ID PKHA6_HUMAN Reviewed; 1048 AA. AC Q9Y2H5; A7MD51; Q5VTI6; DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 4. DT 10-AUG-2010, entry version 75. DE RecName: Full=Pleckstrin homology domain-containing family A member 6; DE Short=PH domain-containing family A member 6; DE AltName: Full=Phosphoinositol 3-phosphate-binding protein 3; DE Short=PEPP-3; GN Name=PLEKHA6; Synonyms=KIAA0969, PEPP3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ILE-43 AND RP LYS-837. RC TISSUE=Brain; RX MEDLINE=99246063; PubMed=10231032; DOI=10.1093/dnares/6.1.63; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIII. RT The complete sequences of 100 new cDNA clones from brain which code RT for large proteins in vitro."; RL DNA Res. 6:63-70(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ILE-43 AND RP LYS-837. 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-492, AND MASS RP SPECTROMETRY. RC TISSUE=Mammary epithelium; RX PubMed=15951569; DOI=10.1074/mcp.M500089-MCP200; RA Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., RA Lauffenburger D.A., White F.M.; RT "Time-resolved mass spectrometry of tyrosine phosphorylation sites in RT the epidermal growth factor receptor signaling network reveals dynamic RT modules."; RL Mol. Cell. Proteomics 4:1240-1250(2005). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-848 AND SER-854, AND RP MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein RT phosphorylation analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-492, AND MASS RP SPECTROMETRY. RC TISSUE=Lung carcinoma; RX PubMed=18083107; DOI=10.1016/j.cell.2007.11.025; RA Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., RA Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., RA Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., RA Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., RA Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; RT "Global survey of phosphotyrosine signaling identifies oncogenic RT kinases in lung cancer."; RL Cell 131:1190-1203(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-492, AND MASS RP SPECTROMETRY. RC TISSUE=Mammary epithelium; RX PubMed=17389395; DOI=10.1073/pnas.0608638104; RA Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; RT "Multiple reaction monitoring for robust quantitative proteomic RT analysis of cellular signaling networks."; RL Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472; SER-476 AND RP SER-867, AND MASS SPECTROMETRY. 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 STRUCTURE BY NMR OF 57-160. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the PH domain of PEPP-3 from human."; RL Submitted (OCT-2007) to the PDB data bank. CC -!- TISSUE SPECIFICITY: Highly expressed in heart, kidney and CC throughout the brain. CC -!- SIMILARITY: Contains 1 PH domain. CC -!- SEQUENCE CAUTION: CC Sequence=BAA76813.2; Type=Erroneous initiation; 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; AB023186; BAA76813.2; ALT_INIT; mRNA. DR EMBL; AL592114; CAH71228.1; -; Genomic_DNA. DR EMBL; BC152475; AAI52476.1; -; mRNA. DR IPI; IPI00007248; -. DR RefSeq; NP_055750.2; -. DR UniGene; Hs.253146; -. DR PDB; 2D9Y; NMR; -; A=57-160. DR PDB; 2YRY; NMR; -; A=46-160. DR PDBsum; 2D9Y; -. DR PDBsum; 2YRY; -. DR ProteinModelPortal; Q9Y2H5; -. DR STRING; Q9Y2H5; -. DR PhosphoSite; Q9Y2H5; -. DR PRIDE; Q9Y2H5; -. DR Ensembl; ENST00000272203; ENSP00000272203; ENSG00000143850; Homo sapiens. DR GeneID; 22874; -. DR KEGG; hsa:22874; -. DR UCSC; uc001hau.1; human. DR CTD; 22874; -. DR GeneCards; GC01M204187; -. DR H-InvDB; HIX0001495; -. DR HGNC; HGNC:17053; PLEKHA6. DR HPA; HPA028152; -. DR MIM; 607771; gene. DR PharmGKB; PA134955964; -. DR eggNOG; prNOG06108; -. DR HOVERGEN; HBG099912; -. DR OrthoDB; EOG9WQ3NG; -. DR PhylomeDB; Q9Y2H5; -. DR NextBio; 43425; -. DR ArrayExpress; Q9Y2H5; -. DR Bgee; Q9Y2H5; -. DR CleanEx; HS_PLEKHA6; -. DR Genevestigator; Q9Y2H5; -. DR GermOnline; ENSG00000143850; Homo sapiens. DR InterPro; IPR011993; PH_type. DR InterPro; IPR001849; Pleckstrin_homology. DR Gene3D; G3DSA:2.30.29.30; PH_type; 1. DR Pfam; PF00169; PH; 1. DR SMART; SM00233; PH; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Phosphoprotein; Polymorphism. FT CHAIN 1 1048 Pleckstrin homology domain-containing FT family A member 6. FT /FTId=PRO_0000053884. FT DOMAIN 59 158 PH. FT COMPBIAS 162 386 Pro-rich. FT MOD_RES 472 472 Phosphoserine. FT MOD_RES 476 476 Phosphoserine. FT MOD_RES 492 492 Phosphotyrosine. FT MOD_RES 744 744 Phosphothreonine (By similarity). FT MOD_RES 777 777 Phosphoserine (By similarity). FT MOD_RES 801 801 Phosphoserine (By similarity). FT MOD_RES 848 848 Phosphoserine. FT MOD_RES 854 854 Phosphoserine. FT MOD_RES 867 867 Phosphoserine. FT VARIANT 43 43 V -> I (in dbSNP:rs10900571). FT /FTId=VAR_037145. FT VARIANT 837 837 R -> K (in dbSNP:rs10900562). FT /FTId=VAR_037146. FT STRAND 62 69 FT STRAND 73 75 FT STRAND 77 85 FT STRAND 88 94 FT STRAND 102 105 FT STRAND 110 113 FT TURN 116 119 FT STRAND 123 129 FT STRAND 131 133 FT STRAND 135 139 FT HELIX 143 155 SQ SEQUENCE 1048 AA; 117128 MW; 230F7CB49C9DDF32 CRC64; MSNKTGGKRP ATTNSDIPNH NMVSEVPPER PSVRATRTAR KAVAFGKRSH SMKRNPNAPV TKAGWLFKQA SSGVKQWNKR WFVLVDRCLF YYKDEKEESI LGSIPLLSFR VAAVQPSDNI SRKHTFKAEH AGVRTYFFSA ESPEEQEAWI QAMGEAARVQ IPPAQKSVPQ AVRHSHEKPD SENVPPSKHH QQPPHNSLPK PEPEAKTRGE GDGRGCEKAE RRPERPEVKK EPPVKANGLP AGPEPASEPG SPYPEGPRVP GGGEQPAQPN GWQYHSPSRP GSTAFPSQDG ETGGHRRSFP PRTNPDKIAQ RKSSMNQLQQ WVNLRRGVPP PEDLRSPSRF YPVSRRVPEY YGPYSSQYPD DYQYYPPGVR PESICSMPAY DRISPPWALE DKRHAFRNGG GPAYQLREWK EPASYGRQDA TVWIPSPSRQ PVYYDELDAA SSSLRRLSLQ PRSHSVPRSP SQGSYSRARI YSPVRSPSAR FERLPPRSED IYADPAAYVM RRSISSPKVP PYPEVFRDSL HTYKLNEQDT DKLLGKLCEQ NKVVREQDRL VQQLRAEKES LESALMGTHQ ELEMFGSQPA YPEKLRHKKD SLQNQLINIR VELSQATTAL TNSTIEYEHL ESEVSALHDD LWEQLNLDTQ NEVLNRQIQK EIWRIQDVME GLRKNNPSRG TDTAKHRGGL GPSATYSSNS PASPLSSASL TSPLSPFSLV SGSQGSPTKP GSNEPKANYE QSKKDPHQTL PLDTPRDISL VPTRQEVEAE KQAALNKVGV VPPRTKSPTD DEVTPSAVVR RNASGLTNGL SSQERPKSAV FPGEGKVKMS VEEQIDRMRR HQSGSMREKR RSLQLPASPA PDPSPRPAYK VVRRHRSIHE VDISNLEAAL RAEEPGGHAY ETPREEIARL RKMELEPQHY DVDINKELST PDKVLIPERY IDLEPDTPLS PEELKEKQKK VERIKTLIAK SSMQNVVPIG EGDSVDVPQD SESQLQEQEK RIEISCALAT EASRRGRMLS VQCATPSPPT SPASPAPPAN PLSSESPRGA DSSYTMRV //