PKHA5_HUMAN
ID PKHA5_HUMAN Reviewed; 1116 AA.
AC Q9HAU0; A0JP03; B4DGS1; E9PHQ3; F5H0I0; Q6NSF8; Q86ST7; Q8N3K6; Q96DY9;
AC Q9BVR4; Q9C0H7; Q9H924; Q9NVK8;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Pleckstrin homology domain-containing family A member 5;
DE Short=PH domain-containing family A member 5;
DE AltName: Full=Phosphoinositol 3-phosphate-binding protein 2;
DE Short=PEPP-2;
GN Name=PLEKHA5; Synonyms=KIAA1686, PEPP2;
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), AND TISSUE SPECIFICITY.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), SUBCELLULAR LOCATION, DOMAIN PH,
RP AND ALTERNATIVE SPLICING.
RX PubMed=22037487; DOI=10.1016/j.gene.2011.10.018;
RA Yamada K., Nomura N., Yamano A., Yamada Y., Wakamatsu N.;
RT "Identification and characterization of splicing variants of PLEKHA5
RT (Plekha5) during brain development.";
RL Gene 492:270-275(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 625-1116 (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 664-1116 (ISOFORM 5).
RC TISSUE=Brain, and Teratocarcinoma;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Amygdala;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 7), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 159-1116 (ISOFORM 3).
RC TISSUE=Colon, Lung, and Placenta;
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-933, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-933, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-855 AND SER-933, 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-933, 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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-809 AND SER-855, 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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; SER-382; SER-410;
RP THR-438; THR-460; SER-568; SER-607; SER-809; SER-855; SER-933 AND SER-937,
RP AND IDENTIFICATION BY 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 [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [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).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-301, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [21]
RP STRUCTURE BY NMR OF 156-271.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PH domain of pleckstrin homology domain-
RT containing protein family A member 5 from human.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- INTERACTION:
CC Q9HAU0; P54259: ATN1; NbExp=2; IntAct=EBI-945934, EBI-945980;
CC Q9HAU0; P54253: ATXN1; NbExp=2; IntAct=EBI-945934, EBI-930964;
CC Q9HAU0; Q5EBL8: PDZD11; NbExp=11; IntAct=EBI-945934, EBI-1644207;
CC Q9HAU0; Q9NWB1: RBFOX1; NbExp=2; IntAct=EBI-945934, EBI-945906;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22037487}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1; Synonyms=S;
CC IsoId=Q9HAU0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HAU0-2; Sequence=VSP_009775;
CC Name=3;
CC IsoId=Q9HAU0-3; Sequence=VSP_009776, VSP_014595;
CC Name=4;
CC IsoId=Q9HAU0-4; Sequence=VSP_009778;
CC Name=5;
CC IsoId=Q9HAU0-5; Sequence=VSP_009777;
CC Name=6; Synonyms=L;
CC IsoId=Q9HAU0-6; Sequence=VSP_044678, VSP_009775, VSP_044679,
CC VSP_009778;
CC Name=7;
CC IsoId=Q9HAU0-7; Sequence=VSP_046861;
CC Name=8;
CC IsoId=Q9HAU0-8; Sequence=VSP_047514, VSP_047515, VSP_009778;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart and kidney.
CC {ECO:0000269|PubMed:11001876}.
CC -!- DOMAIN: Specifically interacts with PI3P, PI4P, PI5P, and PI(3,5)P2.
CC {ECO:0000269|PubMed:22037487}.
CC -!- MISCELLANEOUS: [Isoform 6]: Specifically expressed in brain.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH70174.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA91742.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB14419.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB21777.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF302150; AAG22817.1; -; mRNA.
DR EMBL; AB642244; BAL45489.1; -; mRNA.
DR EMBL; AB051473; BAB21777.2; ALT_INIT; mRNA.
DR EMBL; AK001529; BAA91742.1; ALT_FRAME; mRNA.
DR EMBL; AK023127; BAB14419.1; ALT_INIT; mRNA.
DR EMBL; AK294739; BAG57882.1; -; mRNA.
DR EMBL; AL834259; CAD38934.1; -; mRNA.
DR EMBL; AC024902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471094; EAW96393.1; -; Genomic_DNA.
DR EMBL; BC000969; AAH00969.1; -; mRNA.
DR EMBL; BC044245; AAH44245.1; -; mRNA.
DR EMBL; BC070174; AAH70174.1; ALT_SEQ; mRNA.
DR EMBL; BC013133; AAH13133.3; -; mRNA.
DR EMBL; BC127092; AAI27093.1; -; mRNA.
DR CCDS; CCDS44840.2; -. [Q9HAU0-2]
DR CCDS; CCDS55809.1; -. [Q9HAU0-7]
DR CCDS; CCDS58213.1; -. [Q9HAU0-6]
DR CCDS; CCDS58214.1; -. [Q9HAU0-8]
DR CCDS; CCDS8682.1; -. [Q9HAU0-1]
DR RefSeq; NP_001137293.2; NM_001143821.2. [Q9HAU0-2]
DR RefSeq; NP_001177789.2; NM_001190860.2. [Q9HAU0-7]
DR RefSeq; NP_001243399.1; NM_001256470.1. [Q9HAU0-6]
DR RefSeq; NP_001243716.1; NM_001256787.1. [Q9HAU0-8]
DR RefSeq; NP_061885.2; NM_019012.5. [Q9HAU0-1]
DR RefSeq; XP_005253457.1; XM_005253400.1. [Q9HAU0-4]
DR RefSeq; XP_011519019.1; XM_011520717.1. [Q9HAU0-2]
DR RefSeq; XP_016874992.1; XM_017019503.1. [Q9HAU0-7]
DR PDB; 2DKP; NMR; -; A=157-271.
DR PDBsum; 2DKP; -.
DR AlphaFoldDB; Q9HAU0; -.
DR BMRB; Q9HAU0; -.
DR SMR; Q9HAU0; -.
DR BioGRID; 119982; 187.
DR IntAct; Q9HAU0; 65.
DR MINT; Q9HAU0; -.
DR GlyConnect; 2872; 1 O-Linked glycan (1 site).
DR GlyGen; Q9HAU0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9HAU0; -.
DR PhosphoSitePlus; Q9HAU0; -.
DR BioMuta; PLEKHA5; -.
DR DMDM; 48474955; -.
DR EPD; Q9HAU0; -.
DR jPOST; Q9HAU0; -.
DR MassIVE; Q9HAU0; -.
DR MaxQB; Q9HAU0; -.
DR PeptideAtlas; Q9HAU0; -.
DR PRIDE; Q9HAU0; -.
DR ProteomicsDB; 20581; -.
DR ProteomicsDB; 25347; -.
DR ProteomicsDB; 69632; -.
DR ProteomicsDB; 81434; -. [Q9HAU0-1]
DR ProteomicsDB; 81435; -. [Q9HAU0-2]
DR ProteomicsDB; 81436; -. [Q9HAU0-3]
DR ProteomicsDB; 81437; -. [Q9HAU0-4]
DR ProteomicsDB; 81438; -. [Q9HAU0-5]
DR TopDownProteomics; Q9HAU0-3; -. [Q9HAU0-3]
DR Antibodypedia; 23890; 97 antibodies from 26 providers.
DR DNASU; 54477; -.
DR Ensembl; ENST00000299275.10; ENSP00000299275.6; ENSG00000052126.15. [Q9HAU0-1]
DR Ensembl; ENST00000424268.5; ENSP00000400411.2; ENSG00000052126.15. [Q9HAU0-8]
DR Ensembl; ENST00000429027.7; ENSP00000404296.2; ENSG00000052126.15. [Q9HAU0-6]
DR Ensembl; ENST00000538714.5; ENSP00000439673.1; ENSG00000052126.15. [Q9HAU0-2]
DR Ensembl; ENST00000540972.5; ENSP00000439396.1; ENSG00000052126.15. [Q9HAU0-7]
DR GeneID; 54477; -.
DR KEGG; hsa:54477; -.
DR MANE-Select; ENST00000429027.7; ENSP00000404296.2; NM_001256470.2; NP_001243399.1. [Q9HAU0-6]
DR UCSC; uc001rdz.5; human. [Q9HAU0-1]
DR CTD; 54477; -.
DR DisGeNET; 54477; -.
DR GeneCards; PLEKHA5; -.
DR HGNC; HGNC:30036; PLEKHA5.
DR HPA; ENSG00000052126; Low tissue specificity.
DR MIM; 607770; gene.
DR neXtProt; NX_Q9HAU0; -.
DR OpenTargets; ENSG00000052126; -.
DR PharmGKB; PA134949896; -.
DR VEuPathDB; HostDB:ENSG00000052126; -.
DR eggNOG; KOG0940; Eukaryota.
DR GeneTree; ENSGT00940000155728; -.
DR HOGENOM; CLU_2673480_0_0_1; -.
DR InParanoid; Q9HAU0; -.
DR OMA; QEIEMHT; -.
DR OrthoDB; 71844at2759; -.
DR PhylomeDB; Q9HAU0; -.
DR TreeFam; TF329090; -.
DR PathwayCommons; Q9HAU0; -.
DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
DR SignaLink; Q9HAU0; -.
DR BioGRID-ORCS; 54477; 14 hits in 1082 CRISPR screens.
DR ChiTaRS; PLEKHA5; human.
DR EvolutionaryTrace; Q9HAU0; -.
DR GeneWiki; PLEKHA5; -.
DR GenomeRNAi; 54477; -.
DR Pharos; Q9HAU0; Tbio.
DR PRO; PR:Q9HAU0; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9HAU0; protein.
DR Bgee; ENSG00000052126; Expressed in mucosa of paranasal sinus and 202 other tissues.
DR ExpressionAtlas; Q9HAU0; baseline and differential.
DR Genevisible; Q9HAU0; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IBA:GO_Central.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IBA:GO_Central.
DR GO; GO:0061458; P:reproductive system development; IEA:Ensembl.
DR CDD; cd13248; PH_PEPP1_2_3; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR040392; PKHA4-7_PH.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF51045; SSF51045; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..1116
FT /note="Pleckstrin homology domain-containing family A
FT member 5"
FT /id="PRO_0000053883"
FT DOMAIN 10..43
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 56..89
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 169..268
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 140..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..978
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1062
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 438
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 460
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 809
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 855
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 933
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 937
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 301
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..108
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047514"
FT VAR_SEQ 77..1116
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046861"
FT VAR_SEQ 275
FT /note="K -> KRITFNF (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:22037487"
FT /id="VSP_044678"
FT VAR_SEQ 615
FT /note="T -> TPEELTLLLIKLRRQQAELSSIREHTLAQLMQLKLEAHSPKNEILSH
FT HLQRNTIYLDHQ (in isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:11214970,
FT ECO:0000303|PubMed:22037487"
FT /id="VSP_009775"
FT VAR_SEQ 615
FT /note="T -> TMKENEPIITMVHTMIENSALRPQLYQQ (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047515"
FT VAR_SEQ 616..650
FT /note="LSQDEGRGTLYKYRPEEVDIDAKLSRLCEQDKVVH -> WGREKVATATGAA
FT EAVASDTHLPRTGSSSPSLLCV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009776"
FT VAR_SEQ 616
FT /note="L -> MKENEPIITMVHTMIENSALRPQLYQQFLRQKSKISLYCL (in
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:22037487"
FT /id="VSP_044679"
FT VAR_SEQ 651..1116
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014595"
FT VAR_SEQ 785..840
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_009777"
FT VAR_SEQ 800
FT /note="E -> EEEEVVPPRPPLPRSYDFTEQPPIIPPLPSDSSSLLCYSRGPVHLPE
FT EKKMYQVQGYPRNGSHC (in isoform 4, isoform 6 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005, ECO:0000303|PubMed:22037487"
FT /id="VSP_009778"
FT CONFLICT 311
FT /note="K -> R (in Ref. 5; BAG57882)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="S -> T (in Ref. 5; BAG57882)"
FT /evidence="ECO:0000305"
FT CONFLICT 627
FT /note="K -> R (in Ref. 5; BAB14419)"
FT /evidence="ECO:0000305"
FT CONFLICT 736
FT /note="M -> T (in Ref. 5; BAB14419)"
FT /evidence="ECO:0000305"
FT CONFLICT 970
FT /note="P -> S (in Ref. 5; BAA91742)"
FT /evidence="ECO:0000305"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:2DKP"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:2DKP"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:2DKP"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:2DKP"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:2DKP"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:2DKP"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:2DKP"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:2DKP"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:2DKP"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:2DKP"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:2DKP"
FT HELIX 253..267
FT /evidence="ECO:0007829|PDB:2DKP"
SQ SEQUENCE 1116 AA; 127464 MW; 327F792F644B9D48 CRC64;
MAADLNLEWI SLPRSWTYGI TRGGRVFFIN EEAKSTTWLH PVTGEAVVTG HRRQSTDLPT
GWEEAYTFEG ARYYINHNER KVTCKHPVTG QPSQDNCIFV VNEQTVATMT SEEKKERPIS
MINEASNYNV TSDYAVHPMS PVGRTSRASK KVHNFGKRSN SIKRNPNAPV VRRGWLYKQD
STGMKLWKKR WFVLSDLCLF YYRDEKEEGI LGSILLPSFQ IALLTSEDHI NRKYAFKAAH
PNMRTYYFCT DTGKEMELWM KAMLDAALVQ TEPVKRVDKI TSENAPTKET NNIPNHRVLI
KPEIQNNQKN KEMSKIEEKK ALEAEKYGFQ KDGQDRPLTK INSVKLNSLP SEYESGSACP
AQTVHYRPIN LSSSENKIVN VSLADLRGGN RPNTGPLYTE ADRVIQRTNS MQQLEQWIKI
QKGRGHEEET RGVISYQTLP RNMPSHRAQI MARYPEGYRT LPRNSKTRPE SICSVTPSTH
DKTLGPGAEE KRRSMRDDTM WQLYEWQQRQ FYNKQSTLPR HSTLSSPKTM VNISDQTMHS
IPTSPSHGSI AAYQGYSPQR TYRSEVSSPI QRGDVTIDRR HRAHHPKHVY VPDRRSVPAG
LTLQSVSPQS LQGKTLSQDE GRGTLYKYRP EEVDIDAKLS RLCEQDKVVH ALEEKLQQLH
KEKYTLEQAL LSASQEIEMH ADNPAAIQTV VLQRDDLQNG LLSTCRELSR ATAELERAWR
EYDKLEYDVT VTRNQMQEQL DHLGEVQTES AGIQRAQIQK ELWRIQDVME GLSKHKQQRG
TTEIGMIGSK PFSTVKYKNE GPDYRLYKSE PELTTVAEVD ESNGEEKSEP VSEIETSVVK
GSHFPVGVVP PRAKSPTPES STIASYVTLR KTKKMMDLRT ERPRSAVEQL CLAESTRPRM
TVEEQMERIR RHQQACLREK KKGLNVIGAS DQSPLQSPSN LRDNPFRTTQ TRRRDDKELD
TAIRENDVKP DHETPATEIV QLKETEPQNV DFSKELKKTE NISYEMLFEP EPNGVNSVEM
MDKERNKDKM PEDVTFSPQD ETQTANHKPE EHPEENTKNS VDEQEETVIS YESTPEVSRG
NQTMAVKSLS PSPESSASPV PSTQPQLTEG SHFMCV
