ID PKHA1_HUMAN Reviewed; 404 AA. AC Q9HB21; B3KQ55; D3DRE2; Q9BVK0; DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2004, sequence version 2. DT 28-JUN-2023, entry version 171. DE RecName: Full=Pleckstrin homology domain-containing family A member 1; DE Short=PH domain-containing family A member 1; DE AltName: Full=Tandem PH domain-containing protein 1; DE Short=TAPP-1; GN Name=PLEKHA1; Synonyms=TAPP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF ARG-28 AND RP ARG-211, TISSUE SPECIFICITY, AND VARIANT ALA-320. RX PubMed=11001876; DOI=10.1042/0264-6021:3510019; RA Dowler S.J., Currie R.A., Campbell D.G., Deak M., Kular G., Downes C.P., RA Alessi D.R.; RT "Identification of pleckstrin-homology-domain-containing proteins with RT novel phosphoinositide-binding specificities."; RL Biochem. J. 351:19-31(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-320. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon, and Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP INTERACTION WITH MPDZ, AND SUBCELLULAR LOCATION. RX PubMed=11802782; DOI=10.1042/0264-6021:3610525; RA Kimber W.A., Trinkle-Mulcahy L., Cheung P.C.F., Deak M., Marsden L.J., RA Kieloch A., Watt S., Javier R.T., Gray A., Downes C.P., Lucocq J.M., RA Alessi D.R.; RT "Evidence that the tandem-pleckstrin-homology-domain-containing protein RT TAPP1 interacts with Ptd(3,4)P2 and the multi-PDZ-domain-containing protein RT MUPP1 in vivo."; RL Biochem. J. 361:525-536(2002). RN [7] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=12101241; DOI=10.1128/mcb.22.15.5479-5491.2002; RA Marshall A.J., Krahn A.K., Ma K., Duronio V., Hou S.; RT "TAPP1 and TAPP2 are targets of phosphatidylinositol 3-kinase signaling in RT B cells: sustained plasma membrane recruitment triggered by the B-cell RT antigen receptor."; RL Mol. Cell. Biol. 22:5479-5491(2002). RN [8] RP INTERACTION WITH PTPN13, AND FUNCTION. RX PubMed=14516276; DOI=10.1042/bj20031154; RA Kimber W.A., Deak M., Prescott A.R., Alessi D.R.; RT "Interaction of the protein tyrosine phosphatase PTPL1 with the RT PtdIns(3,4)P2-binding adaptor protein TAPP1."; RL Biochem. J. 376:525-535(2003). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 190-292, FUNCTION, AND MUTAGENESIS RP OF ALA-203; VAL-204; MET-205 AND ASN-207. RX PubMed=11513726; DOI=10.1042/0264-6021:3580287; RA Thomas C.C., Dowler S.J., Deak M., Alessi D.R., van Aalten D.M.F.; RT "Crystal structure of the phosphatidylinositol 3,4-bisphosphate-binding RT pleckstrin homology (PH) domain of tandem PH-domain-containing protein 1 RT (TAPP1): molecular basis of lipid specificity."; RL Biochem. J. 358:287-294(2001). CC -!- FUNCTION: Binds specifically to phosphatidylinositol 3,4-diphosphate CC (PtdIns3,4P2), but not to other phosphoinositides. May recruit other CC proteins to the plasma membrane. {ECO:0000269|PubMed:11001876, CC ECO:0000269|PubMed:11513726, ECO:0000269|PubMed:14516276}. CC -!- SUBUNIT: Interacts with MPDZ and PTPN13. {ECO:0000269|PubMed:11802782, CC ECO:0000269|PubMed:14516276}. CC -!- INTERACTION: CC Q9HB21; O75970: MPDZ; NbExp=6; IntAct=EBI-2652984, EBI-821405; CC Q9HB21; Q9P0V3: SH3BP4; NbExp=2; IntAct=EBI-2652984, EBI-1049513; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11802782, CC ECO:0000269|PubMed:12101241}. Cell membrane CC {ECO:0000269|PubMed:11802782, ECO:0000269|PubMed:12101241}; Peripheral CC membrane protein. Nucleus {ECO:0000269|PubMed:11802782, CC ECO:0000269|PubMed:12101241}. Note=Locates to the plasma membrane after CC treatments that stimulate the production of PtdIns3,4P2. CC {ECO:0000269|PubMed:11802782}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9HB21-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9HB21-2; Sequence=VSP_043091; CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle, thymus, CC pancreas, placenta and lung. Detected at low levels in brain, heart, CC peripheral blood leukocytes, testis, ovary, spinal cord, thyroid, CC kidney, liver, small intestine and colon. {ECO:0000269|PubMed:11001876, CC ECO:0000269|PubMed:12101241}. CC -!- DOMAIN: Binds to membranes enriched in PtdIns3,4P2 via the C-terminal CC PH domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF286160; AAG15197.1; -; mRNA. DR EMBL; AK057463; BAG51917.1; -; mRNA. DR EMBL; BX664700; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX842242; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471066; EAW49315.1; -; Genomic_DNA. DR EMBL; CH471066; EAW49316.1; -; Genomic_DNA. DR EMBL; CH471066; EAW49318.1; -; Genomic_DNA. DR EMBL; CH471066; EAW49319.1; -; Genomic_DNA. DR EMBL; BC001136; AAH01136.1; -; mRNA. DR EMBL; BC042458; AAH42458.1; -; mRNA. DR CCDS; CCDS55730.1; -. [Q9HB21-2] DR CCDS; CCDS7629.1; -. [Q9HB21-1] DR RefSeq; NP_001001974.1; NM_001001974.2. [Q9HB21-1] DR RefSeq; NP_001182537.1; NM_001195608.1. [Q9HB21-2] DR RefSeq; NP_001317107.1; NM_001330178.1. DR RefSeq; NP_067635.2; NM_021622.4. [Q9HB21-1] DR RefSeq; XP_005270073.1; XM_005270016.1. DR RefSeq; XP_005270078.1; XM_005270021.4. DR RefSeq; XP_016871969.1; XM_017016480.1. DR RefSeq; XP_016871970.1; XM_017016481.1. DR RefSeq; XP_016871971.1; XM_017016482.1. [Q9HB21-1] DR RefSeq; XP_016871979.1; XM_017016490.1. DR RefSeq; XP_016871980.1; XM_017016491.1. DR PDB; 1EAZ; X-ray; 1.40 A; A=182-303. DR PDBsum; 1EAZ; -. DR AlphaFoldDB; Q9HB21; -. DR SMR; Q9HB21; -. DR BioGRID; 121880; 101. DR IntAct; Q9HB21; 39. DR MINT; Q9HB21; -. DR STRING; 9606.ENSP00000357986; -. DR ChEMBL; CHEMBL3763005; -. DR DrugBank; DB04272; Citric acid. DR GlyCosmos; Q9HB21; 5 sites, 2 glycans. DR GlyGen; Q9HB21; 6 sites, 2 O-linked glycans (6 sites). DR iPTMnet; Q9HB21; -. DR PhosphoSitePlus; Q9HB21; -. DR BioMuta; PLEKHA1; -. DR DMDM; 48474647; -. DR EPD; Q9HB21; -. DR jPOST; Q9HB21; -. DR MassIVE; Q9HB21; -. DR MaxQB; Q9HB21; -. DR PaxDb; Q9HB21; -. DR PeptideAtlas; Q9HB21; -. DR ProteomicsDB; 81474; -. [Q9HB21-1] DR ProteomicsDB; 81475; -. [Q9HB21-2] DR Antibodypedia; 1178; 204 antibodies from 27 providers. DR DNASU; 59338; -. DR Ensembl; ENST00000368988.5; ENSP00000357984.2; ENSG00000107679.15. [Q9HB21-2] DR Ensembl; ENST00000368990.8; ENSP00000357986.3; ENSG00000107679.15. [Q9HB21-1] DR Ensembl; ENST00000392799.7; ENSP00000376547.3; ENSG00000107679.15. [Q9HB21-1] DR Ensembl; ENST00000433307.2; ENSP00000394416.1; ENSG00000107679.15. [Q9HB21-1] DR GeneID; 59338; -. DR KEGG; hsa:59338; -. DR MANE-Select; ENST00000368990.8; ENSP00000357986.3; NM_001001974.4; NP_001001974.1. DR UCSC; uc001lge.3; human. [Q9HB21-1] DR AGR; HGNC:14335; -. DR CTD; 59338; -. DR DisGeNET; 59338; -. DR GeneCards; PLEKHA1; -. DR HGNC; HGNC:14335; PLEKHA1. DR HPA; ENSG00000107679; Low tissue specificity. DR MIM; 607772; gene. DR neXtProt; NX_Q9HB21; -. DR OpenTargets; ENSG00000107679; -. DR PharmGKB; PA33401; -. DR VEuPathDB; HostDB:ENSG00000107679; -. DR eggNOG; ENOG502QT2K; Eukaryota. DR GeneTree; ENSGT00940000155157; -. DR HOGENOM; CLU_055135_2_0_1; -. DR InParanoid; Q9HB21; -. DR OMA; GMECLEG; -. DR OrthoDB; 11085at2759; -. DR PhylomeDB; Q9HB21; -. DR TreeFam; TF329516; -. DR PathwayCommons; Q9HB21; -. DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane. DR SignaLink; Q9HB21; -. DR BioGRID-ORCS; 59338; 17 hits in 1158 CRISPR screens. DR ChiTaRS; PLEKHA1; human. DR EvolutionaryTrace; Q9HB21; -. DR GeneWiki; PLEKHA1; -. DR GenomeRNAi; 59338; -. DR Pharos; Q9HB21; Tbio. DR PRO; PR:Q9HB21; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q9HB21; protein. DR Bgee; ENSG00000107679; Expressed in upper leg skin and 197 other tissues. DR ExpressionAtlas; Q9HB21; baseline and differential. DR Genevisible; Q9HB21; HS. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB. DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB. DR GO; GO:0008209; P:androgen metabolic process; IEA:Ensembl. DR GO; GO:0050853; P:B cell receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB. DR GO; GO:0045184; P:establishment of protein localization; IDA:UniProtKB. DR GO; GO:0008210; P:estrogen metabolic process; IEA:Ensembl. DR GO; GO:0060325; P:face morphogenesis; IEA:Ensembl. DR GO; GO:0033327; P:Leydig cell differentiation; IEA:Ensembl. DR GO; GO:0001553; P:luteinization; IEA:Ensembl. DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl. DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:UniProtKB. DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IDA:UniProtKB. DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl. DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl. DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl. DR GO; GO:0031529; P:ruffle organization; IDA:UniProtKB. DR GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl. DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. DR CDD; cd13270; PH1_TAPP1_2; 1. DR CDD; cd13271; PH2_TAPP1_2; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR PANTHER; PTHR14336:SF4; PLECKSTRIN HOMOLOGY DOMAIN-CONTAINING FAMILY A MEMBER 1; 1. DR PANTHER; PTHR14336; TANDEM PH DOMAIN CONTAINING PROTEIN; 1. DR Pfam; PF00169; PH; 2. DR SMART; SM00233; PH; 2. DR SUPFAM; SSF50729; PH domain-like; 2. DR PROSITE; PS50003; PH_DOMAIN; 2. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm; KW Lipid-binding; Membrane; Nucleus; Phosphoprotein; Reference proteome; KW Repeat. FT CHAIN 1..404 FT /note="Pleckstrin homology domain-containing family A FT member 1" FT /id="PRO_0000053873" FT DOMAIN 7..112 FT /note="PH 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT DOMAIN 191..289 FT /note="PH 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT REGION 291..332 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 355..404 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 313..332 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 361..380 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 332 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 362 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT VAR_SEQ 301..404 FT /note="EHPPGPSESKHAFRPTNAATATSHSTASRSNSLVSTFTMEKRGFYESLAKVK FT PGNFKVQTVSPREPASKVTEQALLRPQSKNGPQEKDCDLVDLDDASLPVSDV -> MRQ FT ARRLSNPCIQRYTSRAGECSTYVGSHANVPS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043091" FT VARIANT 320 FT /note="T -> A (in dbSNP:rs1045216)" FT /evidence="ECO:0000269|PubMed:11001876, ECO:0000269|Ref.4" FT /id="VAR_024562" FT MUTAGEN 28 FT /note="R->L: No effect on phosphatidylinositide binding." FT /evidence="ECO:0000269|PubMed:11001876" FT MUTAGEN 203..205 FT /note="AVM->GGG: Abolishes phosphatidylinositide binding." FT MUTAGEN 203..205 FT /note="AVM->GLV: Binds both PtdIns3,4P2 and PtdIns3,4,5P3." FT MUTAGEN 203..204 FT /note="AV->GG: Binds both PtdIns3,4P2 and PtdIns3,4,5P3." FT MUTAGEN 203 FT /note="A->G: Binds both PtdIns3,4P2 and PtdIns3,4,5P3." FT /evidence="ECO:0000269|PubMed:11513726" FT MUTAGEN 204 FT /note="V->L: No effect." FT /evidence="ECO:0000269|PubMed:11513726" FT MUTAGEN 205 FT /note="M->V: No effect." FT /evidence="ECO:0000269|PubMed:11513726" FT MUTAGEN 207 FT /note="N->T: No effect." FT /evidence="ECO:0000269|PubMed:11513726" FT MUTAGEN 211 FT /note="R->L: Abolishes phosphatidylinositide binding." FT /evidence="ECO:0000269|PubMed:11001876" FT STRAND 193..201 FT /evidence="ECO:0007829|PDB:1EAZ" FT TURN 203..205 FT /evidence="ECO:0007829|PDB:1EAZ" FT STRAND 208..215 FT /evidence="ECO:0007829|PDB:1EAZ" FT STRAND 217..225 FT /evidence="ECO:0007829|PDB:1EAZ" FT STRAND 232..236 FT /evidence="ECO:0007829|PDB:1EAZ" FT HELIX 237..239 FT /evidence="ECO:0007829|PDB:1EAZ" FT STRAND 242..245 FT /evidence="ECO:0007829|PDB:1EAZ" FT HELIX 249..252 FT /evidence="ECO:0007829|PDB:1EAZ" FT STRAND 255..261 FT /evidence="ECO:0007829|PDB:1EAZ" FT STRAND 266..270 FT /evidence="ECO:0007829|PDB:1EAZ" FT HELIX 274..290 FT /evidence="ECO:0007829|PDB:1EAZ" SQ 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 //