ADAP1_HUMAN
ID ADAP1_HUMAN Reviewed; 374 AA.
AC O75689; A4D2Q2; B3KRZ4; B4DVA6; F6XZ68; H7C2Q4;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Arf-GAP with dual PH domain-containing protein 1;
DE AltName: Full=Centaurin-alpha-1;
DE Short=Cnt-a1;
DE AltName: Full=Putative MAPK-activating protein PM25;
GN Name=ADAP1; Synonyms=CENTA1;
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF ARG-149 AND ARG-273.
RC TISSUE=Blood {ECO:0000269|PubMed:10448098};
RX PubMed=10448098; DOI=10.1006/bbrc.1999.1065;
RA Venkateswarlu K., Cullen P.J.;
RT "Molecular cloning and functional characterization of a human homologue of
RT centaurin-alpha.";
RL Biochem. Biophys. Res. Commun. 262:237-244(1999).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAA07024.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF CYS-21; CYS-24; ARG-149 AND ARG-273, AND VARIANT SER-241.
RC TISSUE=Peripheral blood {ECO:0000312|EMBL:CAA07024.1};
RX PubMed=10333475; DOI=10.1042/bj3400359;
RA Venkateswarlu K., Oatey P.B., Tavare J.M., Jackson T.R., Cullen P.J.;
RT "Identification of centaurin-alpha1 as a potential in vivo
RT phosphatidylinositol 3,4,5-trisphosphate-binding protein that is
RT functionally homologous to the yeast ADP-ribosylation factor (ARF) GTPase-
RT activating protein, Gcs1.";
RL Biochem. J. 340:359-363(1999).
RN [3] {ECO:0000312|EMBL:AAD11414.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-241.
RC TISSUE=Brain {ECO:0000312|EMBL:AAD11414.1};
RA Horstmeyer A., Reiser G.;
RT "Molecular identification of a high-affinity
RT Ins(1,3,4,5)tetrakisphosphate/phosphatidylinositol(3,4, 5)trisphosphate
RT binding protein from human brain, p42IP4.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305, ECO:0000312|EMBL:BAC77402.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-241.
RC TISSUE=Lung fibroblast;
RX PubMed=12761501; DOI=10.1038/sj.onc.1206406;
RA Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y.,
RA Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.;
RT "Large-scale identification and characterization of human genes that
RT activate NF-kappaB and MAPK signaling pathways.";
RL Oncogene 22:3307-3318(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Small intestine;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [7] {ECO:0000312|EMBL:AAD11414.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000312|EMBL:AAH33747.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-241.
RC TISSUE=Brain {ECO:0000312|EMBL:AAH33747.1};
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 [9] {ECO:0000305}
RP INTERACTION WITH PRKCA; PRKCI; PRKCZ AND PRKD1, AND PHOSPHORYLATION AT
RP SER-87 AND THR-276.
RX PubMed=12893243; DOI=10.1016/s0006-291x(03)01187-2;
RA Zemlickova E., Dubois T., Kerai P., Clokie S., Cronshaw A.D.,
RA Wakefield R.I.D., Johannes F.-J., Aitken A.;
RT "Centaurin-alpha(1) associates with and is phosphorylated by isoforms of
RT protein kinase C.";
RL Biochem. Biophys. Res. Commun. 307:459-465(2003).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-272, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11] {ECO:0000312|EMBL:AAD11414.1}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 3-370.
RG Structural genomics consortium (SGC);
RT "Crystal structure of full length centaurin alpha-1.";
RL Submitted (DEC-2008) to the PDB data bank.
CC -!- FUNCTION: GTPase-activating protein for the ADP ribosylation factor
CC family (Probable). Binds phosphatidylinositol 3,4,5-trisphosphate
CC (PtdInsP3) and inositol 1,3,4,5-tetrakisphosphate (InsP4).
CC {ECO:0000269|PubMed:10448098, ECO:0000303|PubMed:10333475,
CC ECO:0000305}.
CC -!- SUBUNIT: Interacts with PRKCA, PRKCI and PRKCZ. Interacts with the N-
CC terminal region of PRKD1. {ECO:0000269|PubMed:12893243}.
CC -!- INTERACTION:
CC O75689; Q92997: DVL3; NbExp=3; IntAct=EBI-714732, EBI-739789;
CC O75689; Q08379: GOLGA2; NbExp=3; IntAct=EBI-714732, EBI-618309;
CC O75689; Q9NQT8: KIF13B; NbExp=6; IntAct=EBI-714732, EBI-766408;
CC O75689; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-714732, EBI-742388;
CC O75689; Q9H190: SDCBP2; NbExp=3; IntAct=EBI-714732, EBI-742426;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Recruited to the plasma
CC membrane upon epidermal growth factor-dependent activation of
CC phosphatidylinositol 4,5-diphosphate (PtdInsP2) 3-kinase.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O75689-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75689-2; Sequence=VSP_054794;
CC Name=3;
CC IsoId=O75689-3; Sequence=VSP_054793;
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in brain and at lower
CC levels in peripheral blood leukocytes. {ECO:0000269|PubMed:10448098}.
CC -!- PTM: Phosphorylated by PRKCA, PRKCI, PRKCZ and PRKD1 in vitro.
CC {ECO:0000269|PubMed:12893243}.
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DR EMBL; AJ006422; CAA07024.1; -; mRNA.
DR EMBL; AF082324; AAD11414.1; -; mRNA.
DR EMBL; AB097049; BAC77402.1; -; mRNA.
DR EMBL; AK300999; BAG62618.1; -; mRNA.
DR EMBL; AC073957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK092471; BAG52556.1; -; mRNA.
DR EMBL; CH236965; EAL23709.1; -; Genomic_DNA.
DR EMBL; CH471144; EAW87183.1; -; Genomic_DNA.
DR EMBL; CH471144; EAW87184.1; -; Genomic_DNA.
DR EMBL; BC033747; AAH33747.1; -; mRNA.
DR CCDS; CCDS5318.1; -. [O75689-1]
DR CCDS; CCDS64576.1; -. [O75689-3]
DR CCDS; CCDS64577.1; -. [O75689-2]
DR PIR; JC7091; JC7091.
DR RefSeq; NP_001271237.1; NM_001284308.1.
DR RefSeq; NP_001271238.1; NM_001284309.1. [O75689-3]
DR RefSeq; NP_001271239.1; NM_001284310.1.
DR RefSeq; NP_001271240.1; NM_001284311.1.
DR RefSeq; NP_006860.1; NM_006869.3. [O75689-1]
DR PDB; 3FEH; X-ray; 1.90 A; A=3-370.
DR PDB; 3FM8; X-ray; 2.30 A; C/D=1-374.
DR PDB; 3LJU; X-ray; 1.70 A; X=3-370.
DR PDB; 3MDB; X-ray; 2.95 A; C/D=1-374.
DR PDBsum; 3FEH; -.
DR PDBsum; 3FM8; -.
DR PDBsum; 3LJU; -.
DR PDBsum; 3MDB; -.
DR AlphaFoldDB; O75689; -.
DR SMR; O75689; -.
DR BioGRID; 116222; 21.
DR DIP; DIP-41731N; -.
DR IntAct; O75689; 11.
DR MINT; O75689; -.
DR STRING; 9606.ENSP00000442682; -.
DR GlyGen; O75689; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75689; -.
DR PhosphoSitePlus; O75689; -.
DR BioMuta; ADAP1; -.
DR EPD; O75689; -.
DR jPOST; O75689; -.
DR MassIVE; O75689; -.
DR MaxQB; O75689; -.
DR PaxDb; O75689; -.
DR PeptideAtlas; O75689; -.
DR PRIDE; O75689; -.
DR ProteomicsDB; 28173; -.
DR ProteomicsDB; 45067; -.
DR ProteomicsDB; 50162; -. [O75689-1]
DR Antibodypedia; 1977; 229 antibodies from 35 providers.
DR DNASU; 11033; -.
DR Ensembl; ENST00000265846.10; ENSP00000265846.5; ENSG00000105963.15. [O75689-1]
DR Ensembl; ENST00000449296.6; ENSP00000407267.2; ENSG00000105963.15. [O75689-3]
DR Ensembl; ENST00000539900.5; ENSP00000442682.1; ENSG00000105963.15. [O75689-2]
DR Ensembl; ENST00000611167.4; ENSP00000481154.1; ENSG00000105963.15. [O75689-3]
DR GeneID; 11033; -.
DR KEGG; hsa:11033; -.
DR MANE-Select; ENST00000265846.10; ENSP00000265846.5; NM_006869.4; NP_006860.2.
DR UCSC; uc003sjn.5; human. [O75689-1]
DR CTD; 11033; -.
DR DisGeNET; 11033; -.
DR GeneCards; ADAP1; -.
DR HGNC; HGNC:16486; ADAP1.
DR HPA; ENSG00000105963; Tissue enhanced (brain, intestine).
DR MIM; 608114; gene.
DR neXtProt; NX_O75689; -.
DR OpenTargets; ENSG00000105963; -.
DR PharmGKB; PA26404; -.
DR VEuPathDB; HostDB:ENSG00000105963; -.
DR eggNOG; KOG0703; Eukaryota.
DR GeneTree; ENSGT00940000155698; -.
DR HOGENOM; CLU_061583_0_0_1; -.
DR InParanoid; O75689; -.
DR OMA; RVPPCYR; -.
DR OrthoDB; 1274375at2759; -.
DR PhylomeDB; O75689; -.
DR TreeFam; TF324540; -.
DR PathwayCommons; O75689; -.
DR Reactome; R-HSA-1251985; Nuclear signaling by ERBB4.
DR SignaLink; O75689; -.
DR SIGNOR; O75689; -.
DR BioGRID-ORCS; 11033; 28 hits in 1068 CRISPR screens.
DR ChiTaRS; ADAP1; human.
DR EvolutionaryTrace; O75689; -.
DR GeneWiki; Centaurin,_alpha_1; -.
DR GenomeRNAi; 11033; -.
DR Pharos; O75689; Tbio.
DR PRO; PR:O75689; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O75689; protein.
DR Bgee; ENSG00000105963; Expressed in C1 segment of cervical spinal cord and 96 other tissues.
DR ExpressionAtlas; O75689; baseline and differential.
DR Genevisible; O75689; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0043533; F:inositol 1,3,4,5 tetrakisphosphate binding; TAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1902936; F:phosphatidylinositol bisphosphate binding; IEA:InterPro.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0043087; P:regulation of GTPase activity; IMP:UniProtKB.
DR CDD; cd13252; PH1_ADAP; 1.
DR CDD; cd01251; PH2_ADAP; 1.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR037849; PH1_ADAP.
DR InterPro; IPR037851; PH2_ADAP.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00169; PH; 2.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 2.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW GTPase activation; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..374
FT /note="Arf-GAP with dual PH domain-containing protein 1"
FT /id="PRO_0000074205"
FT DOMAIN 7..126
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT DOMAIN 129..230
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 252..356
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 21..44
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT MOD_RES 87
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:12893243"
FT MOD_RES 272
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 276
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000269|PubMed:12893243"
FT VAR_SEQ 1..72
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054793"
FT VAR_SEQ 1..27
FT /note="MAKERRRAVLELLQRPGNARCADCGAP -> MFQFVFSRVYCINPARRKWKE
FT FEKMLGCAEEGHASLGR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054794"
FT VARIANT 241
FT /note="G -> S (in dbSNP:rs10256887)"
FT /evidence="ECO:0000269|PubMed:10333475,
FT ECO:0000269|PubMed:12761501, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.3"
FT /id="VAR_047470"
FT MUTAGEN 21
FT /note="C->A: Loss of GTPase-activating activity."
FT /evidence="ECO:0000269|PubMed:10333475"
FT MUTAGEN 24
FT /note="C->A: Loss of GTPase-activating activity."
FT /evidence="ECO:0000269|PubMed:10333475"
FT MUTAGEN 149
FT /note="R->C: 40-45% reduction in PtdInsP2 3-kinase
FT dependent membrane localization. Almost complete loss of
FT PtdInsP2 3-kinase dependent membrane localization; when
FT associated with C-273."
FT /evidence="ECO:0000269|PubMed:10333475,
FT ECO:0000269|PubMed:10448098"
FT MUTAGEN 273
FT /note="R->C: 70% reduction in PtdInsP2 3-kinase dependent
FT membrane localization. Almost complete loss of PtdInsP2 3-
FT kinase dependent membrane localization; when associated
FT with C-149."
FT /evidence="ECO:0000269|PubMed:10333475,
FT ECO:0000269|PubMed:10448098"
FT CONFLICT 215
FT /note="G -> R (in Ref. 5; BAG52556)"
FT /evidence="ECO:0000305"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:3LJU"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:3LJU"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:3LJU"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:3LJU"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:3LJU"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:3LJU"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:3LJU"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:3LJU"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:3LJU"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:3LJU"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:3LJU"
FT HELIX 78..85
FT /evidence="ECO:0007829|PDB:3LJU"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:3LJU"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:3LJU"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:3LJU"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:3LJU"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:3LJU"
FT STRAND 129..139
FT /evidence="ECO:0007829|PDB:3LJU"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3LJU"
FT STRAND 146..154
FT /evidence="ECO:0007829|PDB:3LJU"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:3LJU"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:3LJU"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:3FEH"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:3LJU"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:3LJU"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:3LJU"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:3LJU"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:3LJU"
FT STRAND 204..211
FT /evidence="ECO:0007829|PDB:3LJU"
FT HELIX 215..236
FT /evidence="ECO:0007829|PDB:3LJU"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:3MDB"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:3LJU"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:3LJU"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:3LJU"
FT STRAND 271..278
FT /evidence="ECO:0007829|PDB:3LJU"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:3LJU"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:3LJU"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:3LJU"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:3LJU"
FT STRAND 323..328
FT /evidence="ECO:0007829|PDB:3LJU"
FT STRAND 333..340
FT /evidence="ECO:0007829|PDB:3LJU"
FT HELIX 341..356
FT /evidence="ECO:0007829|PDB:3LJU"
FT HELIX 363..369
FT /evidence="ECO:0007829|PDB:3LJU"
SQ SEQUENCE 374 AA; 43395 MW; 38547281FB09D9B9 CRC64;
MAKERRRAVL ELLQRPGNAR CADCGAPDPD WASYTLGVFI CLSCSGIHRN IPQVSKVKSV
RLDAWEEAQV EFMASHGNDA ARARFESKVP SFYYRPTPSD CQLLREQWIR AKYERQEFIY
PEKQEPYSAG YREGFLWKRG RDNGQFLSRK FVLTEREGAL KYFNRNDAKE PKAVMKIEHL
NATFQPAKIG HPHGLQVTYL KDNSTRNIFI YHEDGKEIVD WFNALRAARF HYLQVAFPGA
GDADLVPKLS RNYLKEGYME KTGPKQTEGF RKRWFTMDDR RLMYFKDPLD AFARGEVFIG
SKESGYTVLH GFPPSTQGHH WPHGITIVTP DRKFLFACET ESDQREWVAA FQKAVDRPML
PQEYAVEAHF KHKP
