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 6 (EC 3.4.19.12) (Deubiquitinating enzyme 6) (Proto-oncogene TRE-2) (Ubiquitin thioesterase 6) (Ubiquitin-specific-processing protease 6)

 UBP6_HUMAN              Reviewed;        1406 AA.
P35125; Q15634; Q86WP6; Q8IWT4;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
19-JUL-2004, sequence version 2.
25-OCT-2017, entry version 149.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 6;
EC=3.4.19.12;
AltName: Full=Deubiquitinating enzyme 6;
AltName: Full=Proto-oncogene TRE-2;
AltName: Full=Ubiquitin thioesterase 6;
AltName: Full=Ubiquitin-specific-processing protease 6;
Name=USP6; Synonyms=HRP1, TRE2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), TISSUE SPECIFICITY, AND
VARIANTS ARG-475 AND GLN-912.
TISSUE=Ewing sarcoma;
PubMed=1565468;
Nakamura T., Hillova J., Mariage-Samson R., Onno M., Huebner K.,
Cannizzaro L.A., Boghosian-Sell L., Croce C.M., Hill M.;
"A novel transcriptional unit of the tre oncogene widely expressed in
human cancer cells.";
Oncogene 7:733-741(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), ALTERNATIVE
SPLICING, TISSUE SPECIFICITY, AND DISCUSSION OF TRE2 EVOLUTION.
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).
[3]
CHARACTERIZATION.
PubMed=8247125; DOI=10.1038/366313a0;
Papa F.R., Hochstrasser M.;
"The yeast DOA4 gene encodes a deubiquitinating enzyme related to a
product of the human tre-2 oncogene.";
Nature 366:313-319(1993).
[4]
MUTAGENESIS OF THR-150 AND ARG-187.
PubMed=14521938; DOI=10.1016/j.bbrc.2003.09.051;
Bizimungu C., De Neve N., Burny A., Bach S., Bontemps F.,
Portetelle D., Vandenbol M.;
"Expression in a RabGAP yeast mutant of two human homologues, one of
which is an oncogene.";
Biochem. Biophys. Res. Commun. 310:498-504(2003).
[5]
SUBCELLULAR LOCATION, AND INTERACTION WITH RAC1 AND CDC42.
PubMed=12612085; DOI=10.1128/MCB.23.6.2151-2161.2003;
Masuda-Robens J.M., Kutney S.N., Qi H., Chou M.M.;
"The TRE17 oncogene encodes a component of a novel effector pathway
for Rho GTPases Cdc42 and Rac1 and stimulates actin remodeling.";
Mol. Cell. Biol. 23:2151-2161(2003).
[6]
CHROMOSOMAL TRANSLOCATION WITH CDH11.
PubMed=15026324; DOI=10.1158/0008-5472.CAN-03-2827;
Oliveira A.M., Hsi B.L., Weremowicz S., Rosenberg A.E., Dal Cin P.,
Joseph N., Bridge J.A., Perez-Atayde A.R., Fletcher J.A.;
"USP6 (Tre2) fusion oncogenes in aneurysmal bone cyst.";
Cancer Res. 64:1920-1923(2004).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ARF6.
PubMed=15509780; DOI=10.1128/MCB.24.22.9752-9762.2004;
Martinu L., Masuda-Robens J.M., Robertson S.E., Santy L.C.,
Casanova J.E., Chou M.M.;
"The TBC (Tre-2/Bub2/Cdc16) domain protein TRE17 regulates plasma
membrane-endosomal trafficking through activation of Arf6.";
Mol. Cell. Biol. 24:9752-9762(2004).
[8]
FUNCTION, INTERACTION WITH CALMODULIN, UBIQUITINATION, AND MUTAGENESIS
OF CYS-541.
PubMed=16127172; DOI=10.1074/jbc.M505220200;
Shen C., Ye Y., Robertson S.E., Lau A.W., Mak D.O., Chou M.M.;
"Calcium/calmodulin regulates ubiquitination of the ubiquitin-specific
protease TRE17/USP6.";
J. Biol. Chem. 280:35967-35973(2005).
[9]
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).
[10]
FUNCTION.
PubMed=20418905; DOI=10.1038/onc.2010.116;
Ye Y., Pringle L.M., Lau A.W., Riquelme D.N., Wang H., Jiang T.,
Lev D., Welman A., Blobel G.A., Oliveira A.M., Chou M.M.;
"TRE17/USP6 oncogene translocated in aneurysmal bone cyst induces
matrix metalloproteinase production via activation of NF-kappaB.";
Oncogene 29:3619-3629(2010).
-!- FUNCTION: Deubiquitinase with an ATP-independent isopeptidase
activity, cleaving at the C-terminus of the ubiquitin moiety.
Catalyzes its own deubiquitination. In vitro, isoform 2, but not
isoform 3, shows deubiquitinating activity. Promotes plasma
membrane localization of ARF6 and selectively regulates ARF6-
dependent endocytic protein trafficking. Is able to initiate
tumorigenesis by inducing the production of matrix
metalloproteinases following NF-kappa-B activation.
{ECO:0000269|PubMed:15509780, ECO:0000269|PubMed:16127172,
ECO:0000269|PubMed:20418905}.
-!- 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).
-!- SUBUNIT: Interacts with RAC1 and CDC42. Interacts (via Rab-GAP TBC
domain) with ARF6. Interacts with calmodulin (CALM1, CALM2 and/or
CALM3); the interaction is calcium-dependent.
{ECO:0000269|PubMed:12612085, ECO:0000269|PubMed:15509780,
ECO:0000269|PubMed:16127172}.
-!- INTERACTION:
Q8N8A2:ANKRD44; NbExp=4; IntAct=EBI-954590, EBI-1245329;
P10916:MYL2; NbExp=5; IntAct=EBI-954590, EBI-725770;
-!- SUBCELLULAR LOCATION: Cell membrane. Cytoplasm. Endosome.
Note=Localizes to the plasma membrane and to filamentous
structures within the cell corresponding to ARF6 regulated tubular
endosomes. Activation of RAC1 and CDC42 can direct the
relocalization of USP6 to the plasma membrane in a manner that
depends on the integrity of the actin cytoskeleton.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P35125-1; Sequence=Displayed;
Name=2; Synonyms=213(ORF2);
IsoId=P35125-2; Sequence=VSP_010878, VSP_010879;
Name=3; Synonyms=210(ORF1), oncTre210p;
IsoId=P35125-3; Sequence=VSP_010880, VSP_010881;
Note=Was shown to be tumorigenic in transfected mice and seems
not to act as GTPase activating protein.;
-!- TISSUE SPECIFICITY: Testis specific. Expressed in various cancer
cell lines. {ECO:0000269|PubMed:12604796,
ECO:0000269|PubMed:1565468}.
-!- DOMAIN: The Rab-GAP TBC domain lacks GTPase activator activity but
is necessary for interaction with ARF6.
-!- PTM: Monubiquitinated; ubiquitination is calmodulin and calcium
dependent. {ECO:0000269|PubMed:16127172}.
-!- DISEASE: Note=A chromosomal aberration involving USP6 is a common
genetic feature of aneurysmal bone cyst, a benign osseous
neoplasm. Translocation t(16;17)(q22;p13) with CDH11. The
translocation generates a fusion gene in which the strong CDH11
promoter is fused to the entire USP6 coding sequence, resulting in
USP6 transcriptional up-regulation (PubMed:15026324).
{ECO:0000269|PubMed:15026324}.
-!- MISCELLANEOUS: The USP6 gene only exists in the primate lineage.
-!- 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/USP6ID530ch17p13.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X63546; CAA45108.1; -; mRNA.
EMBL; X63547; CAA45111.1; -; mRNA.
EMBL; AY143550; AAN38838.1; -; mRNA.
EMBL; AY163314; AAO21348.1; -; Genomic_DNA.
CCDS; CCDS11069.2; -. [P35125-1]
PIR; S57867; S57867.
PIR; S57868; S22158.
PIR; S57874; S22155.
RefSeq; NP_001291213.1; NM_001304284.1.
RefSeq; NP_004496.2; NM_004505.3. [P35125-1]
RefSeq; XP_011522352.1; XM_011524050.1. [P35125-1]
RefSeq; XP_011522353.1; XM_011524051.2. [P35125-1]
RefSeq; XP_011522354.1; XM_011524052.2. [P35125-1]
RefSeq; XP_011522355.1; XM_011524053.2. [P35125-1]
RefSeq; XP_011522356.1; XM_011524054.2. [P35125-1]
RefSeq; XP_011522357.1; XM_011524055.2. [P35125-1]
RefSeq; XP_011522358.1; XM_011524056.2. [P35125-1]
RefSeq; XP_011522361.1; XM_011524059.2. [P35125-3]
RefSeq; XP_016880779.1; XM_017025290.1. [P35125-1]
UniGene; Hs.448851; -.
ProteinModelPortal; P35125; -.
SMR; P35125; -.
BioGrid; 114552; 13.
IntAct; P35125; 5.
MINT; MINT-2865848; -.
STRING; 9606.ENSP00000250066; -.
MEROPS; C19.009; -.
iPTMnet; P35125; -.
PhosphoSitePlus; P35125; -.
BioMuta; USP6; -.
DMDM; 50403738; -.
EPD; P35125; -.
MaxQB; P35125; -.
PaxDb; P35125; -.
PeptideAtlas; P35125; -.
PRIDE; P35125; -.
DNASU; 9098; -.
Ensembl; ENST00000250066; ENSP00000250066; ENSG00000129204. [P35125-1]
Ensembl; ENST00000572949; ENSP00000461581; ENSG00000129204. [P35125-3]
Ensembl; ENST00000574788; ENSP00000460380; ENSG00000129204. [P35125-1]
GeneID; 9098; -.
KEGG; hsa:9098; -.
UCSC; uc002gau.2; human. [P35125-1]
CTD; 9098; -.
DisGeNET; 9098; -.
EuPathDB; HostDB:ENSG00000129204.16; -.
GeneCards; USP6; -.
H-InvDB; HIX0202554; -.
HGNC; HGNC:12629; USP6.
HPA; HPA046969; -.
MIM; 604334; gene.
neXtProt; NX_P35125; -.
OpenTargets; ENSG00000129204; -.
PharmGKB; PA37254; -.
eggNOG; KOG1102; Eukaryota.
eggNOG; KOG1870; Eukaryota.
eggNOG; COG5210; LUCA.
eggNOG; COG5560; LUCA.
GeneTree; ENSGT00670000097750; -.
HOGENOM; HOG000154762; -.
InParanoid; P35125; -.
KO; K11837; -.
OMA; VHDSNIK; -.
OrthoDB; EOG091G01VD; -.
PhylomeDB; P35125; -.
TreeFam; TF324190; -.
SIGNOR; P35125; -.
ChiTaRS; USP6; human.
GeneWiki; USP6; -.
GenomeRNAi; 9098; -.
PRO; PR:P35125; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000129204; -.
CleanEx; HS_USP6; -.
ExpressionAtlas; P35125; baseline and differential.
Genevisible; P35125; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005764; C:lysosome; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:UniProtKB.
GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
GO; GO:0003676; F:nucleic acid binding; TAS:ProtInc.
GO; GO:0017137; F:Rab GTPase binding; IBA:GO_Central.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:UniProtKB.
GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
GO; GO:0006464; P:cellular protein modification process; NAS:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
GO; GO:0031338; P:regulation of vesicle fusion; IBA:GO_Central.
GO; GO:0060627; P:regulation of vesicle-mediated transport; IDA:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR000195; Rab-GTPase-TBC_dom.
InterPro; IPR035969; Rab-GTPase_TBC_sf.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
Pfam; PF00566; RabGAP-TBC; 1.
Pfam; PF00443; UCH; 1.
SMART; SM00164; TBC; 1.
SUPFAM; SSF47923; SSF47923; 2.
PROSITE; PS50086; TBC_RABGAP; 1.
PROSITE; PS00972; USP_1; 1.
PROSITE; PS00973; USP_2; 1.
PROSITE; PS50235; USP_3; 1.
1: Evidence at protein level;
Alternative splicing; Calmodulin-binding; Cell membrane;
Chromosomal rearrangement; Complete proteome; Cytoplasm; Endosome;
Hydrolase; Membrane; Polymorphism; Protease; Proto-oncogene;
Reference proteome; Thiol protease; Ubl conjugation;
Ubl conjugation pathway.
CHAIN 1 1406 Ubiquitin carboxyl-terminal hydrolase 6.
/FTId=PRO_0000080625.
DOMAIN 100 292 Rab-GAP TBC. {ECO:0000255|PROSITE-
ProRule:PRU00163}.
DOMAIN 532 1369 USP.
ACT_SITE 541 541 Nucleophile.
ACT_SITE 1328 1328 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
VAR_SEQ 1 317 Missing (in isoform 2).
{ECO:0000303|PubMed:1565468}.
/FTId=VSP_010878.
VAR_SEQ 318 359 GLWARLRNQFFDTWAMNDDTVLKHLRASTKKLTRKQGDLPP
P -> MPQRLPHARQHTPLPLGSADYRRVVSVRPQGPHRDP
KDSRDA (in isoform 2).
{ECO:0000303|PubMed:1565468}.
/FTId=VSP_010879.
VAR_SEQ 774 786 NFPQDNQKVQLSV -> ISPLHHLQMECSP (in
isoform 3). {ECO:0000303|PubMed:1565468}.
/FTId=VSP_010880.
VAR_SEQ 787 1406 Missing (in isoform 3).
{ECO:0000303|PubMed:1565468}.
/FTId=VSP_010881.
VARIANT 475 475 W -> R (in dbSNP:rs8073787).
{ECO:0000269|PubMed:1565468}.
/FTId=VAR_051522.
VARIANT 525 525 V -> I (in dbSNP:rs2304449).
/FTId=VAR_059749.
VARIANT 912 912 R -> Q (in dbSNP:rs9899177).
{ECO:0000269|PubMed:1565468}.
/FTId=VAR_051523.
MUTAGEN 150 150 T->R: Does not restore GAP activity in
yeast complementation assay.
{ECO:0000269|PubMed:14521938}.
MUTAGEN 187 187 R->Q: Does not restore GAP activity in
yeast complementation assay.
{ECO:0000269|PubMed:14521938}.
MUTAGEN 541 541 C->S: Loss of enzyme activity.
{ECO:0000269|PubMed:16127172}.
CONFLICT 963 963 N -> I (in Ref. 1; CAA45111).
{ECO:0000305}.
SEQUENCE 1406 AA; 158658 MW; D3A6822CEB441DB3 CRC64;
MDMVENADSL QAQERKDILM KYDKGHRAGL PEDKGPEPVG INSSIDRFGI LHETELPPVT
AREAKKIRRE MTRTSKWMEM LGEWETYKHS SKLIDRVYKG IPMNIRGPVW SVLLNIQEIK
LKNPGRYQIM KERGKRSSEH IHHIDLDVRT TLRNHVFFRD RYGAKQRELF YILLAYSEYN
PEVGYCRDLS HITALFLLYL PEEDAFWALV QLLASERHSL PGFHSPNGGT VQGLQDQQEH
VVPKSQPKTM WHQDKEGLCG QCASLGCLLR NLIDGISLGL TLRLWDVYLV EGEQVLMPIT
SIALKVQQKR LMKTSRCGLW ARLRNQFFDT WAMNDDTVLK HLRASTKKLT RKQGDLPPPA
KREQGSLAPR PVPASRGGKT LCKGYRQAPP GPPAQFQRPI CSASPPWASR FSTPCPGGAV
REDTYPVGTQ GVPSLALAQG GPQGSWRFLE WKSMPRLPTD LDIGGPWFPH YDFEWSCWVR
AISQEDQLAT CWQAEHCGEV HNKDMSWPEE MSFTANSSKI DRQKVPTEKG ATGLSNLGNT
CFMNSSIQCV SNTQPLTQYF ISGRHLYELN RTNPIGMKGH MAKCYGDLVQ ELWSGTQKSV
APLKLRRTIA KYAPKFDGFQ QQDSQELLAF LLDGLHEDLN RVHEKPYVEL KDSDGRPDWE
VAAEAWDNHL RRNRSIIVDL FHGQLRSQVK CKTCGHISVR FDPFNFLSLP LPMDSYMDLE
ITVIKLDGTT PVRYGLRLNM DEKYTGLKKQ LRDLCGLNSE QILLAEVHDS NIKNFPQDNQ
KVQLSVSGFL CAFEIPVPSS PISASSPTQI DFSSSPSTNG MFTLTTNGDL PKPIFIPNGM
PNTVVPCGTE KNFTNGMVNG HMPSLPDSPF TGYIIAVHRK MMRTELYFLS PQENRPSLFG
MPLIVPCTVH TRKKDLYDAV WIQVSWLARP LPPQEASIHA QDRDNCMGYQ YPFTLRVVQK
DGNSCAWCPQ YRFCRGCKID CGEDRAFIGN AYIAVDWHPT ALHLRYQTSQ ERVVDKHESV
EQSRRAQAEP INLDSCLRAF TSEEELGESE MYYCSKCKTH CLATKKLDLW RLPPFLIIHL
KRFQFVNDQW IKSQKIVRFL RESFDPSAFL VPRDPALCQH KPLTPQGDEL SKPRILAREV
KKVDAQSSAG KEDMLLSKSP SSLSANISSS PKGSPSSSRK SGTSCPSSKN SSPNSSPRTL
GRSKGRLRLP QIGSKNKPSS SKKNLDASKE NGAGQICELA DALSRGHMRG GSQPELVTPQ
DHEVALANGF LYEHEACGNG CGDGYSNGQL GNHSEEDSTD DQREDTHIKP IYNLYAISCH
SGILSGGHYI TYAKNPNCKW YCYNDSSCEE LHPDEIDTDS AYILFYEQQG IDYAQFLPKI
DGKKMADTSS TDEDSESDYE KYSMLQ


Related products :

Catalog number Product name Quantity
EIAAB45092 Deubiquitinating enzyme 6,Homo sapiens,HRP1,Human,Proto-oncogene TRE-2,TRE2,Ubiquitin carboxyl-terminal hydrolase 6,Ubiquitin thiolesterase 6,Ubiquitin-specific-processing protease 6,USP6
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
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
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
EIAAB45058 Deubiquitinating enzyme 40,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 40,Ubiquitin thiolesterase 40,Ubiquitin-specific-processing protease 40,Usp40
EIAAB45007 Bos taurus,Bovine,Deubiquitinating enzyme 20,Ubiquitin carboxyl-terminal hydrolase 20,Ubiquitin thiolesterase 20,Ubiquitin-specific-processing protease 20,USP20
EIAAB45017 Deubiquitinating enzyme 24,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 24,Ubiquitin thiolesterase 24,Ubiquitin-specific-processing protease 24,Usp24
EIAAB45014 Bos taurus,Bovine,Deubiquitinating enzyme 22,Ubiquitin carboxyl-terminal hydrolase 22,Ubiquitin thiolesterase 22,Ubiquitin-specific-processing protease 22,USP22


 

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