpesvirus-associated ubiquitin-specific protease,Homo sapiens,Human,Ubiquitin carboxyl-terminal hydrolase 7,Ubiquitin thioesterase 7,Ubiquitin-specific-processing pro
EIAAB45057 Deubiquitinating enzyme 4,Homo sapiens,Human,Ubiquitin carboxyl-terminal hydrolase 4,Ubiquitin thiolesterase 4,Ubiquitin-specific-processing protease 4,Ubiquitous nuclear protein homolog,UNP,UNPH,USP4
EIAAB45055 Deubiquitinating enzyme 4,Rat,Rattus norvegicus,Ubiquitin carboxyl-terminal hydrolase 4,Ubiquitin thioesterase 4,Ubiquitin-specific-processing protease 4,Usp4
EIAAB44991 Deubiquitinating enzyme 16,Homo sapiens,Human,MSTP039,Ubiquitin carboxyl-terminal hydrolase 16,Ubiquitin thiolesterase 16,Ubiquitin-processing protease UBP-M,Ubiquitin-specific-processing protease 16,
EIAAB45002 41 kDa ubiquitin-specific protease,Deubiquitinating enzyme 2,Rat,Rattus norvegicus,Ubiquitin carboxyl-terminal hydrolase 2,Ubiquitin thiolesterase 2,Ubiquitin-specific-processing protease 2,Ubiquitin-
EIAAB45093 Chicken,Deubiquitinating enzyme 7,Gallus gallus,Ubiquitin carboxyl-terminal hydrolase 7,Ubiquitin thioesterase 7,Ubiquitin-specific-processing protease 7,USP7
EIAAB45022 Deubiquitinating enzyme 27,Homo sapiens,Human,Ubiquitin carboxyl-terminal hydrolase 22-like,Ubiquitin carboxyl-terminal hydrolase 27,Ubiquitin thiolesterase 27,Ubiquitin-specific-processing protease 2
EIAAB45023 Deubiquitinating enzyme 27,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 27,Ubiquitin thiolesterase 27,Ubiquitin-specific-processing protease 27,Usp27,Usp27x,X-linked ubiquitin carboxyl-ter
EIAAB44981 Deubiquitinating enzyme 12,Mouse,Mus musculus,Ubh1,Ubiquitin carboxyl-terminal hydrolase 12,Ubiquitin thiolesterase 12,Ubiquitin-hydrolyzing enzyme 1,Ubiquitin-specific-processing protease 12,Usp12
EIAAB45005 41 kDa ubiquitin-specific protease,Deubiquitinating enzyme 2,Homo sapiens,Human,Ubiquitin carboxyl-terminal hydrolase 2,Ubiquitin thiolesterase 2,Ubiquitin-specific-processing protease 2,UBP41,USP2
EIAAB45004 41 kDa ubiquitin-specific protease,Deubiquitinating enzyme 2,MNCb-0190,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 2,Ubiquitin thiolesterase 2,Ubiquitin-specific-processing protease 2,Ubp
EIAAB45001 41 kDa ubiquitin-specific protease,Bos taurus,Bovine,Deubiquitinating enzyme 2,Ubiquitin carboxyl-terminal hydrolase 2,Ubiquitin thiolesterase 2,Ubiquitin-specific-processing protease 2,UBP41,USP2
EIAAB45076 Deubiquitinating enzyme 48,Rat,Rattus norvegicus,Synaptic ubiquitin-specific protease,synUSP,Ubiquitin carboxyl-terminal hydrolase 48,Ubiquitin thiolesterase 48,Ubiquitin-specific-processing protease
EIAAB45095 Deubiquitinating enzyme 7,Hausp,Herpesvirus-associated ubiquitin-specific protease,mHAUSP,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 7,Ubiquitin thioesterase 7,Ubiquitin-specific-process
EIAAB45094 Deubiquitinating enzyme 7,Hausp,Herpesvirus-associated ubiquitin-specific protease,Rat,Rattus norvegicus,rHAUSP,Ubiquitin carboxyl-terminal hydrolase 7,Ubiquitin thioesterase 7,Ubiquitin-specific-proc
EIAAB44983 Deubiquitinating enzyme 12,Homo sapiens,Human,UBH1,Ubiquitin carboxyl-terminal hydrolase 12,Ubiquitin thiolesterase 12,Ubiquitin-hydrolyzing enzyme 1,Ubiquitin-specific-processing protease 12,USP12,US
EIAAB45098 Deubiquitinating enzyme 8,Kiaa0055,Mouse,mUBPy,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 8,Ubiquitin isopeptidase Y,Ubiquitin thiolesterase 8,Ubiquitin-specific-processing protease 8,Ubpy,Usp
EIAAB45039 Deubiquitinating enzyme 33,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 33,Ubiquitin thiolesterase 33,Ubiquitin-specific-processing protease 33,Usp33,Vdu1,VHL-interacting deubiquitinating
EIAAB45097 Deubiquitinating enzyme 8,Homo sapiens,hUBPy,Human,KIAA0055,Ubiquitin carboxyl-terminal hydrolase 8,Ubiquitin isopeptidase Y,Ubiquitin thiolesterase 8,Ubiquitin-specific-processing protease 8,UBPY,USP
EIAAB45050 Deubiquitinating enzyme 37,Pig,Sus scrofa,Ubiquitin carboxyl-terminal hydrolase 37,Ubiquitin thiolesterase 37,Ubiquitin-specific-processing protease 37,USP37
EIAAB45067 Inactive deubiquitinating enzyme 44,Inactive ubiquitin carboxyl-terminal hydrolase 44,Inactive ubiquitin thioesterase 44,Inactive ubiquitin-specific-processing protease 44,Mouse,Mus musculus,Usp44
EIAAB45021 Deubiquitinating enzyme 26,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 26,Ubiquitin thiolesterase 26,Ubiquitin-specific-processing protease 26,Usp26
EIAAB45028 Deubiquitinating enzyme 29,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 29,Ubiquitin thiolesterase 29,Ubiquitin-specific-processing protease 29,Usp29
EIAAB45033 Deubiquitinating enzyme 3,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 3,Ubiquitin thiolesterase 3,Ubiquitin-specific-processing protease 3,Usp3


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur