PHLB2_HUMAN
ID PHLB2_HUMAN Reviewed; 1253 AA.
AC Q86SQ0; A5PKZ3; Q59EA8; Q68CY3; Q6NT98; Q8N8U8; Q8NAB1; Q8NCU5;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Pleckstrin homology-like domain family B member 2;
DE AltName: Full=Protein LL5-beta;
GN Name=PHLDB2; Synonyms=LL5B;
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, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, INTERACTION WITH FLNC, BINDING TO PTDINS(3,4,5)P3, AND
RP MUTAGENESIS OF 1162-LYS-ARG-1163.
RX PubMed=12376540; DOI=10.1074/jbc.m208352200;
RA Paranavitane V., Coadwell W.J., Eguinoa A., Hawkins P.T., Stephens L.;
RT "LL5beta is a phosphatidylinositol (3,4,5)-trisphosphate sensor that can
RT bind the cytoskeletal adaptor, gamma-filamin.";
RL J. Biol. Chem. 278:1328-1335(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RA Guo J.H., Yu L.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Aortic endothelium;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-1156 (ISOFORM 2), AND VARIANT SER-941.
RC TISSUE=Lung;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-788 (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-787 (ISOFORM 1).
RC TISSUE=Spleen;
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 [8]
RP BINDING TO PHOSPHOINOSITIDES.
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-73; SER-157; SER-212;
RP SER-334; SER-351; SER-384; SER-387; SER-415; SER-468; SER-489; SER-501;
RP SER-513; THR-550; THR-574 AND THR-898, AND IDENTIFICATION BY MASS
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489; SER-501 AND THR-504, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, AND IDENTIFICATION BY
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-334; SER-415; SER-468
RP AND THR-898, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-384; SER-387;
RP SER-420; SER-468 AND THR-550, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Seems to be involved in the assembly of the postsynaptic
CC apparatus. May play a role in acetyl-choline receptor (AChR)
CC aggregation in the postsynaptic membrane (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:12376540}.
CC -!- SUBUNIT: Interacts with FLNC. {ECO:0000269|PubMed:12376540}.
CC -!- INTERACTION:
CC Q86SQ0; P21333: FLNA; NbExp=3; IntAct=EBI-2798483, EBI-350432;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12376540}. Membrane
CC {ECO:0000269|PubMed:12376540}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12376540}. Note=Translocates to the plasma membrane
CC at high levels of PtdIns(3,4,5)P3. At low levels of PtdIns(3,4,5)P3 is
CC translocated to vesicular compartments.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86SQ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86SQ0-2; Sequence=VSP_016745;
CC Name=3;
CC IsoId=Q86SQ0-3; Sequence=VSP_016744, VSP_016745;
CC -!- DOMAIN: The PH domain mediates the binding to phosphoinositides.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH69194.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAD93140.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ496194; CAD42711.1; -; mRNA.
DR EMBL; AF506820; AAM33634.1; -; mRNA.
DR EMBL; AB209903; BAD93140.1; ALT_INIT; mRNA.
DR EMBL; CR749654; CAH18447.1; -; mRNA.
DR EMBL; CH471052; EAW79690.1; -; Genomic_DNA.
DR EMBL; BC069194; AAH69194.1; ALT_SEQ; mRNA.
DR EMBL; BC142678; AAI42679.1; -; mRNA.
DR EMBL; BC150210; AAI50211.1; -; mRNA.
DR EMBL; AK092996; BAC04014.1; -; mRNA.
DR EMBL; AK096151; BAC04713.1; -; mRNA.
DR CCDS; CCDS2962.1; -. [Q86SQ0-2]
DR CCDS; CCDS46885.1; -. [Q86SQ0-3]
DR CCDS; CCDS46886.1; -. [Q86SQ0-1]
DR RefSeq; NP_001127909.1; NM_001134437.1. [Q86SQ0-3]
DR RefSeq; NP_001127910.1; NM_001134438.1. [Q86SQ0-1]
DR RefSeq; NP_001127911.1; NM_001134439.1. [Q86SQ0-1]
DR RefSeq; NP_665696.1; NM_145753.2. [Q86SQ0-2]
DR AlphaFoldDB; Q86SQ0; -.
DR SMR; Q86SQ0; -.
DR BioGRID; 124661; 135.
DR DIP; DIP-42196N; -.
DR IntAct; Q86SQ0; 51.
DR MINT; Q86SQ0; -.
DR STRING; 9606.ENSP00000405405; -.
DR iPTMnet; Q86SQ0; -.
DR PhosphoSitePlus; Q86SQ0; -.
DR BioMuta; PHLDB2; -.
DR DMDM; 84029396; -.
DR EPD; Q86SQ0; -.
DR jPOST; Q86SQ0; -.
DR MassIVE; Q86SQ0; -.
DR MaxQB; Q86SQ0; -.
DR PaxDb; Q86SQ0; -.
DR PeptideAtlas; Q86SQ0; -.
DR PRIDE; Q86SQ0; -.
DR ProteomicsDB; 69604; -. [Q86SQ0-1]
DR ProteomicsDB; 69605; -. [Q86SQ0-2]
DR ProteomicsDB; 69606; -. [Q86SQ0-3]
DR Antibodypedia; 34806; 45 antibodies from 12 providers.
DR DNASU; 90102; -.
DR Ensembl; ENST00000393923.7; ENSP00000377500.3; ENSG00000144824.21. [Q86SQ0-3]
DR Ensembl; ENST00000393925.7; ENSP00000377502.3; ENSG00000144824.21. [Q86SQ0-1]
DR Ensembl; ENST00000412622.5; ENSP00000405292.1; ENSG00000144824.21. [Q86SQ0-2]
DR Ensembl; ENST00000431670.7; ENSP00000405405.2; ENSG00000144824.21. [Q86SQ0-1]
DR Ensembl; ENST00000481953.5; ENSP00000418319.1; ENSG00000144824.21. [Q86SQ0-2]
DR GeneID; 90102; -.
DR KEGG; hsa:90102; -.
DR MANE-Select; ENST00000431670.7; ENSP00000405405.2; NM_001134438.2; NP_001127910.1.
DR UCSC; uc003dyc.4; human. [Q86SQ0-1]
DR CTD; 90102; -.
DR DisGeNET; 90102; -.
DR GeneCards; PHLDB2; -.
DR HGNC; HGNC:29573; PHLDB2.
DR HPA; ENSG00000144824; Low tissue specificity.
DR MIM; 610298; gene.
DR neXtProt; NX_Q86SQ0; -.
DR OpenTargets; ENSG00000144824; -.
DR PharmGKB; PA134884060; -.
DR VEuPathDB; HostDB:ENSG00000144824; -.
DR eggNOG; ENOG502QUWG; Eukaryota.
DR GeneTree; ENSGT00940000156371; -.
DR HOGENOM; CLU_003180_3_0_1; -.
DR InParanoid; Q86SQ0; -.
DR OMA; XEKVKLD; -.
DR OrthoDB; 70229at2759; -.
DR PhylomeDB; Q86SQ0; -.
DR TreeFam; TF329165; -.
DR PathwayCommons; Q86SQ0; -.
DR SignaLink; Q86SQ0; -.
DR BioGRID-ORCS; 90102; 17 hits in 1072 CRISPR screens.
DR ChiTaRS; PHLDB2; human.
DR GeneWiki; PHLDB2; -.
DR GenomeRNAi; 90102; -.
DR Pharos; Q86SQ0; Tbio.
DR PRO; PR:Q86SQ0; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q86SQ0; protein.
DR Bgee; ENSG00000144824; Expressed in left ventricle myocardium and 178 other tissues.
DR ExpressionAtlas; Q86SQ0; baseline and differential.
DR Genevisible; Q86SQ0; HS.
DR GO; GO:0045180; C:basal cortex; IDA:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; IMP:UniProtKB.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IMP:UniProtKB.
DR GO; GO:1903690; P:negative regulation of wound healing, spreading of epidermal cells; IMP:UniProtKB.
DR GO; GO:1904261; P:positive regulation of basement membrane assembly involved in embryonic body morphogenesis; IMP:UniProtKB.
DR GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
DR GO; GO:0010470; P:regulation of gastrulation; IMP:UniProtKB.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IGI:UniProtKB.
DR CDD; cd14673; PH_PHLDB1_2; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037810; PHLDB1/2/3_PH.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1253
FT /note="Pleckstrin homology-like domain family B member 2"
FT /id="PRO_0000053894"
FT DOMAIN 1143..1246
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 584..696
FT /evidence="ECO:0000255"
FT COILED 722..807
FT /evidence="ECO:0000255"
FT COILED 1032..1098
FT /evidence="ECO:0000255"
FT COMPBIAS 19..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1N2"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1N2"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1N2"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1N2"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1N2"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 504
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 550
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 574
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 898
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1
FT /note="M -> MEEEDTKREVPKEDGVGDVQHFDSSKIM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_016744"
FT VAR_SEQ 668..710
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT ECO:0000303|Ref.2"
FT /id="VSP_016745"
FT VARIANT 941
FT /note="P -> S (in dbSNP:rs3749298)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_024760"
FT MUTAGEN 1162..1163
FT /note="KR->AA: Loss of binding to PtdIns(3,4,5)P3."
FT /evidence="ECO:0000269|PubMed:12376540"
FT CONFLICT 96
FT /note="Y -> H (in Ref. 7; BAC04014)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="T -> A (in Ref. 4; CAH18447)"
FT /evidence="ECO:0000305"
FT CONFLICT 585
FT /note="Q -> E (in Ref. 1; CAD42711)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1253 AA; 142158 MW; D0950E96AEE1B020 CRC64;
MEEHSYIQKE LDLQNGSLEE DSVVHSVEND SQNMMESLSP KKYSSSLRFK ANGDYSGSYL
TLSQPVPAKR SPSPLGTSVR SSPSLAKIQG SKQFSYDGTD KNIPMKPPTP LLNTTSSLSG
YPLGRADFDH YTGRDSERAL RLSEKPPYSK YSSRHKSHDN VYSLGGLEGR KASGSLLAMW
NGSSLSDAGP PPISRSGAAS MPSSPKQARK MSIQDSLALQ PKLTRHKELA SENINLRTRK
YSSSSLSHMG AYSRSLPRLY RATENQLTPL SLPPRNSLGN SKRTKLGEKD LPHSVIDNDN
YLNFSSLSSG ALPYKTSASE GNPYVSSTLS VPASPRVARK MLLASTSSCA SDDFDQASYV
GTNPSHSLLA GESDRVFATR RNFSCGSVEF DEADLESLRQ ASGTPQPALR ERKSSISSIS
GRDDLMDYHR RQREERLREQ EMERLERQRL ETILSLCAEY TKPDSRLSTG TTVEDVQKIN
KELEKLQLSD EESVFEEALM SPDTRYRCHR KDSLPDADLA SCGSLSQSSA SFFTPRSTRN
DELLSDLTRT PPPPSSTFPK ASSESSYLSI LPKTPEGISE EQRSQELAAM EETRIVILNN
LEELKQKIKD INDQMDESFR ELDMECALLD GEQKSETTEL MKEKEILDHL NRKIAELEKN
IVGEKTKEKV KLDAEREKLE RLQELYSEQK TQLDNCPESM REQLQQQLKR DADLLDVESK
HFEDLEFQQL EHESRLDEEK ENLTQQLLRE VAEYQRNIVS RKEKISALKK QANHIVQQAQ
REQDHFVKEK NNLIMMLQRE KENLCNLEKK YSSLSGGKGF PVNPNTLKEG YISVNEINEP
CGNSTNLSPS TQFPADADAV ATEPATAVLA SQPQSKEHFR SLEERKKQHK EGLYLSDTLP
RKKTTSSISP HFSSATMGRS ITPKAHLPLG QSNSCGSVLP PSLAAMAKDS ESRRMLRGYN
HQQMSEGHRQ KSEFYNRTAS ESNVYLNSFH YPDHSYKDQA FDTLSLDSSD SMETSISACS
PDNISSASTS NIARIEEMER LLKQAHAEKT RLLESREREM EAKKRALEEE KRRREILEKR
LQEETSQRQK LIEKEVKIRE RQRAQARPLT RYLPVRKEDF DLRSHVETAG HNIDTCYHVS
ITEKTCRGFL IKMGGKIKTW KKRWFVFDRN KRTFSYYADK HETKLKGVIY FQAIEEVYYD
HLKNANKSPN PLLTFSVKTH DRIYYMVAPS PEAMRIWMDV IVTGAEGYTH FLL
