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 33 (EC 3.4.19.12) (Deubiquitinating enzyme 33) (Ubiquitin thioesterase 33) (Ubiquitin-specific-processing protease 33) (VHL-interacting deubiquitinating enzyme 1) (hVDU1)

 UBP33_HUMAN             Reviewed;         942 AA.
Q8TEY7; Q8TEY6; Q96AV6; Q9H9F0; Q9UPQ5;
10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
28-FEB-2018, entry version 154.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 33;
EC=3.4.19.12;
AltName: Full=Deubiquitinating enzyme 33;
AltName: Full=Ubiquitin thioesterase 33;
AltName: Full=Ubiquitin-specific-processing protease 33;
AltName: Full=VHL-interacting deubiquitinating enzyme 1;
Short=hVDU1;
Name=USP33; Synonyms=KIAA1097, VDU1;
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 1 AND 2), UBIQUITINATION,
INTERACTION WITH VHL, AND TISSUE SPECIFICITY.
PubMed=11739384; DOI=10.1074/jbc.M108269200;
Li Z., Na X., Wang D., Schoen S.R., Messing E.M., Wu G.;
"Ubiquitination of a novel deubiquitinating enzyme requires direct
binding to von Hippel-Lindau tumor suppressor protein.";
J. Biol. Chem. 277:4656-4662(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=10470851; DOI=10.1093/dnares/6.3.197;
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:197-205(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[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]
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).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, 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]
INTERACTION WITH SELENBP1, AND SUBCELLULAR LOCATION.
PubMed=19118533; DOI=10.1016/j.bbrc.2008.12.110;
Jeong J.Y., Wang Y., Sytkowski A.J.;
"Human selenium binding protein-1 (hSP56) interacts with VDU1 in a
selenium-dependent manner.";
Biochem. Biophys. Res. Commun. 379:583-588(2009).
[9]
FUNCTION, INTERACTION WITH ADRB2, AND MUTAGENESIS OF CYS-194 AND
HIS-673.
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).
[10]
FUNCTION, INTERACTION WITH ARRB1 AND ARRB2, AND MUTAGENESIS OF CYS-194
AND HIS-673.
PubMed=19363159; DOI=10.1073/pnas.0901083106;
Shenoy S.K., Modi A.S., Shukla A.K., Xiao K., Berthouze M., Ahn S.,
Wilkinson K.D., Miller W.E., Lefkowitz R.J.;
"Beta-arrestin-dependent signaling and trafficking of 7-transmembrane
receptors is reciprocally regulated by the deubiquitinase USP33 and
the E3 ligase Mdm2.";
Proc. Natl. Acad. Sci. U.S.A. 106:6650-6655(2009).
[11]
ALTERNATIVE SPLICING (ISOFORM 3), AND SUBCELLULAR LOCATION.
PubMed=21801292; DOI=10.1111/j.1600-0854.2011.01261.x;
Thorne C., Eccles R.L., Coulson J.M., Urbe S., Clague M.J.;
"Isoform-specific localization of the deubiquitinase USP33 to the
Golgi apparatus.";
Traffic 12:1563-1574(2011).
[12]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CCP110, DEVELOPMENTAL
STAGE, AND MUTAGENESIS OF CYS-194 AND HIS-673.
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, 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).
[14]
STRUCTURE BY NMR OF 36-130, ZINC-BINDING, AND DOMAIN UBP-TYPE ZINC
FINGER.
PubMed=17766394; DOI=10.1110/ps.072967807;
Allen M.D., Bycroft M.;
"The solution structure of the ZnF UBP domain of USP33/VDU1.";
Protein Sci. 16:2072-2075(2007).
-!- FUNCTION: Deubiquitinating enzyme involved in various processes
such as centrosome duplication, cellular migration and beta-2
adrenergic receptor/ADRB2 recycling. Involved in regulation of
centrosome duplication by mediating deubiquitination of CCP110 in
S and G2/M phase, leading to stabilize CCP110 during the period
which centrioles duplicate and elongate. Involved in cell
migration via its interaction with intracellular domain of ROBO1,
leading to regulate the Slit signaling. Plays a role in
commissural axon guidance cross the ventral midline of the neural
tube in a Slit-dependent manner, possibly by mediating the
deubiquitination of ROBO1. Acts as a regulator of G-protein
coupled receptor (GPCR) signaling by mediating the
deubiquitination of beta-arrestins (ARRB1 and ARRB2) and 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, 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. Mediates
deubiquitination of both 'Lys-48'- and 'Lys-63'-linked
polyubiquitin chains. {ECO:0000269|PubMed:12865408,
ECO:0000269|PubMed:19363159, ECO:0000269|PubMed:19424180,
ECO:0000269|PubMed:23486064}.
-!- 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 ARRB1, ARRB2, ADRB2, DIO2
and ROBO1. Interacts with SELENBP1; in a selenium-dependent
manner. Interacts with CCP110. {ECO:0000269|PubMed:11739384,
ECO:0000269|PubMed:12865408, ECO:0000269|PubMed:19118533,
ECO:0000269|PubMed:19363159, ECO:0000269|PubMed:19424180,
ECO:0000269|PubMed:23486064}.
-!- INTERACTION:
Q13228:SELENBP1; NbExp=5; IntAct=EBI-719307, EBI-711619;
-!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
{ECO:0000269|PubMed:19118533}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000269|PubMed:23486064}. Note=Associates with centrosomes
predominantly in S and G2 phases but less in G1 phase
(PubMed:23486064). {ECO:0000269|PubMed:23486064}.
-!- SUBCELLULAR LOCATION: Isoform 3: Golgi apparatus
{ECO:0000269|PubMed:21801292}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8TEY7-1; Sequence=Displayed;
Name=2;
IsoId=Q8TEY7-2; Sequence=VSP_008591;
Name=3;
IsoId=Q8TEY7-3; Sequence=VSP_008592, VSP_008593, VSP_008594;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:11739384}.
-!- DEVELOPMENTAL STAGE: Increased expression in S and early G2 phases
and lower levels in late G2 and M phases.
{ECO:0000269|PubMed:23486064}.
-!- DOMAIN: The UBP-type zinc finger binds 3 zinc ions. However, it
does not bind ubiquitin, probably because the conserved Arg in
position 86 is replaced by a Glu residue.
{ECO:0000269|PubMed:17766394}.
-!- PTM: Ubiquitinated via a VHL-dependent pathway for proteasomal
degradation. {ECO:0000269|PubMed:11739384}.
-!- SIMILARITY: Belongs to the peptidase C19 family. USP20/USP33
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA83049.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF383172; AAL78314.1; -; mRNA.
EMBL; AF383173; AAL78315.1; -; mRNA.
EMBL; AB029020; BAA83049.1; ALT_INIT; mRNA.
EMBL; AK022864; BAB14279.1; -; mRNA.
EMBL; AC114487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC016663; AAH16663.1; -; mRNA.
CCDS; CCDS678.1; -. [Q8TEY7-1]
CCDS; CCDS679.1; -. [Q8TEY7-2]
CCDS; CCDS680.1; -. [Q8TEY7-3]
RefSeq; NP_055832.3; NM_015017.4. [Q8TEY7-1]
RefSeq; NP_963918.1; NM_201624.2. [Q8TEY7-2]
RefSeq; NP_963920.1; NM_201626.2. [Q8TEY7-3]
UniGene; Hs.480597; -.
PDB; 2UZG; NMR; -; A=36-130.
PDBsum; 2UZG; -.
ProteinModelPortal; Q8TEY7; -.
SMR; Q8TEY7; -.
BioGrid; 116671; 57.
CORUM; Q8TEY7; -.
DIP; DIP-48942N; -.
IntAct; Q8TEY7; 10.
MINT; Q8TEY7; -.
STRING; 9606.ENSP00000350009; -.
MEROPS; C19.037; -.
iPTMnet; Q8TEY7; -.
PhosphoSitePlus; Q8TEY7; -.
BioMuta; USP33; -.
DMDM; 116242838; -.
EPD; Q8TEY7; -.
MaxQB; Q8TEY7; -.
PaxDb; Q8TEY7; -.
PeptideAtlas; Q8TEY7; -.
PRIDE; Q8TEY7; -.
DNASU; 23032; -.
Ensembl; ENST00000357428; ENSP00000350009; ENSG00000077254. [Q8TEY7-1]
Ensembl; ENST00000370792; ENSP00000359828; ENSG00000077254. [Q8TEY7-3]
Ensembl; ENST00000370793; ENSP00000359829; ENSG00000077254. [Q8TEY7-1]
Ensembl; ENST00000370794; ENSP00000359830; ENSG00000077254. [Q8TEY7-2]
GeneID; 23032; -.
KEGG; hsa:23032; -.
UCSC; uc001dht.5; human. [Q8TEY7-1]
CTD; 23032; -.
DisGeNET; 23032; -.
EuPathDB; HostDB:ENSG00000077254.14; -.
GeneCards; USP33; -.
H-InvDB; HIX0159957; -.
HGNC; HGNC:20059; USP33.
HPA; HPA005719; -.
MIM; 615146; gene.
neXtProt; NX_Q8TEY7; -.
OpenTargets; ENSG00000077254; -.
PharmGKB; PA134955343; -.
eggNOG; ENOG410IN4T; Eukaryota.
eggNOG; ENOG410ZG0F; LUCA.
GeneTree; ENSGT00860000133682; -.
HOGENOM; HOG000286031; -.
HOVERGEN; HBG054196; -.
InParanoid; Q8TEY7; -.
KO; K11848; -.
OMA; PRKAGYI; -.
OrthoDB; EOG091G02UV; -.
PhylomeDB; Q8TEY7; -.
TreeFam; TF352179; -.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
ChiTaRS; USP33; human.
EvolutionaryTrace; Q8TEY7; -.
GeneWiki; USP33; -.
GenomeRNAi; 23032; -.
PRO; PR:Q8TEY7; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000077254; -.
CleanEx; HS_USP33; -.
ExpressionAtlas; Q8TEY7; baseline and differential.
Genevisible; Q8TEY7; HS.
GO; GO:0044297; C:cell body; IEA:Ensembl.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; IDA:HPA.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0030891; C:VCB complex; TAS:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IMP:UniProtKB.
GO; GO:0001664; F:G-protein coupled receptor binding; IPI:UniProtKB.
GO; GO:0017160; F:Ral GTPase binding; IPI:UniProtKB.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:UniProtKB.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0009267; P:cellular response to starvation; IDA:UniProtKB.
GO; GO:0051298; P:centrosome duplication; IMP:UniProtKB.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0032091; P:negative regulation of protein binding; IMP:UniProtKB.
GO; GO:0032092; P:positive regulation of protein binding; IMP:UniProtKB.
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:0050821; P:protein stabilization; IMP:CACAO.
GO; GO:0010506; P:regulation of autophagy; IMP: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; TAS:UniProtKB.
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;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Cytoskeleton; Endocytosis; Golgi apparatus; Hydrolase; Metal-binding;
Phosphoprotein; Protease; Reference proteome; Repeat; Thiol protease;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 942 Ubiquitin carboxyl-terminal hydrolase 33.
/FTId=PRO_0000080664.
DOMAIN 185 715 USP.
DOMAIN 717 810 DUSP 1. {ECO:0000255|PROSITE-
ProRule:PRU00613}.
DOMAIN 818 921 DUSP 2. {ECO:0000255|PROSITE-
ProRule:PRU00613}.
ZN_FING 59 123 UBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00502}.
ACT_SITE 194 194 Nucleophile.
ACT_SITE 673 673 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
MOD_RES 377 377 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 439 439 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
VAR_SEQ 1 31 Missing (in isoform 2).
{ECO:0000303|PubMed:10470851,
ECO:0000303|PubMed:11739384}.
/FTId=VSP_008591.
VAR_SEQ 552 559 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_008592.
VAR_SEQ 834 836 LNR -> VKK (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_008593.
VAR_SEQ 837 942 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_008594.
MUTAGEN 194 194 C->S: Abolishes deubiquitinating
activity. Does not inhibit lysosomal
trafficking of ADRB2; when associated
with Q-673. {ECO:0000269|PubMed:19363159,
ECO:0000269|PubMed:19424180,
ECO:0000269|PubMed:23486064}.
MUTAGEN 673 673 H->Q: Abolishes deubiquitinating
activity. Does not inhibit lysosomal
trafficking of ADRB2; when associated
with S-194. {ECO:0000269|PubMed:19363159,
ECO:0000269|PubMed:19424180,
ECO:0000269|PubMed:23486064}.
CONFLICT 241 241 H -> Y (in Ref. 1; AAL78314/AAL78315 and
2; BAA83049). {ECO:0000305}.
CONFLICT 428 428 S -> L (in Ref. 3; BAB14279).
{ECO:0000305}.
CONFLICT 617 617 K -> R (in Ref. 3; BAB14279).
{ECO:0000305}.
HELIX 40 44 {ECO:0000244|PDB:2UZG}.
HELIX 50 56 {ECO:0000244|PDB:2UZG}.
TURN 57 59 {ECO:0000244|PDB:2UZG}.
STRAND 62 64 {ECO:0000244|PDB:2UZG}.
STRAND 72 74 {ECO:0000244|PDB:2UZG}.
TURN 86 89 {ECO:0000244|PDB:2UZG}.
HELIX 91 98 {ECO:0000244|PDB:2UZG}.
STRAND 103 106 {ECO:0000244|PDB:2UZG}.
TURN 107 110 {ECO:0000244|PDB:2UZG}.
STRAND 111 114 {ECO:0000244|PDB:2UZG}.
TURN 115 118 {ECO:0000244|PDB:2UZG}.
STRAND 119 121 {ECO:0000244|PDB:2UZG}.
SEQUENCE 942 AA; 106727 MW; 10A3AD632B901A74 CRC64;
MTGSNSHITI LTLKVLPHFE SLGKQEKIPN KMSAFRNHCP HLDSVGEITK EDLIQKSLGT
CQDCKVQGPN LWACLENRCS YVGCGESQVD HSTIHSQETK HYLTVNLTTL RVWCYACSKE
VFLDRKLGTQ PSLPHVRQPH QIQENSVQDF KIPSNTTLKT PLVAVFDDLD IEADEEDELR
ARGLTGLKNI GNTCYMNAAL QALSNCPPLT QFFLDCGGLA RTDKKPAICK SYLKLMTELW
HKSRPGSVVP TTLFQGIKTV NPTFRGYSQQ DAQEFLRCLM DLLHEELKEQ VMEVEEDPQT
ITTEETMEED KSQSDVDFQS CESCSNSDRA ENENGSRCFS EDNNETTMLI QDDENNSEMS
KDWQKEKMCN KINKVNSEGE FDKDRDSISE TVDLNNQETV KVQIHSRASE YITDVHSNDL
STPQILPSNE GVNPRLSASP PKSGNLWPGL APPHKKAQSA SPKRKKQHKK YRSVISDIFD
GTIISSVQCL TCDRVSVTLE TFQDLSLPIP GKEDLAKLHS SSHPTSIVKA GSCGEAYAPQ
GWIAFFMEYV KRFVVSCVPS WFWGPVVTLQ DCLAAFFARD ELKGDNMYSC EKCKKLRNGV
KFCKVQNFPE ILCIHLKRFR HELMFSTKIS THVSFPLEGL DLQPFLAKDS PAQIVTYDLL
SVICHHGTAS SGHYIAYCRN NLNNLWYEFD DQSVTEVSES TVQNAEAYVL FYRKSSEEAQ
KERRRISNLL NIMEPSLLQF YISRQWLNKF KTFAEPGPIS NNDFLCIHGG VPPRKAGYIE
DLVLMLPQNI WDNLYSRYGG GPAVNHLYIC HTCQIEAEKI EKRRKTELEI FIRLNRAFQK
EDSPATFYCI SMQWFREWES FVKGKDGDPP GPIDNTKIAV TKCGNVMLRQ GADSGQISEE
TWNFLQSIYG GGPEVILRPP VVHVDPDILQ AEEKIEVETR SL


Related products :

Catalog number Product name Quantity
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
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
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,
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
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
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
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
EIAAB45061 Bos taurus,Bovine,Deubiquitinating enzyme 42,Ubiquitin carboxyl-terminal hydrolase 42,Ubiquitin thiolesterase 42,Ubiquitin-specific-processing protease 42,USP42
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


 

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