PKHA1_HUMAN
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 03-AUG-2022, entry version 166.
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.
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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. [Q9HB21-1]
DR RefSeq; XP_016871970.1; XM_017016481.1. [Q9HB21-1]
DR RefSeq; XP_016871971.1; XM_017016482.1. [Q9HB21-1]
DR RefSeq; XP_016871979.1; XM_017016490.1. [Q9HB21-2]
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; 79.
DR IntAct; Q9HB21; 23.
DR MINT; Q9HB21; -.
DR STRING; 9606.ENSP00000357986; -.
DR ChEMBL; CHEMBL3763005; -.
DR DrugBank; DB04272; Citric acid.
DR GlyGen; Q9HB21; 5 sites, 2 O-linked glycans (5 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 PRIDE; Q9HB21; -.
DR ProteomicsDB; 81474; -. [Q9HB21-1]
DR ProteomicsDB; 81475; -. [Q9HB21-2]
DR Antibodypedia; 1178; 180 antibodies from 26 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 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; ISKXMNA; -.
DR OrthoDB; 1513983at2759; -.
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; 14 hits in 1080 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 Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF00169; PH; 2.
DR SMART; SM00233; PH; 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
