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Ubiquitin carboxyl-terminal hydrolase 28 (EC 3.4.19.12) (Deubiquitinating enzyme 28) (Ubiquitin thioesterase 28) (Ubiquitin-specific-processing protease 28)

 UBP28_HUMAN             Reviewed;        1077 AA.
Q96RU2; B0YJC0; B0YJC1; Q6NZX9; Q9P213;
27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
31-JAN-2018, entry version 153.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 28;
EC=3.4.19.12;
AltName: Full=Deubiquitinating enzyme 28;
AltName: Full=Ubiquitin thioesterase 28;
AltName: Full=Ubiquitin-specific-processing protease 28;
Name=USP28; Synonyms=KIAA1515;
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).
PubMed=11597335; DOI=10.1186/gb-2001-2-10-research0043;
Valero R., Bayes M., Francisca Sanchez-Font M., Gonzalez-Angulo O.,
Gonzalez-Duarte R., Marfany G.;
"Characterization of alternatively spliced products and tissue-
specific isoforms of USP28 and USP25.";
Genome Biol. 2:RESEARCH0043.1-RESEARCH0043.10(2001).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Eye;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 289-1077 (ISOFORM 2).
TISSUE=Brain;
PubMed=10819331; DOI=10.1093/dnares/7.2.143;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:143-150(2000).
[7]
FUNCTION, INTERACTION WITH TP53BP1, PHOSPHORYLATION AT SER-67 AND
SER-714, AND MUTAGENESIS OF CYS-171.
PubMed=16901786; DOI=10.1016/j.cell.2006.06.039;
Zhang D., Zaugg K., Mak T.W., Elledge S.J.;
"A role for the deubiquitinating enzyme USP28 in control of the DNA-
damage response.";
Cell 126:529-542(2006).
[8]
FUNCTION, AND INTERACTION WITH FBXW7.
PubMed=17873522; DOI=10.4161/cc.6.19.4804;
Popov N., Herold S., Llamazares M., Schulein C., Eilers M.;
"Fbw7 and Usp28 regulate myc protein stability in response to DNA
damage.";
Cell Cycle 6:2327-2331(2007).
[9]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FBXW7, AND
MUTAGENESIS OF CYS-171.
PubMed=17558397; DOI=10.1038/ncb1601;
Popov N., Wanzel M., Madiredjo M., Zhang D., Beijersbergen R.,
Bernards R., Moll R., Elledge S.J., Eilers M.;
"The ubiquitin-specific protease USP28 is required for MYC
stability.";
Nat. Cell Biol. 9:765-774(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[11]
FUNCTION.
PubMed=18662541; DOI=10.1016/j.cell.2008.05.043;
Bassermann F., Frescas D., Guardavaccaro D., Busino L.,
Peschiaroli A., Pagano M.;
"The Cdc14B-Cdh1-Plk1 axis controls the G2 DNA-damage-response
checkpoint.";
Cell 134:256-267(2008).
[12]
DEGRADATION, AND INDUCTION.
PubMed=20046830; DOI=10.1371/journal.pone.0008531;
Li Q., Kluz T., Sun H., Costa M.;
"Mechanisms of c-myc degradation by nickel compounds and hypoxia.";
PLoS ONE 4:E8531-E8531(2009).
[13]
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, 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).
[15]
FUNCTION, INTERACTION WITH PRKD1 AND ZNF304, PHOSPHORYLATION,
MUTAGENESIS OF CYS-171 AND SER-899, AND INDUCTION.
PubMed=24623306; DOI=10.7554/eLife.02313;
Serra R.W., Fang M., Park S.M., Hutchinson L., Green M.R.;
"A KRAS-directed transcriptional silencing pathway that mediates the
CpG island methylator phenotype.";
Elife 3:E02313-E02313(2014).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1048, 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).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-99, SUMOYLATION [LARGE SCALE
ANALYSIS] AT LYS-759 (ISOFORM 2), AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[18]
STRUCTURE BY NMR OF 22-132.
Northeast structural genomics consortium (NESG);
"NMR solution structure of the N-terminal domain of human USP28.";
Submitted (JUL-2012) to the PDB data bank.
-!- FUNCTION: Deubiquitinase involved in DNA damage response
checkpoint and MYC proto-oncogene stability. Involved in DNA
damage induced apoptosis by specifically deubiquitinating proteins
of the DNA damage pathway such as CLSPN. Also involved in G2 DNA
damage checkpoint, by deubiquitinating CLSPN, and preventing its
degradation by the anaphase promoting complex/cyclosome (APC/C).
In contrast, it does not deubiquitinate PLK1. Specifically
deubiquitinates MYC in the nucleoplasm, leading to prevent MYC
degradation by the proteasome: acts by specifically interacting
with isoform 1 of FBXW7 (FBW7alpha) in the nucleoplasm and
counteracting ubiquitination of MYC by the SCF(FBW7) complex. In
contrast, it does not interact with isoform 4 of FBXW7 (FBW7gamma)
in the nucleolus, allowing MYC degradation and explaining the
selective MYC degradation in the nucleolus. Deubiquitinates
ZNF304, hence preventing ZNF304 degradation by the proteasome and
leading to the activated KRAS-mediated promoter hypermethylation
and transcriptional silencing of tumor suppressor genes (TSGs) in
a subset of colorectal cancers (CRC) cells (PubMed:24623306).
{ECO:0000269|PubMed:16901786, ECO:0000269|PubMed:17558397,
ECO:0000269|PubMed:17873522, ECO:0000269|PubMed:18662541,
ECO:0000269|PubMed:24623306}.
-!- 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 ZNF304 (PubMed:24623306). Interacts with
PRKD1 (PubMed:24623306). Interacts with TP53BP1 (PubMed:16901786).
Interacts with isoform 1 of FBXW7; following DNA damage,
dissociates from FBXW7 leading to degradation of MYC
(PubMed:17873522, PubMed:17558397) (PubMed:17873522).
{ECO:0000269|PubMed:16901786, ECO:0000269|PubMed:17558397,
ECO:0000269|PubMed:17873522, ECO:0000269|PubMed:24623306}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
{ECO:0000269|PubMed:17558397}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q96RU2-1; Sequence=Displayed;
Name=2;
IsoId=Q96RU2-2; Sequence=VSP_015580;
Note=Contains a glycyl lysine isopeptide (Lys-Gly) (interchain
with G-Cter in SUMO2) at position 759.
{ECO:0000244|PubMed:28112733};
Name=3;
IsoId=Q96RU2-3; Sequence=VSP_057359, VSP_057360;
Note=No experimental confirmation available.;
-!- INDUCTION: Down-regulated upon hypoxia (PubMed:20046830). Up-
regulated by the transcription factor c-Jun/JUN in a KRAS-
dependent manner in colorectal cancer (CRC) cells
(PubMed:24623306). {ECO:0000269|PubMed:20046830,
ECO:0000269|PubMed:24623306}.
-!- PTM: Degradaded upon nickel ion level or hypoxia exposure.
-!- PTM: Phosphorylated upon DNA damage at Ser-67 and Ser-714, by ATM
or ATR (PubMed:16901786). Phosphorylated by PRKD1
(PubMed:24623306). {ECO:0000269|PubMed:16901786,
ECO:0000269|PubMed:24623306}.
-!- SIMILARITY: Belongs to the peptidase C19 family. USP28 subfamily.
{ECO:0000305}.
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EMBL; AF266283; AAK58565.1; -; mRNA.
EMBL; EF445045; ACA06098.1; -; Genomic_DNA.
EMBL; EF445045; ACA06099.1; -; Genomic_DNA.
EMBL; AP001874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP003170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF455523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF459544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471065; EAW67232.1; -; Genomic_DNA.
EMBL; BC065928; AAH65928.1; -; mRNA.
EMBL; AB040948; BAA96039.1; -; mRNA.
CCDS; CCDS31680.1; -. [Q96RU2-1]
RefSeq; NP_001333187.1; NM_001346258.1. [Q96RU2-2]
RefSeq; NP_001333202.1; NM_001346273.1. [Q96RU2-3]
RefSeq; NP_065937.1; NM_020886.3. [Q96RU2-1]
UniGene; Hs.503891; -.
PDB; 2LVA; NMR; -; A=22-132.
PDB; 2MUU; NMR; -; A=1-120.
PDBsum; 2LVA; -.
PDBsum; 2MUU; -.
ProteinModelPortal; Q96RU2; -.
SMR; Q96RU2; -.
BioGrid; 121683; 70.
IntAct; Q96RU2; 12.
MINT; MINT-8415329; -.
STRING; 9606.ENSP00000003302; -.
ChEMBL; CHEMBL2157853; -.
MEROPS; C19.054; -.
iPTMnet; Q96RU2; -.
PhosphoSitePlus; Q96RU2; -.
BioMuta; USP28; -.
DMDM; 20140700; -.
EPD; Q96RU2; -.
MaxQB; Q96RU2; -.
PaxDb; Q96RU2; -.
PeptideAtlas; Q96RU2; -.
PRIDE; Q96RU2; -.
Ensembl; ENST00000003302; ENSP00000003302; ENSG00000048028. [Q96RU2-1]
Ensembl; ENST00000537706; ENSP00000445743; ENSG00000048028. [Q96RU2-3]
GeneID; 57646; -.
KEGG; hsa:57646; -.
UCSC; uc001poh.4; human. [Q96RU2-1]
CTD; 57646; -.
DisGeNET; 57646; -.
EuPathDB; HostDB:ENSG00000048028.11; -.
GeneCards; USP28; -.
HGNC; HGNC:12625; USP28.
HPA; HPA006778; -.
HPA; HPA006779; -.
MIM; 610748; gene.
neXtProt; NX_Q96RU2; -.
OpenTargets; ENSG00000048028; -.
PharmGKB; PA37250; -.
eggNOG; KOG1863; Eukaryota.
eggNOG; COG5077; LUCA.
GeneTree; ENSGT00390000016082; -.
HOGENOM; HOG000007956; -.
HOVERGEN; HBG056030; -.
InParanoid; Q96RU2; -.
KO; K21122; -.
OMA; CIASTTQ; -.
OrthoDB; EOG091G00QR; -.
PhylomeDB; Q96RU2; -.
TreeFam; TF329035; -.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
SIGNOR; Q96RU2; -.
ChiTaRS; USP28; human.
GenomeRNAi; 57646; -.
PRO; PR:Q96RU2; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000048028; -.
CleanEx; HS_USP28; -.
ExpressionAtlas; Q96RU2; baseline and differential.
Genevisible; Q96RU2; HS.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:UniProtKB.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IMP:UniProtKB.
GO; GO:0008283; P:cell proliferation; IMP:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB.
GO; GO:0000077; P:DNA damage checkpoint; IMP:UniProtKB.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
GO; GO:0007265; P:Ras protein signal transduction; IMP:UniProtKB.
GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
GO; GO:0010212; P:response to ionizing radiation; IDA:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR009060; UBA-like_sf.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
Pfam; PF00443; UCH; 1.
SUPFAM; SSF46934; SSF46934; 1.
PROSITE; PS00972; USP_1; 1.
PROSITE; PS00973; USP_2; 1.
PROSITE; PS50235; USP_3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; DNA damage;
DNA repair; Hydrolase; Isopeptide bond; Nucleus; Phosphoprotein;
Protease; Reference proteome; Thiol protease; Ubl conjugation;
Ubl conjugation pathway.
CHAIN 1 1077 Ubiquitin carboxyl-terminal hydrolase 28.
/FTId=PRO_0000080657.
DOMAIN 97 116 UIM. {ECO:0000305}.
DOMAIN 162 650 USP.
ACT_SITE 171 171 Nucleophile.
ACT_SITE 600 600 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
MOD_RES 67 67 Phosphoserine.
{ECO:0000269|PubMed:16901786}.
MOD_RES 375 375 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 550 550 Phosphoserine.
{ECO:0000250|UniProtKB:Q5I043}.
MOD_RES 714 714 Phosphoserine.
{ECO:0000269|PubMed:16901786}.
MOD_RES 1048 1048 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
CROSSLNK 99 99 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 583 583 P -> E (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_057359.
VAR_SEQ 584 1077 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_057360.
VAR_SEQ 769 800 Missing (in isoform 2).
{ECO:0000303|PubMed:10819331}.
/FTId=VSP_015580.
MUTAGEN 171 171 C->A: Abolishes deubiquitinase activity.
{ECO:0000269|PubMed:16901786,
ECO:0000269|PubMed:17558397,
ECO:0000269|PubMed:24623306}.
MUTAGEN 899 899 S->A: Prevents ZNF304 ubiquitination
reduction. {ECO:0000269|PubMed:24623306}.
CONFLICT 289 303 VQLFYGTFLTEGVRE -> IVIVMSFLKSLSLCL (in
Ref. 4; BAA96039). {ECO:0000305}.
HELIX 7 9 {ECO:0000244|PDB:2MUU}.
HELIX 23 32 {ECO:0000244|PDB:2LVA}.
HELIX 37 46 {ECO:0000244|PDB:2LVA}.
TURN 47 49 {ECO:0000244|PDB:2LVA}.
HELIX 51 58 {ECO:0000244|PDB:2LVA}.
HELIX 60 63 {ECO:0000244|PDB:2LVA}.
STRAND 71 73 {ECO:0000244|PDB:2MUU}.
TURN 84 86 {ECO:0000244|PDB:2MUU}.
STRAND 95 97 {ECO:0000244|PDB:2MUU}.
HELIX 100 111 {ECO:0000244|PDB:2LVA}.
HELIX 121 123 {ECO:0000244|PDB:2LVA}.
SEQUENCE 1077 AA; 122491 MW; 799C758888C67B82 CRC64;
MTAELQQDDA AGAADGHGSS CQMLLNQLRE ITGIQDPSFL HEALKASNGD ITQAVSLLTD
ERVKEPSQDT VATEPSEVEG SAANKEVLAK VIDLTHDNKD DLQAAIALSL LESPKIQADG
RDLNRMHEAT SAETKRSKRK RCEVWGENPN PNDWRRVDGW PVGLKNVGNT CWFSAVIQSL
FQLPEFRRLV LSYSLPQNVL ENCRSHTEKR NIMFMQELQY LFALMMGSNR KFVDPSAALD
LLKGAFRSSE EQQQDVSEFT HKLLDWLEDA FQLAVNVNSP RNKSENPMVQ LFYGTFLTEG
VREGKPFCNN ETFGQYPLQV NGYRNLDECL EGAMVEGDVE LLPSDHSVKY GQERWFTKLP
PVLTFELSRF EFNQSLGQPE KIHNKLEFPQ IIYMDRYMYR SKELIRNKRE CIRKLKEEIK
ILQQKLERYV KYGSGPARFP LPDMLKYVIE FASTKPASES CPPESDTHMT LPLSSVHCSV
SDQTSKESTS TESSSQDVES TFSSPEDSLP KSKPLTSSRS SMEMPSQPAP RTVTDEEINF
VKTCLQRWRS EIEQDIQDLK TCIASTTQTI EQMYCDPLLR QVPYRLHAVL VHEGQANAGH
YWAYIYNQPR QSWLKYNDIS VTESSWEEVE RDSYGGLRNV SAYCLMYIND KLPYFNAEAA
PTESDQMSEV EALSVELKHY IQEDNWRFEQ EVEEWEEEQS CKIPQMESST NSSSQDYSTS
QEPSVASSHG VRCLSSEHAV IVKEQTAQAI ANTARAYEKS GVEAALSEVM LSPAMQGVIL
AIAKARQTFD RDGSEAGLIK AFHEEYSRLY QLAKETPTSH SDPRLQHVLV YFFQNEAPKR
VVERTLLEQF ADKNLSYDER SISIMKVAQA KLKEIGPDDM NMEEYKKWHE DYSLFRKVSV
YLLTGLELYQ KGKYQEALSY LVYAYQSNAA LLMKGPRRGV KESVIALYRR KCLLELNAKA
ASLFETNDDH SVTEGINVMN ELIIPCIHLI INNDISKDDL DAIEVMRNHW CSYLGQDIAE
NLQLCLGEFL PRLLDPSAEI IVLKEPPTIR PNSPYDLCSR FAAVMESIQG VSTVTVK


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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


 

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