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 32 (EC 3.4.19.12) (Deubiquitinating enzyme 32) (Renal carcinoma antigen NY-REN-60) (Ubiquitin thioesterase 32) (Ubiquitin-specific-processing protease 32)

 UBP32_HUMAN             Reviewed;        1604 AA.
Q8NFA0; Q7Z5T3; Q9BX85; Q9Y591;
10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
10-OCT-2018, entry version 157.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 32;
EC=3.4.19.12;
AltName: Full=Deubiquitinating enzyme 32;
AltName: Full=Renal carcinoma antigen NY-REN-60;
AltName: Full=Ubiquitin thioesterase 32;
AltName: Full=Ubiquitin-specific-processing protease 32;
Flags: Precursor;
Name=USP32; Synonyms=USP10;
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).
TISSUE=Brain;
PubMed=12604796; DOI=10.1073/pnas.0437015100;
Paulding C.A., Ruvolo M., Haber D.A.;
"The Tre2 (USP6) oncogene is a hominoid-specific gene.";
Proc. Natl. Acad. Sci. U.S.A. 100:2507-2511(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 331-1604 (ISOFORM 1).
TISSUE=Testis;
Sha J.H.;
"Identification of a novel ubiquitin specific protease gene related to
testes development from human testes cDNA library.";
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Uterus;
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 536-1363 (ISOFORM 1), AND IDENTIFICATION
AS A RENAL CANCER ANTIGEN.
PubMed=10508479;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-
cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[7]
ISOPRENYLATION AT CYS-1601.
PubMed=17411337; DOI=10.1371/journal.pcbi.0030066;
Maurer-Stroh S., Koranda M., Benetka W., Schneider G., Sirota F.L.,
Eisenhaber F.;
"Towards complete sets of farnesylated and geranylgeranylated
proteins.";
PLoS Comput. Biol. 3:634-648(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1173, 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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1372, 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).
[10]
CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=20549504; DOI=10.1007/s00335-010-9268-4;
Akhavantabasi S., Akman H.B., Sapmaz A., Keller J., Petty E.M.,
Erson A.E.;
"USP32 is an active, membrane-bound ubiquitin protease overexpressed
in breast cancers.";
Mamm. Genome 21:388-397(2010).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1372, 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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1350; SER-1372; SER-1376
AND SER-1588, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1454, 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).
-!- 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:20549504}.
-!- INTERACTION:
Q8IUH5:ZDHHC17; NbExp=2; IntAct=EBI-2511075, EBI-524753;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
{ECO:0000305}. Golgi apparatus {ECO:0000269|PubMed:20549504}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8NFA0-1; Sequence=Displayed;
Name=2;
IsoId=Q8NFA0-2; Sequence=VSP_056307, VSP_056308;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF533230; AAM97922.1; -; mRNA.
EMBL; AF350251; AAK30207.1; -; mRNA.
EMBL; AC003962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC025048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC037475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC104763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC054344; AAH54344.1; -; mRNA.
EMBL; AF155116; AAD42882.1; -; mRNA.
CCDS; CCDS32697.1; -. [Q8NFA0-1]
RefSeq; NP_115971.2; NM_032582.3. [Q8NFA0-1]
UniGene; Hs.132868; -.
ProteinModelPortal; Q8NFA0; -.
SMR; Q8NFA0; -.
BioGrid; 124189; 44.
DIP; DIP-53613N; -.
IntAct; Q8NFA0; 32.
MINT; Q8NFA0; -.
STRING; 9606.ENSP00000300896; -.
iPTMnet; Q8NFA0; -.
PhosphoSitePlus; Q8NFA0; -.
SwissPalm; Q8NFA0; -.
BioMuta; USP32; -.
DMDM; 47606649; -.
EPD; Q8NFA0; -.
MaxQB; Q8NFA0; -.
PaxDb; Q8NFA0; -.
PeptideAtlas; Q8NFA0; -.
PRIDE; Q8NFA0; -.
ProteomicsDB; 73280; -.
DNASU; 84669; -.
Ensembl; ENST00000300896; ENSP00000300896; ENSG00000170832. [Q8NFA0-1]
Ensembl; ENST00000393003; ENSP00000376727; ENSG00000170832. [Q8NFA0-2]
GeneID; 84669; -.
KEGG; hsa:84669; -.
UCSC; uc002iyo.2; human. [Q8NFA0-1]
CTD; 84669; -.
DisGeNET; 84669; -.
EuPathDB; HostDB:ENSG00000170832.12; -.
GeneCards; USP32; -.
HGNC; HGNC:19143; USP32.
HPA; HPA044365; -.
MIM; 607740; gene.
neXtProt; NX_Q8NFA0; -.
OpenTargets; ENSG00000170832; -.
PharmGKB; PA134982542; -.
eggNOG; KOG0044; Eukaryota.
eggNOG; KOG1870; Eukaryota.
eggNOG; COG5560; LUCA.
GeneTree; ENSGT00670000097750; -.
HOGENOM; HOG000007511; -.
HOVERGEN; HBG057958; -.
InParanoid; Q8NFA0; -.
KO; K11837; -.
OMA; SDNNNQC; -.
OrthoDB; EOG091G01VD; -.
PhylomeDB; Q8NFA0; -.
TreeFam; TF324190; -.
ChiTaRS; USP32; human.
GenomeRNAi; 84669; -.
PRO; PR:Q8NFA0; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000170832; Expressed in 219 organ(s), highest expression level in corpus callosum.
CleanEx; HS_USP10; -.
CleanEx; HS_USP32; -.
ExpressionAtlas; Q8NFA0; baseline and differential.
Genevisible; Q8NFA0; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
CDD; cd00051; EFh; 1.
InterPro; IPR035927; DUSP-like_sf.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR038765; Papain_like_cys_pep_sf.
InterPro; IPR006615; Pept_C19_DUSP.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR028135; Ub_USP-typ.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
Pfam; PF06337; DUSP; 1.
Pfam; PF13202; EF-hand_5; 2.
Pfam; PF14836; Ubiquitin_3; 1.
Pfam; PF00443; UCH; 1.
SMART; SM00695; DUSP; 1.
SMART; SM00054; EFh; 2.
SUPFAM; SSF143791; SSF143791; 2.
SUPFAM; SSF47473; SSF47473; 2.
SUPFAM; SSF54001; SSF54001; 3.
PROSITE; PS51283; DUSP; 1.
PROSITE; PS00018; EF_HAND_1; 2.
PROSITE; PS50222; EF_HAND_2; 3.
PROSITE; PS00972; USP_1; 1.
PROSITE; PS00973; USP_2; 1.
PROSITE; PS50235; USP_3; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Complete proteome; Golgi apparatus;
Hydrolase; Lipoprotein; Membrane; Metal-binding; Methylation;
Phosphoprotein; Polymorphism; Prenylation; Protease;
Reference proteome; Repeat; Thiol protease; Ubl conjugation pathway.
CHAIN 1 1601 Ubiquitin carboxyl-terminal hydrolase 32.
/FTId=PRO_0000080663.
PROPEP 1602 1604 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000396658.
DOMAIN 91 126 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 228 263 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 264 299 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 369 585 DUSP. {ECO:0000255|PROSITE-
ProRule:PRU00613}.
DOMAIN 734 1567 USP.
CA_BIND 241 252 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 277 288 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
ACT_SITE 743 743 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
ACT_SITE 1526 1526 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
MOD_RES 1173 1173 Phosphotyrosine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1350 1350 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1372 1372 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1376 1376 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1454 1454 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1588 1588 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1601 1601 Cysteine methyl ester. {ECO:0000255}.
LIPID 1601 1601 S-farnesyl cysteine. {ECO:0000255}.
VAR_SEQ 380 390 GWLERESRYGL -> TLETDQIYTRN (in isoform
2). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_056307.
VAR_SEQ 391 1604 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056308.
VARIANT 76 76 H -> Y (in dbSNP:rs7208980).
/FTId=VAR_051536.
VARIANT 1469 1469 A -> G (in dbSNP:rs3207630).
/FTId=VAR_051537.
VARIANT 1568 1568 G -> R (in dbSNP:rs1053621).
/FTId=VAR_051538.
VARIANT 1578 1578 T -> I (in dbSNP:rs1053625).
/FTId=VAR_051539.
CONFLICT 884 884 H -> R (in Ref. 2; AAK30207).
{ECO:0000305}.
CONFLICT 1167 1167 C -> S (in Ref. 2; AAK30207).
{ECO:0000305}.
SEQUENCE 1604 AA; 181656 MW; A621F764B76321E3 CRC64;
MGAKESRIGF LSYEEALRRV TDVELKRLKD AFKRTCGLSY YMGQHCFIRE VLGDGVPPKV
AEVIYCSFGG TSKGLHFNNL IVGLVLLTRG KDEEKAKYIF SLFSSESGNY VIREEMERML
HVVDGKVPDT LRKCFSEGEK VNYEKFRNWL FLNKDAFTFS RWLLSGGVYV TLTDDSDTPT
FYQTLAGVTH LEESDIIDLE KRYWLLKAQS RTGRFDLETF GPLVSPPIRP SLSEGLFNAF
DENRDNHIDF KEISCGLSAC CRGPLAERQK FCFKVFDVDR DGVLSRVELR DMVVALLEVW
KDNRTDDIPE LHMDLSDIVE GILNAHDTTK MGHLTLEDYQ IWSVKNVLAN EFLNLLFQVC
HIVLGLRPAT PEEEGQIIRG WLERESRYGL QAGHNWFIIS MQWWQQWKEY VKYDANPVVI
EPSSVLNGGK YSFGTAAHPM EQVEDRIGSS LSYVNTTEEK FSDNISTASE ASETAGSGFL
YSATPGADVC FARQHNTSDN NNQCLLGANG NILLHLNPQK PGAIDNQPLV TQEPVKATSL
TLEGGRLKRT PQLIHGRDYE MVPEPVWRAL YHWYGANLAL PRPVIKNSKT DIPELELFPR
YLLFLRQQPA TRTQQSNIWV NMGNVPSPNA PLKRVLAYTG CFSRMQTIKE IHEYLSQRLR
IKEEDMRLWL YNSENYLTLL DDEDHKLEYL KIQDEQHLVI EVRNKDMSWP EEMSFIANSS
KIDRHKVPTE KGATGLSNLG NTCFMNSSIQ CVSNTQPLTQ YFISGRHLYE LNRTNPIGMK
GHMAKCYGDL VQELWSGTQK NVAPLKLRWT IAKYAPRFNG FQQQDSQELL AFLLDGLHED
LNRVHEKPYV ELKDSDGRPD WEVAAEAWDN HLRRNRSIVV DLFHGQLRSQ VKCKTCGHIS
VRFDPFNFLS LPLPMDSYMH LEITVIKLDG TTPVRYGLRL NMDEKYTGLK KQLSDLCGLN
SEQILLAEVH GSNIKNFPQD NQKVRLSVSG FLCAFEIPVP VSPISASSPT QTDFSSSPST
NEMFTLTTNG DLPRPIFIPN GMPNTVVPCG TEKNFTNGMV NGHMPSLPDS PFTGYIIAVH
RKMMRTELYF LSSQKNRPSL FGMPLIVPCT VHTRKKDLYD AVWIQVSRLA SPLPPQEASN
HAQDCDDSMG YQYPFTLRVV QKDGNSCAWC PWYRFCRGCK IDCGEDRAFI GNAYIAVDWD
PTALHLRYQT SQERVVDEHE SVEQSRRAQA EPINLDSCLR AFTSEEELGE NEMYYCSKCK
THCLATKKLD LWRLPPILII HLKRFQFVNG RWIKSQKIVK FPRESFDPSA FLVPRDPALC
QHKPLTPQGD ELSEPRILAR EVKKVDAQSS AGEEDVLLSK SPSSLSANII SSPKGSPSSS
RKSGTSCPSS KNSSPNSSPR TLGRSKGRLR LPQIGSKNKL SSSKENLDAS KENGAGQICE
LADALSRGHV LGGSQPELVT PQDHEVALAN GFLYEHEACG NGYSNGQLGN HSEEDSTDDQ
REDTRIKPIY NLYAISCHSG ILGGGHYVTY AKNPNCKWYC YNDSSCKELH PDEIDTDSAY
ILFYEQQGID YAQFLPKTDG KKMADTSSMD EDFESDYKKY CVLQ


Related products :

Catalog number Product name Quantity
EIAAB45037 Deubiquitinating enzyme 32,Homo sapiens,Human,Renal carcinoma antigen NY-REN-60,Ubiquitin carboxyl-terminal hydrolase 32,Ubiquitin thiolesterase 32,Ubiquitin-specific-processing protease 32,USP10,USP3
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
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
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
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
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
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
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
EIAAB45048 Bos taurus,Bovine,Deubiquitinating enzyme 37,Ubiquitin carboxyl-terminal hydrolase 37,Ubiquitin thiolesterase 37,Ubiquitin-specific-processing protease 37,USP37
EIAAB45038 Bos taurus,Bovine,Deubiquitinating enzyme 33,Ubiquitin carboxyl-terminal hydrolase 33,Ubiquitin thiolesterase 33,Ubiquitin-specific-processing protease 33,USP33
EIAAB45033 Deubiquitinating enzyme 3,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 3,Ubiquitin thiolesterase 3,Ubiquitin-specific-processing protease 3,Usp3
EIAAB44970 Deubiquitinating enzyme 1,Rat,Rattus norvegicus,Ubiquitin carboxyl-terminal hydrolase 1,Ubiquitin thiolesterase 1,Ubiquitin-specific-processing protease 1,Usp1


 

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