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Pleckstrin homology domain-containing family A member 1 (PH domain-containing family A member 1) (Tandem PH domain-containing protein 1) (TAPP-1)

 PKHA1_HUMAN             Reviewed;         404 AA.
Q9HB21; B3KQ55; D3DRE2; Q9BVK0;
29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
29-MAR-2004, sequence version 2.
22-NOV-2017, entry version 139.
RecName: Full=Pleckstrin homology domain-containing family A member 1;
Short=PH domain-containing family A member 1;
AltName: Full=Tandem PH domain-containing protein 1;
Short=TAPP-1;
Name=PLEKHA1; Synonyms=TAPP1;
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), FUNCTION, MUTAGENESIS OF
ARG-28 AND ARG-211, TISSUE SPECIFICITY, AND VARIANT ALA-320.
PubMed=11001876; DOI=10.1042/0264-6021:3510019;
Dowler S.J., Currie R.A., Campbell D.G., Deak M., Kular G.,
Downes C.P., Alessi D.R.;
"Identification of pleckstrin-homology-domain-containing proteins with
novel phosphoinositide-binding specificities.";
Biochem. J. 351:19-31(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-320.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon, and Testis;
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]
INTERACTION WITH MPDZ, AND SUBCELLULAR LOCATION.
PubMed=11802782; DOI=10.1042/0264-6021:3610525;
Kimber W.A., Trinkle-Mulcahy L., Cheung P.C.F., Deak M., Marsden L.J.,
Kieloch A., Watt S., Javier R.T., Gray A., Downes C.P., Lucocq J.M.,
Alessi D.R.;
"Evidence that the tandem-pleckstrin-homology-domain-containing
protein TAPP1 interacts with Ptd(3,4)P2 and the multi-PDZ-domain-
containing protein MUPP1 in vivo.";
Biochem. J. 361:525-536(2002).
[7]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12101241; DOI=10.1128/MCB.22.15.5479-5491.2002;
Marshall A.J., Krahn A.K., Ma K., Duronio V., Hou S.;
"TAPP1 and TAPP2 are targets of phosphatidylinositol 3-kinase
signaling in B cells: sustained plasma membrane recruitment triggered
by the B-cell antigen receptor.";
Mol. Cell. Biol. 22:5479-5491(2002).
[8]
INTERACTION WITH PTPN13, AND FUNCTION.
PubMed=14516276; DOI=10.1042/BJ20031154;
Kimber W.A., Deak M., Prescott A.R., Alessi D.R.;
"Interaction of the protein tyrosine phosphatase PTPL1 with the
PtdIns(3,4)P2-binding adaptor protein TAPP1.";
Biochem. J. 376:525-535(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, 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].
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=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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, 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).
[13]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 190-292, FUNCTION, AND
MUTAGENESIS OF ALA-203; VAL-204; MET-205 AND ASN-207.
PubMed=11513726; DOI=10.1042/0264-6021:3580287;
Thomas C.C., Dowler S.J., Deak M., Alessi D.R., van Aalten D.M.F.;
"Crystal structure of the phosphatidylinositol 3,4-bisphosphate-
binding pleckstrin homology (PH) domain of tandem PH-domain-containing
protein 1 (TAPP1): molecular basis of lipid specificity.";
Biochem. J. 358:287-294(2001).
-!- FUNCTION: Binds specifically to phosphatidylinositol 3,4-
diphosphate (PtdIns3,4P2), but not to other phosphoinositides. May
recruit other proteins to the plasma membrane.
{ECO:0000269|PubMed:11001876, ECO:0000269|PubMed:11513726,
ECO:0000269|PubMed:14516276}.
-!- SUBUNIT: Interacts with MPDZ and PTPN13.
{ECO:0000269|PubMed:11802782, ECO:0000269|PubMed:14516276}.
-!- INTERACTION:
O75970:MPDZ; NbExp=6; IntAct=EBI-2652984, EBI-821405;
Q9P0V3:SH3BP4; NbExp=2; IntAct=EBI-2652984, EBI-1049513;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11802782,
ECO:0000269|PubMed:12101241}. Cell membrane
{ECO:0000269|PubMed:11802782, ECO:0000269|PubMed:12101241};
Peripheral membrane protein. Nucleus {ECO:0000269|PubMed:11802782,
ECO:0000269|PubMed:12101241}. Note=Locates to the plasma membrane
after treatments that stimulate the production of PtdIns3,4P2.
{ECO:0000269|PubMed:11802782}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9HB21-1; Sequence=Displayed;
Name=2;
IsoId=Q9HB21-2; Sequence=VSP_043091;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle, thymus,
pancreas, placenta and lung. Detected at low levels in brain,
heart, peripheral blood leukocytes, testis, ovary, spinal cord,
thyroid, kidney, liver, small intestine and colon.
{ECO:0000269|PubMed:11001876, ECO:0000269|PubMed:12101241}.
-!- DOMAIN: Binds to membranes enriched in PtdIns3,4P2 via the C-
terminal PH domain.
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EMBL; AF286160; AAG15197.1; -; mRNA.
EMBL; AK057463; BAG51917.1; -; mRNA.
EMBL; BX664700; CAI23597.1; -; Genomic_DNA.
EMBL; BX842242; CAI23597.1; JOINED; Genomic_DNA.
EMBL; CH471066; EAW49315.1; -; Genomic_DNA.
EMBL; CH471066; EAW49316.1; -; Genomic_DNA.
EMBL; CH471066; EAW49318.1; -; Genomic_DNA.
EMBL; CH471066; EAW49319.1; -; Genomic_DNA.
EMBL; BC001136; AAH01136.1; -; mRNA.
EMBL; BC042458; AAH42458.1; -; mRNA.
CCDS; CCDS55730.1; -. [Q9HB21-2]
CCDS; CCDS7629.1; -. [Q9HB21-1]
RefSeq; NP_001001974.1; NM_001001974.2. [Q9HB21-1]
RefSeq; NP_001182537.1; NM_001195608.1. [Q9HB21-2]
RefSeq; NP_001317107.1; NM_001330178.1.
RefSeq; NP_067635.2; NM_021622.4. [Q9HB21-1]
RefSeq; XP_005270073.1; XM_005270016.1. [Q9HB21-1]
RefSeq; XP_005270078.1; XM_005270021.4. [Q9HB21-2]
RefSeq; XP_016871969.1; XM_017016480.1. [Q9HB21-1]
RefSeq; XP_016871970.1; XM_017016481.1. [Q9HB21-1]
RefSeq; XP_016871971.1; XM_017016482.1. [Q9HB21-1]
RefSeq; XP_016871979.1; XM_017016490.1. [Q9HB21-2]
RefSeq; XP_016871980.1; XM_017016491.1. [Q9HB21-2]
UniGene; Hs.643512; -.
UniGene; Hs.738826; -.
PDB; 1EAZ; X-ray; 1.40 A; A=182-303.
PDBsum; 1EAZ; -.
ProteinModelPortal; Q9HB21; -.
SMR; Q9HB21; -.
BioGrid; 121880; 18.
IntAct; Q9HB21; 9.
MINT; MINT-275100; -.
STRING; 9606.ENSP00000357986; -.
ChEMBL; CHEMBL3763005; -.
DrugBank; DB04272; Citric Acid.
iPTMnet; Q9HB21; -.
PhosphoSitePlus; Q9HB21; -.
BioMuta; PLEKHA1; -.
DMDM; 48474647; -.
EPD; Q9HB21; -.
MaxQB; Q9HB21; -.
PaxDb; Q9HB21; -.
PeptideAtlas; Q9HB21; -.
PRIDE; Q9HB21; -.
DNASU; 59338; -.
Ensembl; ENST00000368988; ENSP00000357984; ENSG00000107679. [Q9HB21-2]
Ensembl; ENST00000368990; ENSP00000357986; ENSG00000107679. [Q9HB21-1]
Ensembl; ENST00000392799; ENSP00000376547; ENSG00000107679. [Q9HB21-1]
Ensembl; ENST00000433307; ENSP00000394416; ENSG00000107679. [Q9HB21-1]
GeneID; 59338; -.
KEGG; hsa:59338; -.
UCSC; uc001lge.3; human. [Q9HB21-1]
CTD; 59338; -.
DisGeNET; 59338; -.
EuPathDB; HostDB:ENSG00000107679.14; -.
GeneCards; PLEKHA1; -.
HGNC; HGNC:14335; PLEKHA1.
HPA; HPA002043; -.
HPA; HPA064795; -.
MalaCards; PLEKHA1; -.
MIM; 607772; gene.
neXtProt; NX_Q9HB21; -.
OpenTargets; ENSG00000107679; -.
PharmGKB; PA33401; -.
eggNOG; ENOG410IF2M; Eukaryota.
eggNOG; ENOG410ZQEQ; LUCA.
GeneTree; ENSGT00440000037398; -.
HOGENOM; HOG000116175; -.
HOVERGEN; HBG053612; -.
InParanoid; Q9HB21; -.
OMA; NPCIQRS; -.
OrthoDB; EOG091G08U3; -.
PhylomeDB; Q9HB21; -.
TreeFam; TF329516; -.
Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
ChiTaRS; PLEKHA1; human.
EvolutionaryTrace; Q9HB21; -.
GeneWiki; PLEKHA1; -.
GenomeRNAi; 59338; -.
PRO; PR:Q9HB21; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000107679; -.
CleanEx; HS_PLEKHA1; -.
ExpressionAtlas; Q9HB21; baseline and differential.
Genevisible; Q9HB21; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB.
GO; GO:0008209; P:androgen metabolic process; IEA:Ensembl.
GO; GO:0050853; P:B cell receptor signaling pathway; IDA:UniProtKB.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB.
GO; GO:0045184; P:establishment of protein localization; IDA:UniProtKB.
GO; GO:0008210; P:estrogen metabolic process; IEA:Ensembl.
GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
GO; GO:0033327; P:Leydig cell differentiation; IEA:Ensembl.
GO; GO:0001553; P:luteinization; IEA:Ensembl.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:UniProtKB.
GO; GO:0060021; P:palate development; IEA:Ensembl.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0031529; P:ruffle organization; IDA:UniProtKB.
GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
Gene3D; 2.30.29.30; -; 2.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
Pfam; PF00169; PH; 2.
SMART; SM00233; PH; 2.
SUPFAM; SSF50729; SSF50729; 2.
PROSITE; PS50003; PH_DOMAIN; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Cytoplasm; Lipid-binding; Membrane; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat.
CHAIN 1 404 Pleckstrin homology domain-containing
family A member 1.
/FTId=PRO_0000053873.
DOMAIN 7 112 PH 1. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 191 289 PH 2. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
MOD_RES 332 332 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 362 362 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
VAR_SEQ 301 404 EHPPGPSESKHAFRPTNAATATSHSTASRSNSLVSTFTMEK
RGFYESLAKVKPGNFKVQTVSPREPASKVTEQALLRPQSKN
GPQEKDCDLVDLDDASLPVSDV -> MRQARRLSNPCIQRY
TSRAGECSTYVGSHANVPS (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043091.
VARIANT 320 320 T -> A (in dbSNP:rs1045216).
{ECO:0000269|PubMed:11001876,
ECO:0000269|Ref.4}.
/FTId=VAR_024562.
MUTAGEN 28 28 R->L: No effect on phosphatidylinositide
binding. {ECO:0000269|PubMed:11001876}.
MUTAGEN 203 205 AVM->GGG: Abolishes phosphatidylinositide
binding.
MUTAGEN 203 205 AVM->GLV: Binds both PtdIns3,4P2 and
PtdIns3,4,5P3.
MUTAGEN 203 204 AV->GG: Binds both PtdIns3,4P2 and
PtdIns3,4,5P3.
MUTAGEN 203 203 A->G: Binds both PtdIns3,4P2 and
PtdIns3,4,5P3.
{ECO:0000269|PubMed:11513726}.
MUTAGEN 204 204 V->L: No effect.
{ECO:0000269|PubMed:11513726}.
MUTAGEN 205 205 M->V: No effect.
{ECO:0000269|PubMed:11513726}.
MUTAGEN 207 207 N->T: No effect.
{ECO:0000269|PubMed:11513726}.
MUTAGEN 211 211 R->L: Abolishes phosphatidylinositide
binding. {ECO:0000269|PubMed:11001876}.
STRAND 193 201 {ECO:0000244|PDB:1EAZ}.
TURN 203 205 {ECO:0000244|PDB:1EAZ}.
STRAND 208 215 {ECO:0000244|PDB:1EAZ}.
STRAND 217 225 {ECO:0000244|PDB:1EAZ}.
STRAND 232 236 {ECO:0000244|PDB:1EAZ}.
HELIX 237 239 {ECO:0000244|PDB:1EAZ}.
STRAND 242 245 {ECO:0000244|PDB:1EAZ}.
HELIX 249 252 {ECO:0000244|PDB:1EAZ}.
STRAND 255 261 {ECO:0000244|PDB:1EAZ}.
STRAND 266 270 {ECO:0000244|PDB:1EAZ}.
HELIX 274 290 {ECO:0000244|PDB:1EAZ}.
SEQUENCE 404 AA; 45553 MW; 6855CD58E1A80F8A CRC64;
MPYVDRQNRI CGFLDIEENE NSGKFLRRYF ILDTREDSFV WYMDNPQNLP SGSSRVGAIK
LTYISKVSDA TKLRPKAEFC FVMNAGMRKY FLQANDQQDL VEWVNVLNKA IKITVPKQSD
SQPNSDNLSR HGECGKKQVS YRTDIVGGVP IITPTQKEEV NECGESIDRN NLKRSQSHLP
YFTPKPPQDS AVIKAGYCVK QGAVMKNWKR RYFQLDENTI GYFKSELEKE PLRVIPLKEV
HKVQECKQSD IMMRDNLFEI VTTSRTFYVQ ADSPEEMHSW IKAVSGAIVA QRGPGRSASS
EHPPGPSESK HAFRPTNAAT ATSHSTASRS NSLVSTFTME KRGFYESLAK VKPGNFKVQT
VSPREPASKV TEQALLRPQS KNGPQEKDCD LVDLDDASLP VSDV


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EIAAB31260 Mouse,Mus musculus,PH domain-containing adaptor PHAD47,PH domain-containing family A member 2,Pleckstrin homology domain-containing family A member 2,Plekha2,Tandem PH domain-containing protein 2,Tapp
EIAAB31259 Homo sapiens,Human,PH domain-containing family A member 2,Pleckstrin homology domain-containing family A member 2,PLEKHA2,Tandem PH domain-containing protein 2,TAPP2,TAPP-2
EIAAB31257 Homo sapiens,Human,PH domain-containing family A member 1,Pleckstrin homology domain-containing family A member 1,PLEKHA1,Tandem PH domain-containing protein 1,TAPP1,TAPP-1
EIAAB31258 Mouse,Mus musculus,PH domain-containing family A member 1,Pleckstrin homology domain-containing family A member 1,Plekha1,Tandem PH domain-containing protein 1,Tapp1,TAPP-1
EIAAB31330 Homo sapiens,Human,PH domain-containing family O member 2,PH domain-containing family Q member 1,Pleckstrin homology domain-containing family O member 2,Pleckstrin homology domain-containing family Q
EIAAB30917 Kiaa0606,Mouse,Mus musculus,PH domain leucine-rich repeat-containing protein phosphatase 1,PH domain-containing family E member 1,Phlpp,Phlpp1,Pleckstrin homology domain-containing family E member 1,P
EIAAB30916 PH domain leucine-rich repeat protein phosphatase 1,PH domain-containing family E member 1,Phlpp,Phlpp1,Pleckstrin homology domain-containing family E member 1,Plekhe1,Rat,Rattus norvegicus,Scop,Supra
EIAAB31275 Evectin-1,Evt1,Mouse,Mus musculus,PH domain-containing family B member 1,PH domain-containing protein in retina 1,Phr1,PHRET1,Pleckstrin homology domain retinal protein 1,Pleckstrin homology domain-co
EIAAB31329 Bos taurus,Bovine,PH domain-containing family O member 2,PH domain-containing family Q member 1,Pleckstrin homology domain-containing family O member 2,Pleckstrin homology domain-containing family Q m
EIAAB31328 Mouse,Mus musculus,PH domain-containing family O member 2,PH domain-containing family Q member 1,Pleckstrin homology domain-containing family O member 2,Pleckstrin homology domain-containing family Q
EIAAB31286 Homo sapiens,Human,PH and FYVE domain-containing protein 2,PH domain-containing family F member 2,Phafin-2,Pleckstrin homology domain-containing family F member 2,PLEKHF2,ZFYVE18,Zinc finger FYVE doma
EIAAB31271 Hadp1,Heart adapter protein 1,Mouse,Mus musculus,PH domain-containing family A member 7,Pleckstrin homology domain-containing family A member 7,Plekha7
EIAAB31310 Gnrpx,Guanine nucleotide-releasing protein x,Mouse,Mus musculus,PH domain-containing family J member 1,Pleckstrin homology domain-containing family J member 1,Plekhj1
EIAAB31313 162 kDa adapter protein,AP162,Homo sapiens,Human,KIAA0356,PH domain-containing family M member 1,Pleckstrin homology domain-containing family M member 1,PLEKHM1
EIAAB31282 Lapf,Lysosome-associated apoptosis-inducing protein containing PH and FYVE domains,Mouse,Mus musculus,PH domain-containing family F member 1,Pleckstrin homology domain-containing family F member 1,Ple
EIAAB31268 Mouse,Mus musculus,Pepp3,PEPP-3,PH domain-containing family A member 6,Phosphoinositol 3-phosphate-binding protein 3,Pleckstrin homology domain-containing family A member 6,Plekha6
EIAAB31266 Mouse,Mus musculus,Pepp1,PEPP-1,PH domain-containing family A member 4,Phosphoinositol 3-phosphate-binding protein 1,Pleckstrin homology domain-containing family A member 4,Plekha4
EIAAB31309 GNRPX,Guanine nucleotide-releasing protein x,Homo sapiens,Human,PH domain-containing family J member 1,Pleckstrin homology domain-containing family J member 1,PLEKHJ1
EIAAB31264 Pepp1,PEPP-1,PH domain-containing family A member 4,Phosphoinositol 3-phosphate-binding protein 1,Pleckstrin homology domain-containing family A member 4,Plekha4,Rat,Rattus norvegicus
EIAAB31265 Homo sapiens,Human,PEPP1,PEPP-1,PH domain-containing family A member 4,Phosphoinositol 3-phosphate-binding protein 1,Pleckstrin homology domain-containing family A member 4,PLEKHA4
EIAAB31293 Homo sapiens,Human,PH domain-containing family G member 4,Pleckstrin homology domain-containing family G member 4,PLEKHG4,PRTPHN1,Puratrophin-1,Purkinje cell atrophy-associated protein 1
EIAAB31269 Homo sapiens,Human,KIAA0969,PEPP3,PEPP-3,PH domain-containing family A member 6,Phosphoinositol 3-phosphate-binding protein 3,Pleckstrin homology domain-containing family A member 6,PLEKHA6
EIAAB31267 Homo sapiens,Human,KIAA1686,PEPP2,PEPP-2,PH domain-containing family A member 5,Phosphoinositol 3-phosphate-binding protein 2,Pleckstrin homology domain-containing family A member 5,PLEKHA5
EIAAB31295 Neuronal RhoA GEF protein,PH domain-containing family G member 5,Pleckstrin homology domain-containing family G member 5,Plekhg5,Rat,Rattus norvegicus,Tech,Transcript highly enriched in cortex and hip
EIAAB31317 Homo sapiens,Human,KIAA0842,PH domain-containing family M member 2,Pleckstrin homology domain-containing family M member 2,PLEKHM2,Salmonella-induced filaments A and kinesin-interacting protein,SifA a


 

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