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) (Ubiquitin thioesterase 6) (Ubiquitin-specific-processing protease 6)

 UBP6_YEAST              Reviewed;         499 AA.
P43593; D6VTP0;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
12-SEP-2018, entry version 176.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 6;
EC=3.4.19.12;
AltName: Full=Deubiquitinating enzyme 6;
AltName: Full=Ubiquitin thioesterase 6;
AltName: Full=Ubiquitin-specific-processing protease 6;
Name=UBP6; OrderedLocusNames=YFR010W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7670463; DOI=10.1038/ng0795-261;
Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M.,
Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K.,
Yamazaki M., Tashiro H., Eki T.;
"Analysis of the nucleotide sequence of chromosome VI from
Saccharomyces cerevisiae.";
Nat. Genet. 10:261-268(1995).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=9344467; DOI=10.1006/abbi.1997.0311;
Park K.C., Woo S.K., Yoo Y.J., Wyndham A.M., Baker R.T., Chung C.H.;
"Purification and characterization of UBP6, a new ubiquitin-specific
protease in Saccharomyces cerevisiae.";
Arch. Biochem. Biophys. 347:78-84(1997).
[4]
FUNCTION.
PubMed=10527495; DOI=10.1006/abio.1999.4234;
Layfield R., Franklin K., Landon M., Walker G., Wang P., Ramage R.,
Brown A., Love S., Urquhart K., Muir T., Baker R., Mayer R.J.;
"Chemically synthesized ubiquitin extension proteins detect distinct
catalytic capacities of deubiquitinating enzymes.";
Anal. Biochem. 274:40-49(1999).
[5]
DOMAIN.
PubMed=10386876; DOI=10.1110/ps.8.6.1268;
Wyndham A.M., Baker R.T., Chelvanayagam G.;
"The Ubp6 family of deubiquitinating enzymes contains a ubiquitin-like
domain: SUb.";
Protein Sci. 8:1268-1275(1999).
[6]
ASSOCIATION WITH THE 26S PROTEASOME, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=11029046; DOI=10.1091/mbc.11.10.3425;
Verma R., Chen S., Feldman R., Schieltz D., Yates J., Dohmen J.,
Deshaies R.J.;
"Proteasomal proteomics: identification of nucleotide-sensitive
proteasome-interacting proteins by mass spectrometric analysis of
affinity-purified proteasomes.";
Mol. Biol. Cell 11:3425-3439(2000).
[7]
IDENTIFICATION BY MASS SPECTROMETRY, ASSOCIATION WITH THE 26S
PROTEASOME, FUNCTION, ACTIVITY REGULATION, AND DOMAIN.
PubMed=12408819; DOI=10.1016/S1097-2765(02)00638-X;
Leggett D.S., Hanna J., Borodovsky A., Crosas B., Schmidt M.,
Baker R.T., Walz T., Ploegh H., Finley D.;
"Multiple associated proteins regulate proteasome structure and
function.";
Mol. Cell 10:495-507(2002).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[9]
FUNCTION.
PubMed=14581483; DOI=10.1074/jbc.M307050200;
Guterman A., Glickman M.H.;
"Complementary roles for Rpn11 and Ubp6 in deubiquitination and
proteolysis by the proteasome.";
J. Biol. Chem. 279:1729-1738(2004).
[10]
FUNCTION.
PubMed=17018280; DOI=10.1016/j.cell.2006.07.038;
Hanna J., Hathaway N.A., Tone Y., Crosas B., Elsasser S.,
Kirkpatrick D.S., Leggett D.S., Gygi S.P., King R.W., Finley D.;
"Deubiquitinating enzyme Ubp6 functions noncatalytically to delay
proteasomal degradation.";
Cell 127:99-111(2006).
[11]
FUNCTION.
PubMed=17190603; DOI=10.1016/j.cell.2006.09.051;
Crosas B., Hanna J., Kirkpatrick D.S., Zhang D.P., Tone Y.,
Hathaway N.A., Buecker C., Leggett D.S., Schmidt M., King R.W.,
Gygi S.P., Finley D.;
"Ubiquitin chains are remodeled at the proteasome by opposing
ubiquitin ligase and deubiquitinating activities.";
Cell 127:1401-1413(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-389, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-389 AND SER-470, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-389, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[15]
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).
[16]
X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 97-499.
Joint center for structural genomics (JCSG);
"Crystal structure of ubiquitin carboxyl-terminal hydrolase 6
(yfr010w) from saccharomyces cerevisiae at 1.74 a resolution.";
Submitted (JUL-2009) to the PDB data bank.
-!- FUNCTION: Predominant proteasome-associated deubiquitinase which
releases ubiquitin from the proteasome targeted ubiquitinated
proteins. Ensures the regeneration of ubiquitin at the proteasome.
Has proteasome-inhibitory activity and delays the degradation of
ubiquitinated proteins to provide a time window allowing gradual
deubiquitination of the substrate. Stabilizes the association of
HUL5 with proteasomes and works in opposition to polyubiquitin
elongation activity of HUL5. {ECO:0000269|PubMed:10527495,
ECO:0000269|PubMed:12408819, ECO:0000269|PubMed:14581483,
ECO:0000269|PubMed:17018280, ECO:0000269|PubMed:17190603,
ECO:0000269|PubMed:9344467}.
-!- 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).
-!- ACTIVITY REGULATION: Activated by it's association with the
proteasome. {ECO:0000269|PubMed:12408819}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 8.5-9. {ECO:0000269|PubMed:9344467};
-!- SUBUNIT: Associates with the regulatory particle (RP) of the
proteasome.
-!- DOMAIN: The N-terminal ubiquitin-like domain is required for
proteasome association and UBP6 activation at the proteasome.
{ECO:0000269|PubMed:10386876, ECO:0000269|PubMed:12408819}.
-!- MISCELLANEOUS: Present with 6770 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the peptidase C19 family. USP14/UBP6
subfamily. {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; D50617; BAA09249.1; -; Genomic_DNA.
EMBL; BK006940; DAA12450.1; -; Genomic_DNA.
PIR; S56265; S56265.
RefSeq; NP_116665.1; NM_001179975.1.
PDB; 1VJV; X-ray; 1.74 A; A=97-499.
PDB; 5A5B; EM; 9.50 A; 8=97-499.
PDB; 5MPC; EM; 7.70 A; 8=1-499.
PDBsum; 1VJV; -.
PDBsum; 5A5B; -.
PDBsum; 5MPC; -.
ProteinModelPortal; P43593; -.
SMR; P43593; -.
BioGrid; 31160; 640.
DIP; DIP-6731N; -.
IntAct; P43593; 25.
MINT; P43593; -.
STRING; 4932.YFR010W; -.
MEROPS; C19.079; -.
MoonProt; P43593; -.
iPTMnet; P43593; -.
MaxQB; P43593; -.
PaxDb; P43593; -.
PRIDE; P43593; -.
EnsemblFungi; BAA09249; BAA09249; BAA09249.
EnsemblFungi; YFR010W; YFR010W; YFR010W.
GeneID; 850562; -.
KEGG; sce:YFR010W; -.
EuPathDB; FungiDB:YFR010W; -.
SGD; S000001906; UBP6.
GeneTree; ENSGT00390000009615; -.
HOGENOM; HOG000202292; -.
InParanoid; P43593; -.
KO; K11843; -.
OMA; KVNQQPK; -.
OrthoDB; EOG092C3DT5; -.
BioCyc; YEAST:G3O-30463-MONOMER; -.
Reactome; R-SCE-5689880; Ub-specific processing proteases.
EvolutionaryTrace; P43593; -.
PRO; PR:P43593; -.
Proteomes; UP000002311; Chromosome VI.
GO; GO:0000502; C:proteasome complex; IPI:SGD.
GO; GO:0005838; C:proteasome regulatory particle; IPI:SGD.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:SGD.
GO; GO:0072671; P:mitochondria-associated ubiquitin-dependent protein catabolic process; IMP:SGD.
GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; IMP:SGD.
GO; GO:0016579; P:protein deubiquitination; IMP:SGD.
GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:CACAO.
InterPro; IPR038765; Papain_like_cys_pep_sf.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR029071; Ubiquitin-like_domsf.
InterPro; IPR000626; Ubiquitin_dom.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
Pfam; PF00443; UCH; 1.
SMART; SM00213; UBQ; 1.
SUPFAM; SSF54001; SSF54001; 1.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS00972; USP_1; 1.
PROSITE; PS00973; USP_2; 1.
PROSITE; PS50235; USP_3; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Hydrolase; Phosphoprotein; Protease;
Reference proteome; Thiol protease; Ubl conjugation pathway.
CHAIN 1 499 Ubiquitin carboxyl-terminal hydrolase 6.
/FTId=PRO_0000080591.
DOMAIN 6 80 Ubiquitin-like.
DOMAIN 109 497 USP.
ACT_SITE 118 118 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
ACT_SITE 447 447 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
MOD_RES 389 389 Phosphothreonine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 470 470 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
HELIX 118 129 {ECO:0000244|PDB:1VJV}.
HELIX 131 138 {ECO:0000244|PDB:1VJV}.
HELIX 142 144 {ECO:0000244|PDB:1VJV}.
HELIX 154 172 {ECO:0000244|PDB:1VJV}.
HELIX 182 191 {ECO:0000244|PDB:1VJV}.
HELIX 193 196 {ECO:0000244|PDB:1VJV}.
HELIX 210 225 {ECO:0000244|PDB:1VJV}.
HELIX 227 230 {ECO:0000244|PDB:1VJV}.
TURN 231 233 {ECO:0000244|PDB:1VJV}.
STRAND 235 243 {ECO:0000244|PDB:1VJV}.
STRAND 246 253 {ECO:0000244|PDB:1VJV}.
STRAND 257 259 {ECO:0000244|PDB:1VJV}.
STRAND 261 263 {ECO:0000244|PDB:1VJV}.
HELIX 272 280 {ECO:0000244|PDB:1VJV}.
STRAND 297 305 {ECO:0000244|PDB:1VJV}.
STRAND 307 314 {ECO:0000244|PDB:1VJV}.
STRAND 317 320 {ECO:0000244|PDB:1VJV}.
TURN 321 324 {ECO:0000244|PDB:1VJV}.
STRAND 325 328 {ECO:0000244|PDB:1VJV}.
STRAND 337 340 {ECO:0000244|PDB:1VJV}.
HELIX 342 344 {ECO:0000244|PDB:1VJV}.
HELIX 347 369 {ECO:0000244|PDB:1VJV}.
HELIX 390 413 {ECO:0000244|PDB:1VJV}.
STRAND 426 442 {ECO:0000244|PDB:1VJV}.
STRAND 445 453 {ECO:0000244|PDB:1VJV}.
STRAND 461 465 {ECO:0000244|PDB:1VJV}.
STRAND 468 472 {ECO:0000244|PDB:1VJV}.
HELIX 474 478 {ECO:0000244|PDB:1VJV}.
HELIX 479 481 {ECO:0000244|PDB:1VJV}.
STRAND 488 496 {ECO:0000244|PDB:1VJV}.
SEQUENCE 499 AA; 57111 MW; DAE54D1F8AC9960C CRC64;
MSGETFEFNI RHSGKVYPIT LSTDATSADL KSKAEELTQV PSARQKYMVK GGLSGEESIK
IYPLIKPGST VMLLGTPDAN LISKPAKKNN FIEDLAPEQQ VQQFAQLPVG FKNMGNTCYL
NATLQALYRV NDLRDMILNY NPSQGVSNSG AQDEEIHKQI VIEMKRCFEN LQNKSFKSVL
PIVLLNTLRK CYPQFAERDS QGGFYKQQDA EELFTQLFHS MSIVFGDKFS EDFRIQFKTT
IKDTANDNDI TVKENESDSK LQCHISGTTN FMRNGLLEGL NEKIEKRSDL TGANSIYSVE
KKISRLPKFL TVQYVRFFWK RSTNKKSKIL RKVVFPFQLD VADMLTPEYA AEKVKVRDEL
RKVEKEKNEK EREIKRRKFD PSSSENVMTP REQYETQVAL NESEKDQWLE EYKKHFPPNL
EKGENPSCVY NLIGVITHQG ANSESGHYQA FIRDELDENK WYKFNDDKVS VVEKEKIESL
AGGGESDSAL ILMYKGFGL


Related products :

Catalog number Product name Quantity
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
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
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
EIAAB45052 Deubiquitinating enzyme 38,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 38,Ubiquitin thiolesterase 38,Ubiquitin-specific-processing protease 38,Usp38
EIAAB45069 Deubiquitinating enzyme 45,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 45,Ubiquitin thiolesterase 45,Ubiquitin-specific-processing protease 45,Usp45
EIAAB45066 Deubiquitinating enzyme 43,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 43,Ubiquitin thiolesterase 43,Ubiquitin-specific-processing protease 43,Usp43
EIAAB45072 Deubiquitinating enzyme 46,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 46,Ubiquitin thiolesterase 46,Ubiquitin-specific-processing protease 46,Usp46
EIAAB45073 Deubiquitinating enzyme 47,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 47,Ubiquitin thiolesterase 47,Ubiquitin-specific-processing protease 47,Usp47


 

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