ARAP3_HUMAN
ID ARAP3_HUMAN Reviewed; 1544 AA.
AC Q8WWN8; B4DIT1; D3DQE3;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 3;
DE AltName: Full=Centaurin-delta-3;
DE Short=Cnt-d3;
GN Name=ARAP3; Synonyms=CENTD3;
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), MUTAGENESIS OF 307-ARG-ARG-308,
RP FUNCTION, AND INTERACTION WITH PHOSPHATIDYLINOSITOL 3-PHOSPHATE.
RX PubMed=11804589; DOI=10.1016/s1097-2765(02)00434-3;
RA Krugmann S., Anderson K.E., Ridley S.H., Risso N., McGregor A.,
RA Coadwell J., Davidson K., Eguinoa A., Ellson C.D., Lipp P., Manifava M.,
RA Ktistakis N., Painter G., Thuring J.W., Cooper M.A., Lim Z.-Y.,
RA Holmes A.B., Dove S.K., Michell R.H., Grewal A., Nazarian A.,
RA Erdjument-Bromage H., Tempst P., Stephens L.R., Hawkins P.T.;
RT "Identification of ARAP3, a novel PI3K effector regulating both Arf and Rho
RT GTPases, by selective capture on phosphoinositide affinity matrices.";
RL Mol. Cell 9:95-108(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Hippocampus;
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=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP REVIEW.
RX PubMed=12015138; DOI=10.1016/s0960-9822(02)00860-6;
RA Santy L.C., Casanova J.E.;
RT "GTPase signaling: bridging the GAP between ARF and Rho.";
RL Curr. Biol. 12:R360-R362(2002).
RN [6]
RP ROLE IN THE INTERNALIZATION OF ANTHRAX TOXIN.
RX PubMed=15569923; DOI=10.1073/pnas.0407794101;
RA Lu Q., Wei W., Kowalski P.E., Chang A.C.Y., Cohen S.N.;
RT "EST-based genome-wide gene inactivation identifies ARAP3 as a host protein
RT affecting cellular susceptibility to anthrax toxin.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:17246-17251(2004).
RN [7]
RP INTERACTION WITH INPPL1.
RX PubMed=17314030; DOI=10.1016/j.cellsig.2006.12.015;
RA Raaijmakers J.H., Deneubourg L., Rehmann H., de Koning J., Zhang Z.,
RA Krugmann S., Erneux C., Bos J.L.;
RT "The PI3K effector Arap3 interacts with the PI(3,4,5)P3 phosphatase SHIP2
RT in a SAM domain-dependent manner.";
RL Cell. Signal. 19:1249-1257(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1444, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1444 AND SER-1480, AND
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1444, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [11]
RP STRUCTURE BY NMR OF 1-80, AND INTERACTION WITH INPPL1.
RX PubMed=19765305; DOI=10.1186/1472-6807-9-59;
RA Leone M., Cellitti J., Pellecchia M.;
RT "The Sam domain of the lipid phosphatase Ship2 adopts a common model to
RT interact with Arap3-Sam and EphA2-Sam.";
RL BMC Struct. Biol. 9:59-59(2009).
RN [12]
RP VARIANTS [LARGE SCALE ANALYSIS] TRP-471; MET-1085 AND PRO-1428.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-
CC activating protein that modulates actin cytoskeleton remodeling by
CC regulating ARF and RHO family members. Is activated by
CC phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can
CC be activated by phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2)
CC binding, albeit with lower efficiency. Acts on ARF6, RAC1, RHOA and
CC CDC42. Plays a role in the internalization of anthrax toxin.
CC {ECO:0000269|PubMed:11804589, ECO:0000269|PubMed:15569923}.
CC -!- SUBUNIT: Interacts (via SAM domain) with INPPL1/SHIP2.
CC {ECO:0000269|PubMed:11804589, ECO:0000269|PubMed:17314030,
CC ECO:0000269|PubMed:19765305}.
CC -!- INTERACTION:
CC Q8WWN8; Q96B97: SH3KBP1; NbExp=4; IntAct=EBI-4402732, EBI-346595;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cell
CC projection, ruffle {ECO:0000250}. Note=Cytoplasmic, and associated with
CC F-actin-rich membrane ruffles and lamellipodia. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WWN8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WWN8-2; Sequence=VSP_056214, VSP_056215;
CC -!- PTM: Tyrosine phosphorylated at a low basal level. PDGF treatment
CC stimulates phosphorylation. Tyrosine phosphorylation is increased in
CC cells that are in the process of becoming attached to a substrate and
CC that start spreading and flattening (By similarity). {ECO:0000250}.
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DR EMBL; AJ310567; CAC83946.1; -; mRNA.
DR EMBL; AK295768; BAG58593.1; -; mRNA.
DR EMBL; AC022420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61904.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61905.1; -; Genomic_DNA.
DR CCDS; CCDS4266.1; -. [Q8WWN8-1]
DR PIR; E59431; E59431.
DR RefSeq; NP_071926.4; NM_022481.5. [Q8WWN8-1]
DR PDB; 2KG5; NMR; -; A=1-80.
DR PDB; 2LNW; NMR; -; B=1404-1412.
DR PDB; 5JCP; X-ray; 2.10 A; A/B=906-1107.
DR PDB; 5JD0; X-ray; 2.30 A; A/B=906-1107.
DR PDB; 7A9B; X-ray; 2.00 A; A/B=1414-1429.
DR PDBsum; 2KG5; -.
DR PDBsum; 2LNW; -.
DR PDBsum; 5JCP; -.
DR PDBsum; 5JD0; -.
DR PDBsum; 7A9B; -.
DR AlphaFoldDB; Q8WWN8; -.
DR SMR; Q8WWN8; -.
DR BioGRID; 122163; 89.
DR IntAct; Q8WWN8; 5.
DR MINT; Q8WWN8; -.
DR STRING; 9606.ENSP00000239440; -.
DR GlyGen; Q8WWN8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WWN8; -.
DR PhosphoSitePlus; Q8WWN8; -.
DR BioMuta; ARAP3; -.
DR DMDM; 73619965; -.
DR EPD; Q8WWN8; -.
DR jPOST; Q8WWN8; -.
DR MassIVE; Q8WWN8; -.
DR MaxQB; Q8WWN8; -.
DR PaxDb; Q8WWN8; -.
DR PeptideAtlas; Q8WWN8; -.
DR PRIDE; Q8WWN8; -.
DR ProteomicsDB; 4328; -.
DR ProteomicsDB; 74915; -. [Q8WWN8-1]
DR Antibodypedia; 27363; 118 antibodies from 30 providers.
DR DNASU; 64411; -.
DR Ensembl; ENST00000239440.9; ENSP00000239440.4; ENSG00000120318.16. [Q8WWN8-1]
DR Ensembl; ENST00000513878.5; ENSP00000421468.1; ENSG00000120318.16. [Q8WWN8-2]
DR GeneID; 64411; -.
DR KEGG; hsa:64411; -.
DR MANE-Select; ENST00000239440.9; ENSP00000239440.4; NM_022481.6; NP_071926.4.
DR UCSC; uc003llm.4; human. [Q8WWN8-1]
DR CTD; 64411; -.
DR DisGeNET; 64411; -.
DR GeneCards; ARAP3; -.
DR HGNC; HGNC:24097; ARAP3.
DR HPA; ENSG00000120318; Low tissue specificity.
DR MIM; 606647; gene.
DR neXtProt; NX_Q8WWN8; -.
DR OpenTargets; ENSG00000120318; -.
DR PharmGKB; PA164715983; -.
DR VEuPathDB; HostDB:ENSG00000120318; -.
DR eggNOG; KOG1117; Eukaryota.
DR GeneTree; ENSGT00940000158869; -.
DR HOGENOM; CLU_002900_0_0_1; -.
DR InParanoid; Q8WWN8; -.
DR OMA; CETVFQS; -.
DR PhylomeDB; Q8WWN8; -.
DR TreeFam; TF105769; -.
DR PathwayCommons; Q8WWN8; -.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR SignaLink; Q8WWN8; -.
DR SIGNOR; Q8WWN8; -.
DR BioGRID-ORCS; 64411; 12 hits in 1077 CRISPR screens.
DR ChiTaRS; ARAP3; human.
DR EvolutionaryTrace; Q8WWN8; -.
DR GeneWiki; CENTD3; -.
DR GenomeRNAi; 64411; -.
DR Pharos; Q8WWN8; Tbio.
DR PRO; PR:Q8WWN8; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8WWN8; protein.
DR Bgee; ENSG00000120318; Expressed in apex of heart and 154 other tissues.
DR ExpressionAtlas; Q8WWN8; baseline and differential.
DR Genevisible; Q8WWN8; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; TAS:UniProtKB.
DR GO; GO:0035021; P:negative regulation of Rac protein signal transduction; IBA:GO_Central.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IBA:GO_Central.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:UniProtKB.
DR CDD; cd04385; RhoGAP_ARAP; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.30.29.30; -; 3.
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; IPR001849; PH_domain.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR037858; RhoGAP_ARAP.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00169; PH; 2.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF07647; SAM_2; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 5.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 3.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Cytoplasm; Cytoskeleton; GTPase activation; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..1544
FT /note="Arf-GAP with Rho-GAP domain, ANK repeat and PH
FT domain-containing protein 3"
FT /id="PRO_0000074215"
FT DOMAIN 4..68
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 287..379
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 394..483
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 480..611
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT DOMAIN 907..1088
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT DOMAIN 1117..1210
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 1223..1325
FT /note="PH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 504..527
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 64..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1422..1544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..98
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1422..1458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1510..1544
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1348
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8R5G7"
FT MOD_RES 1403
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8R5G7"
FT MOD_RES 1408
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8R5G7"
FT MOD_RES 1444
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 1..338
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056214"
FT VAR_SEQ 1371..1383
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056215"
FT VARIANT 218
FT /note="D -> H (in dbSNP:rs1031904)"
FT /id="VAR_048330"
FT VARIANT 471
FT /note="R -> W (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1562420371)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036180"
FT VARIANT 1085
FT /note="I -> M (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036181"
FT VARIANT 1428
FT /note="T -> P (in a breast cancer sample; somatic mutation;
FT dbSNP:rs61749636)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036182"
FT MUTAGEN 307..308
FT /note="RR->AA: Loss of PtdIns(3,4,5)P3 binding."
FT /evidence="ECO:0000269|PubMed:11804589"
FT HELIX 9..13
FT /evidence="ECO:0007829|PDB:2KG5"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:2KG5"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:2KG5"
FT HELIX 22..27
FT /evidence="ECO:0007829|PDB:2KG5"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:2KG5"
FT HELIX 41..47
FT /evidence="ECO:0007829|PDB:2KG5"
FT HELIX 52..62
FT /evidence="ECO:0007829|PDB:2KG5"
FT TURN 63..67
FT /evidence="ECO:0007829|PDB:2KG5"
FT HELIX 909..911
FT /evidence="ECO:0007829|PDB:5JCP"
FT STRAND 918..920
FT /evidence="ECO:0007829|PDB:5JCP"
FT HELIX 921..933
FT /evidence="ECO:0007829|PDB:5JCP"
FT TURN 934..936
FT /evidence="ECO:0007829|PDB:5JCP"
FT TURN 938..942
FT /evidence="ECO:0007829|PDB:5JCP"
FT HELIX 947..960
FT /evidence="ECO:0007829|PDB:5JCP"
FT HELIX 961..963
FT /evidence="ECO:0007829|PDB:5JCP"
FT TURN 968..970
FT /evidence="ECO:0007829|PDB:5JCP"
FT HELIX 973..986
FT /evidence="ECO:0007829|PDB:5JCP"
FT STRAND 987..989
FT /evidence="ECO:0007829|PDB:5JCP"
FT HELIX 994..996
FT /evidence="ECO:0007829|PDB:5JCP"
FT HELIX 997..1004
FT /evidence="ECO:0007829|PDB:5JCP"
FT HELIX 1009..1022
FT /evidence="ECO:0007829|PDB:5JCP"
FT HELIX 1025..1043
FT /evidence="ECO:0007829|PDB:5JCP"
FT HELIX 1045..1048
FT /evidence="ECO:0007829|PDB:5JCP"
FT HELIX 1052..1064
FT /evidence="ECO:0007829|PDB:5JCP"
FT HELIX 1071..1082
FT /evidence="ECO:0007829|PDB:5JCP"
FT HELIX 1084..1087
FT /evidence="ECO:0007829|PDB:5JCP"
FT HELIX 1092..1099
FT /evidence="ECO:0007829|PDB:5JCP"
FT STRAND 1420..1424
FT /evidence="ECO:0007829|PDB:7A9B"
SQ SEQUENCE 1544 AA; 169844 MW; 40C03A22591B2B6F CRC64;
MAAPQDLDIA VWLATVHLEQ YADTFRRHGL ATAGAARGLG HEELKQLGIS ATGHRKRILR
LLQTGTEEGS LDPKSDSAME PSPSPAPQAQ PPKPVPKPRT VFGGLSGPAT TQRPGLSPAL
GGPGVSRSPE PSPRPPPLPT SSSEQSSALN TVEMMPNSIY FGLDSRGRAQ AAQDKAPDSS
QISAPTPALR PTTGTVHIMD PGCLYYGVQP VGTPGAPDRR ESRGVCQGRA EHRLSRQDLE
AREDAGYASL ELPGDSTLLS PTLETEETSD DLISPYASFS FTADRLTPLL SGWLDKLSPQ
GNYVFQRRFV QFNGRSLMYF GSDKDPFPKG VIPLTAIEMT RSSKDNKFQV ITGQRVFVFR
TESEAQRDMW CSTLQSCLKE QRLLGHPRPP QPPRPLRTGM LELRGHKAKV FAALSPGELA
LYKSEQAFSL GIGICFIELQ GCSVRETKSR SFDLLTPHRC FSFTAESGGA RQSWAAALQE
AVTETLSDYE VAEKIWSNRA NRQCADCGSS RPDWAAVNLG VVICKQCAGQ HRALGSGISK
VQSLKLDTSV WSNEIVQLFI VLGNDRANRF WAGTLPPGEG LHPDATPGPR GEFISRKYRL
GLFRKPHPQY PDHSQLLQAL CAAVARPNLL KNMTQLLCVE AFEGEEPWFP PAPDGSCPGL
LPSDPSPGVY NEVVVRATYS GFLYCSPVSN KAGPSPPRRG RDAPPRLWCV LGAALEMFAS
ENSPEPLSLI QPQDIVCLGV SPPPTDPGDR FPFSFELILA GGRIQHFGTD GADSLEAWTS
AVGKWFSPLS CHQLLGPGLL RLGRLWLRSP SHTAPAPGLW LSGFGLLRGD HLFLCSAPGP
GPPAPEDMVH LRRLQEISVV SAADTPDKKE HLVLVETGRT LYLQGEGRLD FTAWNAAIGG
AAGGGGTGLQ EQQMSRGDIP IIVDACISFV TQHGLRLEGV YRKGGARARS LRLLAEFRRD
ARSVKLRPGE HFVEDVTDTL KRFFRELDDP VTSARLLPRW REAAELPQKN QRLEKYKDVI
GCLPRVNRRT LATLIGHLYR VQKCAALNQM CTRNLALLFA PSVFQTDGRG EHEVRVLQEL
IDGYISVFDI DSDQVAQIDL EVSLITTWKD VQLSQAGDLI MEVYIEQQLP DNCVTLKVSP
TLTAEELTNQ VLEMRGTAAG MDLWVTFEIR EHGELERPLH PKEKVLEQAL QWCQLPEPCS
ASLLLKKVPL AQAGCLFTGI RRESPRVGLL RCREEPPRLL GSRFQERFFL LRGRCLLLLK
EKKSSKPERE WPLEGAKVYL GIRKKLKPPT PWGFTLILEK MHLYLSCTDE DEMWDWTTSI
LKAQHDDQQP VVLRRHSSSD LARQKFGTMP LLPIRGDDSG ATLLSANQTL RRLHNRRTLS
MFFPMKSSQG SVEEQEELEE PVYEEPVYEE VGAFPELIQD TSTSFSTTRE WTVKPENPLT
SQKSLDQPFL SKSSTLGQEE RPPEPPPGPP SKSSPQARGS LEEQLLQELS SLILRKGETT
AGLGSPSQPS SPQSPSPTGL PTQTPGFPTQ PPCTSSPPSS QPLT
