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 24-JAN-2024, entry version 164. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ILE-43 AND 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., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT 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., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., 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., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., 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., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., 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 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 project: RT 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 phosphorylation RT 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 AND RP SER-940, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 SCALE RP 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). 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 -!- INTERACTION: CC Q9Y2H5; Q9H832: UBE2Z; NbExp=3; IntAct=EBI-1171228, EBI-720977; CC -!- TISSUE SPECIFICITY: Highly expressed in heart, kidney and throughout CC 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 PDB; 2D9Y; NMR; -; A=57-160. DR PDB; 2YRY; NMR; -; A=46-160. DR PDBsum; 2D9Y; -. DR PDBsum; 2YRY; -. DR AlphaFoldDB; Q9Y2H5; -. DR BMRB; Q9Y2H5; -. DR SMR; Q9Y2H5; -. DR BioGRID; 116541; 51. DR IntAct; Q9Y2H5; 8. DR MINT; Q9Y2H5; -. DR STRING; 9606.ENSP00000272203; -. DR GlyGen; Q9Y2H5; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q9Y2H5; -. DR PhosphoSitePlus; Q9Y2H5; -. DR SwissPalm; Q9Y2H5; -. DR BioMuta; PLEKHA6; -. DR DMDM; 160334379; -. DR EPD; Q9Y2H5; -. DR jPOST; Q9Y2H5; -. DR MassIVE; Q9Y2H5; -. DR MaxQB; Q9Y2H5; -. DR PaxDb; 9606-ENSP00000272203; -. DR PeptideAtlas; Q9Y2H5; -. DR ProteomicsDB; 85784; -. DR Pumba; Q9Y2H5; -. DR Antibodypedia; 34556; 118 antibodies from 20 providers. DR DNASU; 22874; -. DR Ensembl; ENST00000272203.8; ENSP00000272203.2; ENSG00000143850.16. DR GeneID; 22874; -. DR KEGG; hsa:22874; -. DR MANE-Select; ENST00000272203.8; ENSP00000272203.2; NM_014935.5; NP_055750.2. DR UCSC; uc001hau.5; human. DR AGR; HGNC:17053; -. DR CTD; 22874; -. DR DisGeNET; 22874; -. DR GeneCards; PLEKHA6; -. DR HGNC; HGNC:17053; PLEKHA6. DR HPA; ENSG00000143850; Low tissue specificity. DR MIM; 607771; gene. DR neXtProt; NX_Q9Y2H5; -. DR OpenTargets; ENSG00000143850; -. DR PharmGKB; PA134955964; -. DR VEuPathDB; HostDB:ENSG00000143850; -. DR eggNOG; ENOG502QQHD; Eukaryota. DR GeneTree; ENSGT00940000159692; -. DR HOGENOM; CLU_008216_0_0_1; -. DR InParanoid; Q9Y2H5; -. DR OrthoDB; 4609983at2759; -. DR PhylomeDB; Q9Y2H5; -. DR TreeFam; TF329090; -. DR PathwayCommons; Q9Y2H5; -. DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane. DR SignaLink; Q9Y2H5; -. DR BioGRID-ORCS; 22874; 6 hits in 1143 CRISPR screens. DR ChiTaRS; PLEKHA6; human. DR EvolutionaryTrace; Q9Y2H5; -. DR GeneWiki; PLEKHA6; -. DR GenomeRNAi; 22874; -. DR Pharos; Q9Y2H5; Tbio. DR PRO; PR:Q9Y2H5; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9Y2H5; Protein. DR Bgee; ENSG00000143850; Expressed in C1 segment of cervical spinal cord and 161 other cell types or tissues. DR ExpressionAtlas; Q9Y2H5; baseline and differential. DR Genevisible; Q9Y2H5; HS. DR CDD; cd13248; PH_PEPP1_2_3; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR040392; PKHA4-7_PH. DR PANTHER; PTHR12752; PHOSPHOINOSITOL 3-PHOSPHATE-BINDING PROTEIN; 1. DR PANTHER; PTHR12752:SF5; PLECKSTRIN HOMOLOGY DOMAIN-CONTAINING FAMILY A MEMBER 6; 1. DR Pfam; PF00169; PH; 1. DR SMART; SM00233; PH; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Phosphoprotein; Reference proteome. FT CHAIN 1..1048 FT /note="Pleckstrin homology domain-containing family A FT member 6" FT /id="PRO_0000053884" FT DOMAIN 59..158 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT REGION 1..36 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 165..318 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 448..467 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 663..746 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 793..858 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 968..989 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1005..1048 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..21 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 171..185 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 201..232 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 269..289 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 682..727 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 819..833 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1018..1032 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 247 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7TQG1" FT MOD_RES 251 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7TQG1" FT MOD_RES 314 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7TQG1" FT MOD_RES 459 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 461 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 472 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 492 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q7TQG1" FT MOD_RES 591 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 744 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q7TQG1" FT MOD_RES 777 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 784 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q7TQG1" FT MOD_RES 801 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7TQG1" FT MOD_RES 848 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243" FT MOD_RES 854 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243" FT MOD_RES 867 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 920 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 940 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1015 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q7TQG1" FT MOD_RES 1017 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1020 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q7TQG1" FT MOD_RES 1021 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7TQG1" FT MOD_RES 1024 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7TQG1" FT VARIANT 43 FT /note="V -> I (in dbSNP:rs10900571)" FT /evidence="ECO:0000269|PubMed:10231032, FT ECO:0000269|PubMed:15489334" FT /id="VAR_037145" FT VARIANT 837 FT /note="R -> K (in dbSNP:rs10900562)" FT /evidence="ECO:0000269|PubMed:10231032, FT ECO:0000269|PubMed:15489334" FT /id="VAR_037146" FT STRAND 62..69 FT /evidence="ECO:0007829|PDB:2D9Y" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:2D9Y" FT STRAND 77..85 FT /evidence="ECO:0007829|PDB:2D9Y" FT STRAND 88..94 FT /evidence="ECO:0007829|PDB:2D9Y" FT STRAND 102..105 FT /evidence="ECO:0007829|PDB:2D9Y" FT STRAND 110..113 FT /evidence="ECO:0007829|PDB:2D9Y" FT TURN 116..119 FT /evidence="ECO:0007829|PDB:2D9Y" FT STRAND 123..129 FT /evidence="ECO:0007829|PDB:2D9Y" FT STRAND 131..133 FT /evidence="ECO:0007829|PDB:2D9Y" FT STRAND 135..139 FT /evidence="ECO:0007829|PDB:2D9Y" FT HELIX 143..155 FT /evidence="ECO:0007829|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 //