PKHO1_HUMAN
ID PKHO1_HUMAN Reviewed; 409 AA.
AC Q53GL0; Q336K5; Q8IZ51; Q9NRV3; Q9UL48;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Pleckstrin homology domain-containing family O member 1;
DE Short=PH domain-containing family O member 1;
DE AltName: Full=C-Jun-binding protein;
DE Short=JBP;
DE AltName: Full=Casein kinase 2-interacting protein 1;
DE Short=CK2-interacting protein 1;
DE Short=CKIP-1;
DE AltName: Full=Osteoclast maturation-associated gene 120 protein;
GN Name=PLEKHO1; Synonyms=CKIP1, OC120; ORFNames=HQ0024c;
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).
RC TISSUE=Lymph node;
RA Kohchi C.;
RT "Identification of a protein that associates with TNF intracellular
RT domain.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Yamane S., Toyosaki-Maeda T., Tsuruta Y., Suzuki R., Ochi T.;
RT "Differential screening of human osteoclast maturation associated genes.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH CK2.
RX PubMed=10799509; DOI=10.1074/jbc.275.19.14295;
RA Bosc D.G., Graham K.C., Saulnier R.B., Zhang C., Prober D., Gietz R.D.,
RA Litchfield D.W.;
RT "Identification and characterization of CKIP-1, a novel pleckstrin homology
RT domain-containing protein that interacts with protein kinase CK2.";
RL J. Biol. Chem. 275:14295-14306(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH JUN AND
RP JUND, CLEAVAGE BY CASPASE-3, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=15706351; DOI=10.1038/sj.emboj.7600532;
RA Zhang L., Xing G., Tie Y., Tang Y., Tian C., Li L., Sun L., Wei H., Zhu Y.,
RA He F.;
RT "Role for the pleckstrin homology domain-containing protein CKIP-1 in AP-1
RT regulation and apoptosis.";
RL EMBO J. 24:766-778(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND PARTIAL NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney, and Muscle;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-409.
RC TISSUE=Fetal liver;
RX PubMed=11483580; DOI=10.1101/gr.175501;
RA Yu Y., Zhang C., Zhou G., Wu S., Qu X., Wei H., Xing G., Dong C., Zhai Y.,
RA Wan J., Ouyang S., Li L., Zhang S., Zhou K., Zhang Y., Wu C., He F.;
RT "Gene expression profiling in human fetal liver and identification of
RT tissue- and developmental-stage-specific genes through compiled expression
RT profiles and efficient cloning of full-length cDNAs.";
RL Genome Res. 11:1392-1403(2001).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CK2.
RX PubMed=11827170; DOI=10.1023/a:1013188101465;
RA Litchfield D.W., Bosc D.G., Canton D.A., Saulnier R.B., Vilk G., Zhang C.;
RT "Functional specialization of CK2 isoforms and characterization of isoform-
RT specific binding partners.";
RL Mol. Cell. Biochem. 227:21-29(2001).
RN [11]
RP SUBCELLULAR LOCATION, INTERACTION WITH CK2, AND MUTAGENESIS OF LYS-42;
RP ARG-44 AND TRP-123.
RX PubMed=15254037; DOI=10.1074/jbc.m407628200;
RA Olsten M.E.K., Canton D.A., Zhang C., Walton P.A., Litchfield D.W.;
RT "The pleckstrin homology domain of CK2 interacting protein-1 is required
RT for interactions and recruitment of protein kinase CK2 to the plasma
RT membrane.";
RL J. Biol. Chem. 279:42114-42127(2004).
RN [12]
RP FUNCTION, INTERACTION WITH PHOSPHATIDYL INOSITOL 3-KINASE, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RX PubMed=14729969; DOI=10.1128/mcb.24.3.1245-1255.2004;
RA Safi A., Vandromme M., Caussanel S., Valdacci L., Baas D., Vidal M.,
RA Brun G., Schaeffer L., Goillot E.;
RT "Role for the pleckstrin homology domain-containing protein CKIP-1 in
RT phosphatidylinositol 3-kinase-regulated muscle differentiation.";
RL Mol. Cell. Biol. 24:1245-1255(2004).
RN [13]
RP FUNCTION, INTERACTION WITH CK2 AND ACTIN CAPPING PROTEINS, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=15831458; DOI=10.1128/mcb.25.9.3519-3534.2005;
RA Canton D.A., Olsten M.E.K., Kim K., Doherty-Kirby A., Lajoie G.,
RA Cooper J.A., Litchfield D.W.;
RT "The pleckstrin homology domain-containing protein CKIP-1 is involved in
RT regulation of cell morphology and the actin cytoskeleton and interaction
RT with actin capping protein.";
RL Mol. Cell. Biol. 25:3519-3534(2005).
RN [14]
RP FUNCTION, INTERACTION WITH ATM, AND SUBCELLULAR LOCATION.
RX PubMed=16325375; DOI=10.1016/j.cellsig.2005.10.017;
RA Zhang L., Tie Y., Tian C., Xing G., Song Y., Zhu Y., Sun Z., He F.;
RT "CKIP-1 recruits nuclear ATM partially to the plasma membrane through
RT interaction with ATM.";
RL Cell. Signal. 18:1386-1395(2006).
RN [15]
RP FUNCTION, INTERACTION WITH ACTIN CAPPING PROTEINS, AND MUTAGENESIS OF
RP ARG-155 AND ARG-157.
RX PubMed=16987810; DOI=10.1074/jbc.m607595200;
RA Canton D.A., Olsten M.E.K., Niederstrasser H., Cooper J.A.,
RA Litchfield D.W.;
RT "The role of CKIP-1 in cell morphology depends on its interaction with
RT actin-capping protein.";
RL J. Biol. Chem. 281:36347-36359(2006).
RN [16]
RP FUNCTION, AND INTERACTION WITH PKB; PTDINS(3,5)P2; PTDINS(4,5)P2 AND
RP PTDINS(3,4,5)P2.
RX PubMed=17942896; DOI=10.1158/0008-5472.can-07-1050;
RA Tokuda E., Fujita N., Oh-hara T., Sato S., Kurata A., Katayama R., Itoh T.,
RA Takenawa T., Miyazono K., Tsuruo T.;
RT "Casein kinase 2-interacting protein-1, a novel Akt pleckstrin homology
RT domain-interacting protein, down-regulates PI3K/Akt signaling and
RT suppresses tumor growth in vivo.";
RL Cancer Res. 67:9666-9676(2007).
RN [17]
RP FUNCTION, INTERACTION WITH IFP35 AND NMI, INDUCTION BY IL2 AND IFNG, TISSUE
RP SPECIFICITY, AND SUBUNIT.
RX PubMed=17197158; DOI=10.1016/j.cellsig.2006.11.002;
RA Zhang L., Tang Y., Tie Y., Tian C., Wang J., Dong Y., Sun Z., He F.;
RT "The PH domain containing protein CKIP-1 binds to IFP35 and Nmi and is
RT involved in cytokine signaling.";
RL Cell. Signal. 19:932-944(2007).
CC -!- FUNCTION: Plays a role in the regulation of the actin cytoskeleton
CC through its interactions with actin capping protein (CP). May function
CC to target CK2 to the plasma membrane thereby serving as an adapter to
CC facilitate the phosphorylation of CP by protein kinase 2 (CK2). Appears
CC to target ATM to the plasma membrane. Appears to also inhibit tumor
CC cell growth by inhibiting AKT-mediated cell-survival. Also implicated
CC in PI3K-regulated muscle differentiation, the regulation of AP-1
CC activity (plasma membrane bound AP-1 regulator that translocates to the
CC nucleus) and the promotion of apoptosis induced by tumor necrosis
CC factor TNF. When bound to PKB, it inhibits it probably by decreasing
CC PKB level of phosphorylation. {ECO:0000269|PubMed:14729969,
CC ECO:0000269|PubMed:15706351, ECO:0000269|PubMed:15831458,
CC ECO:0000269|PubMed:16325375, ECO:0000269|PubMed:16987810,
CC ECO:0000269|PubMed:17197158, ECO:0000269|PubMed:17942896}.
CC -!- SUBUNIT: Heterodimer or homodimer. Interacts with CK2 and actin capping
CC subunits (capping protein CP-alpha and CP-beta). CKIP1 and CK2 together
CC inhibit the activity of actin capping protein at the barbed ends of
CC actin filaments. Interacts with ATM, IFP35, JUN, JUND, NMI and PI3K.
CC Interacts with AKT1, AKT2 and AKT3 (each isozyme of PKB),
CC PtdIns(3,5)P2, PtdIns(4,5)P2 and PtdIns(3,4,5)P2.
CC {ECO:0000269|PubMed:10799509, ECO:0000269|PubMed:11827170,
CC ECO:0000269|PubMed:14729969, ECO:0000269|PubMed:15254037,
CC ECO:0000269|PubMed:15706351, ECO:0000269|PubMed:15831458,
CC ECO:0000269|PubMed:16325375, ECO:0000269|PubMed:16987810,
CC ECO:0000269|PubMed:17197158, ECO:0000269|PubMed:17942896}.
CC -!- INTERACTION:
CC Q53GL0; Q08AM2: ADAM33; NbExp=3; IntAct=EBI-949945, EBI-10225815;
CC Q53GL0; Q12982: BNIP2; NbExp=3; IntAct=EBI-949945, EBI-752094;
CC Q53GL0; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-949945, EBI-12244618;
CC Q53GL0; Q8WVX3-2: C4orf3; NbExp=3; IntAct=EBI-949945, EBI-12003442;
CC Q53GL0; Q96LK0: CEP19; NbExp=3; IntAct=EBI-949945, EBI-741885;
CC Q53GL0; Q4VAQ0: COL8A2; NbExp=3; IntAct=EBI-949945, EBI-10241815;
CC Q53GL0; P78329: CYP4F2; NbExp=3; IntAct=EBI-949945, EBI-1752413;
CC Q53GL0; Q7Z4F1: LRP10; NbExp=3; IntAct=EBI-949945, EBI-2830349;
CC Q53GL0; Q15546: MMD; NbExp=3; IntAct=EBI-949945, EBI-17873222;
CC Q53GL0; Q9H115: NAPB; NbExp=3; IntAct=EBI-949945, EBI-3921185;
CC Q53GL0; P62195: PSMC5; NbExp=10; IntAct=EBI-949945, EBI-357745;
CC Q53GL0; Q9HCE7: SMURF1; NbExp=2; IntAct=EBI-949945, EBI-976466;
CC Q53GL0; Q9HCE7-2: SMURF1; NbExp=4; IntAct=EBI-949945, EBI-9845742;
CC Q53GL0; C9JKN6: THSD7B; NbExp=3; IntAct=EBI-949945, EBI-17192156;
CC Q53GL0; A2RU14: TMEM218; NbExp=3; IntAct=EBI-949945, EBI-10173151;
CC Q53GL0; P01375: TNF; NbExp=3; IntAct=EBI-949945, EBI-359977;
CC Q53GL0; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-949945, EBI-765817;
CC Q53GL0; Q8N609: TRAM1L1; NbExp=3; IntAct=EBI-949945, EBI-11996766;
CC Q53GL0; Q86UF1: TSPAN33; NbExp=3; IntAct=EBI-949945, EBI-12045841;
CC Q53GL0; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-949945, EBI-12195249;
CC Q53GL0; Q93009: USP7; NbExp=3; IntAct=EBI-949945, EBI-302474;
CC Q53GL0; Q15836: VAMP3; NbExp=3; IntAct=EBI-949945, EBI-722343;
CC Q53GL0; O95159: ZFPL1; NbExp=3; IntAct=EBI-949945, EBI-718439;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10799509,
CC ECO:0000269|PubMed:11827170, ECO:0000269|PubMed:14729969,
CC ECO:0000269|PubMed:15254037, ECO:0000269|PubMed:16325375}; Peripheral
CC membrane protein {ECO:0000305|PubMed:14729969}. Nucleus
CC {ECO:0000269|PubMed:10799509, ECO:0000269|PubMed:11827170,
CC ECO:0000269|PubMed:15706351}. Cytoplasm {ECO:0000269|PubMed:15706351}.
CC Note=Predominantly localized to the plasma membrane through the binding
CC to phosphatidylinositol 3-phosphate (PubMed:14729969). In C2C12 cells,
CC with the absence of growth factor, it is found in the nucleus
CC (PubMed:14729969). It rapidly translocates to the plasma membrane after
CC insulin stimulation (PubMed:14729969). In response to TNF, it
CC translocates from the plasma membrane to the cytoplasm and then to the
CC nucleus accompanied by cleavage by caspase-3 (PubMed:15706351).
CC However, the subcellular location is highly dependent of the cell type,
CC and this explains why it is found exclusively at the plasma membrane,
CC in some type of cells (Probable). {ECO:0000269|PubMed:14729969,
CC ECO:0000269|PubMed:15706351, ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q53GL0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q53GL0-2; Sequence=VSP_029282;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in skeletal muscle and heart,
CC moderately in kidney, liver, brain and placenta and sparingly in the
CC pancreas and lung. Easily detectable in cell lines such as MOLT-4,
CC HEK293 and Jurkat. {ECO:0000269|PubMed:17197158}.
CC -!- INDUCTION: Up-regulated by IFNG/IFN-gamma and IL2/interleukin-2 or in
CC C2C12 cells. {ECO:0000269|PubMed:14729969,
CC ECO:0000269|PubMed:17197158}.
CC -!- PTM: C-terminal fragments could be released during apoptosis via
CC caspase-3-dependent cleavage. {ECO:0000269|PubMed:15706351}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF13461.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAQ13826.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF168676; AAF89644.1; -; mRNA.
DR EMBL; AF192912; AAQ13826.1; ALT_INIT; mRNA.
DR EMBL; AF291105; AAK28027.1; -; mRNA.
DR EMBL; AF217956; AAK71509.1; -; mRNA.
DR EMBL; AK222921; BAD96641.1; -; mRNA.
DR EMBL; AL358073; CAI14264.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53580.1; -; Genomic_DNA.
DR EMBL; BC010149; AAH10149.1; -; mRNA.
DR EMBL; BC023533; AAH23533.2; -; mRNA.
DR EMBL; AF073836; AAF13461.1; ALT_INIT; mRNA.
DR CCDS; CCDS945.1; -. [Q53GL0-1]
DR RefSeq; NP_001291651.1; NM_001304722.1.
DR RefSeq; NP_001291652.1; NM_001304723.1.
DR RefSeq; NP_001291653.1; NM_001304724.1.
DR RefSeq; NP_057358.2; NM_016274.5. [Q53GL0-1]
DR RefSeq; XP_016856909.1; XM_017001420.1.
DR PDB; 3AA1; X-ray; 1.90 A; C=148-170.
DR PDBsum; 3AA1; -.
DR AlphaFoldDB; Q53GL0; -.
DR SMR; Q53GL0; -.
DR BioGRID; 119355; 81.
DR DIP; DIP-46903N; -.
DR IntAct; Q53GL0; 82.
DR MINT; Q53GL0; -.
DR STRING; 9606.ENSP00000358120; -.
DR iPTMnet; Q53GL0; -.
DR PhosphoSitePlus; Q53GL0; -.
DR BioMuta; PLEKHO1; -.
DR DMDM; 160419242; -.
DR EPD; Q53GL0; -.
DR jPOST; Q53GL0; -.
DR MassIVE; Q53GL0; -.
DR MaxQB; Q53GL0; -.
DR PaxDb; Q53GL0; -.
DR PeptideAtlas; Q53GL0; -.
DR PRIDE; Q53GL0; -.
DR ProteomicsDB; 62483; -. [Q53GL0-1]
DR ProteomicsDB; 62484; -. [Q53GL0-2]
DR Antibodypedia; 35196; 195 antibodies from 30 providers.
DR DNASU; 51177; -.
DR Ensembl; ENST00000369124.5; ENSP00000358120.4; ENSG00000023902.14. [Q53GL0-1]
DR GeneID; 51177; -.
DR KEGG; hsa:51177; -.
DR MANE-Select; ENST00000369124.5; ENSP00000358120.4; NM_016274.6; NP_057358.2.
DR UCSC; uc001ett.4; human. [Q53GL0-1]
DR CTD; 51177; -.
DR DisGeNET; 51177; -.
DR GeneCards; PLEKHO1; -.
DR HGNC; HGNC:24310; PLEKHO1.
DR HPA; ENSG00000023902; Tissue enhanced (intestine).
DR MIM; 608335; gene.
DR neXtProt; NX_Q53GL0; -.
DR OpenTargets; ENSG00000023902; -.
DR PharmGKB; PA142671167; -.
DR VEuPathDB; HostDB:ENSG00000023902; -.
DR eggNOG; ENOG502QSPU; Eukaryota.
DR GeneTree; ENSGT00530000063760; -.
DR HOGENOM; CLU_052292_0_0_1; -.
DR InParanoid; Q53GL0; -.
DR OMA; KPDRGAT; -.
DR OrthoDB; 929437at2759; -.
DR PhylomeDB; Q53GL0; -.
DR TreeFam; TF333115; -.
DR PathwayCommons; Q53GL0; -.
DR SignaLink; Q53GL0; -.
DR BioGRID-ORCS; 51177; 15 hits in 1087 CRISPR screens.
DR ChiTaRS; PLEKHO1; human.
DR EvolutionaryTrace; Q53GL0; -.
DR GeneWiki; PLEKHO1; -.
DR GenomeRNAi; 51177; -.
DR Pharos; Q53GL0; Tbio.
DR PRO; PR:Q53GL0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q53GL0; protein.
DR Bgee; ENSG00000023902; Expressed in lower esophagus muscularis layer and 166 other tissues.
DR ExpressionAtlas; Q53GL0; baseline and differential.
DR Genevisible; Q53GL0; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0036195; C:muscle cell projection membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle membrane; IBA:GO_Central.
DR GO; GO:0072673; P:lamellipodium morphogenesis; IEA:Ensembl.
DR GO; GO:0007520; P:myoblast fusion; IEA:Ensembl.
DR GO; GO:0051451; P:myoblast migration; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR GO; GO:1901739; P:regulation of myoblast fusion; IBA:GO_Central.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR028452; CKIP-1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR043448; PKHO1/2.
DR PANTHER; PTHR15871; PTHR15871; 1.
DR PANTHER; PTHR15871:SF1; PTHR15871:SF1; 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; Alternative splicing; Cell membrane; Cytoplasm; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Tumor suppressor.
FT CHAIN 1..409
FT /note="Pleckstrin homology domain-containing family O
FT member 1"
FT /id="PRO_0000310423"
FT DOMAIN 21..132
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..193
FT /note="Interaction with capping proteins (CPs)"
FT REGION 136..308
FT /note="Interaction with ATM, CKIP, IFP35 and NMI"
FT /evidence="ECO:0000269|PubMed:16325375,
FT ECO:0000269|PubMed:17197158"
FT REGION 218..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..409
FT /note="Negative regulator of AP-1 activity"
FT REGION 325..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 155
FT /note="Interacts with capping protein"
FT SITE 157
FT /note="Interacts with capping protein"
FT SITE 310..311
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000255"
FT SITE 345..346
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000255"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIY0"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIY0"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BJM5"
FT VAR_SEQ 142..175
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_029282"
FT VARIANT 21
FT /note="P -> A (in dbSNP:rs2306235)"
FT /id="VAR_037034"
FT MUTAGEN 42
FT /note="K->C: No effect on subcellular localization. No
FT effect on subcellular localization; when associated with C-
FT 44. Disruption of membrane localization, loss of
FT phospholipid binding and impaired interaction with CK2;
FT when associated with W-123. Disruption of membrane
FT localization, loss of phospholipid binding and impaired
FT interaction with CK2; when associated with C-44 and W-123."
FT /evidence="ECO:0000269|PubMed:15254037"
FT MUTAGEN 44
FT /note="R->C: No effect on subcellular localization. No
FT effect on subcellular localization; when associated with C-
FT 42. Disruption of membrane localization, loss of
FT phospholipid binding and impaired interaction with CK2;
FT when associated with W-123. Disruption of membrane
FT localization, loss of phospholipid binding and impaired
FT interaction with CK2; when associated with C-42 and W-123."
FT /evidence="ECO:0000269|PubMed:15254037"
FT MUTAGEN 123
FT /note="W->A: Disruption of membrane localization and
FT impaired interaction with CK2. Loss of phospholipid
FT binding; when associated with C-42. Loss of phospholipid
FT binding; when associated with C-44. Disruption of membrane
FT localization, loss of phospholipid binding and impaired
FT interaction with CK2; when associated with C-42 and C-44."
FT /evidence="ECO:0000269|PubMed:15254037"
FT MUTAGEN 133
FT /note="R->A: No effect on binding to capping proteins and
FT loss of phospholipid binding; when associated with A-135
FT and A-137."
FT MUTAGEN 133
FT /note="R->E: No effect on binding to capping proteins; when
FT associated with E-135."
FT MUTAGEN 135
FT /note="K->A: No effect on binding to capping proteins; when
FT associated with A-133 and A-137."
FT MUTAGEN 135
FT /note="K->E: No effect on binding to capping proteins; when
FT associated with E-133."
FT MUTAGEN 137
FT /note="R->A: No effect on binding to capping proteins; when
FT associated with A-133 and A-135."
FT MUTAGEN 155
FT /note="R->A: No change in cell morphology and actin
FT cytoskeleton. Great loss of binding to capping proteins;
FT when associated with A-157. Great loss of binding to
FT capping proteins; when associated with A-157 and A-159."
FT /evidence="ECO:0000269|PubMed:16987810"
FT MUTAGEN 155
FT /note="R->E: No change in cell morphology and actin
FT cytoskeleton. Great loss of binding to capping proteins and
FT no change in cell morphology and actin cytoskeleton; when
FT associated with E-157."
FT /evidence="ECO:0000269|PubMed:16987810"
FT MUTAGEN 157
FT /note="R->A: No change in cell morphology and actin
FT cytoskeleton. Great loss of binding to capping proteins;
FT when associated with A-155. Great loss of binding to
FT capping proteins; when associated with A-155 and A-159."
FT /evidence="ECO:0000269|PubMed:16987810"
FT MUTAGEN 157
FT /note="R->E: No change in cell morphology and actin
FT cytoskeleton. Great loss of binding to capping proteins and
FT no change in cell morphology and actin cytoskeleton; when
FT associated with E-155."
FT /evidence="ECO:0000269|PubMed:16987810"
FT MUTAGEN 159
FT /note="K->A: Great loss of binding to capping proteins;
FT when associated with A-155 and A-157."
FT CONFLICT 1..10
FT /note="MMKKNNSAKR -> VRRCCRGWRSPVFTNPHVSPLSTAPAHWAPGRPAAGSL
FT GLRVSPEPPPERGSLPPGERSPAASKPPSSPS (in Ref. 8; AAH23533)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="R -> H (in Ref. 5; BAD96641)"
FT /evidence="ECO:0000305"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:3AA1"
SQ SEQUENCE 409 AA; 46237 MW; 5077D6B559EB9F78 CRC64;
MMKKNNSAKR GPQDGNQQPA PPEKVGWVRK FCGKGIFREI WKNRYVVLKG DQLYISEKEV
KDEKNIQEVF DLSDYEKCEE LRKSKSRSKK NHSKFTLAHS KQPGNTAPNL IFLAVSPEEK
ESWINALNSA ITRAKNRILD EVTVEEDSYL AHPTRDRAKI QHSRRPPTRG HLMAVASTST
SDGMLTLDLI QEEDPSPEEP TSCAESFRVD LDKSVAQLAG SRRRADSDRI QPSADRASSL
SRPWEKTDKG ATYTPQAPKK LTPTEKGRCA SLEEILSQRD AASARTLQLR AEEPPTPALP
NPGQLSRIQD LVARKLEETQ ELLAEVQGLG DGKRKAKDPP RSPPDSESEQ LLLETERLLG
EASSNWSQAK RVLQEVRELR DLYRQMDLQT PDSHLRQTTP HSQYRKSLM
