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Ubiquitin carboxyl-terminal hydrolase 25 (EC 3.4.19.12) (Deubiquitinating enzyme 25) (USP on chromosome 21) (Ubiquitin thioesterase 25) (Ubiquitin-specific-processing protease 25)

 UBP25_HUMAN             Reviewed;        1055 AA.
Q9UHP3; C0LSZ0; Q6DHZ9; Q9H9W1;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
10-AUG-2010, sequence version 4.
22-NOV-2017, entry version 170.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 25;
EC=3.4.19.12;
AltName: Full=Deubiquitinating enzyme 25;
AltName: Full=USP on chromosome 21;
AltName: Full=Ubiquitin thioesterase 25;
AltName: Full=Ubiquitin-specific-processing protease 25;
Name=USP25; Synonyms=USP21;
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 USP25A AND USP25B), AND TISSUE
SPECIFICITY.
TISSUE=Fetal brain;
PubMed=10644437; DOI=10.1006/geno.1999.6025;
Valero R., Marfany G., Gonzalez-Angulo O., Gonzalez-Gonzalez G.,
Puelles L., Gonzalez-Duarte R.;
"USP25, a novel gene encoding a deubiquitinating enzyme, is located in
the gene-poor region 21q11.2.";
Genomics 62:395-405(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM USP25A), AND FUNCTION.
PubMed=10612803;
DOI=10.1002/(SICI)1098-2264(200002)27:2<153::AID-GCC6>3.0.CO;2-A;
Groet J., Ives J.H., Jones T.A., Danton M., Flomen R.H., Sheer D.,
Hrascan R., Pavelic K., Nizetic D.;
"Narrowing of the region of allelic loss in 21q11-21 in squamous non-
small cell lung carcinoma and cloning of a novel ubiquitin-specific
protease gene from the deleted segment.";
Genes Chromosomes Cancer 27:153-161(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM USP25M).
Valero R., Bosch-Comas A., Denuc A., Gonzalez-Duarte R., Marfany G.;
Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
[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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM USP25A).
TISSUE=Placenta;
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 319-1055 (ISOFORM USP25A).
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).
[7]
ALTERNATIVE SPLICING, FUNCTION, AND TISSUE SPECIFICITY.
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).
[8]
ALTERNATIVE SPLICING, INTERACTION WITH ACTA1; FLNC; GAPDH AND MYBPC1,
INDUCTION, SUBCELLULAR LOCATION, AND POSSIBLE FUNCTION.
PubMed=16501887; DOI=10.1007/s00018-005-5533-1;
Bosch-Comas A., Lindsten K., Gonzalez-Duarte R., Masucci M.G.,
Marfany G.;
"The ubiquitin-specific protease USP25 interacts with three sarcomeric
proteins.";
Cell. Mol. Life Sci. 63:723-734(2006).
[9]
SUMOYLATION AT LYS-99, FUNCTION, INTERACTION WITH SUMO1; SUMO3 AND
UBIQUITIN, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF
VAL-91; ILE-92 AND LYS-99.
PubMed=18538659; DOI=10.1016/j.molcel.2008.03.021;
Meulmeester E., Kunze M., Hsiao H.H., Urlaub H., Melchior F.;
"Mechanism and consequences for paralog-specific sumoylation of
ubiquitin-specific protease 25.";
Mol. Cell 30:610-619(2008).
[10]
UBIQUITINATION AT LYS-99, DEUBIQUITINATION, ACTIVE SITE CYS-178,
ACETYLATION, PHOSPHORYLATION, SUMOYLATION, FUNCTION, SUBCELLULAR
LOCATION, SUBUNIT, AND MUTAGENESIS OF LYS-99 AND CYS-178.
PubMed=19440361; DOI=10.1371/journal.pone.0005571;
Denuc A., Bosch-Comas A., Gonzalez-Duarte R., Marfany G.;
"The UBA-UIM domains of the USP25 regulate the enzyme ubiquitination
state and modulate substrate recognition.";
PLoS ONE 4:E5571-E5571(2009).
[11]
INTERACTION WITH SYK, PHOSPHORYLATION AT TYR-740, AND MUTAGENESIS OF
TYR-740; THR-878; TYR-880 AND ILE-883.
PubMed=19909739; DOI=10.1016/j.yexcr.2009.10.023;
Cholay M., Reverdy C., Benarous R., Colland F., Daviet L.;
"Functional interaction between the ubiquitin-specific protease 25 and
the SYK tyrosine kinase.";
Exp. Cell Res. 316:667-675(2010).
[12]
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
-!- FUNCTION: Deubiquitinating enzyme that hydrolyzes ubiquitin
moieties conjugated to substrates and thus, functions to process
newly synthesized Ubiquitin, to recycle ubiquitin molecules or to
edit polyubiquitin chains and prevents proteasomal degradation of
substrates. Hydrolyzes both 'Lys-48'- and 'Lys-63'-linked
tetraubiquitin chains.
-!- FUNCTION: The muscle-specific isoform (USP25m) may have a role in
the regulation of muscular differentiation and function.
-!- 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: Homodimer or oligomer. Interacts with ACTA1 (via its C-
terminus); the interaction occurs for all isoforms but is
strongest for isoform USP25m in muscle differentiating cells.
Interacts (isoform USP25m only) with MYBPC1; the interaction
prevents proteasomal degradation of MYBPC1. Interacts (isoform
USP25m only) with FLNC (via filament repeats 17-18, 20-21 and 24).
Interacts with GAPDH. Interacts with SUMO3; the interaction
sumoylates efficiently USP25. Interacts with SUMO2; the
interaction sumoylates efficiently USP25. Interacts with SUMO1;
the interaction only weakly sumoylates USP25. Interacts with SYK;
phosphorylates USP25 and regulates USP25 intracellular levels.
{ECO:0000269|PubMed:16501887, ECO:0000269|PubMed:18538659,
ECO:0000269|PubMed:19440361, ECO:0000269|PubMed:19909739}.
-!- INTERACTION:
O15481:MAGEB4; NbExp=3; IntAct=EBI-2513462, EBI-751857;
P54725:RAD23A; NbExp=7; IntAct=EBI-2513462, EBI-746453;
P61956:SUMO2; NbExp=5; IntAct=EBI-2513462, EBI-473220;
P43405:SYK; NbExp=6; IntAct=EBI-2513462, EBI-78302;
Q9BTV4:TMEM43; NbExp=4; IntAct=EBI-2513462, EBI-721293;
Q9BUY5:ZNF426; NbExp=3; IntAct=EBI-2513462, EBI-743265;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16501887,
ECO:0000269|PubMed:19440361}.
-!- SUBCELLULAR LOCATION: Isoform USP25m: Cytoplasm {ECO:0000250}.
Nucleus {ECO:0000250}. Note=Some transient punctuate nuclear
location in myotubes during myocyte development. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=USP25a;
IsoId=Q9UHP3-2; Sequence=Displayed;
Name=USP25b;
IsoId=Q9UHP3-1; Sequence=VSP_039632;
Name=USP25m; Synonyms=Muscle-specific isoform;
IsoId=Q9UHP3-3; Sequence=VSP_039631;
-!- TISSUE SPECIFICITY: Isoform USP25a is found in most adult and
fetal tissues; expression is moderately high in testis, pancreas,
kidney, skeletal muscle, liver, lung, placenta, brain, heart, but
very low in peripheral blood, colon, small intestine, ovary,
prostate, thymus and spleen. Isoform USP25b is found in all
tissues except heart and skeletal muscle. Isoform USP25m is heart
and skeletal muscle specific. {ECO:0000269|PubMed:10644437,
ECO:0000269|PubMed:11597335}.
-!- INDUCTION: The muscle-specific isoform (USP25m) is up-regulated
during myocyte differentiation. Levels increase up to 100-fold
towards completion of differentiation.
{ECO:0000269|PubMed:16501887}.
-!- PTM: Acetylated. {ECO:0000269|PubMed:19440361}.
-!- PTM: Sumoylation impairs binding to and hydrolysis of ubiquitin
chains. Sumoylated preferentially with SUMO2 or SUMO3.
Desumoylated by SENP1. Regulated by ubiquitination on the same
residue. {ECO:0000269|PubMed:19440361}.
-!- PTM: Preferentially monoubiquitinated but can also be
polyubiquitinated. Autodeubiquitinated. Ubiquitination activates
the enzymatic activity either by preventing sumoylation or by
allowing novel interactions. {ECO:0000269|PubMed:19440361}.
-!- PTM: Phosphorylation in the C-terminal by SYK regulates USP25
cellular levels. {ECO:0000269|PubMed:19440361,
ECO:0000269|PubMed:19909739}.
-!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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EMBL; AF170562; AAF32263.1; -; mRNA.
EMBL; AF134213; AAF24998.1; -; mRNA.
EMBL; FJ763652; ACN76567.1; -; mRNA.
EMBL; CH471079; EAX10041.1; -; Genomic_DNA.
EMBL; BC075792; AAH75792.1; -; mRNA.
EMBL; AK022574; BAB14107.1; -; mRNA.
CCDS; CCDS33515.1; -. [Q9UHP3-2]
CCDS; CCDS63336.1; -. [Q9UHP3-3]
CCDS; CCDS63337.1; -. [Q9UHP3-1]
RefSeq; NP_001269970.1; NM_001283041.1. [Q9UHP3-3]
RefSeq; NP_001269971.1; NM_001283042.1. [Q9UHP3-1]
RefSeq; NP_037528.3; NM_013396.4. [Q9UHP3-2]
UniGene; Hs.743994; -.
PDB; 2MUX; NMR; -; A=1-146.
PDB; 5GP7; X-ray; 1.50 A; B=1046-1055.
PDBsum; 2MUX; -.
PDBsum; 5GP7; -.
ProteinModelPortal; Q9UHP3; -.
SMR; Q9UHP3; -.
BioGrid; 118895; 53.
IntAct; Q9UHP3; 26.
MINT; MINT-1188384; -.
STRING; 9606.ENSP00000285679; -.
MEROPS; C19.041; -.
iPTMnet; Q9UHP3; -.
PhosphoSitePlus; Q9UHP3; -.
DMDM; 302393833; -.
EPD; Q9UHP3; -.
MaxQB; Q9UHP3; -.
PaxDb; Q9UHP3; -.
PeptideAtlas; Q9UHP3; -.
PRIDE; Q9UHP3; -.
DNASU; 29761; -.
Ensembl; ENST00000285679; ENSP00000285679; ENSG00000155313. [Q9UHP3-2]
Ensembl; ENST00000285681; ENSP00000285681; ENSG00000155313. [Q9UHP3-1]
Ensembl; ENST00000400183; ENSP00000383044; ENSG00000155313. [Q9UHP3-3]
GeneID; 29761; -.
KEGG; hsa:29761; -.
UCSC; uc002yjy.3; human. [Q9UHP3-2]
CTD; 29761; -.
DisGeNET; 29761; -.
EuPathDB; HostDB:ENSG00000155313.15; -.
GeneCards; USP25; -.
HGNC; HGNC:12624; USP25.
HPA; HPA018297; -.
HPA; HPA024142; -.
MIM; 604736; gene.
neXtProt; NX_Q9UHP3; -.
OpenTargets; ENSG00000155313; -.
PharmGKB; PA37249; -.
eggNOG; KOG1863; Eukaryota.
eggNOG; COG5077; LUCA.
GeneTree; ENSGT00390000016082; -.
HOGENOM; HOG000007956; -.
HOVERGEN; HBG056030; -.
InParanoid; Q9UHP3; -.
KO; K11849; -.
OMA; TKSSWEE; -.
OrthoDB; EOG091G00QR; -.
PhylomeDB; Q9UHP3; -.
TreeFam; TF329035; -.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
ChiTaRS; USP25; human.
GenomeRNAi; 29761; -.
PRO; PR:Q9UHP3; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000155313; -.
CleanEx; HS_USP21; -.
CleanEx; HS_USP25; -.
ExpressionAtlas; Q9UHP3; baseline and differential.
Genevisible; Q9UHP3; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0051117; F:ATPase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0008233; F:peptidase activity; TAS:ProtInc.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IMP:UniProtKB.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; TAS:Reactome.
GO; GO:0043130; F:ubiquitin binding; NAS:ParkinsonsUK-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
GO; GO:1904455; F:ubiquitin-specific protease activity involved in negative regulation of ERAD pathway; NAS:ParkinsonsUK-UCL.
GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
GO; GO:1904293; P:negative regulation of ERAD pathway; IMP:ParkinsonsUK-UCL.
GO; GO:0016579; P:protein deubiquitination; IDA:ParkinsonsUK-UCL.
GO; GO:0071108; P:protein K48-linked deubiquitination; IMP:UniProtKB.
GO; GO:0070536; P:protein K63-linked deubiquitination; IMP:UniProtKB.
GO; GO:0006508; P:proteolysis; TAS:ProtInc.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR009060; UBA-like_sf.
InterPro; IPR003903; UIM_dom.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
Pfam; PF00443; UCH; 1.
Pfam; PF02809; UIM; 2.
SMART; SM00726; UIM; 1.
SUPFAM; SSF46934; SSF46934; 1.
PROSITE; PS50330; UIM; 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; Coiled coil; Complete proteome;
Cytoplasm; Hydrolase; Isopeptide bond; Nucleus; Phosphoprotein;
Protease; Reference proteome; Repeat; Thiol protease; Ubl conjugation;
Ubl conjugation pathway.
CHAIN 1 1055 Ubiquitin carboxyl-terminal hydrolase 25.
/FTId=PRO_0000080653.
DOMAIN 14 57 UBA-like.
DOMAIN 97 116 UIM 1. {ECO:0000255|PROSITE-
ProRule:PRU00213}.
DOMAIN 123 140 UIM 2. {ECO:0000255|PROSITE-
ProRule:PRU00213}.
DOMAIN 169 657 USP.
REGION 77 102 SUMO interaction domain (SIM).
COILED 541 578 {ECO:0000255}.
COILED 684 717 {ECO:0000255}.
MOTIF 89 95 Required for SUMO paralog-specific
binding.
ACT_SITE 178 178 {ECO:0000269|PubMed:19440361}.
ACT_SITE 599 599 {ECO:0000250}.
ACT_SITE 607 607 {ECO:0000250}.
MOD_RES 85 85 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 740 740 Phosphotyrosine.
{ECO:0000269|PubMed:19909739}.
CROSSLNK 99 99 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
CROSSLNK 99 99 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate. {ECO:0000269|PubMed:19440361}.
VAR_SEQ 779 779 S -> SIMMTPNMQGIIMAIGKSRSVYDRCGPEAGFFK
(in isoform USP25b).
{ECO:0000303|PubMed:10644437}.
/FTId=VSP_039632.
VAR_SEQ 779 779 S -> SKPENTTSQPLSNQRVVEVAIPHVGKFMIESKEGGY
DDEIMMTPNMQGIIMAIGKSRSVYDRCGPEAGFFK (in
isoform USP25m). {ECO:0000303|Ref.3}.
/FTId=VSP_039631.
MUTAGEN 91 91 V->A: No interaction with SUMO3; when
associated with A-92.
{ECO:0000269|PubMed:18538659}.
MUTAGEN 92 92 I->A: No interaction with SUMO3; when
associated with A-91.
{ECO:0000269|PubMed:18538659}.
MUTAGEN 99 99 K->R: Abolishes sumoylation. Decreased
enzymatic activity.
{ECO:0000269|PubMed:18538659,
ECO:0000269|PubMed:19440361}.
MUTAGEN 178 178 C->S: Abrogates deubiquitinating
activity. No effect on homo- or
oligomerization.
{ECO:0000269|PubMed:19440361}.
MUTAGEN 740 740 Y->F: No effect on interaction with SYK.
{ECO:0000269|PubMed:19909739}.
MUTAGEN 878 878 T->I: No effect on interaction with SYK.
{ECO:0000269|PubMed:19909739}.
MUTAGEN 880 880 Y->F: No effect on interaction with SYK.
{ECO:0000269|PubMed:19909739}.
MUTAGEN 883 883 I->S: No effect on interaction with SYK.
{ECO:0000269|PubMed:19909739}.
CONFLICT 544 544 E -> K (in Ref. 1; AAF32263 and 3;
ACN76567). {ECO:0000305}.
HELIX 12 27 {ECO:0000244|PDB:2MUX}.
HELIX 33 43 {ECO:0000244|PDB:2MUX}.
HELIX 47 55 {ECO:0000244|PDB:2MUX}.
STRAND 61 64 {ECO:0000244|PDB:2MUX}.
STRAND 69 71 {ECO:0000244|PDB:2MUX}.
HELIX 100 116 {ECO:0000244|PDB:2MUX}.
HELIX 125 136 {ECO:0000244|PDB:2MUX}.
SEQUENCE 1055 AA; 122218 MW; 0B9CECDCAD619CF2 CRC64;
MTVEQNVLQQ SAAQKHQQTF LNQLREITGI NDTQILQQAL KDSNGNLELA VAFLTAKNAK
TPQQEETTYY QTALPGNDRY ISVGSQADTN VIDLTGDDKD DLQRAIALSL AESNRAFRET
GITDEEQAIS RVLEASIAEN KACLKRTPTE VWRDSRNPYD RKRQDKAPVG LKNVGNTCWF
SAVIQSLFNL LEFRRLVLNY KPPSNAQDLP RNQKEHRNLP FMRELRYLFA LLVGTKRKYV
DPSRAVEILK DAFKSNDSQQ QDVSEFTHKL LDWLEDAFQM KAEEETDEEK PKNPMVELFY
GRFLAVGVLE GKKFENTEMF GQYPLQVNGF KDLHECLEAA MIEGEIESLH SENSGKSGQE
HWFTELPPVL TFELSRFEFN QALGRPEKIH NKLEFPQVLY LDRYMHRNRE ITRIKREEIK
RLKDYLTVLQ QRLERYLSYG SGPKRFPLVD VLQYALEFAS SKPVCTSPVD DIDASSPPSG
SIPSQTLPST TEQQGALSSE LPSTSPSSVA AISSRSVIHK PFTQSRIPPD LPMHPAPRHI
TEEELSVLES CLHRWRTEIE NDTRDLQESI SRIHRTIELM YSDKSMIQVP YRLHAVLVHE
GQANAGHYWA YIFDHRESRW MKYNDIAVTK SSWEELVRDS FGGYRNASAY CLMYINDKAQ
FLIQEEFNKE TGQPLVGIET LPPDLRDFVE EDNQRFEKEL EEWDAQLAQK ALQEKLLASQ
KLRESETSVT TAQAAGDPEY LEQPSRSDFS KHLKEETIQI ITKASHEHED KSPETVLQSA
IKLEYARLVK LAQEDTPPET DYRLHHVVVY FIQNQAPKKI IEKTLLEQFG DRNLSFDERC
HNIMKVAQAK LEMIKPEEVN LEEYEEWHQD YRKFRETTMY LIIGLENFQR ESYIDSLLFL
ICAYQNNKEL LSKGLYRGHD EELISHYRRE CLLKLNEQAA ELFESGEDRE VNNGLIIMNE
FIVPFLPLLL VDEMEEKDIL AVEDMRNRWC SYLGQEMEPH LQEKLTDFLP KLLDCSMEIK
SFHEPPKLPS YSTHELCERF ARIMLSLSRT PADGR


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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
EIAAB45018 Deubiquitinating enzyme 25,Homo sapiens,Human,Ubiquitin carboxyl-terminal hydrolase 25,Ubiquitin thiolesterase 25,Ubiquitin-specific-processing protease 25,USP on chromosome 21,USP21,USP25
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
EIAAB45076 Deubiquitinating enzyme 48,Rat,Rattus norvegicus,Synaptic ubiquitin-specific protease,synUSP,Ubiquitin carboxyl-terminal hydrolase 48,Ubiquitin thiolesterase 48,Ubiquitin-specific-processing protease
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
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
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
EIAAB44982 Bos taurus,Bovine,Deubiquitinating enzyme 12,Ubiquitin carboxyl-terminal hydrolase 12,Ubiquitin thiolesterase 12,Ubiquitin-specific-processing protease 12,USP12
EIAAB45069 Deubiquitinating enzyme 45,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 45,Ubiquitin thiolesterase 45,Ubiquitin-specific-processing protease 45,Usp45
EIAAB45021 Deubiquitinating enzyme 26,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 26,Ubiquitin thiolesterase 26,Ubiquitin-specific-processing protease 26,Usp26
EIAAB44985 Deubiquitinating enzyme 14,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 14,Ubiquitin thiolesterase 14,Ubiquitin-specific-processing protease 14,Usp14


 

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