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SH2 domain-containing protein 4A (Protein SH(2)A) (Protein phosphatase 1 regulatory subunit 38)

 SH24A_HUMAN             Reviewed;         454 AA.
Q9H788; B4DDR1; Q5XKC1; Q6NXE9; Q86YM2; Q96C88; Q9H7F7;
02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
10-OCT-2018, entry version 145.
RecName: Full=SH2 domain-containing protein 4A;
AltName: Full=Protein SH(2)A;
AltName: Full=Protein phosphatase 1 regulatory subunit 38;
Name=SH2D4A; Synonyms=PPP1R38, SH2A;
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] (ISOFORMS 1 AND 2), AND
VARIANTS GLY-209; GLY-216 AND ALA-263.
TISSUE=Adipose tissue;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ASN-275.
TISSUE=Ovary, Prostate, and Uterus;
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]
NUCLEOTIDE SEQUENCE [MRNA] OF 172-454 (ISOFORM 1), AND TISSUE
SPECIFICITY.
TISSUE=Liver;
PubMed=12476414;
Dai S., Zhao Y., Ding Q.;
"A novel member of SH(2) signaling protein family: cloning and
characterization of SH(2)A gene.";
Zhonghua Yi Xue Yi Chuan Xue Za Zhi 19:458-462(2002).
[5]
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, 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).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18641339; DOI=10.4049/jimmunol.181.3.2019;
Lapinski P.E., Oliver J.A., Kamen L.A., Hughes E.D., Saunders T.L.,
King P.D.;
"Genetic analysis of SH2D4A, a novel adapter protein related to T
cell-specific adapter and adapter protein in lymphocytes of unknown
function, reveals a redundant function in T cells.";
J. Immunol. 181:2019-2027(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, 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]
FUNCTION, AND INTERACTION WITH ESR1.
PubMed=19712589; DOI=10.5483/BMBRep.2009.42.8.516;
Li T., Li W., Lu J., Liu H., Li Y., Zhao Y.;
"SH2D4A regulates cell proliferation via the ERalpha/PLC-gamma/PKC
pathway.";
BMB Rep. 42:516-522(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261 AND SER-315, 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).
[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-315, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-315, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, 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: Inhibits estrogen-induced cell proliferation by
competing with PLCG for binding to ESR1, blocking the effect of
estrogen on PLCG and repressing estrogen-induced proliferation.
May play a role in T-cell development and function.
{ECO:0000269|PubMed:18641339, ECO:0000269|PubMed:19712589}.
-!- SUBUNIT: Interacts with ESR1. {ECO:0000269|PubMed:19712589}.
-!- INTERACTION:
P13196:ALAS1; NbExp=3; IntAct=EBI-747035, EBI-3905054;
O14936:CASK; NbExp=3; IntAct=EBI-747035, EBI-1215506;
P0C7W6:CCDC172; NbExp=3; IntAct=EBI-747035, EBI-2548868;
Q01850:CDR2; NbExp=5; IntAct=EBI-747035, EBI-1181367;
Q8NHQ1:CEP70; NbExp=3; IntAct=EBI-10308083, EBI-739624;
Q8TAP6:CEP76; NbExp=3; IntAct=EBI-747035, EBI-742887;
Q9UJU6:DBNL; NbExp=6; IntAct=EBI-747035, EBI-751783;
A1L4K1:FSD2; NbExp=5; IntAct=EBI-747035, EBI-5661036;
Q08379:GOLGA2; NbExp=5; IntAct=EBI-747035, EBI-618309;
P62993:GRB2; NbExp=3; IntAct=EBI-747035, EBI-401755;
P14317:HCLS1; NbExp=6; IntAct=EBI-747035, EBI-750369;
Q6NT76:HMBOX1; NbExp=5; IntAct=EBI-747035, EBI-2549423;
Q13422:IKZF1; NbExp=3; IntAct=EBI-747035, EBI-745305;
Q6A162:KRT40; NbExp=5; IntAct=EBI-747035, EBI-10171697;
O95751:LDOC1; NbExp=5; IntAct=EBI-747035, EBI-740738;
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-747035, EBI-741037;
P43364:MAGEA11; NbExp=2; IntAct=EBI-747035, EBI-739552;
P43360:MAGEA6; NbExp=5; IntAct=EBI-747035, EBI-1045155;
Q5JR59:MTUS2; NbExp=3; IntAct=EBI-10308083, EBI-742948;
Q7Z6G3-2:NECAB2; NbExp=5; IntAct=EBI-747035, EBI-10172876;
Q9Y2I6:NINL; NbExp=3; IntAct=EBI-747035, EBI-719716;
Q86Y26:NUTM1; NbExp=3; IntAct=EBI-747035, EBI-10178410;
Q5VU43:PDE4DIP; NbExp=3; IntAct=EBI-747035, EBI-1105124;
Q8ND90:PNMA1; NbExp=5; IntAct=EBI-747035, EBI-302345;
P62136:PPP1CA; NbExp=2; IntAct=EBI-747035, EBI-357253;
P62140:PPP1CB; NbExp=15; IntAct=EBI-747035, EBI-352350;
O43586:PSTPIP1; NbExp=3; IntAct=EBI-747035, EBI-1050964;
Q6NUQ1:RINT1; NbExp=5; IntAct=EBI-747035, EBI-726876;
Q6FGM0:SH3GL1; NbExp=3; IntAct=EBI-747035, EBI-10173690;
Q99961:SH3GL1; NbExp=5; IntAct=EBI-747035, EBI-697911;
Q86WV1:SKAP1; NbExp=3; IntAct=EBI-747035, EBI-2477305;
O94875:SORBS2; NbExp=3; IntAct=EBI-10308083, EBI-311323;
O60504:SORBS3; NbExp=5; IntAct=EBI-747035, EBI-741237;
Q96R06:SPAG5; NbExp=3; IntAct=EBI-747035, EBI-413317;
O75886:STAM2; NbExp=3; IntAct=EBI-10308083, EBI-373258;
O75558:STX11; NbExp=3; IntAct=EBI-747035, EBI-714135;
O75410:TACC1; NbExp=3; IntAct=EBI-747035, EBI-624237;
Q9UBB9:TFIP11; NbExp=5; IntAct=EBI-747035, EBI-1105213;
Q12933:TRAF2; NbExp=5; IntAct=EBI-747035, EBI-355744;
P36406:TRIM23; NbExp=3; IntAct=EBI-747035, EBI-740098;
P14373:TRIM27; NbExp=3; IntAct=EBI-747035, EBI-719493;
Q5T124:UBXN11; NbExp=3; IntAct=EBI-747035, EBI-746004;
Q8N6Y0:USHBP1; NbExp=3; IntAct=EBI-10308083, EBI-739895;
Q8N1B4:VPS52; NbExp=3; IntAct=EBI-747035, EBI-2799833;
Q05516:ZBTB16; NbExp=3; IntAct=EBI-10308083, EBI-711925;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18641339}.
Note=Located at podocyte foot processes. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9H788-1; Sequence=Displayed;
Name=2;
IsoId=Q9H788-2; Sequence=VSP_042784;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Aberrantly expressed
in some cancers. {ECO:0000269|PubMed:12476414}.
-!- SEQUENCE CAUTION:
Sequence=AAH67117.1; Type=Frameshift; Positions=392; Evidence={ECO:0000305};
Sequence=AAO41715.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAO41715.1; Type=Erroneous termination; Positions=455; Note=Translated as stop.; Evidence={ECO:0000305};
Sequence=BAB14935.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AK024620; BAB14935.1; ALT_INIT; mRNA.
EMBL; AK024799; BAB15010.1; -; mRNA.
EMBL; AK293301; BAG56822.1; -; mRNA.
EMBL; AC068880; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC014525; AAH14525.2; -; mRNA.
EMBL; BC067117; AAH67117.1; ALT_FRAME; mRNA.
EMBL; BC082982; AAH82982.1; -; mRNA.
EMBL; AY190323; AAO41715.1; ALT_SEQ; mRNA.
CCDS; CCDS55206.1; -. [Q9H788-2]
CCDS; CCDS6009.1; -. [Q9H788-1]
RefSeq; NP_001167630.1; NM_001174159.1. [Q9H788-1]
RefSeq; NP_001167631.1; NM_001174160.1. [Q9H788-2]
RefSeq; NP_071354.2; NM_022071.3. [Q9H788-1]
UniGene; Hs.303208; -.
ProteinModelPortal; Q9H788; -.
SMR; Q9H788; -.
BioGrid; 121977; 62.
ELM; Q9H788; -.
IntAct; Q9H788; 79.
STRING; 9606.ENSP00000265807; -.
iPTMnet; Q9H788; -.
PhosphoSitePlus; Q9H788; -.
BioMuta; SH2D4A; -.
DMDM; 74725117; -.
EPD; Q9H788; -.
MaxQB; Q9H788; -.
PaxDb; Q9H788; -.
PeptideAtlas; Q9H788; -.
PRIDE; Q9H788; -.
ProteomicsDB; 81087; -.
ProteomicsDB; 81088; -. [Q9H788-2]
Ensembl; ENST00000265807; ENSP00000265807; ENSG00000104611. [Q9H788-1]
Ensembl; ENST00000518040; ENSP00000429482; ENSG00000104611. [Q9H788-2]
Ensembl; ENST00000519207; ENSP00000428684; ENSG00000104611. [Q9H788-1]
GeneID; 63898; -.
KEGG; hsa:63898; -.
UCSC; uc003wzb.4; human. [Q9H788-1]
CTD; 63898; -.
DisGeNET; 63898; -.
EuPathDB; HostDB:ENSG00000104611.11; -.
GeneCards; SH2D4A; -.
HGNC; HGNC:26102; SH2D4A.
HPA; HPA001871; -.
HPA; HPA001919; -.
MIM; 614968; gene.
neXtProt; NX_Q9H788; -.
OpenTargets; ENSG00000104611; -.
PharmGKB; PA134891945; -.
eggNOG; ENOG410IEFY; Eukaryota.
eggNOG; ENOG410XPPJ; LUCA.
GeneTree; ENSGT00570000079047; -.
HOGENOM; HOG000031527; -.
HOVERGEN; HBG057918; -.
InParanoid; Q9H788; -.
KO; K17577; -.
OMA; PYDVLCN; -.
OrthoDB; EOG091G08HG; -.
PhylomeDB; Q9H788; -.
TreeFam; TF336893; -.
SignaLink; Q9H788; -.
ChiTaRS; SH2D4A; human.
GeneWiki; SH2D4A; -.
GenomeRNAi; 63898; -.
PRO; PR:Q9H788; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000104611; Expressed in 188 organ(s), highest expression level in oviduct epithelium.
CleanEx; HS_SH2D4A; -.
ExpressionAtlas; Q9H788; baseline and differential.
Genevisible; Q9H788; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0019902; F:phosphatase binding; IDA:UniProtKB.
GO; GO:0010923; P:negative regulation of phosphatase activity; IDA:UniProtKB.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
Pfam; PF00017; SH2; 1.
SMART; SM00252; SH2; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Phosphoprotein;
Polymorphism; Reference proteome; SH2 domain.
CHAIN 1 454 SH2 domain-containing protein 4A.
/FTId=PRO_0000233133.
DOMAIN 347 440 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
COMPBIAS 172 177 Poly-Ser.
MOD_RES 118 118 Phosphoserine.
{ECO:0000250|UniProtKB:Q9D7V1}.
MOD_RES 124 124 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 261 261 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 315 315 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 60 MLKQILSEMYIDPDLLAELSEEQKQILFFKMREEQIRRWKE
REAAMERKESLPVKPRPKK -> MWRVIEPPCPGAPST
(in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042784.
VARIANT 209 209 E -> G (in dbSNP:rs35647122).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_051350.
VARIANT 216 216 E -> G (in dbSNP:rs4921637).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_026055.
VARIANT 263 263 G -> A (in dbSNP:rs877386).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_026056.
VARIANT 275 275 S -> N (in dbSNP:rs34608771).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_051351.
CONFLICT 95 95 N -> T (in Ref. 1; BAB14935).
{ECO:0000305}.
CONFLICT 179 179 N -> T (in Ref. 4; AAO41715).
{ECO:0000305}.
CONFLICT 238 238 K -> R (in Ref. 4; AAO41715).
{ECO:0000305}.
CONFLICT 253 253 A -> V (in Ref. 4; AAO41715).
{ECO:0000305}.
CONFLICT 291 291 K -> E (in Ref. 1; BAB14935).
{ECO:0000305}.
CONFLICT 346 346 P -> S (in Ref. 4; AAO41715).
{ECO:0000305}.
CONFLICT 440 440 C -> R (in Ref. 1; BAB14935).
{ECO:0000305}.
SEQUENCE 454 AA; 52727 MW; 2FC21D4E07FDA922 CRC64;
MLKQILSEMY IDPDLLAELS EEQKQILFFK MREEQIRRWK EREAAMERKE SLPVKPRPKK
ENGKSVHWKL GADKEVWVWV MGEHHLDKPY DVLCNEIIAE RARLKAEQEA EEPRKTHSEE
FTNSLKTKSQ YHDLQAPDNQ QTKDIWKKVA EKEELEQGSR PAPTLEEEKI RSLSSSSRNI
QQMLADSINR MKAYAFHQKK ESMKKKQDEE INQIEEERTK QICKSWKEDS EWQASLRKSK
AADEKRRSLA KQAREDYKRL SLGAQKGRGG ERLQSPLRVP QKPERPPLPP KPQFLNSGAY
PQKPLRNQGV VRTLSSSAQE DIIRWFKEEQ LPLRAGYQKT SDTIAPWFHG ILTLKKANEL
LLSTGMPGSF LIRVSERIKG YALSYLSEDG CKHFLIDASA DAYSFLGVDQ LQHATLADLV
EYHKEEPITS LGKELLLYPC GQQDQLPDYL ELFE


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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
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
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
EIAAB29458 Homo sapiens,Human,PP2A subunit B isoform PR48,PPP2R3B,PPP2R3L,Protein phosphatase 2A 48 kDa regulatory subunit,Serine_threonine-protein phosphatase 2A regulatory subunit B'' subunit beta
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
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
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
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
E1323h ELISA kit Calcineurin subunit B type 1,CNA2,CNB,Homo sapiens,Human,PPP3R1,Protein phosphatase 2B regulatory subunit 1,Protein phosphatase 3 regulatory subunit B alpha isoform 1 96T
E1323h ELISA Calcineurin subunit B type 1,CNA2,CNB,Homo sapiens,Human,PPP3R1,Protein phosphatase 2B regulatory subunit 1,Protein phosphatase 3 regulatory subunit B alpha isoform 1 96T
U1323h CLIA Calcineurin subunit B type 1,CNA2,CNB,Homo sapiens,Human,PPP3R1,Protein phosphatase 2B regulatory subunit 1,Protein phosphatase 3 regulatory subunit B alpha isoform 1 96T
U1323b CLIA Bos taurus,Bovine,Calcineurin subunit B type 1,CNA2,CNB,PPP3R1,Protein phosphatase 2B regulatory subunit 1,Protein phosphatase 3 regulatory subunit B alpha isoform 1 96T
E1323r ELISA Calcineurin subunit B type 1,Cna2,Cnb,Ppp3r1,Protein phosphatase 2B regulatory subunit 1,Protein phosphatase 3 regulatory subunit B alpha isoform 1,Rat,Rattus norvegicus 96T
E1323b ELISA Bos taurus,Bovine,Calcineurin subunit B type 1,CNA2,CNB,PPP3R1,Protein phosphatase 2B regulatory subunit 1,Protein phosphatase 3 regulatory subunit B alpha isoform 1 96T
U1323r CLIA Calcineurin subunit B type 1,Cna2,Cnb,Ppp3r1,Protein phosphatase 2B regulatory subunit 1,Protein phosphatase 3 regulatory subunit B alpha isoform 1,Rat,Rattus norvegicus 96T
E1323b ELISA kit Bos taurus,Bovine,Calcineurin subunit B type 1,CNA2,CNB,PPP3R1,Protein phosphatase 2B regulatory subunit 1,Protein phosphatase 3 regulatory subunit B alpha isoform 1 96T
E1323r ELISA kit Calcineurin subunit B type 1,Cna2,Cnb,Ppp3r1,Protein phosphatase 2B regulatory subunit 1,Protein phosphatase 3 regulatory subunit B alpha isoform 1,Rat,Rattus norvegicus 96T
U1323m CLIA Calcineurin subunit B type 1,Cnb,Mouse,Mus musculus,Ppp3r1,Protein phosphatase 2B regulatory subunit 1,Protein phosphatase 3 regulatory subunit B alpha isoform 1 96T
E1323m ELISA Calcineurin subunit B type 1,Cnb,Mouse,Mus musculus,Ppp3r1,Protein phosphatase 2B regulatory subunit 1,Protein phosphatase 3 regulatory subunit B alpha isoform 1 96T
E1323m ELISA kit Calcineurin subunit B type 1,Cnb,Mouse,Mus musculus,Ppp3r1,Protein phosphatase 2B regulatory subunit 1,Protein phosphatase 3 regulatory subunit B alpha isoform 1 96T
EIAAB05267 Calcineurin subunit B type 2,Mouse,Mus musculus,Ppp3r2,Protein phosphatase 2B regulatory subunit 2,Protein phosphatase 3 regulatory subunit B beta isoform


 

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