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Ubiquitin carboxyl-terminal hydrolase 7 (EC 3.4.19.12) (Deubiquitinating enzyme 7) (Herpesvirus-associated ubiquitin-specific protease) (mHAUSP) (Ubiquitin thioesterase 7) (Ubiquitin-specific-processing protease 7)

 UBP7_MOUSE              Reviewed;        1103 AA.
Q6A4J8; Q3UX92; Q496Y5; Q8BW01;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
13-SEP-2004, sequence version 1.
18-JUL-2018, entry version 119.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 7;
EC=3.4.19.12 {ECO:0000269|PubMed:14719112, ECO:0000269|PubMed:21268065};
AltName: Full=Deubiquitinating enzyme 7;
AltName: Full=Herpesvirus-associated ubiquitin-specific protease;
Short=mHAUSP;
AltName: Full=Ubiquitin thioesterase 7;
AltName: Full=Ubiquitin-specific-processing protease 7;
Name=Usp7; Synonyms=Hausp;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
TISSUE SPECIFICITY, INTERACTION WITH TP53, AND MUTAGENESIS OF CYS-224.
PubMed=14719112;
Lim S.-K., Shin J.-M., Kim Y.-S., Baek K.-H.;
"Identification and characterization of murine mHAUSP encoding a
deubiquitinating enzyme that regulates the status of p53
ubiquitination.";
Int. J. Oncol. 24:357-364(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-545 (ISOFORM 2), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 832-1103.
STRAIN=C57BL/6J; TISSUE=Egg, and Stomach;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 214-1103 (ISOFORM 3).
STRAIN=C57BL/6J; TISSUE=Brain;
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).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-50 AND SER-54,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=19946331; DOI=10.1038/onc.2009.427;
Kon N., Kobayashi Y., Li M., Brooks C.L., Ludwig T., Gu W.;
"Inactivation of HAUSP in vivo modulates p53 function.";
Oncogene 29:1270-1279(2010).
[7]
FUNCTION, INTERACTION WITH DNMT1 AND UHRF1, AND MUTAGENESIS OF
CYS-224.
PubMed=21268065; DOI=10.1002/jcb.22998;
Qin W., Leonhardt H., Spada F.;
"Usp7 and Uhrf1 control ubiquitination and stability of the
maintenance DNA methyltransferase Dnmt1.";
J. Cell. Biochem. 112:439-444(2011).
[8]
FUNCTION.
PubMed=23973222; DOI=10.1016/j.immuni.2013.05.018;
van Loosdregt J., Fleskens V., Fu J., Brenkman A.B., Bekker C.P.,
Pals C.E., Meerding J., Berkers C.R., Barbi J., Grone A., Sijts A.J.,
Maurice M.M., Kalkhoven E., Prakken B.J., Ovaa H., Pan F., Zaiss D.M.,
Coffer P.J.;
"Stabilization of the transcription factor Foxp3 by the deubiquitinase
USP7 increases Treg-cell-suppressive capacity.";
Immunity 39:259-271(2013).
[9]
FUNCTION, AND INTERACTION WITH EPOP.
PubMed=27863226; DOI=10.1016/j.molcel.2016.10.019;
Liefke R., Karwacki-Neisius V., Shi Y.;
"EPOP interacts with elongin BC and USP7 to modulate the chromatin
landscape.";
Mol. Cell 64:659-672(2016).
-!- FUNCTION: Hydrolase that deubiquitinates target proteins such as
FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN, KMT2E and DAXX
(PubMed:21268065, PubMed:14719112, PubMed:19946331). Together with
DAXX, prevents MDM2 self-ubiquitination and enhances the E3 ligase
activity of MDM2 towards p53/TP53, thereby promoting p53/TP53
ubiquitination and proteasomal degradation. Deubiquitinates
p53/TP53, preventing degradation of p53/TP53, and enhances
p53/TP53-dependent transcription regulation, cell growth
repression and apoptosis. Deubiquitinates p53/TP53 and MDM2 and
strongly stabilizes p53/TP53 even in the presence of excess MDM2,
and also induces p53/TP53-dependent cell growth repression and
apoptosis. Deubiquitination of FOXO4 in presence of hydrogen
peroxide is not dependent on p53/TP53 and inhibits FOXO4-induced
transcriptional activity. In association with DAXX, is involved in
the deubiquitination and translocation of PTEN from the nucleus to
the cytoplasm, both processes that are counteracted by PML.
Deubiquitinates KMT2E preventing KMT2E proteasomal-mediated
degradation (By similarity). Involved in cell proliferation during
early embryonic development. Involved in transcription-coupled
nucleotide excision repair (TC-NER) in response to UV damage:
recruited to DNA damage sites following interaction with
KIAA1530/UVSSA and promotes deubiquitination of ERCC6, preventing
UV-induced degradation of ERCC6 (By similarity). Involved in
maintenance of DNA methylation via its interaction with UHRF1 and
DNMT1: acts by mediating deubiquitination of UHRF1 and DNMT1,
preventing their degradation and promoting DNA methylation by
DNMT1. Deubiquitinates alkylation repair enzyme ALKBH3. OTUD4
recruits USP7 and USP9X to stabilize ALKBH3, thereby promoting the
repair of alkylated DNA lesions (By similarity). Acts as a
chromatin regulator via its association with the Polycomb group
(PcG) multiprotein PRC1-like complex; may act by deubiquitinating
components of the PRC1-like complex (By similarity). Able to
mediate deubiquitination of histone H2B; it is however unsure
whether this activity takes place in vivo (PubMed:27863226).
Exhibits a preference towards 'Lys-48'-linked ubiquitin chains.
Increases regulatory T-cells (Treg) suppressive capacity by
deubiquitinating and stabilizing the transcription factor FOXP3
which is crucial for Treg cell function (PubMed:23973222).
{ECO:0000250|UniProtKB:Q93009, ECO:0000269|PubMed:23973222,
ECO:0000269|PubMed:27863226}.
-!- 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:14719112, ECO:0000269|PubMed:21268065}.
-!- SUBUNIT: Monomer. Homodimer. Part of a complex with DAXX, MDM2,
RASSF1 and USP7. Part of a complex with DAXX, MDM2 and USP7.
Interacts with MDM2; the interaction is independent of p53/TP53.
Interacts with DAXX; the interaction is direct and independent of
MDM2 and p53/TP53. Component of a complex composed of KMT2E, OGT
and USP7; the complex stabilizes KMT2E, preventing KMT2E
ubiquitination and proteosomal-mediated degradation (By
similarity). Interacts (via MATH domain) with KMT2E (By
similarity). Interacts with OGT (By similarity). Interacts with
FOXO4; the interaction is enhanced in presence of hydrogen
peroxide and occurs independently of p53/TP53. Interacts with
p53/TP53; the interaction is enhanced in response to DNA damage;
the interaction is impaired by TSPYL5. Interacts with PTEN; the
interaction is direct. Interacts with ATXN1 and the strength of
interaction is influenced by the length of the poly-Gln region in
ATXN1. A weaker interaction seen with mutants having longer poly-
Gln regions. Interacts with KIAA1530/UVSSA. Interacts with MEX3C
and antagonizes its ability to degrade mRNA (By similarity).
Interacts with DNMT1 and UHRF1 (PubMed:21268065). Interacts with
FOXP3 (By similarity). Interacts (via MATH domain) with RNF220 (By
similarity). Associated component of the Polycomb group (PcG)
multiprotein PRC1-like complex (By similarity). Interacts with
EPOP (PubMed:27863226). Interacts with OTUD4 and USP9X; the
interaction is direct (By similarity).
{ECO:0000250|UniProtKB:Q93009, ECO:0000269|PubMed:14719112,
ECO:0000269|PubMed:21268065, ECO:0000269|PubMed:27863226}.
-!- INTERACTION:
O08586:Pten; NbExp=2; IntAct=EBI-1216254, EBI-1186266;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q93009}.
Cytoplasm {ECO:0000250|UniProtKB:Q93009}. Nucleus, PML body
{ECO:0000250|UniProtKB:Q93009}. Chromosome
{ECO:0000250|UniProtKB:Q93009}. Note=Present in a minority of ND10
nuclear bodies. Association with ICP0/VMW110 at early times of
infection leads to an increased proportion of USP7-containing
ND10. Colocalizes with ATXN1 in the nucleus. Colocalized with DAXX
in speckled structures. Colocalized with PML and PTEN in
promyelocytic leukemia protein (PML) nuclear bodies.
{ECO:0000250|UniProtKB:Q93009}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q6A4J8-1; Sequence=Displayed;
Name=2;
IsoId=Q6A4J8-2; Sequence=VSP_021952;
Name=3;
IsoId=Q6A4J8-3; Sequence=VSP_021953, VSP_021954;
-!- TISSUE SPECIFICITY: Expressed at high levels in brain, lung,
thymus and testis. Expressed at low levels in the liver.
{ECO:0000269|PubMed:14719112}.
-!- DEVELOPMENTAL STAGE: Expressed in embryo at 3.5 and from 7.5 to
10.5 dpc (at protein level).
-!- DOMAIN: The C-terminus plays a role in its oligomerization.
{ECO:0000250}.
-!- PTM: Polyneddylated. {ECO:0000250}.
-!- PTM: Not sumoylated. {ECO:0000250}.
-!- PTM: Polyubiquitinated. Ubiquitinated at Lys-870 (By similarity).
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Led to early embryonic lethality. Show
disorganized germinal layers without the formation of a
proamniotic cavity. Many of the surviving cells were trophoblastic
giant cells with large nuclei. {ECO:0000269|PubMed:19946331}.
-!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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EMBL; AF548565; AAQ12339.1; -; mRNA.
EMBL; AK075830; BAC35992.1; -; mRNA.
EMBL; AK135814; BAE22671.1; -; mRNA.
EMBL; BC100666; AAI00667.1; -; mRNA.
CCDS; CCDS49755.1; -. [Q6A4J8-1]
RefSeq; NP_001003918.2; NM_001003918.2.
UniGene; Mm.295330; -.
ProteinModelPortal; Q6A4J8; -.
SMR; Q6A4J8; -.
BioGrid; 232963; 13.
DIP; DIP-38603N; -.
IntAct; Q6A4J8; 6.
MINT; Q6A4J8; -.
STRING; 10090.ENSMUSP00000124093; -.
MEROPS; C19.016; -.
iPTMnet; Q6A4J8; -.
PhosphoSitePlus; Q6A4J8; -.
EPD; Q6A4J8; -.
PaxDb; Q6A4J8; -.
PeptideAtlas; Q6A4J8; -.
PRIDE; Q6A4J8; -.
DNASU; 252870; -.
GeneID; 252870; -.
KEGG; mmu:252870; -.
UCSC; uc007ycx.1; mouse. [Q6A4J8-1]
CTD; 7874; -.
MGI; MGI:2182061; Usp7.
eggNOG; KOG1863; Eukaryota.
eggNOG; COG5077; LUCA.
HOGENOM; HOG000160240; -.
HOVERGEN; HBG018029; -.
InParanoid; Q6A4J8; -.
KO; K11838; -.
PhylomeDB; Q6A4J8; -.
ChiTaRS; Usp7; mouse.
PRO; PR:Q6A4J8; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_USP7; -.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0001741; C:XY body; IDA:MGI.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IMP:UniProtKB.
GO; GO:1990380; F:Lys48-specific deubiquitinase activity; ISS:UniProtKB.
GO; GO:0002039; F:p53 binding; ISO:MGI.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
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:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0035616; P:histone H2B conserved C-terminal lysine deubiquitination; IMP:UniProtKB.
GO; GO:0010216; P:maintenance of DNA methylation; ISO:MGI.
GO; GO:0035520; P:monoubiquitinated protein deubiquitination; ISO:MGI.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:MGI.
GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:1901537; P:positive regulation of DNA demethylation; ISS:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
GO; GO:0050821; P:protein stabilization; ISO:MGI.
GO; GO:0051090; P:regulation of DNA binding transcription factor activity; ISS:UniProtKB.
GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; ISS:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
Gene3D; 2.60.210.10; -; 1.
InterPro; IPR002083; MATH/TRAF_dom.
InterPro; IPR038765; Papain_like_cys_pep_sf.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR008974; TRAF-like.
InterPro; IPR024729; USP7_ICP0-binding_dom.
InterPro; IPR029346; USP_C.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
Pfam; PF00917; MATH; 1.
Pfam; PF00443; UCH; 1.
Pfam; PF14533; USP7_C2; 1.
Pfam; PF12436; USP7_ICP0_bdg; 1.
SMART; SM00061; MATH; 1.
SUPFAM; SSF49599; SSF49599; 1.
SUPFAM; SSF54001; SSF54001; 1.
PROSITE; PS50144; MATH; 1.
PROSITE; PS00972; USP_1; 1.
PROSITE; PS00973; USP_2; 1.
PROSITE; PS50235; USP_3; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Chromosome; Complete proteome;
Cytoplasm; Developmental protein; DNA damage; DNA repair; Hydrolase;
Isopeptide bond; Nucleus; Phosphoprotein; Protease;
Reference proteome; Thiol protease; Ubl conjugation;
Ubl conjugation pathway.
CHAIN 1 1103 Ubiquitin carboxyl-terminal hydrolase 7.
/FTId=PRO_0000268006.
DOMAIN 69 196 MATH. {ECO:0000255|PROSITE-
ProRule:PRU00129}.
DOMAIN 215 522 USP.
REGION 1 209 Interaction with TSPYL5.
{ECO:0000250|UniProtKB:Q93009}.
REGION 54 209 Interaction with p53/TP53 and MDM2.
{ECO:0000250|UniProtKB:Q93009}.
REGION 71 206 Necessary for nuclear localization.
{ECO:0000250|UniProtKB:Q93009}.
COMPBIAS 4 17 Gln-rich.
ACT_SITE 224 224 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093,
ECO:0000269|PubMed:14719112,
ECO:0000269|PubMed:21268065}.
ACT_SITE 465 465 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 54 54 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 870 870 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q93009}.
MOD_RES 964 964 Phosphoserine.
{ECO:0000250|UniProtKB:Q93009}.
MOD_RES 1085 1085 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q93009}.
MOD_RES 1097 1097 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q93009}.
CROSSLNK 870 870 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q93009}.
CROSSLNK 870 870 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:Q93009}.
CROSSLNK 883 883 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q93009}.
VAR_SEQ 1 27 MNHQQQQQQQQKAGEQQLSEPEDMEME -> MASSTSPPRS
PSGGILTQDTIYFPQSNIISELLPWYLRYTPPEVPSTSVIT
KFILVNCPWNEGIEYQ (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_021952.
VAR_SEQ 974 974 E -> ECLQ (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_021953.
VAR_SEQ 1094 1103 YLEKAIKIHN -> LGLC (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_021954.
MUTAGEN 224 224 C->S: Loss of p53/TP53-deubiquitinating
activity. {ECO:0000269|PubMed:14719112,
ECO:0000269|PubMed:21268065}.
CONFLICT 162 162 E -> K (in Ref. 2; BAE22671).
{ECO:0000305}.
SEQUENCE 1103 AA; 128475 MW; 989DFE733F0D961E CRC64;
MNHQQQQQQQ QKAGEQQLSE PEDMEMEAGD TDDPPRITQN PVINGNVTLS DGHSNAEEDM
EDDTSWRSEA TFQFTVERFS RLSESVLSPP CFVRNLPWKI MVMPRFYPDR PHQKSVGFFL
QCNAESDSTS WSCHAQAVLK IINYRDDDKS FSRRISHLFF HEENDWGFSN FMAWSEVTDP
EKGFIDDDKV TFEVFVQADA PHGVAWDSKK HTGYVGLKNQ GATCYMNSLL QTLFFTNQLR
KAVYMMPTEG DDSSKSVPLA LQRVFYELQH SDKPVGTKKL TKSFGWETLD SFMQHDVQEL
CRVLLDNVEN KMKGTCVEGT IPKLFRGKMV SYIQCKDVDY RSDRREDYYD IQLSIKGKKN
IFESFVDYVA VEQLDGDNKY DAGEHGLQEA EKGVKFLTLP PVLHLQLMRF MYDPQTDQNI
KINDRFEFPE QLPLDEFLQK TDPKDPANYI LHAVLVHSGD NHGGHYVVYL NPKGDGKWCK
FDDDVVSRCT KEEAIEHNYG GHDDDLSVRH CTNAYMLVYI RESKLSEVLQ AVTDHDIPQQ
LVERLQEEKR IEAQKRKERQ EAHLYMQVQI VAEDQFCGHQ GNDMYDEEKV RYTVFKVLKN
SSLAEFVQSL SQTMGFPQDQ IRLWPMQARS NGTKRPAMLD NEADGNKTMI ELSDNENPWT
IFLETVDPEL AASGATLPKF DKDHDVMLFL KMYDPKTRSL NYCGHIYTPI SCKIRDLLPV
MCDRAGFIQD TSLILYEEVK PNLTERIQDY DVSLDKALDE LMDGDIIVFQ KDDPENDNSE
LPTAKEYFRD LYHRVDVIFC DKTIPNDPGF VVTLSNRMNY FQVAKTVAQR LNTDPMLLQF
FKSQGYRDGP GNPLRHNYEG TLRDLLQFFK PRQPKKLYYQ QLKMKITDFE NRRSFKCIWL
NSQFREEEIT LYPDKHGCVR DLLEECKKAV ELGDKASGRL RLLEIVSYKI IGVHQEDELL
ECLSPATSRT FRIEEIPLDQ VDIDKENEML ITVAHFHKEV FGTFGIPFLL RIHQGEHFRE
VMKRIQSLLD IQEKEFEKFK FAIVMMGRHQ YINEDEYEVN LKDFEPQPGN MSHPRPWLGL
DHFNKAPKRS RYTYLEKAIK IHN


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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
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
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
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-
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
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
EIAAB45076 Deubiquitinating enzyme 48,Rat,Rattus norvegicus,Synaptic ubiquitin-specific protease,synUSP,Ubiquitin carboxyl-terminal hydrolase 48,Ubiquitin thiolesterase 48,Ubiquitin-specific-processing protease
EIAAB45055 Deubiquitinating enzyme 4,Rat,Rattus norvegicus,Ubiquitin carboxyl-terminal hydrolase 4,Ubiquitin thioesterase 4,Ubiquitin-specific-processing protease 4,Usp4
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,
EIAAB45035 Deubiquitinating enzyme 30,Homo sapiens,Human,Ubiquitin carboxyl-terminal hydrolase 30,Ubiquitin thiolesterase 30,Ubiquitin-specific-processing protease 30,Ub-specific protease 30,USP30
EIAAB45034 Deubiquitinating enzyme 30,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 30,Ubiquitin thiolesterase 30,Ubiquitin-specific-processing protease 30,Ub-specific protease 30,Usp30
EIAAB45003 41 kDa ubiquitin-specific protease,Chicken,Deubiquitinating enzyme 2,Gallus gallus,Ubiquitin carboxyl-terminal hydrolase 2,Ubiquitin thiolesterase 2,Ubiquitin-specific-processing protease 2,UBP41,USP2
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
EIAAB45093 Chicken,Deubiquitinating enzyme 7,Gallus gallus,Ubiquitin carboxyl-terminal hydrolase 7,Ubiquitin thioesterase 7,Ubiquitin-specific-processing protease 7,USP7
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
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
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
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
EIAAB45050 Deubiquitinating enzyme 37,Pig,Sus scrofa,Ubiquitin carboxyl-terminal hydrolase 37,Ubiquitin thiolesterase 37,Ubiquitin-specific-processing protease 37,USP37
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
EIAAB45061 Bos taurus,Bovine,Deubiquitinating enzyme 42,Ubiquitin carboxyl-terminal hydrolase 42,Ubiquitin thiolesterase 42,Ubiquitin-specific-processing protease 42,USP42
EIAAB45025 Deubiquitinating enzyme 28,Rat,Rattus norvegicus,Ubiquitin carboxyl-terminal hydrolase 28,Ubiquitin thiolesterase 28,Ubiquitin-specific-processing protease 28,Usp28
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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