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Serine/threonine-protein phosphatase 6 regulatory subunit 2 (SAPS domain family member 2)

 PP6R2_HUMAN             Reviewed;         966 AA.
O75170; A6PVG3; B7Z7T3; Q5U5P3; Q7Z2L2; Q7Z5G5; Q7Z731; Q9UGB9;
25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
15-JAN-2008, sequence version 2.
07-APR-2021, entry version 167.
RecName: Full=Serine/threonine-protein phosphatase 6 regulatory subunit 2;
AltName: Full=SAPS domain family member 2;
Name=PPP6R2; Synonyms=KIAA0685, PP6R2, SAPS2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=9734811; DOI=10.1093/dnares/5.3.169;
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. X. The
complete sequences of 100 new cDNA clones from brain which can code for
large proteins in vitro.";
DNA Res. 5:169-176(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Testis;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 6).
TISSUE=Brain, Lymph, Muscle, Placenta, 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).
[5]
FUNCTION, INTERACTION WITH PPP6C AND NFKBIE, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=16769727; DOI=10.1074/jbc.m601772200;
Stefansson B., Brautigan D.L.;
"Protein phosphatase 6 subunit with conserved Sit4-associated protein
domain targets IkappaBepsilon.";
J. Biol. Chem. 281:22624-22634(2006).
[6]
INTERACTION WITH PPP6C AND ANKRD28.
PubMed=18186651; DOI=10.1021/bi7022877;
Stefansson B., Ohama T., Daugherty A.E., Brautigan D.L.;
"Protein phosphatase 6 regulatory subunits composed of ankyrin repeat
domains.";
Biochemistry 47:1442-1451(2008).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the
kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, 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).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, 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).
[11]
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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289 AND SER-828, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, 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).
-!- FUNCTION: Regulatory subunit of protein phosphatase 6 (PP6). May
function as a scaffolding PP6 subunit. Involved in the PP6-mediated
dephosphorylation of NFKBIE opposing its degradation in response to
TNF-alpha. {ECO:0000269|PubMed:16769727}.
-!- SUBUNIT: Protein phosphatase 6 (PP6) holoenzyme is proposed to be a
heterotrimeric complex formed by the catalytic subunit, a SAPS domain-
containing subunit (PP6R) and an ankyrin repeat-domain containing
regulatory subunit (ARS). Interacts with PPP6C and NFKBIE. Interacts
with ANKRD28. {ECO:0000269|PubMed:16769727,
ECO:0000269|PubMed:18186651}.
-!- INTERACTION:
O75170; O15084: ANKRD28; NbExp=7; IntAct=EBI-359739, EBI-359567;
O75170; O00221: NFKBIE; NbExp=2; IntAct=EBI-359739, EBI-355098;
O75170; O00743: PPP6C; NbExp=9; IntAct=EBI-359739, EBI-359751;
O75170-4; P42858: HTT; NbExp=3; IntAct=EBI-11079164, EBI-466029;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16769727}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=O75170-1; Sequence=Displayed;
Name=2;
IsoId=O75170-2; Sequence=VSP_030758, VSP_030759, VSP_030760,
VSP_030761;
Name=3;
IsoId=O75170-3; Sequence=VSP_037768, VSP_030758, VSP_030760;
Name=4;
IsoId=O75170-4; Sequence=VSP_030758, VSP_030760;
Name=5;
IsoId=O75170-5; Sequence=VSP_030760;
Name=6;
IsoId=O75170-6; Sequence=VSP_037767, VSP_030758, VSP_030760;
-!- TISSUE SPECIFICITY: Ubiquitously expressed with strongest expression in
the testis followed by liver, heart, kidney, brain and placenta.
{ECO:0000269|PubMed:16769727}.
-!- SIMILARITY: Belongs to the SAPS family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA31660.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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EMBL; AB014585; BAA31660.2; ALT_INIT; mRNA.
EMBL; AK302472; BAH13719.1; -; mRNA.
EMBL; AL096767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL671545; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL954743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000976; AAH00976.2; -; mRNA.
EMBL; BC006568; AAH06568.1; -; mRNA.
EMBL; BC032664; AAH32664.1; -; mRNA.
EMBL; BC041698; AAH41698.1; -; mRNA.
EMBL; BC052995; AAH52995.1; -; mRNA.
CCDS; CCDS33681.1; -. [O75170-4]
CCDS; CCDS56235.1; -. [O75170-3]
CCDS; CCDS56236.1; -. [O75170-2]
CCDS; CCDS74881.1; -. [O75170-5]
PIR; T00357; T00357.
RefSeq; NP_001229827.1; NM_001242898.1. [O75170-5]
RefSeq; NP_001229828.1; NM_001242899.1. [O75170-3]
RefSeq; NP_001229829.1; NM_001242900.1. [O75170-2]
RefSeq; NP_055493.2; NM_014678.4. [O75170-4]
RefSeq; XP_006724497.1; XM_006724434.1.
RefSeq; XP_016884612.1; XM_017029123.1. [O75170-1]
RefSeq; XP_016884613.1; XM_017029124.1. [O75170-1]
RefSeq; XP_016884617.1; XM_017029128.1.
RefSeq; XP_016884620.1; XM_017029131.1.
RefSeq; XP_016884621.1; XM_017029132.1. [O75170-4]
BioGRID; 115053; 82.
CORUM; O75170; -.
DIP; DIP-27539N; -.
IntAct; O75170; 61.
MINT; O75170; -.
STRING; 9606.ENSP00000478417; -.
ChEMBL; CHEMBL4105960; -.
GlyGen; O75170; 1 site, 1 O-linked glycan (1 site).
iPTMnet; O75170; -.
PhosphoSitePlus; O75170; -.
BioMuta; PPP6R2; -.
EPD; O75170; -.
jPOST; O75170; -.
MassIVE; O75170; -.
MaxQB; O75170; -.
PaxDb; O75170; -.
PeptideAtlas; O75170; -.
PRIDE; O75170; -.
ProteomicsDB; 49835; -. [O75170-1]
ProteomicsDB; 49836; -. [O75170-2]
ProteomicsDB; 49837; -. [O75170-3]
ProteomicsDB; 49838; -. [O75170-4]
ProteomicsDB; 49839; -. [O75170-5]
ProteomicsDB; 49840; -. [O75170-6]
Antibodypedia; 28539; 74 antibodies.
Ensembl; ENST00000216061; ENSP00000216061; ENSG00000100239. [O75170-1]
Ensembl; ENST00000359139; ENSP00000352051; ENSG00000100239. [O75170-2]
Ensembl; ENST00000395741; ENSP00000379090; ENSG00000100239. [O75170-3]
Ensembl; ENST00000395744; ENSP00000379093; ENSG00000100239. [O75170-4]
Ensembl; ENST00000612753; ENSP00000478417; ENSG00000100239. [O75170-5]
GeneID; 9701; -.
KEGG; hsa:9701; -.
UCSC; uc003bky.3; human. [O75170-1]
CTD; 9701; -.
DisGeNET; 9701; -.
GeneCards; PPP6R2; -.
HGNC; HGNC:19253; PPP6R2.
HPA; ENSG00000100239; Low tissue specificity.
MIM; 610877; gene.
neXtProt; NX_O75170; -.
OpenTargets; ENSG00000100239; -.
PharmGKB; PA165378360; -.
VEuPathDB; HostDB:ENSG00000100239.15; -.
eggNOG; KOG2073; Eukaryota.
GeneTree; ENSGT00390000009899; -.
HOGENOM; CLU_012598_0_0_1; -.
InParanoid; O75170; -.
OMA; FEACCGD; -.
PhylomeDB; O75170; -.
TreeFam; TF313227; -.
PathwayCommons; O75170; -.
BioGRID-ORCS; 9701; 8 hits in 992 CRISPR screens.
ChiTaRS; PPP6R2; human.
GenomeRNAi; 9701; -.
Pharos; O75170; Tdark.
PRO; PR:O75170; -.
Proteomes; UP000005640; Chromosome 22.
RNAct; O75170; protein.
Bgee; ENSG00000100239; Expressed in right hemisphere of cerebellum and 227 other tissues.
ExpressionAtlas; O75170; baseline and differential.
Genevisible; O75170; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0019903; F:protein phosphatase binding; IEA:InterPro.
GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IBA:GO_Central.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR007587; SAPS.
PANTHER; PTHR12634; PTHR12634; 1.
Pfam; PF04499; SAPS; 2.
SUPFAM; SSF48371; SSF48371; 1.
1: Evidence at protein level;
Alternative splicing; Cytoplasm; Phosphoprotein; Reference proteome.
CHAIN 1..966
/note="Serine/threonine-protein phosphatase 6 regulatory
subunit 2"
/id="PRO_0000046098"
COMPBIAS 820..825
/note="Poly-Ser"
MOD_RES 289
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
ECO:0007744|PubMed:24275569"
MOD_RES 771
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q8R3Q2"
MOD_RES 828
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
VAR_SEQ 58..84
/note="Missing (in isoform 6)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_037767"
VAR_SEQ 244
/note="S -> SR (in isoform 3)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_037768"
VAR_SEQ 535..561
/note="Missing (in isoform 2, isoform 3, isoform 4 and
isoform 6)"
/evidence="ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9734811"
/id="VSP_030758"
VAR_SEQ 709
/note="E -> EA (in isoform 2)"
/evidence="ECO:0000303|PubMed:9734811"
/id="VSP_030759"
VAR_SEQ 792..799
/note="SQASYFAV -> F (in isoform 2, isoform 3, isoform 4,
isoform 5 and isoform 6)"
/evidence="ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9734811"
/id="VSP_030760"
VAR_SEQ 952..966
/note="KTDAPPEGAALNGPV -> QMPRQKELP (in isoform 2)"
/evidence="ECO:0000303|PubMed:9734811"
/id="VSP_030761"
VARIANT 633
/note="D -> E (in dbSNP:rs11555194)"
/id="VAR_058402"
VARIANT 732
/note="R -> K (in dbSNP:rs13057311)"
/id="VAR_058403"
CONFLICT 224
/note="D -> G (in Ref. 2; BAH13719)"
/evidence="ECO:0000305"
CONFLICT 806
/note="A -> T (in Ref. 2; BAH13719)"
/evidence="ECO:0000305"
CONFLICT 835
/note="Q -> H (in Ref. 4; AAH52995)"
/evidence="ECO:0000305"
SEQUENCE 966 AA; 104942 MW; D3BC10EADB98FB62 CRC64;
MFWKFDLNTT SHVDKLLDKE HVTLQELMDE DDILQECKAQ NQKLLDFLCR QQCMEELVSL
ITQDPPLDME EKVRFKYPNT ACELLTCDVP QISDRLGGDE SLLSLLYDFL DHEPPLNPLL
ASFFSKTIGN LIARKTEQVI TFLKKKDKFI SLVLKHIGTS ALMDLLLRLV SCVEPAGLRQ
DVLHWLNEEK VIQRLVELIH PSQDEDRQSN ASQTLCDIVR LGRDQGSQLQ EALEPDPLLT
ALESQDCVEQ LLKNMFDGDR TESCLVSGTQ VLLTLLETRR VGTEGLVDSF SQGLERSYAV
SSSVLHGIEP RLKDFHQLLL NPPKKKAILT TIGVLEEPLG NARLHGARLM AALLHTNTPS
INQELCRLNT MDLLLDLFFK YTWNNFLHFQ VELCIAAILS HAAREERTEA SGSESRVEPP
HENGNRSLET PQPAASLPDN TMVTHLFQKC CLVQRILEAW EANDHTQAAG GMRRGNMGHL
TRIANAVVQN LERGPVQTHI SEVIRGLPAD CRGRWESFVE ETLTETNRRN TVDLVSTHHL
HSSSEDEDIE GAFPNELSLQ QAFSDYQIQQ MTANFVDQFG FNDEEFADQD DNINAPFDRI
AEINFNIDAD EDSPSAALFE ACCSDRIQPF DDDEDEDIWE DSDTRCAARV MARPRFGAPH
ASESCSKNGP ERGGQDGKAS LEAHRDAPGA GAPPAPGKKE APPVEGDSEG AMWTAVFDEP
ANSTPTAPGV VRDVGSSVWA AGTSAPEEKG WAKFTDFQPF CCSESGPRCS SPVDTECSHA
EGSRSQGPEK ASQASYFAVS PASPCAWNVC VTRKAPLLAS DSSSSGGSHS EDGDQKAASA
MDAVSRGPGR EAPPLPTVAR TEEAVGRVGC ADSRLLSPAC PAPKEVTAAP AVAVPPEATV
AITTALSKAG PAIPTPAVSS ALAVAVPLGP IMAVTAAPAM VATLGTVTKD GKTDAPPEGA
ALNGPV


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Catalog number Product name Quantity
EIAAB31948 Kiaa0685,Mouse,Mus musculus,Pp6r2,Ppp6r2,SAPS domain family member 2,Saps2,Serine_threonine-protein phosphatase 6 regulatory subunit 2
EIAAB31946 Kiaa1115,Mouse,Mus musculus,Pp6r1,Ppp6r1,SAPS domain family member 1,Saps1,Serine_threonine-protein phosphatase 6 regulatory subunit 1
EIAAB31949 D19Ertd703e,Kiaa1558,Mouse,Mus musculus,Pp6r3,Ppp6r3,SAPS domain family member 3,Saps3,Serine_threonine-protein phosphatase 6 regulatory subunit 3
EIAAB31947 Homo sapiens,Human,KIAA0685,PP6R2,PPP6R2,SAPS domain family member 2,SAPS2,Serine_threonine-protein phosphatase 6 regulatory subunit 2
EIAAB31945 Homo sapiens,Human,KIAA1115,PP6R1,PPP6R1,SAPS domain family member 1,SAPS1,Serine_threonine-protein phosphatase 6 regulatory subunit 1
EIAAB31951 Chicken,Gallus gallus,PP6R3,PPP6R3,RCJMB04_2j4,SAPS domain family member 3,SAPS3,Serine_threonine-protein phosphatase 6 regulatory subunit 3
EIAAB31950 C11orf23,Homo sapiens,Human,KIAA1558,PP6R3,PPP6R3,SAPL,SAPS domain family member 3,SAPS3,Serine_threonine-protein phosphatase 6 regulatory subunit 3,Sporulation-induced transcript 4-associated protein
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
P2R3C_RAT ELISA Kit FOR Serine per threonine-protein phosphatase 2A regulatory subunit B'' subunit gamma; organism: Rat; gene name: Ppp2r3c 96T
P2R3A_MOUSE ELISA Kit FOR Serine per threonine-protein phosphatase 2A regulatory subunit B'' subunit alpha; organism: Mouse; gene name: Ppp2r3a 96T
P2R3C_MOUSE ELISA Kit FOR Serine per threonine-protein phosphatase 2A regulatory subunit B'' subunit gamma; organism: Mouse; gene name: Ppp2r3c 96T
H0412 Serine threonine-protein phosphatase 1 regulatory subunit 10 (PPP1R10), Rat, ELISA Kit 96T
UBIA1_RAT Human ELISA Kit FOR Serine per threonine-protein phosphatase 4 regulatory subunit 2 96T
H0459 Serine threonine-protein phosphatase 4 regulatory subunit 1 (PPP4R1), Rat, ELISA Kit 96T
DIDO1_MOUSE Human ELISA Kit FOR Serine per threonine-protein phosphatase 4 regulatory subunit 2 96T
E0797r Human ELISA Kit FOR Serine per threonine-protein phosphatase 4 regulatory subunit 3A 96T
PP4R2_MOUSE Mouse ELISA Kit FOR Serine per threonine-protein phosphatase 4 regulatory subunit 2 96T
E1549r Mouse ELISA Kit FOR Serine per threonine-protein phosphatase 4 regulatory subunit 3A 96T
E0072h Human ELISA Kit FOR Serine per threonine-protein phosphatase 4 regulatory subunit 2 96T
E0791c Human ELISA Kit FOR Serine per threonine-protein phosphatase 4 regulatory subunit 3B 96T
P4R3B_MOUSE Mouse ELISA Kit FOR Serine per threonine-protein phosphatase 4 regulatory subunit 3B 96T
H0411 Serine threonine-protein phosphatase 1 regulatory subunit 10 (PPP1R10), Pig, ELISA Kit 96T
E0822c Mouse ELISA Kit FOR Serine per threonine-protein phosphatase 6 regulatory subunit 3 96T
E1679p Human ELISA Kit FOR Serine per threonine-protein phosphatase 1 regulatory subunit 10 96T
Pathways :
WP1659: Glycine, serine and threonine metabolism
WP1909: Signal regulatory protein (SIRP) family interactions
WP2292: Chemokine signaling pathway
WP1644: DNA replication
WP731: Sterol regulatory element binding protein related
WP1654: gamma-Hexachlorocyclohexane degradation
WP1694: Pyrimidine metabolism
WP2199: Seed Development
WP2272: Pathogenic Escherichia coli infection
WP1689: Porphyrin and chlorophyll metabolism
WP1493: Carbon assimilation C4 pathway
WP1693: Purine metabolism
WP1566: Citrate cycle (TCA cycle)
WP1663: Homologous recombination
WP1672: Mismatch repair
WP2185: Purine metabolism
WP1834: Interactions of the immunoglobulin superfamily (IgSF) member proteins
WP1049: G Protein Signaling Pathways
WP1680: Oxidative phosphorylation
WP931: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1690: Propanoate metabolism
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP1901: Regulatory RNA pathways
WP2353: vitamin B9 (folate) biosynthesis pathway

Related Genes :
[Ppp2r2b] Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform (PP2A subunit B isoform B55-beta) (PP2A subunit B isoform PR55-beta) (PP2A subunit B isoform R2-beta) (PP2A subunit B isoform beta)
[Ptpa Ppp2r4] Serine/threonine-protein phosphatase 2A activator (EC 5.2.1.8) (PP2A, subunit B', PR53 isoform) (Phosphotyrosyl phosphatase activator) (PTPA) (Serine/threonine-protein phosphatase 2A regulatory subunit 4) (Serine/threonine-protein phosphatase 2A regulatory subunit B')
[paa-1 F48E8.5] Probable serine/threonine-protein phosphatase PP2A regulatory subunit (Protein phosphatase PP2A regulatory subunit A)
[RTS1 SCS1 YOR014W OR26.04] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform (PP2A, B subunit, B' delta isoform) (Protein RTS1) (Protein SCS1)
[Ppp2ca] Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (PP2A-alpha) (EC 3.1.3.16)
[rsa-1 C25A1.9] Serine/threonine-protein phosphatase 2A regulatory subunit rsa-1 (Regulator of spindle assembly protein 1) (Serine/threonine-protein phosphatase 2A 72kDa regulatory subunit rsa-1) (Serine/threonine-protein phosphatase 2A regulatory subunit B'' rsa-1)
[Ppp2r1a] Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (PP2A subunit A isoform PR65-alpha) (PP2A subunit A isoform R1-alpha)
[PTPA PPP2R4] Serine/threonine-protein phosphatase 2A activator (EC 5.2.1.8) (PP2A, subunit B', PR53 isoform) (Phosphotyrosyl phosphatase activator) (PTPA) (Serine/threonine-protein phosphatase 2A regulatory subunit 4) (Serine/threonine-protein phosphatase 2A regulatory subunit B')
[Ppp2cb] Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform (PP2A-beta) (EC 3.1.3.16)
[sur-6 F26E4.1] Serine/threonine-protein phosphatase 2A regulatory subunit sur-6 (Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit sur-6) (Serine/threonine-protein phosphatase 2A regulatory subunit B sur-6) (SUR-6/B55) (SUR-6/PR55)
[PP2AA3 DF2 At1g13320 T6J4.8] Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A gamma isoform (AtA gamma) (PP2A, subunit A, gamma isoform)
[Ppp4r3b Kiaa1387 Pp4r3b Smek2] Serine/threonine-protein phosphatase 4 regulatory subunit 3B (SMEK homolog 2)
[PPP2R3A PPP2R3] Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit alpha (PP2A subunit B isoform PR72/PR130) (PP2A subunit B isoform R3 isoform) (PP2A subunit B isoforms B''-PR72/PR130) (PP2A subunit B isoforms B72/B130) (Serine/threonine-protein phosphatase 2A 72/130 kDa regulatory subunit B)
[Ppp2r2b] Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform (PP2A subunit B isoform B55-beta) (PP2A subunit B isoform BRB) (PP2A subunit B isoform PR55-beta) (PP2A subunit B isoform R2-beta) (PP2A subunit B isoform beta)
[PP2AA1 EER1 RCN1 REGA At1g25490 F2J7.19] Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (AtA alpha) (PP2A, subunit A, alpha isoform) (PR-65 A) (Protein ROOTS CURL IN NAPHTHYLPHTHALAMIC ACID 1) (Protein enhancer of ethylene-response 1)
[PPP2R5D] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform (PP2A B subunit isoform B'-delta) (PP2A B subunit isoform B56-delta) (PP2A B subunit isoform PR61-delta) (PP2A B subunit isoform R5-delta)
[PPP2R2A] Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform (PP2A subunit B isoform B55-alpha) (PP2A subunit B isoform PR55-alpha) (PP2A subunit B isoform R2-alpha) (PP2A subunit B isoform alpha)
[PPP2R5C KIAA0044] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform (PP2A B subunit isoform B'-gamma) (PP2A B subunit isoform B56-gamma) (PP2A B subunit isoform PR61-gamma) (PP2A B subunit isoform R5-gamma) (Renal carcinoma antigen NY-REN-29)
[PPP2R2B] Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform (PP2A subunit B isoform B55-beta) (PP2A subunit B isoform PR55-beta) (PP2A subunit B isoform R2-beta) (PP2A subunit B isoform beta)
[PPP2R1A] Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (Medium tumor antigen-associated 61 kDa protein) (PP2A subunit A isoform PR65-alpha) (PP2A subunit A isoform R1-alpha)
[PPP2R1B] Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform (PP2A subunit A isoform PR65-beta) (PP2A subunit A isoform R1-beta)
[ppfr-1 F16A11.3] Serine/threonine-protein phosphatase 4 regulatory subunit 1
[PPP2R5A] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform (PP2A B subunit isoform B'-alpha) (PP2A B subunit isoform B56-alpha) (PP2A B subunit isoform PR61-alpha) (PR61alpha) (PP2A B subunit isoform R5-alpha)
[PPP2R3B PPP2R3L] Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta (PP2A subunit B isoform PR48) (Protein phosphatase 2A 48 kDa regulatory subunit)
[Ppp1ca Ppp1a] Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PP-1A) (EC 3.1.3.16)
[Ppp2r5a] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform (PP2A B subunit isoform B'-alpha) (PP2A B subunit isoform B56-alpha) (PP2A B subunit isoform PR61-alpha) (PR61alpha) (PP2A B subunit isoform R5-alpha)
[Ppp2r3d Ppp2r3a Ppp2r6] Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit delta (PP2A B''-PR59) (PP2A PR59) (Protein phosphatase 2A, 59 kDa regulatory subunit B) (Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit alpha)
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Non-structural protein 2A-alpha (NS2A-alpha); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[PPP2R5B] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform (PP2A B subunit isoform B'-beta) (PP2A B subunit isoform B56-beta) (PP2A B subunit isoform PR61-beta) (PP2A B subunit isoform R5-beta)
[Ppp3ca Calna] Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform (EC 3.1.3.16) (CAM-PRP catalytic subunit) (Calmodulin-dependent calcineurin A subunit alpha isoform) (CNA alpha)

Bibliography :
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