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Ubiquitin carboxyl-terminal hydrolase 37 (EC 3.4.19.12) (Deubiquitinating enzyme 37) (Ubiquitin thioesterase 37) (Ubiquitin-specific-processing protease 37)

 UBP37_HUMAN             Reviewed;         979 AA.
Q86T82; A2RUQ8; B7ZM38; B7ZM41; E9PHL3; Q2KHT2; Q53S10; Q7Z3A5;
Q9HCH8;
10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
13-JUL-2010, sequence version 2.
28-MAR-2018, entry version 131.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 37;
EC=3.4.19.12 {ECO:0000269|PubMed:27296872};
AltName: Full=Deubiquitinating enzyme 37;
AltName: Full=Ubiquitin thioesterase 37;
AltName: Full=Ubiquitin-specific-processing protease 37;
Name=USP37; Synonyms=KIAA1594;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
SER-979.
TISSUE=Spinal cord;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-979.
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
SER-979.
TISSUE=Testis;
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 [LARGE SCALE MRNA] OF 49-979 (ISOFORM 1), AND
VARIANT SER-979.
TISSUE=Brain;
PubMed=10997877; DOI=10.1093/dnares/7.4.271;
Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes.
XVIII. The complete sequences of 100 new cDNA clones from brain which
code for large proteins in vitro.";
DNA Res. 7:273-281(2000).
[6]
TISSUE SPECIFICITY, AND ENZYME ACTIVITY.
PubMed=14715245; DOI=10.1016/j.bbrc.2003.12.050;
Quesada V., Diaz-Perales A., Gutierrez-Fernandez A., Garabaya C.,
Cal S., Lopez-Otin C.;
"Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
proteases.";
Biochem. Biophys. Res. Commun. 314:54-62(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-650 AND SER-652, 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).
[8]
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).
[9]
FUNCTION, UBIQUITINATION, PHOSPHORYLATION AT SER-628 BY CDK2, DOMAIN
KEN BOX 3, DEVELOPMENTAL STAGE, INDUCTION, INTERACTION WITH FZR1, AND
MUTAGENESIS OF 32-LYS--ASN-34; 71-ARG-LEU-74; 96-ARG-LEU-99;
160-ARG-LEU-163; 221-LYS--ASN-223; CYS-350; 782-LYS--ASN-784 AND
SER-628.
PubMed=21596315; DOI=10.1016/j.molcel.2011.03.027;
Huang X., Summers M.K., Pham V., Lill J.R., Liu J., Lee G.,
Kirkpatrick D.S., Jackson P.K., Fang G., Dixit V.M.;
"Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) and
promote S phase entry.";
Mol. Cell 42:511-523(2011).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170; SER-210 AND
SER-770, 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).
[11]
CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-350, INTERACTION WITH CDT1, AND
FUNCTION.
PubMed=27296872; DOI=10.1016/j.molonc.2016.05.008;
Hernandez-Perez S., Cabrera E., Amoedo H., Rodriguez-Acebes S.,
Koundrioukoff S., Debatisse M., Mendez J., Freire R.;
"USP37 deubiquitinates Cdt1 and contributes to regulate DNA
replication.";
Mol. Oncol. 10:1196-1206(2016).
-!- FUNCTION: Deubiquitinase that antagonizes the anaphase-promoting
complex (APC/C) during G1/S transition by mediating
deubiquitination of cyclin-A (CCNA1 and CCNA2), thereby promoting
S phase entry. Specifically mediates deubiquitination of 'Lys-11'-
linked polyubiquitin chains, a specific ubiquitin-linkage type
mediated by the APC/C complex. Also mediates deubiquitination of
'Lys-48'-linked polyubiquitin chains in vitro. Phosphorylation at
Ser-628 during G1/S phase maximizes the deubiquitinase activity,
leading to prevent degradation of cyclin-A (CCNA1 and CCNA2)
(PubMed:21596315). Plays an important role in the regulation of
DNA replication by stabilizing the licensing factor CDT1
(PubMed:27296872). {ECO:0000269|PubMed:21596315,
ECO:0000269|PubMed:27296872}.
-!- 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:14715245, ECO:0000269|PubMed:27296872}.
-!- SUBUNIT: Interacts with FZR1/CDH1 (PubMed:21596315). Interacts
with CDT1 (PubMed:27296872). {ECO:0000269|PubMed:21596315,
ECO:0000269|PubMed:27296872}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q86T82-1; Sequence=Displayed;
Name=2;
IsoId=Q86T82-2; Sequence=VSP_041740, VSP_041741;
-!- TISSUE SPECIFICITY: Expressed in brain and prostate.
{ECO:0000269|PubMed:14715245}.
-!- DEVELOPMENTAL STAGE: Induced in G1 phase, accumulates at G1/S
transition, and degraded in late mitosis following ubiquitination
and degradation by the APC(CDH1) complex.
{ECO:0000269|PubMed:21596315}.
-!- INDUCTION: Induced by E2F transcription factors in G1.
{ECO:0000269|PubMed:21596315}.
-!- DOMAIN: The KEN box 3 is required for interaction with FZR1/CDH1
and is essential for APC(CDH1)-mediated ubiquitination.
{ECO:0000269|PubMed:21596315}.
-!- PTM: Polyubiquitinated via 'Lys-11'-linked ubiquitin by the
APC(CDH1) complex during late mitosis, leading to its degradation.
Able to mediate auto-deubiquitination.
{ECO:0000269|PubMed:21596315}.
-!- PTM: Phosphorylated at Ser-628 by CDK2 during G1/S phase but not
during mitosis; phosphorylation at Ser-628 is required for
deubiquitinase activity. Also polyubiquitinated during early G1
phase, without leading to degradation.
{ECO:0000269|PubMed:21596315}.
-!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAY14887.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AL832645; CAD89955.1; -; mRNA.
EMBL; BX538024; CAD97970.1; -; mRNA.
EMBL; AC012510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC073838; AAY14887.1; ALT_SEQ; Genomic_DNA.
EMBL; CH471063; EAW70621.1; -; Genomic_DNA.
EMBL; BC112901; AAI12902.1; -; mRNA.
EMBL; BC133007; AAI33008.1; -; mRNA.
EMBL; BC133009; AAI33010.1; -; mRNA.
EMBL; BC144249; AAI44250.1; -; mRNA.
EMBL; BC144252; AAI44253.1; -; mRNA.
EMBL; AB046814; BAB13420.1; -; mRNA.
RefSeq; NP_065986.2; NM_020935.2.
RefSeq; XP_005246777.1; XM_005246720.2. [Q86T82-1]
RefSeq; XP_005246778.1; XM_005246721.3. [Q86T82-1]
RefSeq; XP_005246779.1; XM_005246722.3. [Q86T82-1]
RefSeq; XP_011509840.1; XM_011511538.2. [Q86T82-1]
UniGene; Hs.166068; -.
PDB; 3U12; X-ray; 2.08 A; A/B=4-125.
PDBsum; 3U12; -.
ProteinModelPortal; Q86T82; -.
SMR; Q86T82; -.
BioGrid; 121720; 98.
IntAct; Q86T82; 3.
MINT; Q86T82; -.
STRING; 9606.ENSP00000258399; -.
MEROPS; C19.053; -.
iPTMnet; Q86T82; -.
PhosphoSitePlus; Q86T82; -.
BioMuta; USP37; -.
DMDM; 300669620; -.
EPD; Q86T82; -.
MaxQB; Q86T82; -.
PaxDb; Q86T82; -.
PeptideAtlas; Q86T82; -.
PRIDE; Q86T82; -.
DNASU; 57695; -.
Ensembl; ENST00000258399; ENSP00000258399; ENSG00000135913. [Q86T82-1]
Ensembl; ENST00000415516; ENSP00000400902; ENSG00000135913. [Q86T82-2]
Ensembl; ENST00000418019; ENSP00000396585; ENSG00000135913. [Q86T82-1]
Ensembl; ENST00000454775; ENSP00000393662; ENSG00000135913. [Q86T82-1]
GeneID; 57695; -.
KEGG; hsa:57695; -.
UCSC; uc002vie.3; human. [Q86T82-1]
CTD; 57695; -.
DisGeNET; 57695; -.
EuPathDB; HostDB:ENSG00000135913.10; -.
GeneCards; USP37; -.
HGNC; HGNC:20063; USP37.
HPA; HPA045160; -.
neXtProt; NX_Q86T82; -.
OpenTargets; ENSG00000135913; -.
PharmGKB; PA134928706; -.
eggNOG; KOG1868; Eukaryota.
eggNOG; ENOG410XP8T; LUCA.
GeneTree; ENSGT00440000033542; -.
HOVERGEN; HBG055893; -.
InParanoid; Q86T82; -.
KO; K11850; -.
OMA; WLQQYDM; -.
OrthoDB; EOG091G01DZ; -.
PhylomeDB; Q86T82; -.
TreeFam; TF323032; -.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
ChiTaRS; USP37; human.
GeneWiki; USP37; -.
GenomeRNAi; 57695; -.
PRO; PR:Q86T82; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000135913; -.
CleanEx; HS_USP37; -.
ExpressionAtlas; Q86T82; baseline and differential.
Genevisible; Q86T82; HS.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:LIFEdb.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:UniProtKB.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; TAS:Reactome.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; IDA:FlyBase.
GO; GO:0035871; P:protein K11-linked deubiquitination; IDA:UniProtKB.
GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:UniProtKB.
GO; GO:0006275; P:regulation of DNA replication; IMP:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
CDD; cd13312; PH_USP37_like; 1.
Gene3D; 2.30.29.180; -; 1.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR003903; UIM_dom.
InterPro; IPR032069; USP37-like_PH.
InterPro; IPR038093; USP37-like_PH_sf.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
Pfam; PF00443; UCH; 1.
Pfam; PF16674; UCH_N; 1.
Pfam; PF02809; UIM; 3.
SMART; SM00726; UIM; 4.
PROSITE; PS50330; UIM; 3.
PROSITE; PS00972; USP_1; 1.
PROSITE; PS00973; USP_2; 1.
PROSITE; PS50235; USP_3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell cycle; Cell division;
Complete proteome; Hydrolase; Mitosis; Phosphoprotein; Polymorphism;
Protease; Reference proteome; Repeat; Thiol protease; Ubl conjugation;
Ubl conjugation pathway.
CHAIN 1 979 Ubiquitin carboxyl-terminal hydrolase 37.
/FTId=PRO_0000080667.
DOMAIN 341 951 USP.
DOMAIN 704 723 UIM 1. {ECO:0000255|PROSITE-
ProRule:PRU00213}.
DOMAIN 806 825 UIM 2. {ECO:0000255|PROSITE-
ProRule:PRU00213}.
DOMAIN 828 847 UIM 3. {ECO:0000255|PROSITE-
ProRule:PRU00213}.
MOTIF 32 34 KEN box 1.
MOTIF 71 79 D-box 1.
MOTIF 96 105 D-box 2.
MOTIF 160 168 D-box 3.
MOTIF 221 223 KEN box 2.
MOTIF 782 784 KEN box 3.
ACT_SITE 350 350 Nucleophile.
{ECO:0000269|PubMed:27296872}.
ACT_SITE 906 906 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
MOD_RES 170 170 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 210 210 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 628 628 Phosphoserine; by CDK2.
{ECO:0000269|PubMed:21596315,
ECO:0000269|PubMed:27296872}.
MOD_RES 650 650 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 652 652 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 770 770 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 72 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_041740.
VAR_SEQ 612 634 ISRPLKASQMVNSCITSPSTPSK -> M (in isoform
2). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_041741.
VARIANT 979 979 L -> S (in dbSNP:rs6436058).
{ECO:0000269|PubMed:10997877,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005,
ECO:0000269|Ref.3}.
/FTId=VAR_059752.
MUTAGEN 32 34 KEN->AAA: No effect.
{ECO:0000269|PubMed:21596315}.
MUTAGEN 71 74 RLML->ALMA: No effect.
{ECO:0000269|PubMed:21596315}.
MUTAGEN 96 99 RLFL->ALFA: No effect.
{ECO:0000269|PubMed:21596315}.
MUTAGEN 160 163 RKVL->AKVA: No effect.
{ECO:0000269|PubMed:21596315}.
MUTAGEN 221 223 KEN->AAA: No effect.
{ECO:0000269|PubMed:21596315}.
MUTAGEN 350 350 C->S: Abolishes deubiquitinase activity.
{ECO:0000269|PubMed:21596315}.
MUTAGEN 628 628 S->A: Abolishes phosphorylation by CDK2,
leading to lower deubiquitinase activity.
{ECO:0000269|PubMed:21596315}.
MUTAGEN 782 784 KEN->AAA: Impaired interaction with
FZR1/CDH1 and subsequent ubiquitination.
{ECO:0000269|PubMed:21596315}.
CONFLICT 223 224 ND -> DG (in Ref. 1; CAD89955).
{ECO:0000305}.
CONFLICT 345 345 N -> K (in Ref. 1; CAD97970).
{ECO:0000305}.
CONFLICT 456 456 V -> I (in Ref. 1; CAD89955).
{ECO:0000305}.
CONFLICT 552 552 F -> I (in Ref. 4; AAI44250).
{ECO:0000305}.
CONFLICT 567 567 S -> I (in Ref. 4; AAI44253).
{ECO:0000305}.
CONFLICT 576 576 N -> Y (in Ref. 4; AAI44253).
{ECO:0000305}.
CONFLICT 731 731 K -> E (in Ref. 1; CAD97970).
{ECO:0000305}.
CONFLICT 905 905 G -> D (in Ref. 1; CAD97970).
{ECO:0000305}.
STRAND 5 14 {ECO:0000244|PDB:3U12}.
TURN 15 17 {ECO:0000244|PDB:3U12}.
STRAND 23 32 {ECO:0000244|PDB:3U12}.
STRAND 35 42 {ECO:0000244|PDB:3U12}.
STRAND 49 52 {ECO:0000244|PDB:3U12}.
TURN 54 56 {ECO:0000244|PDB:3U12}.
STRAND 57 64 {ECO:0000244|PDB:3U12}.
STRAND 69 76 {ECO:0000244|PDB:3U12}.
STRAND 81 88 {ECO:0000244|PDB:3U12}.
HELIX 89 103 {ECO:0000244|PDB:3U12}.
SEQUENCE 979 AA; 110170 MW; 9F47F06A744EA449 CRC64;
MSPLKIHGPI RIRSMQTGIT KWKEGSFEIV EKENKVSLVV HYNTGGIPRI FQLSHNIKNV
VLRPSGAKQS RLMLTLQDNS FLSIDKVPSK DAEEMRLFLD AVHQNRLPAA MKPSQGSGSF
GAILGSRTSQ KETSRQLSYS DNQASAKRGS LETKDDIPFR KVLGNPGRGS IKTVAGSGIA
RTIPSLTSTS TPLRSGLLEN RTEKRKRMIS TGSELNEDYP KENDSSSNNK AMTDPSRKYL
TSSREKQLSL KQSEENRTSG LLPLQSSSFY GSRAGSKEHS SGGTNLDRTN VSSQTPSAKR
SLGFLPQPVP LSVKKLRCNQ DYTGWNKPRV PLSSHQQQQL QGFSNLGNTC YMNAILQSLF
SLQSFANDLL KQGIPWKKIP LNALIRRFAH LLVKKDICNS ETKKDLLKKV KNAISATAER
FSGYMQNDAH EFLSQCLDQL KEDMEKLNKT WKTEPVSGEE NSPDISATRA YTCPVITNLE
FEVQHSIICK ACGEIIPKRE QFNDLSIDLP RRKKPLPPRS IQDSLDLFFR AEELEYSCEK
CGGKCALVRH KFNRLPRVLI LHLKRYSFNV ALSLNNKIGQ QVIIPRYLTL SSHCTENTKP
PFTLGWSAHM AISRPLKASQ MVNSCITSPS TPSKKFTFKS KSSLALCLDS DSEDELKRSV
ALSQRLCEML GNEQQQEDLE KDSKLCPIEP DKSELENSGF DRMSEEELLA AVLEISKRDA
SPSLSHEDDD KPTSSPDTGF AEDDIQEMPE NPDTMETEKP KTITELDPAS FTEITKDCDE
NKENKTPEGS QGEVDWLQQY DMEREREEQE LQQALAQSLQ EQEAWEQKED DDLKRATELS
LQEFNNSFVD ALGSDEDSGN EDVFDMEYTE AEAEELKRNA ETGNLPHSYR LISVVSHIGS
TSSSGHYISD VYDIKKQAWF TYNDLEVSKI QEAAVQSDRD RSGYIFFYMH KEIFDELLET
EKNSQSLSTE VGKTTRQAL


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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


 

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