Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Serine/threonine-protein phosphatase 1 regulatory subunit 10 (MHC class I region proline-rich protein CAT53) (PP1-binding protein of 114 kDa) (Phosphatase 1 nuclear targeting subunit) (Protein FB19) (p99)

 PP1RA_HUMAN             Reviewed;         940 AA.
Q96QC0; O00405;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
22-NOV-2017, entry version 148.
RecName: Full=Serine/threonine-protein phosphatase 1 regulatory subunit 10;
AltName: Full=MHC class I region proline-rich protein CAT53;
AltName: Full=PP1-binding protein of 114 kDa;
AltName: Full=Phosphatase 1 nuclear targeting subunit;
AltName: Full=Protein FB19;
AltName: Full=p99;
Name=PPP1R10; Synonyms=CAT53, FB19, PNUTS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=9784381; DOI=10.1006/bbrc.1998.9354;
Totaro A., Grifa A., Carella M., Rommens J.M., Valentino M.A.,
Roetto A., Zelante L., Gasparini P.;
"Cloning of a new gene (FB19) within HLA class I region.";
Biochem. Biophys. Res. Commun. 250:555-557(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Raha-Chowdhury R., Andrews S.R., Gruen J.R.;
"CAT53: a protein phosphatase 1 nuclear targeting subunit encoded in
MHC class 1 may take part in memory and learning.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Shiina S., Tamiya G., Oka A., Inoko H.;
"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Shiina T., Ota M., Katsuyama Y., Hashimoto N., Inoko H.;
"Genome diversity in HLA: a new strategy for detection of genetic
polymorphisms in expressed genes within the HLA class III and class I
regions.";
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
PROTEIN SEQUENCE OF 164-173; 261-270; 410-413; 437-444 AND 483-488,
FUNCTION IN PPP1CA AND PPP1CC INHIBITION, INTERACTION WITH PPP1CC,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Cervix carcinoma;
PubMed=9450550; DOI=10.1016/S0014-5793(97)01485-3;
Kreivi J.P., Trinkle-Mulcahy L., Lyon C.E., Morrice N.A., Cohen P.,
Lamond A.I.;
"Purification and characterisation of p99, a nuclear modulator of
protein phosphatase 1 activity.";
FEBS Lett. 420:57-62(1997).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-256, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313 AND SER-591, 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).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-256; SER-313 AND
SER-591, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-256; SER-313 AND
SER-398, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313; SER-382; SER-545
AND SER-591, 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).
[17]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-665 AND ARG-693, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[18]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-179 AND LYS-262, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Scaffold protein which mediates the formation of the
PTW/PP1 phosphatase complex by providing a binding platform to
each component of the complex. The PTW/PP1 phosphatase complex
plays a role in the control of chromatin structure and cell cycle
progression during the transition from mitosis into interphase.
Mediates interaction of WDR82 and PPP1CA. Inhibitor of PPP1CA and
PPP1CC phosphatase activities. Has inhibitory activity on PPP1CA
only when phosphorylated. Binds to mRNA, single-stranded DNA
(ssDNA), poly(A) and poly(G) homopolymers (By similarity).
{ECO:0000250, ECO:0000269|PubMed:9450550}.
-!- SUBUNIT: Component of the PTW/PP1 phosphatase complex, composed of
PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC.
Interacts with PPP1CC. Interacts with PPP1CA, WDR82 and TOX4 (By
similarity). {ECO:0000250}.
-!- INTERACTION:
P62136:PPP1CA; NbExp=3; IntAct=EBI-1210346, EBI-357253;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00649, ECO:0000269|PubMed:9450550}. Note=Found in
discrete nucleoplasmic bodies and within nucleoli. Associates with
chromatin during interphase, excluded from condensed chromosomes
during early mitosis and is reloaded onto chromosomes at the late
telophase (By similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung,
liver, skeletal muscle, kidney and pancreas.
{ECO:0000269|PubMed:9450550, ECO:0000269|PubMed:9784381}.
-!- PTM: Phosphorylated on Ser-398 by PKA within the region necessary
for interaction with PPP1CA. {ECO:0000250}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Y13247; CAA73697.1; -; mRNA.
EMBL; AJ544537; CAD67521.1; -; mRNA.
EMBL; BA000025; BAB63324.1; -; Genomic_DNA.
EMBL; AB088097; BAC54929.1; -; Genomic_DNA.
EMBL; AL662800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL662825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX248507; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS4681.1; -.
PIR; JE0291; JE0291.
RefSeq; NP_002705.2; NM_002714.3.
RefSeq; XP_006715193.1; XM_006715130.2.
RefSeq; XP_011513024.1; XM_011514722.1.
RefSeq; XP_016866484.1; XM_017010995.1.
UniGene; Hs.106019; -.
ProteinModelPortal; Q96QC0; -.
SMR; Q96QC0; -.
BioGrid; 111506; 47.
CORUM; Q96QC0; -.
DIP; DIP-39343N; -.
ELM; Q96QC0; -.
IntAct; Q96QC0; 20.
MINT; MINT-1197376; -.
STRING; 9606.ENSP00000365694; -.
iPTMnet; Q96QC0; -.
PhosphoSitePlus; Q96QC0; -.
BioMuta; PPP1R10; -.
DMDM; 61214507; -.
EPD; Q96QC0; -.
MaxQB; Q96QC0; -.
PaxDb; Q96QC0; -.
PeptideAtlas; Q96QC0; -.
PRIDE; Q96QC0; -.
TopDownProteomics; Q96QC0; -.
Ensembl; ENST00000376511; ENSP00000365694; ENSG00000204569.
Ensembl; ENST00000383586; ENSP00000373080; ENSG00000206489.
Ensembl; ENST00000420949; ENSP00000413554; ENSG00000230995.
Ensembl; ENST00000424446; ENSP00000407181; ENSG00000231737.
Ensembl; ENST00000426299; ENSP00000389299; ENSG00000235291.
Ensembl; ENST00000429597; ENSP00000407310; ENSG00000238104.
Ensembl; ENST00000449113; ENSP00000416060; ENSG00000227804.
GeneID; 5514; -.
KEGG; hsa:5514; -.
UCSC; uc003nqn.3; human.
CTD; 5514; -.
DisGeNET; 5514; -.
EuPathDB; HostDB:ENSG00000204569.9; -.
GeneCards; PPP1R10; -.
H-InvDB; HIX0165052; -.
H-InvDB; HIX0166290; -.
H-InvDB; HIX0166579; -.
H-InvDB; HIX0166833; -.
H-InvDB; HIX0167082; -.
H-InvDB; HIX0167322; -.
H-InvDB; HIX0167569; -.
HGNC; HGNC:9284; PPP1R10.
HPA; CAB025501; -.
HPA; HPA047248; -.
HPA; HPA056756; -.
MIM; 603771; gene.
neXtProt; NX_Q96QC0; -.
OpenTargets; ENSG00000204569; -.
PharmGKB; PA33612; -.
eggNOG; ENOG410IGTC; Eukaryota.
eggNOG; ENOG410XP4M; LUCA.
GeneTree; ENSGT00530000063820; -.
HOGENOM; HOG000049285; -.
HOVERGEN; HBG053646; -.
InParanoid; Q96QC0; -.
KO; K17552; -.
OMA; TVTWPEE; -.
OrthoDB; EOG091G07K1; -.
PhylomeDB; Q96QC0; -.
TreeFam; TF105541; -.
ChiTaRS; PPP1R10; human.
GeneWiki; PPP1R10; -.
GenomeRNAi; 5514; -.
PRO; PR:Q96QC0; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000204569; -.
CleanEx; HS_PPP1R10; -.
ExpressionAtlas; Q96QC0; baseline and differential.
Genevisible; Q96QC0; HS.
GO; GO:0000785; C:chromatin; ISS:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0006606; P:protein import into nucleus; TAS:ProtInc.
Gene3D; 1.20.930.10; -; 1.
Gene3D; 4.10.1000.10; -; 1.
InterPro; IPR003617; TFIIS/CRSP70_N_sub.
InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
InterPro; IPR017923; TFIIS_N.
InterPro; IPR000571; Znf_CCCH.
InterPro; IPR036855; Znf_CCCH_sf.
Pfam; PF08711; Med26; 1.
Pfam; PF00642; zf-CCCH; 1.
SMART; SM00509; TFS2N; 1.
SMART; SM00356; ZnF_C3H1; 1.
SUPFAM; SSF47676; SSF47676; 1.
SUPFAM; SSF90229; SSF90229; 1.
PROSITE; PS51319; TFIIS_N; 1.
PROSITE; PS50103; ZF_C3H1; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; DNA-binding;
Isopeptide bond; Metal-binding; Methylation; Nucleus; Phosphoprotein;
Polymorphism; Protein phosphatase inhibitor; Reference proteome;
RNA-binding; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 940 Serine/threonine-protein phosphatase 1
regulatory subunit 10.
/FTId=PRO_0000071510.
DOMAIN 73 147 TFIIS N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00649}.
ZN_FING 906 934 C3H1-type. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
REGION 1 348 Interaction with TOX4. {ECO:0000250}.
REGION 382 450 Essential for PPP1CA inhibition.
{ECO:0000250}.
REGION 388 417 Necessary for interaction with PPP1CA.
{ECO:0000250}.
REGION 393 408 Necessary for interaction with PPP1CC.
{ECO:0000269|PubMed:9450550}.
REGION 418 619 Interaction with WDR82. {ECO:0000250}.
MOTIF 420 423 PP1-binding motif.
COMPBIAS 304 310 Poly-Lys.
COMPBIAS 540 904 Gly-rich.
MOD_RES 256 256 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 313 313 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 382 382 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 398 398 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 545 545 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 591 591 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 665 665 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 693 693 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 738 738 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q80W00}.
CROSSLNK 179 179 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 262 262 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 173 173 R -> P (in dbSNP:rs16897725).
/FTId=VAR_051747.
CONFLICT 225 225 K -> E (in Ref. 1; CAA73697).
{ECO:0000305}.
CONFLICT 861 861 P -> L (in Ref. 1; CAA73697).
{ECO:0000305}.
CONFLICT 875 875 P -> Q (in Ref. 1; CAA73697).
{ECO:0000305}.
SEQUENCE 940 AA; 99058 MW; 49EE42961D734121 CRC64;
MGSGPIDPKE LLKGLDSFLN RDGEVKSVDG ISKIFSLMKE ARKMVSRCTY LNILLQTRSP
EILVKFIDVG GYKLLNNWLT YSKTTNNIPL LQQILLTLQH LPLTVDHLKQ NNTAKLVKQL
SKSSEDEELR KLASVLVSDW MAVIRSQSST QPAEKDKKKR KDEGKSRTTL PERPLTEVKA
ETRAEEAPEK KREKPKSLRT TAPSHAKFRS TGLELETPSL VPVKKNASTV VVSDKYNLKP
IPLKRQSNVA APGDATPPAE KKYKPLNTTP NATKEIKVKI IPPQPMEGLG FLDALNSAPV
PGIKIKKKKK VLSPTAAKPS PFEGKTSTEP STAKPSSPEP APPSEAMDAD RPGTPVPPVE
VPELMDTASL EPGALDAKPV ESPGDPNQLT RKGRKRKSVT WPEEGKLREY FYFELDETER
VNVNKIKDFG EAAKREILSD RHAFETARRL SHDNMEEKVP WVCPRPLVLP SPLVTPGSNS
QERYIQAERE KGILQELFLN KESPHEPDPE PYEPIPPKLI PLDEECSMDE TPYVETLEPG
GSGGSPDGAG GSKLPPVLAN LMGSMGAGKG PQGPGGGGIN VQEILTSIMG SPNSHPSEEL
LKQPDYSDKI KQMLVPHGLL GPGPIANGFP PGGPGGPKGM QHFPPGPGGP MPGPHGGPGG
PVGPRLLGPP PPPRGGDPFW DGPGDPMRGG PMRGGPGPGP GPYHRGRGGR GGNEPPPPPP
PFRGARGGRS GGGPPNGRGG PGGGMVGGGG HRPHEGPGGG MGNSSGHRPH EGPGGGMGSG
HRPHEGPGGS MGGGGGHRPH EGPGGGISGG SGHRPHEGPG GGMGAGGGHR PHEGPGGSMG
GSGGHRPHEG PGHGGPHGHR PHDVPGHRGH DHRGPPPHEH RGHDGPGHGG GGHRGHDGGH
SHGGDMSNRP VCRHFMMKGN CRYENNCAFY HPGVNGPPLP


Related products :

Catalog number Product name Quantity
EIAAB31901 CAT53,FB19,Homo sapiens,Human,MHC class I region proline-rich protein CAT53,p99,Phosphatase 1 nuclear targeting subunit,PNUTS,PP1-binding protein of 114 kDa,PPP1R10,Protein FB19,Serine_threonine-prote
EIAAB31902 CAT53,FB19,MHC class I region proline-rich protein CAT53,Pig,PPP1R10,Protein FB19,Serine_threonine-protein phosphatase 1 regulatory subunit 10,Sus scrofa
EIAAB31899 Cat53,MHC class I region proline-rich protein CAT53,Phosphatase 1 nuclear targeting subunit,Pnuts,Ppp1r10,Protein PNUTS,Rat,Rattus norvegicus,Serine_threonine-protein phosphatase 1 regulatory subunit
EIAAB31900 Cat53,MHC class I region proline-rich protein CAT53,Mouse,Mus musculus,Pnuts,Ppp1r10,Serine_threonine-protein phosphatase 1 regulatory subunit 10
EIAAB32117 Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL,Homo sapiens,Human,PP1 subunit R4,PPP1R3B,PPP1R4,Protein phosphatase 1 regulatory subunit 3B,Protein phosphatase 1 regulatory sub
EIAAB32116 Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL,Mouse,Mus musculus,PP1 subunit R4,Ppp1r3b,Ppp1r4,Protein phosphatase 1 regulatory subunit 3B,Protein phosphatase 1 regulatory sub
EIAAB26151 Homo sapiens,Human,MBS,Myosin phosphatase target subunit 1,Myosin phosphatase-targeting subunit 1,MYPT1,PPP1R12A,Protein phosphatase 1 regulatory subunit 12A,Protein phosphatase myosin-binding subunit
EIAAB26152 Mbs,MBSP,Myosin phosphatase target subunit 1,Myosin phosphatase-targeting subunit 1,Mypt1,PP-1M,Ppp1r12a,Protein phosphatase 1 regulatory subunit 12A,Protein phosphatase myosin-binding subunit,Protein
EIAAB32114 33 kDa glycogen-binding protein,Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL,PP1 subunit R4,Ppp1r3b,Ppp1r4,Protein phosphatase 1 regulatory subunit 3B,Protein phosphatase 1 r
EIAAB32120 Homo sapiens,Human,PP1 subunit R5,PPP1R3C,PPP1R5,Protein phosphatase 1 regulatory subunit 3C,Protein phosphatase 1 regulatory subunit 5,Protein targeting to glycogen,PTG
EIAAB32112 Oryctolagus cuniculus,PP1G,PPP1R3A,Protein phosphatase 1 glycogen-associated regulatory subunit,Protein phosphatase 1 regulatory subunit 3A,Protein phosphatase type-1 glycogen targeting subunit,Rabbit
EIAAB32113 Homo sapiens,Human,PP1G,PPP1R3A,Protein phosphatase 1 glycogen-associated regulatory subunit,Protein phosphatase 1 regulatory subunit 3A,Protein phosphatase type-1 glycogen targeting subunit,RG1
EIAAB32121 Mouse,Mus musculus,PP1 subunit R5,Ppp1r3c,Ppp1r5,Protein phosphatase 1 regulatory subunit 3C,Protein phosphatase 1 regulatory subunit 5,Protein targeting to glycogen,PTG
EIAAB32118 PP1 subunit R5,Ppp1r3c,Ppp1r5,Protein phosphatase 1 regulatory subunit 3C,Protein phosphatase 1 regulatory subunit 5,Protein targeting to glycogen,PTG,Rat,Rattus norvegicus
EIAAB32119 Bos taurus,Bovine,PP1 subunit R5,PPP1R3C,PPP1R5,Protein phosphatase 1 regulatory subunit 3C,Protein phosphatase 1 regulatory subunit 5,Protein targeting to glycogen,PTG
EIAAB32111 Mouse,Mus musculus,Pp1g,Ppp1r3a,Protein phosphatase 1 glycogen-associated regulatory subunit,Protein phosphatase 1 regulatory subunit 3A,Protein phosphatase type-1 glycogen targeting subunit,RG1
EIAAB32122 Homo sapiens,Human,PP1 subunit R6,PPP1R3D,PPP1R6,Protein phosphatase 1 regulatory subunit 3D,Protein phosphatase 1 regulatory subunit 6,Protein phosphatase 1-binding subunit R6
EIAAB31850 Homo sapiens,Human,LENG3,MBS85,PPP1R12C,Protein phosphatase 1 myosin-binding subunit of 85 kDa,Protein phosphatase 1 myosin-binding subunit p85,Protein phosphatase 1 regulatory subunit 12C
EIAAB26156 Homo sapiens,Human,Myosin phosphatase target subunit 2,Myosin phosphatase-targeting subunit 2,MYPT2,PPP1R12B,Protein phosphatase 1 regulatory subunit 12B
EIAAB26154 Mouse,Mus musculus,Myosin phosphatase target subunit 1,Myosin phosphatase-targeting subunit 1,Mypt1,Ppp1r12a,Protein phosphatase 1 regulatory subunit 12A
EIAAB26155 Mouse,Mus musculus,Myosin phosphatase target subunit 2,Myosin phosphatase-targeting subunit 2,Mypt2,Ppp1r12b,Protein phosphatase 1 regulatory subunit 12B
E15032b Human ELISA Kit FOR Serine per threonine-protein phosphatase 2A regulatory subunit B'' subunit beta 96T
P2R3C_MOUSE Mouse ELISA Kit FOR Serine per threonine-protein phosphatase 2A regulatory subunit B'' subunit gamma 96T
EIAAB31851 Mbs85,Mouse,Mus musculus,Ppp1r12c,Protein phosphatase 1 myosin-binding subunit of 85 kDa,Protein phosphatase 1 myosin-binding subunit p85,Protein phosphatase 1 regulatory subunit 12C
P2R3C_RAT ELISA Kit FOR Serine per threonine-protein phosphatase 2A regulatory subunit B'' subunit gamma; organism: Rat; gene name: Ppp2r3c 96T


 

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