PKHN1_HUMAN
ID PKHN1_HUMAN Reviewed; 611 AA.
AC Q494U1; Q494U2; Q5SV98; Q9H0M7;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Pleckstrin homology domain-containing family N member 1;
DE Short=PH domain-containing family N member 1;
DE AltName: Full=Cardiolipin and phosphatidic acid-binding protein {ECO:0000303|PubMed:18191643, ECO:0000303|PubMed:29180010};
GN Name=PLEKHN1;
GN Synonyms=CLPABP {ECO:0000303|PubMed:18191643, ECO:0000303|PubMed:29180010};
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 VARIANT PRO-487.
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
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 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 (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
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 [5]
RP FUNCTION, INTERACTION WITH C1QBP AND ELAVL1, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION AT TYR-302 AND TYR-456, MUTAGENESIS OF TYR-302 AND TYR-456,
RP TISSUE SPECIFICITY, AND DOMAIN PH.
RX PubMed=18191643; DOI=10.1016/j.bbamcr.2007.12.009;
RA Sano E., Shono S., Tashiro K., Konishi H., Yamauchi E., Taniguchi H.;
RT "Novel tyrosine phosphorylated and cardiolipin-binding protein CLPABP
RT functions as mitochondrial RNA granule.";
RL Biochim. Biophys. Acta 1783:1036-1047(2008).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559, AND IDENTIFICATION BY
RP 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 [8]
RP MYRISTOYLATION AT GLY-2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-2.
RX PubMed=25043870; DOI=10.1016/j.ab.2014.07.006;
RA Takamitsu E., Fukunaga K., Iio Y., Moriya K., Utsumi T.;
RT "Cell-free identification of novel N-myristoylated proteins from
RT complementary DNA resources using bioorthogonal myristic acid analogues.";
RL Anal. Biochem. 464:83-93(2014).
RN [9]
RP INTERACTION WITH ELAVL1, AND SUBCELLULAR LOCATION.
RX PubMed=27616329; DOI=10.1016/j.bbalip.2016.09.006;
RA Nishino T., Matsunaga R., Jikihara H., Uchida M., Maeda A., Qi G., Abe T.,
RA Kiyonari H., Tashiro S., Inagaki-Ohara K., Shimamoto F., Konishi H.;
RT "Antagonizing effect of CLPABP on the function of HuR as a regulator of
RT ARE-containing leptin mRNA stability and the effect of its depletion on
RT obesity in old male mouse.";
RL Biochim. Biophys. Acta 1861:1816-1827(2016).
RN [10]
RP FUNCTION, MYRISTOYLATION AT GLY-2, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP GLY-2, AND DOMAIN PH.
RX PubMed=29180010; DOI=10.1016/j.bbrc.2017.11.112;
RA Maeda A., Uchida M., Nishikawa S., Nishino T., Konishi H.;
RT "Role of N-myristoylation in stability and subcellular localization of the
RT CLPABP protein.";
RL Biochem. Biophys. Res. Commun. 495:1249-1256(2018).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH BID.
RX PubMed=29531808; DOI=10.1038/s41420-017-0006-5;
RA Kuriyama S., Tsuji T., Sakuma T., Yamamoto T., Tanaka M.;
RT "PLEKHN1 promotes apoptosis by enhancing Bax-Bak hetero-oligomerization
RT through interaction with Bid in human colon cancer.";
RL Cell. Death. Discov. 4:11-11(2018).
CC -!- FUNCTION: Controls the stability of the leptin mRNA harboring an AU-
CC rich element (ARE) in its 3' UTR, in cooperation with the RNA
CC stabilizer ELAVL1 (PubMed:29180010). Decreases the stability of the
CC leptin mRNA by antagonizing the function of ELAVL1 by inducing its
CC atypical recruitment from the nucleus to the cytosol (By similarity).
CC Binds to cardiolipin (CL), phosphatidic acid (PA), phosphatidylinositol
CC 4-phosphate (PtdIns(4)P) and phosphatidylserine (PS) (PubMed:18191643).
CC Promotes apoptosis by enhancing BAX-BAK hetero-oligomerization via
CC interaction with BID in colon cancer cells (PubMed:29531808) (By
CC similarity). {ECO:0000250|UniProtKB:Q8C886,
CC ECO:0000269|PubMed:18191643, ECO:0000269|PubMed:29180010,
CC ECO:0000269|PubMed:29531808}.
CC -!- SUBUNIT: Found in a complex with cytochrome c mRNA and various
CC ribosomal proteins. Interacts with C1QBP (PubMed:18191643). Interacts
CC with ELAVL1 (PubMed:18191643, PubMed:29531808). Interacts with BID
CC (PubMed:29531808). {ECO:0000269|PubMed:18191643,
CC ECO:0000269|PubMed:29531808}.
CC -!- INTERACTION:
CC Q494U1; Q8NA61: CBY2; NbExp=3; IntAct=EBI-10241513, EBI-741724;
CC Q494U1; O60711: LPXN; NbExp=3; IntAct=EBI-10241513, EBI-744222;
CC Q494U1; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-10241513, EBI-741037;
CC Q494U1; Q04864: REL; NbExp=4; IntAct=EBI-10241513, EBI-307352;
CC Q494U1; Q8HWS3: RFX6; NbExp=3; IntAct=EBI-10241513, EBI-746118;
CC Q494U1; Q86VP1: TAX1BP1; NbExp=4; IntAct=EBI-10241513, EBI-529518;
CC Q494U1; P15884: TCF4; NbExp=4; IntAct=EBI-10241513, EBI-533224;
CC Q494U1; Q13625-3: TP53BP2; NbExp=3; IntAct=EBI-10241513, EBI-10175039;
CC Q494U1; Q13077: TRAF1; NbExp=4; IntAct=EBI-10241513, EBI-359224;
CC Q494U1; P14373: TRIM27; NbExp=3; IntAct=EBI-10241513, EBI-719493;
CC Q494U1; Q5ZXN6: ankX; Xeno; NbExp=7; IntAct=EBI-10241513, EBI-26359852;
CC Q494U1-3; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-12014286, EBI-11096309;
CC Q494U1-3; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-12014286, EBI-357530;
CC Q494U1-3; Q03989: ARID5A; NbExp=3; IntAct=EBI-12014286, EBI-948603;
CC Q494U1-3; P54253: ATXN1; NbExp=6; IntAct=EBI-12014286, EBI-930964;
CC Q494U1-3; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-12014286, EBI-739580;
CC Q494U1-3; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-12014286, EBI-11524851;
CC Q494U1-3; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12014286, EBI-3867333;
CC Q494U1-3; Q5TD97: FHL5; NbExp=3; IntAct=EBI-12014286, EBI-750641;
CC Q494U1-3; P49639: HOXA1; NbExp=3; IntAct=EBI-12014286, EBI-740785;
CC Q494U1-3; Q15323: KRT31; NbExp=3; IntAct=EBI-12014286, EBI-948001;
CC Q494U1-3; O76013-2: KRT36; NbExp=3; IntAct=EBI-12014286, EBI-11958506;
CC Q494U1-3; P78385: KRT83; NbExp=3; IntAct=EBI-12014286, EBI-10221390;
CC Q494U1-3; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-12014286, EBI-11749135;
CC Q494U1-3; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-12014286, EBI-12805508;
CC Q494U1-3; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-12014286, EBI-11962084;
CC Q494U1-3; O60711: LPXN; NbExp=3; IntAct=EBI-12014286, EBI-744222;
CC Q494U1-3; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-12014286, EBI-11522433;
CC Q494U1-3; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-12014286, EBI-10271199;
CC Q494U1-3; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-12014286, EBI-22310682;
CC Q494U1-3; Q9NR12: PDLIM7; NbExp=3; IntAct=EBI-12014286, EBI-350517;
CC Q494U1-3; Q9NWS0: PIH1D1; NbExp=3; IntAct=EBI-12014286, EBI-357318;
CC Q494U1-3; Q5JR12: PPM1J; NbExp=3; IntAct=EBI-12014286, EBI-13292717;
CC Q494U1-3; Q96T49: PPP1R16B; NbExp=3; IntAct=EBI-12014286, EBI-10293968;
CC Q494U1-3; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-12014286, EBI-12000762;
CC Q494U1-3; P54646: PRKAA2; NbExp=3; IntAct=EBI-12014286, EBI-1383852;
CC Q494U1-3; P49023-2: PXN; NbExp=3; IntAct=EBI-12014286, EBI-11954250;
CC Q494U1-3; Q04864-2: REL; NbExp=3; IntAct=EBI-12014286, EBI-10829018;
CC Q494U1-3; O60504: SORBS3; NbExp=3; IntAct=EBI-12014286, EBI-741237;
CC Q494U1-3; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-12014286, EBI-529518;
CC Q494U1-3; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-12014286, EBI-11952721;
CC Q494U1-3; Q13077: TRAF1; NbExp=3; IntAct=EBI-12014286, EBI-359224;
CC Q494U1-3; Q15654: TRIP6; NbExp=3; IntAct=EBI-12014286, EBI-742327;
CC Q494U1-3; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-12014286, EBI-11975223;
CC Q494U1-3; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-12014286, EBI-12040603;
CC Q494U1-3; Q9NQZ6: ZC4H2; NbExp=3; IntAct=EBI-12014286, EBI-747993;
CC Q494U1-3; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-12014286, EBI-11962468;
CC Q494U1-3; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-12014286, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25043870};
CC Lipid-anchor {ECO:0000269|PubMed:25043870}. Mitochondrion
CC {ECO:0000269|PubMed:27616329, ECO:0000269|PubMed:29531808}.
CC Mitochondrion membrane {ECO:0000269|PubMed:18191643,
CC ECO:0000269|PubMed:29180010}. Note=Interaction with C1QBP and
CC phosphorylation is essential for its mitochondrial localization.
CC Localizes on the microtubule in the form of small granules.
CC {ECO:0000269|PubMed:18191643}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q494U1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q494U1-2; Sequence=VSP_059838, VSP_059839;
CC Name=3;
CC IsoId=Q494U1-3; Sequence=VSP_059839, VSP_059840;
CC -!- TISSUE SPECIFICITY: Ubiquitous (PubMed:18191643). Epressed in several
CC cancer cell lines of differing origin (PubMed:29531808).
CC {ECO:0000269|PubMed:18191643, ECO:0000269|PubMed:29531808}.
CC -!- INDUCTION: Up-regulated by hypoxia. {ECO:0000269|PubMed:29531808}.
CC -!- DOMAIN: Both PH domains are essential for its mitochondrial
CC localization. {ECO:0000269|PubMed:18191643,
CC ECO:0000269|PubMed:29180010}.
CC -!- PTM: Phosphorylation is essential for its mitochondrial localization
CC and regulates its interaction with C1QBP.
CC {ECO:0000269|PubMed:18191643}.
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DR EMBL; AL136730; CAB66664.1; -; mRNA.
DR EMBL; AL645608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471183; EAW56299.1; -; Genomic_DNA.
DR EMBL; BC101386; AAI01387.1; -; mRNA.
DR EMBL; BC101387; AAI01388.1; -; mRNA.
DR CCDS; CCDS4.1; -. [Q494U1-1]
DR CCDS; CCDS53256.1; -. [Q494U1-3]
DR RefSeq; NP_001153656.1; NM_001160184.1. [Q494U1-3]
DR RefSeq; NP_115505.2; NM_032129.2. [Q494U1-1]
DR AlphaFoldDB; Q494U1; -.
DR SMR; Q494U1; -.
DR BioGRID; 123864; 55.
DR IntAct; Q494U1; 54.
DR MINT; Q494U1; -.
DR STRING; 9606.ENSP00000368720; -.
DR iPTMnet; Q494U1; -.
DR PhosphoSitePlus; Q494U1; -.
DR BioMuta; PLEKHN1; -.
DR DMDM; 160419245; -.
DR EPD; Q494U1; -.
DR jPOST; Q494U1; -.
DR MassIVE; Q494U1; -.
DR MaxQB; Q494U1; -.
DR PeptideAtlas; Q494U1; -.
DR PRIDE; Q494U1; -.
DR ProteomicsDB; 61938; -. [Q494U1-1]
DR ProteomicsDB; 61939; -. [Q494U1-2]
DR ProteomicsDB; 61940; -. [Q494U1-3]
DR Antibodypedia; 51118; 10 antibodies from 6 providers.
DR DNASU; 84069; -.
DR Ensembl; ENST00000379407.7; ENSP00000368717.2; ENSG00000187583.11. [Q494U1-3]
DR Ensembl; ENST00000379409.6; ENSP00000368719.2; ENSG00000187583.11. [Q494U1-2]
DR Ensembl; ENST00000379410.8; ENSP00000368720.3; ENSG00000187583.11. [Q494U1-1]
DR GeneID; 84069; -.
DR KEGG; hsa:84069; -.
DR MANE-Select; ENST00000379410.8; ENSP00000368720.3; NM_032129.3; NP_115505.2.
DR UCSC; uc001acd.4; human. [Q494U1-1]
DR CTD; 84069; -.
DR DisGeNET; 84069; -.
DR GeneCards; PLEKHN1; -.
DR HGNC; HGNC:25284; PLEKHN1.
DR HPA; ENSG00000187583; Group enriched (esophagus, skin, vagina).
DR neXtProt; NX_Q494U1; -.
DR OpenTargets; ENSG00000187583; -.
DR PharmGKB; PA142671166; -.
DR VEuPathDB; HostDB:ENSG00000187583; -.
DR eggNOG; ENOG502QSRE; Eukaryota.
DR GeneTree; ENSGT00390000003618; -.
DR HOGENOM; CLU_031048_0_0_1; -.
DR InParanoid; Q494U1; -.
DR OMA; SQCVPQA; -.
DR OrthoDB; 474079at2759; -.
DR PhylomeDB; Q494U1; -.
DR TreeFam; TF316105; -.
DR PathwayCommons; Q494U1; -.
DR SignaLink; Q494U1; -.
DR BioGRID-ORCS; 84069; 102 hits in 1061 CRISPR screens.
DR GenomeRNAi; 84069; -.
DR Pharos; Q494U1; Tbio.
DR PRO; PR:Q494U1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q494U1; protein.
DR Bgee; ENSG00000187583; Expressed in lower esophagus mucosa and 117 other tissues.
DR ExpressionAtlas; Q494U1; baseline and differential.
DR Genevisible; Q494U1; HS.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1901612; F:cardiolipin binding; IDA:UniProtKB.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:UniProtKB.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IDA:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
DR CDD; cd13323; PH_PLEKHN1; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR042835; PLEKHN1.
DR InterPro; IPR037839; PLEKHN1_PH.
DR PANTHER; PTHR46882; PTHR46882; 1.
DR SMART; SM00233; PH; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Lipoprotein; Membrane; Mitochondrion;
KW Myristate; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25043870,
FT ECO:0000269|PubMed:29180010"
FT CHAIN 2..611
FT /note="Pleckstrin homology domain-containing family N
FT member 1"
FT /id="PRO_0000309363"
FT DOMAIN 96..192
FT /note="PH 1"
FT DOMAIN 222..319
FT /note="PH 2"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..100
FT /note="Interaction with C1QBP"
FT /evidence="ECO:0000269|PubMed:18191643"
FT REGION 323..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 302
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18191643"
FT MOD_RES 456
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18191643"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25043870,
FT ECO:0000269|PubMed:29180010"
FT VAR_SEQ 162
FT /note="G -> GVWDASRAPRGTPDPGLGEGPALWLRSTCVYVCALSALPAG (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_059838"
FT VAR_SEQ 204
FT /note="Q -> QGSCGDELPWTLQ (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_059839"
FT VAR_SEQ 385..431
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_059840"
FT VARIANT 487
FT /note="R -> P (in dbSNP:rs3829740)"
FT /evidence="ECO:0000269|PubMed:11230166"
FT /id="VAR_036946"
FT MUTAGEN 2
FT /note="G->A: Loss of myristoylation, reduced protein
FT stability, morphological alterations in mitochondria but no
FT effect on its mitochondrial localization. Loss of cell
FT membrane localization leading to localization to
FT intracellular organelles."
FT /evidence="ECO:0000269|PubMed:25043870,
FT ECO:0000269|PubMed:29180010"
FT MUTAGEN 302
FT /note="Y->F: Loss of phosphorylation and interaction with
FT C1QBP; when associated with F-456."
FT /evidence="ECO:0000269|PubMed:18191643"
FT MUTAGEN 456
FT /note="Y->F: Loss of phosphorylation and interaction with
FT C1QBP; when associated with F-302."
FT /evidence="ECO:0000269|PubMed:18191643"
FT CONFLICT 560
FT /note="P -> S (in Ref. 4; AAI01388)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 611 AA; 66409 MW; 4163BA09DF9525C9 CRC64;
MGNSHCVPQA PRRLRASFSR KPSLKGNRED SARMSAGLPG PEAARSGDAA ANKLFHYIPG
TDILDLENQR ENLEQPFLSV FKKGRRRVPV RNLGKVVHYA KVQLRFQHSQ DVSDCYLELF
PAHLYFQAHG SEGLTFQGLL PLTELSVCPL EGSREHAFQI TGPLPAPLLV LCPSRAELDR
WLYHLEKQTA LLGGPRRCHS APPQRRLTRL RTASGHEPGG SAVCASRVKL QHLPAQEQWD
RLLVLYPTSL AIFSEELDGL CFKGELPLRA VHINLEEKEK QIRSFLIEGP LINTIRVVCA
SYEDYGHWLL CLRAVTHREG APPLPGAESF PGSQVMGSGR GSLSSGGQTS WDSGCLAPPS
TRTSHSLPES SVPSTVGCSS QHTPDQANSD RASIGRRRTE LRRSGSSRSP GSKARAEGRG
PVTPLHLDLT QLHRLSLESS PDAPDHTSET SHSPLYADPY TPPATSHRRV TDVRGLEEFL
SAMQSARGPT PSSPLPSVPV SVPASDPRSC SSGPAGPYLL SKKGALQSRA AQRHRGSAKD
GGPQPPDAPQ LVSSAREGSP EPWLPLTDGR SPRRSRDPGY DHLWDETLSS SHQKCPQLGG
PEASGGLVQW I
