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 22-NOV-2017, entry version 133. 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 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 SER-848 AND SER-854, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472 AND SER-867, AND RP IDENTIFICATION BY 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-777; SER-867; THR-920 RP AND SER-940, 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459; SER-461; SER-591; RP SER-777 AND SER-1017, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [8] 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 -!- SEQUENCE CAUTION: CC Sequence=BAA76813.2; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC152475; AAI52476.1; -; mRNA. DR CCDS; CCDS1444.1; -. DR RefSeq; NP_055750.2; NM_014935.4. DR RefSeq; XP_005245025.2; XM_005244968.4. 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 SMR; Q9Y2H5; -. DR BioGrid; 116541; 7. DR IntAct; Q9Y2H5; 4. DR STRING; 9606.ENSP00000272203; -. DR iPTMnet; Q9Y2H5; -. DR PhosphoSitePlus; Q9Y2H5; -. DR SwissPalm; Q9Y2H5; -. DR BioMuta; PLEKHA6; -. DR DMDM; 160334379; -. DR EPD; Q9Y2H5; -. DR MaxQB; Q9Y2H5; -. DR PaxDb; Q9Y2H5; -. DR PeptideAtlas; Q9Y2H5; -. DR PRIDE; Q9Y2H5; -. DR DNASU; 22874; -. DR Ensembl; ENST00000272203; ENSP00000272203; ENSG00000143850. DR GeneID; 22874; -. DR KEGG; hsa:22874; -. DR UCSC; uc001hau.5; human. DR CTD; 22874; -. DR DisGeNET; 22874; -. DR EuPathDB; HostDB:ENSG00000143850.12; -. DR GeneCards; PLEKHA6; -. DR H-InvDB; HIX0001495; -. DR HGNC; HGNC:17053; PLEKHA6. DR HPA; HPA028152; -. DR HPA; HPA054311; -. DR MIM; 607771; gene. DR neXtProt; NX_Q9Y2H5; -. DR OpenTargets; ENSG00000143850; -. DR PharmGKB; PA134955964; -. DR eggNOG; ENOG410IKMF; Eukaryota. DR eggNOG; ENOG410ZX2B; LUCA. DR GeneTree; ENSGT00530000063012; -. DR HOGENOM; HOG000115554; -. DR HOVERGEN; HBG099912; -. DR InParanoid; Q9Y2H5; -. DR PhylomeDB; Q9Y2H5; -. DR TreeFam; TF329090; -. DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane. DR ChiTaRS; PLEKHA6; human. DR EvolutionaryTrace; Q9Y2H5; -. DR GeneWiki; PLEKHA6; -. DR GenomeRNAi; 22874; -. DR PRO; PR:Q9Y2H5; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000143850; -. DR CleanEx; HS_PLEKHA6; -. DR ExpressionAtlas; Q9Y2H5; baseline and differential. DR Genevisible; Q9Y2H5; HS. DR Gene3D; 2.30.29.30; -; 1. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR Pfam; PF00169; PH; 1. DR SMART; SM00233; PH; 1. DR SUPFAM; SSF50729; SSF50729; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Phosphoprotein; Polymorphism; KW Reference proteome. FT CHAIN 1 1048 Pleckstrin homology domain-containing FT family A member 6. FT /FTId=PRO_0000053884. FT DOMAIN 59 158 PH. {ECO:0000255|PROSITE- FT ProRule:PRU00145}. FT COMPBIAS 162 386 Pro-rich. FT MOD_RES 247 247 Phosphoserine. FT {ECO:0000250|UniProtKB:Q7TQG1}. FT MOD_RES 251 251 Phosphoserine. FT {ECO:0000250|UniProtKB:Q7TQG1}. FT MOD_RES 314 314 Phosphoserine. FT {ECO:0000250|UniProtKB:Q7TQG1}. FT MOD_RES 459 459 Phosphoserine. FT {ECO:0000244|PubMed:24275569}. FT MOD_RES 461 461 Phosphoserine. FT {ECO:0000244|PubMed:24275569}. FT MOD_RES 472 472 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 492 492 Phosphotyrosine. FT {ECO:0000250|UniProtKB:Q7TQG1}. FT MOD_RES 591 591 Phosphoserine. FT {ECO:0000244|PubMed:24275569}. FT MOD_RES 744 744 Phosphothreonine. FT {ECO:0000250|UniProtKB:Q7TQG1}. FT MOD_RES 777 777 Phosphoserine. FT {ECO:0000244|PubMed:23186163, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 784 784 Phosphothreonine. FT {ECO:0000250|UniProtKB:Q7TQG1}. FT MOD_RES 801 801 Phosphoserine. FT {ECO:0000250|UniProtKB:Q7TQG1}. FT MOD_RES 848 848 Phosphoserine. FT {ECO:0000244|PubMed:16964243}. FT MOD_RES 854 854 Phosphoserine. FT {ECO:0000244|PubMed:16964243}. FT MOD_RES 867 867 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 920 920 Phosphothreonine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 940 940 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 1015 1015 Phosphothreonine. FT {ECO:0000250|UniProtKB:Q7TQG1}. FT MOD_RES 1017 1017 Phosphoserine. FT {ECO:0000244|PubMed:24275569}. FT MOD_RES 1020 1020 Phosphothreonine. FT {ECO:0000250|UniProtKB:Q7TQG1}. FT MOD_RES 1021 1021 Phosphoserine. FT {ECO:0000250|UniProtKB:Q7TQG1}. FT MOD_RES 1024 1024 Phosphoserine. FT {ECO:0000250|UniProtKB:Q7TQG1}. FT VARIANT 43 43 V -> I (in dbSNP:rs10900571). FT {ECO:0000269|PubMed:10231032, FT ECO:0000269|PubMed:15489334}. FT /FTId=VAR_037145. FT VARIANT 837 837 R -> K (in dbSNP:rs10900562). FT {ECO:0000269|PubMed:10231032, FT ECO:0000269|PubMed:15489334}. FT /FTId=VAR_037146. FT STRAND 62 69 {ECO:0000244|PDB:2D9Y}. FT STRAND 73 75 {ECO:0000244|PDB:2D9Y}. FT STRAND 77 85 {ECO:0000244|PDB:2D9Y}. FT STRAND 88 94 {ECO:0000244|PDB:2D9Y}. FT STRAND 102 105 {ECO:0000244|PDB:2D9Y}. FT STRAND 110 113 {ECO:0000244|PDB:2D9Y}. FT TURN 116 119 {ECO:0000244|PDB:2D9Y}. FT STRAND 123 129 {ECO:0000244|PDB:2D9Y}. FT STRAND 131 133 {ECO:0000244|PDB:2D9Y}. FT STRAND 135 139 {ECO:0000244|PDB:2D9Y}. FT HELIX 143 155 {ECO:0000244|PDB:2D9Y}. 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 //