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Protein phosphatase 1D (EC 3.1.3.16) (Protein phosphatase 2C isoform delta) (PP2C-delta) (Protein phosphatase magnesium-dependent 1 delta) (p53-induced protein phosphatase 1)

 PPM1D_HUMAN             Reviewed;         605 AA.
O15297; Q53XP4; Q6P991; Q8IVR6;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
12-SEP-2018, entry version 169.
RecName: Full=Protein phosphatase 1D;
EC=3.1.3.16;
AltName: Full=Protein phosphatase 2C isoform delta;
Short=PP2C-delta;
AltName: Full=Protein phosphatase magnesium-dependent 1 delta;
AltName: Full=p53-induced protein phosphatase 1;
Name=PPM1D; Synonyms=WIP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, AND SUBCELLULAR
LOCATION.
PubMed=9177166; DOI=10.1073/pnas.94.12.6048;
Fiscella M., Zhang H., Fan S., Sakaguchi K., Shen S., Mercer W.E.,
Vande Woude G.F., O'Connor P.M., Appella E.;
"Wip1, a novel human protein phosphatase that is induced in response
to ionizing radiation in a p53-dependent manner.";
Proc. Natl. Acad. Sci. U.S.A. 94:6048-6053(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[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] (ISOFORMS 1 AND 2), AND VARIANT
GLN-322.
TISSUE=Brain, and Skin;
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, INTERACTION WITH CHEK1, INDUCTION, AND MUTAGENESIS OF
ASP-314.
PubMed=15870257; DOI=10.1101/gad.1291305;
Lu X., Nannenga B., Donehower L.A.;
"PPM1D dephosphorylates Chk1 and p53 and abrogates cell cycle
checkpoints.";
Genes Dev. 19:1162-1174(2005).
[7]
FUNCTION IN APOPTOSIS, FUNCTION IN DEPHOSPHORYLATION OF CHEK2, AND
INTERACTION WITH CHEK2.
PubMed=16311512; DOI=10.1038/sj.cdd.4401801;
Fujimoto H., Onishi N., Kato N., Takekawa M., Xu X.Z., Kosugi A.,
Kondo T., Imamura M., Oishi I., Yoda A., Minami Y.;
"Regulation of the antioncogenic Chk2 kinase by the oncogenic Wip1
phosphatase.";
Cell Death Differ. 13:1170-1180(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[9]
FUNCTION, AND INTERACTION WITH MAPK14.
PubMed=21283629; DOI=10.1371/journal.pone.0016427;
An H., Lu X., Liu D., Yarbrough W.G.;
"LZAP inhibits p38 MAPK (p38) phosphorylation and activity by
facilitating p38 association with the wild-type p53 induced
phosphatase 1 (WIP1).";
PLoS ONE 6:E16427-E16427(2011).
[10]
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).
[11]
FUNCTION, INVOLVEMENT IN BC, INVOLVEMENT IN OC, VARIANT OC
446-SER--CYS-605 DEL, VARIANTS BC 462-GLN--CYS-605 DEL;
478-CYS--CYS-605 DEL; 484-LEU--CYS-605 DEL AND 538-LEU--CYS-605 DEL,
AND CHARACTERIZATION OF VARIANT BC 462-GLN--CYS-605 DEL.
PubMed=23242139; DOI=10.1038/nature11725;
Breast and Ovarian Cancer Susceptibility Collaboration;
Wellcome Trust Case Control Consortium;
Ruark E., Snape K., Humburg P., Loveday C., Bajrami I., Brough R.,
Rodrigues D.N., Renwick A., Seal S., Ramsay E., Del Vechio Duarte S.,
Rivas M.A., Warren-Perry M., Zachariou A., Campion-Flora A., Hanks S.,
Murray A., Ansari Pour N., Douglas J., Gregory L., Rimmer A.,
Walker N.M., Yang T.P., Adlard J.W., Barwell J., Berg J., Brady A.F.,
Brewer C., Brice G., Chapman C., Cook J., Davidson R., Donaldson A.,
Douglas F., Eccles D., Evans D.G., Greenhalgh L., Henderson A.,
Izatt L., Kumar A., Lalloo F., Miedzybrodzka Z., Morrison P.J.,
Paterson J., Porteous M., Rogers M.T., Shanley S., Walker L., Gore M.,
Houlston R., Brown M.A., Caufield M.J., Deloukas P., McCarthy M.I.,
Todd J.A., Turnbull C., Reis-Filho J.S., Ashworth A., Antoniou A.C.,
Lord C.J., Donnelly P., Rahman N.;
"Mosaic PPM1D mutations are associated with predisposition to breast
and ovarian cancer.";
Nature 493:406-410(2013).
[12]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INVOLVEMENT IN IDDGIP, AND
VARIANTS IDDGIP 404-GLN--CYS-605 DEL; 407-CYS--CYS-605 DEL;
427-TRP--CYS-605 DEL; 447-GLU--CYS-605 DEL AND 552-ARG--CYS-605 DEL.
PubMed=28343630; DOI=10.1016/j.ajhg.2017.02.005;
Deciphering Developmental Disorders Study;
Jansen S., Geuer S., Pfundt R., Brough R., Ghongane P., Herkert J.C.,
Marco E.J., Willemsen M.H., Kleefstra T., Hannibal M., Shieh J.T.,
Lynch S.A., Flinter F., FitzPatrick D.R., Gardham A., Bernhard B.,
Ragge N., Newbury-Ecob R., Bernier R., Kvarnung M., Magnusson E.A.,
Wessels M.W., van Slegtenhorst M.A., Monaghan K.G., de Vries P.,
Veltman J.A., Lord C.J., Vissers L.E., de Vries B.B.;
"De novo truncating mutations in the last and penultimate exons of
PPM1D cause an intellectual disability syndrome.";
Am. J. Hum. Genet. 100:650-658(2017).
-!- FUNCTION: Involved in the negative regulation of p53 expression
(PubMed:23242139). Required for the relief of p53-dependent
checkpoint mediated cell cycle arrest. Binds to and
dephosphorylates 'Ser-15' of TP53 and 'Ser-345' of CHEK1 which
contributes to the functional inactivation of these proteins
(PubMed:15870257, PubMed:16311512). Mediates MAPK14
dephosphorylation and inactivation (PubMed:21283629). Is also an
important regulator of global heterochromatin silencing and
critical in maintaining genome integrity (By similarity).
{ECO:0000250|UniProtKB:Q9QZ67, ECO:0000269|PubMed:15870257,
ECO:0000269|PubMed:16311512, ECO:0000269|PubMed:21283629,
ECO:0000269|PubMed:23242139}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 2 magnesium or manganese ions per subunit.
{ECO:0000250};
-!- SUBUNIT: Interacts with CHEK1 and CHEK2; dephosphorylates them.
Interacts with MAPK14 (PubMed:21283629).
{ECO:0000269|PubMed:15870257, ECO:0000269|PubMed:16311512,
ECO:0000269|PubMed:21283629}.
-!- INTERACTION:
P16104:H2AFX; NbExp=3; IntAct=EBI-1551512, EBI-494830;
Q00987:MDM2; NbExp=4; IntAct=EBI-1551512, EBI-389668;
Q13950:RUNX2; NbExp=4; IntAct=EBI-1551512, EBI-976402;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28343630,
ECO:0000269|PubMed:9177166}. Cytoplasm, cytosol
{ECO:0000269|PubMed:28343630}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O15297-1; Sequence=Displayed;
Name=2;
IsoId=O15297-2; Sequence=VSP_056377, VSP_056378;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in fetal and adult brain. Also
detected in fetal liver and skeletal muscle, but not in their
adult counterparts. {ECO:0000269|PubMed:28343630}.
-!- INDUCTION: By p53/TP53. {ECO:0000269|PubMed:15870257,
ECO:0000269|PubMed:9177166}.
-!- DISEASE: Intellectual developmental disorder with gastrointestinal
difficulties and high pain threshold (IDDGIP) [MIM:617450]: An
autosomal dominant neurodevelopmental disorder characterized by
mild to severe intellectual disability, psychomotor developmental
delay, speech delay, and behavioral manifestations including
attention deficit-hyperactivity disorder, autism and anxiety
disorders. Most patients have variable additional features,
including feeding and gastrointestinal difficulties, high pain
threshold, hypersensitivity to sound, hypotonia, broad-based gait,
and dysmorphic features, including mild facial abnormalities,
strabismus, and small hands and feet.
{ECO:0000269|PubMed:28343630}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy
originating from breast epithelial tissue. Breast neoplasms can be
distinguished by their histologic pattern. Invasive ductal
carcinoma is by far the most common type. Breast cancer is
etiologically and genetically heterogeneous. Important genetic
factors have been indicated by familial occurrence and bilateral
involvement. Mutations at more than one locus can be involved in
different families or even in the same case.
{ECO:0000269|PubMed:23242139}. Note=Disease susceptibility may be
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer
defines malignancies originating from ovarian tissue. Although
many histologic types of ovarian tumors have been described,
epithelial ovarian carcinoma is the most common form. Ovarian
cancers are often asymptomatic and the recognized signs and
symptoms, even of late-stage disease, are vague. Consequently,
most patients are diagnosed with advanced disease.
{ECO:0000269|PubMed:23242139}. Note=Disease susceptibility may be
associated with variations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the PP2C family.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PPM1DID41803ch17q23.html";
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EMBL; U78305; AAB61637.1; -; mRNA.
EMBL; BT009780; AAP88782.1; -; mRNA.
EMBL; AC011921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC110602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC111155; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471179; EAW51408.1; -; Genomic_DNA.
EMBL; CH471179; EAW51409.1; -; Genomic_DNA.
EMBL; BC016480; AAH16480.1; -; mRNA.
EMBL; BC042418; AAH42418.1; -; mRNA.
EMBL; BC060877; AAH60877.1; -; mRNA.
CCDS; CCDS11625.1; -. [O15297-1]
RefSeq; NP_003611.1; NM_003620.3. [O15297-1]
UniGene; Hs.286073; -.
ProteinModelPortal; O15297; -.
BioGrid; 114065; 28.
CORUM; O15297; -.
DIP; DIP-38281N; -.
IntAct; O15297; 40.
MINT; O15297; -.
STRING; 9606.ENSP00000306682; -.
BindingDB; O15297; -.
ChEMBL; CHEMBL1938224; -.
DEPOD; O15297; -.
iPTMnet; O15297; -.
PhosphoSitePlus; O15297; -.
BioMuta; PPM1D; -.
EPD; O15297; -.
MaxQB; O15297; -.
PaxDb; O15297; -.
PeptideAtlas; O15297; -.
PRIDE; O15297; -.
ProteomicsDB; 48570; -.
DNASU; 8493; -.
Ensembl; ENST00000305921; ENSP00000306682; ENSG00000170836. [O15297-1]
Ensembl; ENST00000392995; ENSP00000376720; ENSG00000170836. [O15297-2]
Ensembl; ENST00000629650; ENSP00000486573; ENSG00000170836. [O15297-2]
GeneID; 8493; -.
KEGG; hsa:8493; -.
UCSC; uc002iyt.3; human. [O15297-1]
CTD; 8493; -.
DisGeNET; 8493; -.
EuPathDB; HostDB:ENSG00000170836.11; -.
GeneCards; PPM1D; -.
HGNC; HGNC:9277; PPM1D.
HPA; HPA022277; -.
MalaCards; PPM1D; -.
MIM; 114480; phenotype.
MIM; 167000; phenotype.
MIM; 605100; gene.
MIM; 617450; phenotype.
neXtProt; NX_O15297; -.
OpenTargets; ENSG00000170836; -.
PharmGKB; PA33605; -.
eggNOG; KOG0698; Eukaryota.
eggNOG; COG0631; LUCA.
GeneTree; ENSGT00920000149079; -.
HOGENOM; HOG000231949; -.
HOVERGEN; HBG058897; -.
InParanoid; O15297; -.
KO; K10147; -.
OMA; PLLHQHR; -.
OrthoDB; EOG091G08LU; -.
PhylomeDB; O15297; -.
TreeFam; TF313481; -.
Reactome; R-HSA-8878166; Transcriptional regulation by RUNX2.
SIGNOR; O15297; -.
GeneWiki; PPM1D; -.
GenomeRNAi; 8493; -.
PRO; PR:O15297; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000170836; Expressed in 206 organ(s), highest expression level in chorionic villus.
CleanEx; HS_PPM1D; -.
ExpressionAtlas; O15297; baseline and differential.
Genevisible; O15297; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0051019; F:mitogen-activated protein kinase binding; IPI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:Reactome.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB.
GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
GO; GO:0006342; P:chromatin silencing; ISS:UniProtKB.
GO; GO:0006306; P:DNA methylation; ISS:UniProtKB.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IMP:UniProtKB.
GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IDA:UniProtKB.
GO; GO:0006470; P:protein dephosphorylation; TAS:ProtInc.
GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
GO; GO:0009314; P:response to radiation; TAS:ProtInc.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
CDD; cd00143; PP2Cc; 1.
InterPro; IPR015655; PP2C.
InterPro; IPR000222; PP2C_BS.
InterPro; IPR036457; PPM-type_dom_sf.
InterPro; IPR001932; PPM-type_phosphatase_dom.
PANTHER; PTHR13832; PTHR13832; 1.
Pfam; PF00481; PP2C; 1.
SMART; SM00332; PP2Cc; 1.
SUPFAM; SSF81606; SSF81606; 2.
PROSITE; PS01032; PPM_1; 1.
PROSITE; PS51746; PPM_2; 1.
1: Evidence at protein level;
Alternative splicing; Autism spectrum disorder; Cell cycle;
Complete proteome; Cytoplasm; Disease mutation; Hydrolase; Magnesium;
Manganese; Mental retardation; Metal-binding; Nucleus; Phosphoprotein;
Polymorphism; Protein phosphatase; Reference proteome.
CHAIN 1 605 Protein phosphatase 1D.
/FTId=PRO_0000057752.
DOMAIN 8 375 PPM-type phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU01082}.
REGION 1 101 Interaction with CHEK1.
{ECO:0000269|PubMed:15870257}.
METAL 105 105 Manganese 1. {ECO:0000250}.
METAL 105 105 Manganese 2. {ECO:0000250}.
METAL 106 106 Manganese 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 314 314 Manganese 2. {ECO:0000250}.
METAL 366 366 Manganese 2. {ECO:0000250}.
MOD_RES 40 40 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 85 85 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 421 430 SLEEDPWPRV -> DFGFELDSRK (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056377.
VAR_SEQ 431 605 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056378.
VARIANT 322 322 P -> Q (in dbSNP:rs17855093).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_070430.
VARIANT 404 605 Missing (in IDDGIP).
{ECO:0000269|PubMed:28343630}.
/FTId=VAR_080081.
VARIANT 407 605 Missing (in IDDGIP).
{ECO:0000269|PubMed:28343630}.
/FTId=VAR_080082.
VARIANT 427 605 Missing (in IDDGIP).
{ECO:0000269|PubMed:28343630}.
/FTId=VAR_080083.
VARIANT 446 605 Missing (in OC; may be associated with
disease susceptibility).
{ECO:0000269|PubMed:23242139}.
/FTId=VAR_080084.
VARIANT 447 605 Missing (in IDDGIP).
{ECO:0000269|PubMed:28343630}.
/FTId=VAR_080085.
VARIANT 462 605 Missing (in BC; may be associated with
disease susceptibility; gain-of-function
mutation that results in increased
negative regulation of p53 expression in
response to ionizing radiation exposure).
{ECO:0000269|PubMed:23242139}.
/FTId=VAR_080086.
VARIANT 478 605 Missing (in BC; may be associated with
disease susceptibility).
{ECO:0000269|PubMed:23242139}.
/FTId=VAR_080087.
VARIANT 484 605 Missing (in BC; may be associated with
disease susceptibility).
{ECO:0000269|PubMed:23242139}.
/FTId=VAR_080088.
VARIANT 538 605 Missing (in BC; may be associated with
disease susceptibility).
{ECO:0000269|PubMed:23242139}.
/FTId=VAR_080089.
VARIANT 552 605 Missing (in IDDGIP).
{ECO:0000269|PubMed:28343630}.
/FTId=VAR_080090.
MUTAGEN 314 314 D->A: Abrogates phosphatase activity.
{ECO:0000269|PubMed:15870257}.
SEQUENCE 605 AA; 66675 MW; E6C5884CF04008B7 CRC64;
MAGLYSLGVS VFSDQGGRKY MEDVTQIVVE PEPTAEEKPS PRRSLSQPLP PRPSPAALPG
GEVSGKGPAV AAREARDPLP DAGASPAPSR CCRRRSSVAF FAVCDGHGGR EAAQFAREHL
WGFIKKQKGF TSSEPAKVCA AIRKGFLACH LAMWKKLAEW PKTMTGLPST SGTTASVVII
RGMKMYVAHV GDSGVVLGIQ DDPKDDFVRA VEVTQDHKPE LPKERERIEG LGGSVMNKSG
VNRVVWKRPR LTHNGPVRRS TVIDQIPFLA VARALGDLWS YDFFSGEFVV SPEPDTSVHT
LDPQKHKYII LGSDGLWNMI PPQDAISMCQ DQEEKKYLMG EHGQSCAKML VNRALGRWRQ
RMLRADNTSA IVICISPEVD NQGNFTNEDE LYLNLTDSPS YNSQETCVMT PSPCSTPPVK
SLEEDPWPRV NSKDHIPALV RSNAFSENFL EVSAEIAREN VQGVVIPSKD PEPLEENCAK
ALTLRIHDSL NNSLPIGLVP TNSTNTVMDQ KNLKMSTPGQ MKAQEIERTP PTNFKRTLEE
SNSGPLMKKH RRNGLSRSSG AQPASLPTTS QRKNSVKLTM RRRLRGQKKI GNPLLHQHRK
TVCVC


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EIAAB33079 Mouse,Mus musculus,Protein-tyrosine phosphatase delta,Ptprd,Receptor-type tyrosine-protein phosphatase delta,R-PTP-delta
EIAAB32079 Homo sapiens,Human,PP2C domain-containing protein phosphatase 1K,PP2C-kappa,PP2C-like mitochondrial protein,PP2CM,PP2C-type mitochondrial phosphoprotein phosphatase,PPM1K,Protein phosphatase 1K, mitoc
EIAAB32070 Fibroblast growth factor-inducible protein 13,FIN13,Fin13,Mouse,Mus musculus,PP2C-gamma,Ppm1c,Ppm1g,Protein phosphatase 1C,Protein phosphatase 1G,Protein phosphatase 2C isoform gamma,Protein phosphata
EIAAB32055 Homo sapiens,Human,PP2C-alpha,PPM1A,PPPM1A,Protein phosphatase 1A,Protein phosphatase 2C isoform alpha,Protein phosphatase IA
EIAAB32081 Homo sapiens,Human,PP2CE,PP2C-epsilon,PPM1L,Protein phosphatase 1L,Protein phosphatase 1-like,Protein phosphatase 2C isoform epsilon
EIAAB32056 Oryctolagus cuniculus,PP2C-alpha,PPM1A,PPPM1A,Protein phosphatase 1A,Protein phosphatase 2C isoform alpha,Protein phosphatase IA,Rabbit
EIAAB32054 Pp2c1,PP2C-alpha,Ppm1a,Pppm1a,Protein phosphatase 1A,Protein phosphatase 2C isoform alpha,Protein phosphatase IA,Rat,Rattus norvegicus
CSB-EL018491HU Human protein phosphatase 1D magnesium-dependent, delta isoform (PPM1D) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL018491MO Mouse protein phosphatase 1D magnesium-dependent, delta isoform (PPM1D) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
EIAAB32082 Kiaa4175,Mouse,Mus musculus,PP2C-epsilon,Ppm1l,Protein phosphatase 1L,Protein phosphatase 1-like,Protein phosphatase 2C isoform epsilon
EIAAB32053 Mouse,Mus musculus,PP2C-alpha,Ppm1a,Pppm1a,Protein phosphatase 1A,Protein phosphatase 2C isoform alpha,Protein phosphatase IA
EIAAB32083 Bos taurus,Bovine,PP2CE,PP2C-epsilon,PPM1L,Protein phosphatase 1L,Protein phosphatase 1-like,Protein phosphatase 2C isoform epsilon
EIAAB32084 Homo sapiens,Human,PP2CE,PP2C-eta,PPM1E,PPM1M,Protein phosphatase 1M,Protein phosphatase 2C isoform eta
EIAAB32085 Mouse,Mus musculus,PP2CE,PP2C-eta,Ppm1e,Ppm1m,Protein phosphatase 1M,Protein phosphatase 2C isoform eta
EIAAB38502 Homo sapiens,Human,Protein tyrosine phosphatase non-receptor type substrate 1-like 2,PTPNS1L2,Signal-regulatory protein delta,SIRPD,SIRP-delta
EIAAB32057 Pp2c2,PP2C-beta,Ppm1b,Pppm1b,Protein phosphatase 1B,Protein phosphatase 2C isoform beta,Rat,Rattus norvegicus
EIAAB32076 Homo sapiens,Human,PP2C-zeta,PPM1J,PPP2CZ,Protein phosphatase 1J,Protein phosphatase 2C isoform zeta
EIAAB32058 Mouse,Mus musculus,Pp2c2,PP2C-beta,Ppm1b,Pppm1b,Protein phosphatase 1B,Protein phosphatase 2C isoform beta
EIAAB32060 Homo sapiens,Human,PP2CB,PP2C-beta,PPM1B,Protein phosphatase 1B,Protein phosphatase 2C isoform beta


 

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