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Ubiquitin carboxyl-terminal hydrolase 20 (EC 3.4.19.12) (Deubiquitinating enzyme 20) (Ubiquitin thioesterase 20) (Ubiquitin-specific-processing protease 20) (VHL-interacting deubiquitinating enzyme 2) (hVDU2)

 UBP20_HUMAN             Reviewed;         914 AA.
Q9Y2K6; Q541F1; Q8IXQ1; Q96LG5; Q9UQN8; Q9UQP0;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
25-OCT-2017, entry version 165.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 20;
EC=3.4.19.12;
AltName: Full=Deubiquitinating enzyme 20;
AltName: Full=Ubiquitin thioesterase 20;
AltName: Full=Ubiquitin-specific-processing protease 20;
AltName: Full=VHL-interacting deubiquitinating enzyme 2;
Short=hVDU2;
Name=USP20; Synonyms=KIAA1003, LSFR3A, VDU2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, UBIQUITINATION, AND INTERACTION
WITH VHL.
PubMed=12056827; DOI=10.1016/S0006-291X(02)00534-X;
Li Z., Wang D., Na X., Schoen S.R., Messing E.M., Wu G.;
"Identification of a deubiquitinating enzyme subfamily as substrates
of the von Hippel-Lindau tumor suppressor.";
Biochem. Biophys. Res. Commun. 294:700-709(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=10231032; DOI=10.1093/dnares/6.1.63;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:63-70(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[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].
TISSUE=Ovary;
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 [GENOMIC DNA] OF 581-803 AND 839-914.
PubMed=10369878; DOI=10.1093/hmg/8.7.1313;
Gilley J., Fried M.;
"Extensive gene order differences within regions of conserved synteny
between the Fugu and human genomes: implications for chromosomal
evolution and the cloning of disease genes.";
Hum. Mol. Genet. 8:1313-1320(1999).
[7]
FUNCTION, AND INTERACTION WITH DIO2.
PubMed=12865408; DOI=10.1172/JCI18348;
Curcio-Morelli C., Zavacki A.M., Christofollete M., Gereben B.,
de Freitas B.C., Harney J.W., Li Z., Wu G., Bianco A.C.;
"Deubiquitination of type 2 iodothyronine deiodinase by von Hippel-
Lindau protein-interacting deubiquitinating enzymes regulates thyroid
hormone activation.";
J. Clin. Invest. 112:189-196(2003).
[8]
FUNCTION, AND INTERACTION WITH HIF1A.
PubMed=15776016; DOI=10.1038/sj.embor.7400377;
Li Z., Wang D., Messing E.M., Wu G.;
"VHL protein-interacting deubiquitinating enzyme 2 deubiquitinates and
stabilizes HIF-1alpha.";
EMBO Rep. 6:373-378(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-258, AND 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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-134, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-377 AND SER-413, 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).
[12]
FUNCTION, INTERACTION WITH ADRB2, AND MUTAGENESIS OF CYS-154 AND
HIS-643.
PubMed=19424180; DOI=10.1038/emboj.2009.128;
Berthouze M., Venkataramanan V., Li Y., Shenoy S.K.;
"The deubiquitinases USP33 and USP20 coordinate beta2 adrenergic
receptor recycling and resensitization.";
EMBO J. 28:1684-1696(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-134, 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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; SER-132; SER-134;
SER-305; THR-377; SER-408 AND SER-413, 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]
SUBCELLULAR LOCATION, AND INTERACTION WITH CCP110.
PubMed=23486064; DOI=10.1038/nature11941;
Li J., D'Angiolella V., Seeley E.S., Kim S., Kobayashi T., Fu W.,
Campos E.I., Pagano M., Dynlacht B.D.;
"USP33 regulates centrosome biogenesis via deubiquitination of the
centriolar protein CP110.";
Nature 495:255-259(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-134, 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).
-!- FUNCTION: Deubiquitinating enzyme involved in beta-2 adrenergic
receptor (ADRB2) recycling. Acts as a regulator of G-protein
coupled receptor (GPCR) signaling by mediating the
deubiquitination beta-2 adrenergic receptor (ADRB2). Plays a
central role in ADRB2 recycling and resensitization after
prolonged agonist stimulation by constitutively binding ADRB2,
mediating deubiquitination of ADRB2 and inhibiting lysosomal
trafficking of ADRB2. Upon dissociation, it is probably
transferred to the translocated beta-arrestins, possibly leading
to beta-arrestins deubiquitination and disengagement from ADRB2.
This suggests the existence of a dynamic exchange between the
ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating
thyroid hormone regulation. Deubiquitinates HIF1A, leading to
stabilize HIF1A and enhance HIF1A-mediated activity. Mediates
deubiquitination of both 'Lys-48'- and 'Lys-63'-linked
polyubiquitin chains. {ECO:0000269|PubMed:12056827,
ECO:0000269|PubMed:12865408, ECO:0000269|PubMed:15776016,
ECO:0000269|PubMed:19424180}.
-!- 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 VHL, leading to its ubiquitination and
subsequent degradation. Interacts with CCP110, DIO2 and HIF1A.
{ECO:0000269|PubMed:12056827, ECO:0000269|PubMed:12865408,
ECO:0000269|PubMed:15776016, ECO:0000269|PubMed:19424180,
ECO:0000269|PubMed:23486064}.
-!- INTERACTION:
P13196:ALAS1; NbExp=3; IntAct=EBI-2511991, EBI-3905054;
Q7L4P6:BEND5; NbExp=3; IntAct=EBI-2511991, EBI-724373;
Q8N7W2-2:BEND7; NbExp=3; IntAct=EBI-2511991, EBI-10181188;
Q8IYA8:CCDC36; NbExp=3; IntAct=EBI-2511991, EBI-8638439;
Q969F0:FATE1; NbExp=3; IntAct=EBI-2511991, EBI-743099;
P43364-2:MAGEA11; NbExp=3; IntAct=EBI-2511991, EBI-10178634;
Q99750:MDFI; NbExp=3; IntAct=EBI-2511991, EBI-724076;
O43597:SPRY2; NbExp=3; IntAct=EBI-2511991, EBI-742487;
P36406:TRIM23; NbExp=3; IntAct=EBI-2511991, EBI-740098;
Q53XM7:VAPB; NbExp=3; IntAct=EBI-2511991, EBI-10178947;
-!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
{ECO:0000269|PubMed:23486064}. Note=According to PubMed:12865408,
it localizes in the endoplasmic reticulum; however the relevance
of such result is unclear.
-!- DOMAIN: The UBP-type zinc finger binds 3 zinc ions. However, it
does not bind ubiquitin, probably because the conserved Arg in
position 55 is replaced by a Glu residue (By similarity).
{ECO:0000250}.
-!- PTM: Ubiquitinated via a VHL-dependent pathway for proteasomal
degradation. {ECO:0000269|PubMed:12056827}.
-!- SIMILARITY: Belongs to the peptidase C19 family. USP20/USP33
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA76847.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AY074877; AAL79676.1; -; mRNA.
EMBL; AB023220; BAA76847.2; ALT_INIT; mRNA.
EMBL; AL158207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471090; EAW87914.1; -; Genomic_DNA.
EMBL; BC039593; AAH39593.1; -; mRNA.
EMBL; Y17457; CAB44350.1; -; Genomic_DNA.
EMBL; Y17459; CAB44352.1; -; Genomic_DNA.
CCDS; CCDS43892.1; -.
RefSeq; NP_001008563.2; NM_001008563.4.
RefSeq; NP_001103773.2; NM_001110303.3.
RefSeq; NP_006667.3; NM_006676.7.
RefSeq; XP_005251722.1; XM_005251665.3.
RefSeq; XP_011516463.1; XM_011518161.2.
RefSeq; XP_011516464.1; XM_011518162.2.
UniGene; Hs.5452; -.
ProteinModelPortal; Q9Y2K6; -.
SMR; Q9Y2K6; -.
BioGrid; 116077; 73.
IntAct; Q9Y2K6; 50.
MINT; MINT-4658328; -.
STRING; 9606.ENSP00000313811; -.
BindingDB; Q9Y2K6; -.
ChEMBL; CHEMBL3232682; -.
MEROPS; C19.025; -.
iPTMnet; Q9Y2K6; -.
PhosphoSitePlus; Q9Y2K6; -.
DMDM; 116242837; -.
EPD; Q9Y2K6; -.
MaxQB; Q9Y2K6; -.
PaxDb; Q9Y2K6; -.
PeptideAtlas; Q9Y2K6; -.
PRIDE; Q9Y2K6; -.
Ensembl; ENST00000315480; ENSP00000313811; ENSG00000136878.
Ensembl; ENST00000358355; ENSP00000351122; ENSG00000136878.
Ensembl; ENST00000372429; ENSP00000361506; ENSG00000136878.
GeneID; 10868; -.
KEGG; hsa:10868; -.
UCSC; uc004byr.4; human.
CTD; 10868; -.
DisGeNET; 10868; -.
EuPathDB; HostDB:ENSG00000136878.12; -.
GeneCards; USP20; -.
H-InvDB; HIX0008459; -.
HGNC; HGNC:12619; USP20.
HPA; HPA006287; -.
HPA; HPA007008; -.
MIM; 615143; gene.
neXtProt; NX_Q9Y2K6; -.
OpenTargets; ENSG00000136878; -.
PharmGKB; PA37245; -.
eggNOG; KOG1870; Eukaryota.
eggNOG; COG5560; LUCA.
GeneTree; ENSGT00860000133682; -.
HOGENOM; HOG000286031; -.
HOVERGEN; HBG054196; -.
InParanoid; Q9Y2K6; -.
KO; K11848; -.
OMA; ADYGQIS; -.
OrthoDB; EOG091G02UV; -.
PhylomeDB; Q9Y2K6; -.
TreeFam; TF352179; -.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
ChiTaRS; USP20; human.
GeneWiki; USP20; -.
GenomeRNAi; 10868; -.
PRO; PR:Q9Y2K6; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000136878; -.
CleanEx; HS_USP20; -.
Genevisible; Q9Y2K6; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IMP:UniProtKB.
GO; GO:0001664; F:G-protein coupled receptor binding; IPI:UniProtKB.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IEA:InterPro.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:UniProtKB.
GO; GO:0070536; P:protein K63-linked deubiquitination; IDA:UniProtKB.
GO; GO:0008277; P:regulation of G-protein coupled receptor protein signaling pathway; IMP:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
Gene3D; 3.30.2230.10; -; 2.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR035927; DUSP-like_sf.
InterPro; IPR006615; Pept_C19_DUSP.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR001607; Znf_UBP.
Pfam; PF06337; DUSP; 2.
Pfam; PF00443; UCH; 1.
Pfam; PF02148; zf-UBP; 1.
SMART; SM00695; DUSP; 2.
SMART; SM00290; ZnF_UBP; 1.
SUPFAM; SSF143791; SSF143791; 2.
PROSITE; PS51283; DUSP; 2.
PROSITE; PS00972; USP_1; 1.
PROSITE; PS00973; USP_2; 1.
PROSITE; PS50235; USP_3; 1.
PROSITE; PS50271; ZF_UBP; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Cytoskeleton; Endocytosis; Hydrolase;
Metal-binding; Phosphoprotein; Polymorphism; Protease;
Reference proteome; Repeat; Thiol protease; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 914 Ubiquitin carboxyl-terminal hydrolase 20.
/FTId=PRO_0000080647.
DOMAIN 145 685 USP.
DOMAIN 687 780 DUSP 1. {ECO:0000255|PROSITE-
ProRule:PRU00613}.
DOMAIN 789 892 DUSP 2. {ECO:0000255|PROSITE-
ProRule:PRU00613}.
ZN_FING 28 92 UBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00502}.
ACT_SITE 154 154 Nucleophile.
ACT_SITE 643 643 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
MOD_RES 112 112 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 132 132 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 134 134 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 258 258 Phosphothreonine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 305 305 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 368 368 Phosphoserine.
{ECO:0000250|UniProtKB:Q8C6M1}.
MOD_RES 377 377 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 408 408 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 413 413 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
VARIANT 103 103 S -> Y (in dbSNP:rs36086252).
/FTId=VAR_051529.
VARIANT 444 444 V -> I (in dbSNP:rs36055332).
/FTId=VAR_051530.
MUTAGEN 154 154 C->S: Abolishes deubiquitinating
activity. Does not inhibit lysosomal
trafficking of ADRB2; when associated
with Q-643.
{ECO:0000269|PubMed:19424180}.
MUTAGEN 643 643 H->Q: Abolishes deubiquitinating
activity. Does not inhibit lysosomal
trafficking of ADRB2; when associated
with S-154.
{ECO:0000269|PubMed:19424180}.
CONFLICT 320 320 A -> V (in Ref. 1; AAL79676 and 2;
BAA76847). {ECO:0000305}.
CONFLICT 359 359 Missing (in Ref. 1; AAL79676, 2;
BAA76847, 4; EAW87914 and 5; AAH39593).
{ECO:0000305}.
CONFLICT 776 776 H -> Q (in Ref. 6; CAB44350).
{ECO:0000305}.
CONFLICT 794 794 R -> M (in Ref. 6; CAB44350).
{ECO:0000305}.
SEQUENCE 914 AA; 102003 MW; DC094570A396D20E CRC64;
MGDSRDLCPH LDSIGEVTKE DLLLKSKGTC QSCGVTGPNL WACLQVACPY VGCGESFADH
STIHAQAKKH NLTVNLTTFR LWCYACEKEV FLEQRLAAPL LGSSSKFSEQ DSPPPSHPLK
AVPIAVADEG ESESEDDDLK PRGLTGMKNL GNSCYMNAAL QALSNCPPLT QFFLECGGLV
RTDKKPALCK SYQKLVSEVW HKKRPSYVVP TSLSHGIKLV NPMFRGYAQQ DTQEFLRCLM
DQLHEELKEP VVATVALTEA RDSDSSDTDE KREGDRSPSE DEFLSCDSSS DRGEGDGQGR
GGGSSQAETE LLIPDEAGRA ISEKERMKDR KFSWGQQRTN SEQVDEDADV DTAMAALDDQ
PAEAQPPSPR SSSPCRTPEP DNDAHLRSSS RPCSPVHHHE GHAKLSSSPP RASPVRMAPS
YVLKKAQVLS AGSRRRKEQR YRSVISDIFD GSILSLVQCL TCDRVSTTVE TFQDLSLPIP
GKEDLAKLHS AIYQNVPAKP GACGDSYAAQ GWLAFIVEYI RRFVVSCTPS WFWGPVVTLE
DCLAAFFAAD ELKGDNMYSC ERCKKLRNGV KYCKVLRLPE ILCIHLKRFR HEVMYSFKIN
SHVSFPLEGL DLRPFLAKEC TSQITTYDLL SVICHHGTAG SGHYIAYCQN VINGQWYEFD
DQYVTEVHET VVQNAEGYVL FYRKSSEEAM RERQQVVSLA AMREPSLLRF YVSREWLNKF
NTFAEPGPIT NQTFLCSHGG IPPHKYHYID DLVVILPQNV WEHLYNRFGG GPAVNHLYVC
SICQVEIEAL AKRRRIEIDT FIKLNKAFQA EESPGVIYCI SMQWFREWEA FVKGKDNEPP
GPIDNSRIAQ VKGSGHVQLK QGADYGQISE ETWTYLNSLY GGGPEIAIRQ SVAQPLGPEN
LHGEQKIEAE TRAV


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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
EIAAB45008 Deubiquitinating enzyme 20,Homo sapiens,Human,hVDU2,KIAA1003,LSFR3A,Ubiquitin carboxyl-terminal hydrolase 20,Ubiquitin thiolesterase 20,Ubiquitin-specific-processing protease 20,USP20,VDU2,VHL-interac
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
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
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
EIAAB45093 Chicken,Deubiquitinating enzyme 7,Gallus gallus,Ubiquitin carboxyl-terminal hydrolase 7,Ubiquitin thioesterase 7,Ubiquitin-specific-processing protease 7,USP7
EIAAB45006 Deubiquitinating enzyme 20,Kiaa1003,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 20,Ubiquitin thiolesterase 20,Ubiquitin-specific-processing protease 20,Usp20,Vdu2,VHL-interacting deubiqui
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,
EIAAB45040 Deubiquitinating enzyme 33,Homo sapiens,Human,hVDU1,KIAA1097,Ubiquitin carboxyl-terminal hydrolase 33,Ubiquitin thiolesterase 33,Ubiquitin-specific-processing protease 33,USP33,VDU1,VHL-interacting de
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-
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
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
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
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
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
EIAAB45076 Deubiquitinating enzyme 48,Rat,Rattus norvegicus,Synaptic ubiquitin-specific protease,synUSP,Ubiquitin carboxyl-terminal hydrolase 48,Ubiquitin thiolesterase 48,Ubiquitin-specific-processing protease
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
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
EIAAB45000 Deubiquitinating enzyme 19,Rat,Rattus norvegicus,Ubiquitin carboxyl-terminal hydrolase 19,Ubiquitin thiolesterase 19,Ubiquitin-specific-processing protease 19,Usp19
EIAAB45063 Deubiquitinating enzyme 42,Rat,Rattus norvegicus,Ubiquitin carboxyl-terminal hydrolase 42,Ubiquitin thiolesterase 42,Ubiquitin-specific-processing protease 42,Usp42
EIAAB45028 Deubiquitinating enzyme 29,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 29,Ubiquitin thiolesterase 29,Ubiquitin-specific-processing protease 29,Usp29


 

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