PPR18_HUMAN
ID PPR18_HUMAN Reviewed; 613 AA.
AC Q6NYC8; A2AB01; A2AIB8; A4UBI6; A6NCB7; A8MSS7; B7ZCV7; Q68CK8; Q6ZTV1;
AC Q6ZUJ6; Q8NDQ4; Q8TF52; Q9BRL9;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Phostensin;
DE AltName: Full=Protein phosphatase 1 F-actin cytoskeleton-targeting subunit;
DE AltName: Full=Protein phosphatase 1 regulatory subunit 18;
GN Name=PPP1R18; Synonyms=HKMT1098, KIAA1949;
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 4), FUNCTION (ISOFORM 4), SUBCELLULAR
RP LOCATION (ISOFORM 4), INTERACTION WITH PROTEIN PHOSPHATASE 1, MUTAGENESIS
RP OF ILE-540 AND PHE-542, AND TISSUE SPECIFICITY.
RX PubMed=17374523; DOI=10.1016/j.bbrc.2007.03.026;
RA Kao S.-C., Chen C.-Y., Wang S.-L., Yang J.-J., Hung W.-C., Chen Y.-C.,
RA Lai N.-S., Liu H.-T., Huang H.-L., Chen H.-C., Lin T.-H., Huang H.-B.;
RT "Identification of phostensin, a PP1 F-actin cytoskeleton targeting
RT subunit.";
RL Biochem. Biophys. Res. Commun. 356:594-598(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII. The
RT complete sequences of 50 new cDNA clones which code for large proteins.";
RL DNA Res. 8:319-327(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hepatoblastoma;
RX PubMed=15221005; DOI=10.1038/sj.onc.1207782;
RA Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S.,
RA Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S.,
RA Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A.;
RT "Expression profiling and differential screening between hepatoblastomas
RT and the corresponding normal livers: identification of high expression of
RT the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas.";
RL Oncogene 23:5901-5911(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP ARG-339.
RC TISSUE=Hippocampus, Synovial cell, and Thymus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Cervix;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS GLY-222 AND
RP ARG-339.
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=B-cell, and Testis;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-368, AND
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-224, 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 [12]
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 [13]
RP IDENTIFICATION BY 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-175; SER-195;
RP THR-199; SER-224 AND SER-368, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND IDENTIFICATION BY
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-133; SER-175;
RP SER-195; SER-224; SER-368 AND SER-490, AND IDENTIFICATION BY MASS
RP 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 [17]
RP FUNCTION (ISOFORM 1), INTERACTION WITH PROTEIN PHOSPHATASE 1, AND
RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 4).
RX PubMed=24434620; DOI=10.3390/ijms15011068;
RA Lin Y.S., Huang H.L., Liu W.T., Lin T.H., Huang H.B.;
RT "Identification of the high molecular weight isoform of phostensin.";
RL Int. J. Mol. Sci. 15:1068-1079(2014).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-224, AND
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).
CC -!- FUNCTION: [Isoform 1]: May target protein phosphatase 1 to F-actin
CC cytoskeleton. {ECO:0000269|PubMed:24434620}.
CC -!- FUNCTION: [Isoform 4]: May target protein phosphatase 1 to F-actin
CC cytoskeleton. {ECO:0000269|PubMed:17374523}.
CC -!- SUBUNIT: Interacts with Protein phosphatase 1 (PP1).
CC {ECO:0000269|PubMed:17374523}.
CC -!- INTERACTION:
CC Q6NYC8; Q8N0Z2: ABRA; NbExp=3; IntAct=EBI-2557469, EBI-3893380;
CC Q6NYC8; Q08043: ACTN3; NbExp=3; IntAct=EBI-2557469, EBI-2880652;
CC Q6NYC8; Q8TD16-2: BICD2; NbExp=3; IntAct=EBI-2557469, EBI-11975051;
CC Q6NYC8; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-2557469, EBI-739580;
CC Q6NYC8; Q9H257: CARD9; NbExp=4; IntAct=EBI-2557469, EBI-751319;
CC Q6NYC8; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-2557469, EBI-11530605;
CC Q6NYC8; Q8NA61: CBY2; NbExp=3; IntAct=EBI-2557469, EBI-741724;
CC Q6NYC8; Q68D86: CCDC102B; NbExp=6; IntAct=EBI-2557469, EBI-10171570;
CC Q6NYC8; Q96JN2-2: CCDC136; NbExp=3; IntAct=EBI-2557469, EBI-10171416;
CC Q6NYC8; Q2TAC2: CCDC57; NbExp=3; IntAct=EBI-2557469, EBI-2808286;
CC Q6NYC8; A6NC98: CCDC88B; NbExp=3; IntAct=EBI-2557469, EBI-347573;
CC Q6NYC8; Q86X02: CDR2L; NbExp=3; IntAct=EBI-2557469, EBI-11063830;
CC Q6NYC8; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-2557469, EBI-739624;
CC Q6NYC8; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-2557469, EBI-3866319;
CC Q6NYC8; P17661: DES; NbExp=6; IntAct=EBI-2557469, EBI-1055572;
CC Q6NYC8; Q86YF9: DZIP1; NbExp=3; IntAct=EBI-2557469, EBI-998108;
CC Q6NYC8; Q9Y262: EIF3L; NbExp=3; IntAct=EBI-2557469, EBI-373519;
CC Q6NYC8; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-2557469, EBI-10175124;
CC Q6NYC8; Q5TD97: FHL5; NbExp=3; IntAct=EBI-2557469, EBI-750641;
CC Q6NYC8; A1L4K1: FSD2; NbExp=6; IntAct=EBI-2557469, EBI-5661036;
CC Q6NYC8; Q96CN9: GCC1; NbExp=3; IntAct=EBI-2557469, EBI-746252;
CC Q6NYC8; P14136: GFAP; NbExp=3; IntAct=EBI-2557469, EBI-744302;
CC Q6NYC8; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-2557469, EBI-2548508;
CC Q6NYC8; Q08379: GOLGA2; NbExp=6; IntAct=EBI-2557469, EBI-618309;
CC Q6NYC8; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-2557469, EBI-5916454;
CC Q6NYC8; Q9HD26-2: GOPC; NbExp=3; IntAct=EBI-2557469, EBI-11102276;
CC Q6NYC8; Q4V328: GRIPAP1; NbExp=4; IntAct=EBI-2557469, EBI-717919;
CC Q6NYC8; Q969Y2: GTPBP3; NbExp=3; IntAct=EBI-2557469, EBI-740290;
CC Q6NYC8; P54257: HAP1; NbExp=3; IntAct=EBI-2557469, EBI-712814;
CC Q6NYC8; Q9NSC5: HOMER3; NbExp=6; IntAct=EBI-2557469, EBI-748420;
CC Q6NYC8; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-2557469, EBI-10961706;
CC Q6NYC8; O75031: HSF2BP; NbExp=3; IntAct=EBI-2557469, EBI-7116203;
CC Q6NYC8; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-2557469, EBI-747204;
CC Q6NYC8; Q8N6L0: KASH5; NbExp=6; IntAct=EBI-2557469, EBI-749265;
CC Q6NYC8; Q7L273: KCTD9; NbExp=3; IntAct=EBI-2557469, EBI-4397613;
CC Q6NYC8; A1A4E9: KRT13; NbExp=3; IntAct=EBI-2557469, EBI-10171552;
CC Q6NYC8; P19012: KRT15; NbExp=6; IntAct=EBI-2557469, EBI-739566;
CC Q6NYC8; P08779: KRT16; NbExp=3; IntAct=EBI-2557469, EBI-356410;
CC Q6NYC8; P08727: KRT19; NbExp=3; IntAct=EBI-2557469, EBI-742756;
CC Q6NYC8; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-2557469, EBI-3044087;
CC Q6NYC8; Q15323: KRT31; NbExp=6; IntAct=EBI-2557469, EBI-948001;
CC Q6NYC8; Q14525: KRT33B; NbExp=3; IntAct=EBI-2557469, EBI-1049638;
CC Q6NYC8; O76011: KRT34; NbExp=3; IntAct=EBI-2557469, EBI-1047093;
CC Q6NYC8; O76013-2: KRT36; NbExp=3; IntAct=EBI-2557469, EBI-11958506;
CC Q6NYC8; Q6A162: KRT40; NbExp=3; IntAct=EBI-2557469, EBI-10171697;
CC Q6NYC8; O95751: LDOC1; NbExp=3; IntAct=EBI-2557469, EBI-740738;
CC Q6NYC8; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-2557469, EBI-1216080;
CC Q6NYC8; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-2557469, EBI-741037;
CC Q6NYC8; Q9Y6D9: MAD1L1; NbExp=3; IntAct=EBI-2557469, EBI-742610;
CC Q6NYC8; P28482: MAPK1; NbExp=3; IntAct=EBI-2557469, EBI-959949;
CC Q6NYC8; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2557469, EBI-16439278;
CC Q6NYC8; Q9UJV3-2: MID2; NbExp=6; IntAct=EBI-2557469, EBI-10172526;
CC Q6NYC8; Q96DV4: MRPL38; NbExp=3; IntAct=EBI-2557469, EBI-720441;
CC Q6NYC8; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-2557469, EBI-742948;
CC Q6NYC8; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-2557469, EBI-11522433;
CC Q6NYC8; I6L9F6: NEFL; NbExp=3; IntAct=EBI-2557469, EBI-10178578;
CC Q6NYC8; P07196: NEFL; NbExp=3; IntAct=EBI-2557469, EBI-475646;
CC Q6NYC8; Q5VU43: PDE4DIP; NbExp=3; IntAct=EBI-2557469, EBI-1105124;
CC Q6NYC8; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-2557469, EBI-14066006;
CC Q6NYC8; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-2557469, EBI-742388;
CC Q6NYC8; P62136: PPP1CA; NbExp=5; IntAct=EBI-2557469, EBI-357253;
CC Q6NYC8; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-2557469, EBI-1105153;
CC Q6NYC8; P41219: PRPH; NbExp=3; IntAct=EBI-2557469, EBI-752074;
CC Q6NYC8; O60504: SORBS3; NbExp=3; IntAct=EBI-2557469, EBI-741237;
CC Q6NYC8; Q96EA4: SPDL1; NbExp=3; IntAct=EBI-2557469, EBI-715381;
CC Q6NYC8; O75558: STX11; NbExp=6; IntAct=EBI-2557469, EBI-714135;
CC Q6NYC8; P15884: TCF4; NbExp=3; IntAct=EBI-2557469, EBI-533224;
CC Q6NYC8; Q8IYF3: TEX11; NbExp=3; IntAct=EBI-2557469, EBI-742397;
CC Q6NYC8; Q8IYF3-3: TEX11; NbExp=3; IntAct=EBI-2557469, EBI-11523345;
CC Q6NYC8; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-2557469, EBI-1105213;
CC Q6NYC8; Q12933: TRAF2; NbExp=3; IntAct=EBI-2557469, EBI-355744;
CC Q6NYC8; P36406: TRIM23; NbExp=3; IntAct=EBI-2557469, EBI-740098;
CC Q6NYC8; P14373: TRIM27; NbExp=7; IntAct=EBI-2557469, EBI-719493;
CC Q6NYC8; Q9BYV2: TRIM54; NbExp=6; IntAct=EBI-2557469, EBI-2130429;
CC Q6NYC8; Q9BVG3: TRIM62; NbExp=3; IntAct=EBI-2557469, EBI-6929619;
CC Q6NYC8; Q86WT6: TRIM69; NbExp=3; IntAct=EBI-2557469, EBI-749955;
CC Q6NYC8; Q86WV8: TSC1; NbExp=3; IntAct=EBI-2557469, EBI-12806590;
CC Q6NYC8; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-2557469, EBI-744794;
CC Q6NYC8; P08670: VIM; NbExp=3; IntAct=EBI-2557469, EBI-353844;
CC Q6NYC8; Q8N1B4: VPS52; NbExp=6; IntAct=EBI-2557469, EBI-2799833;
CC Q6NYC8; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-2557469, EBI-12030590;
CC Q6NYC8; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-2557469, EBI-527853;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:24434620}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:17374523}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=110 kDa, phostensin-beta;
CC IsoId=Q6NYC8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NYC8-2; Sequence=VSP_014258, VSP_014259;
CC Name=3;
CC IsoId=Q6NYC8-3; Sequence=VSP_057118, VSP_057119;
CC Name=4; Synonyms=26kDa, phostensin-alpha;
CC IsoId=Q6NYC8-4; Sequence=VSP_057117;
CC -!- TISSUE SPECIFICITY: Isoform 4 is predominantly expressed in leukocytes
CC and spleen. {ECO:0000269|PubMed:17374523}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB85535.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ988947; ABL61261.1; -; mRNA.
DR EMBL; AB075829; BAB85535.1; ALT_INIT; mRNA.
DR EMBL; AB073600; BAD38640.1; -; mRNA.
DR EMBL; AK124880; BAG54110.1; -; mRNA.
DR EMBL; AK125639; BAC86229.1; -; mRNA.
DR EMBL; AK126182; BAC86478.1; -; mRNA.
DR EMBL; AL832318; CAD38613.1; -; mRNA.
DR EMBL; BX647622; CAI46080.1; -; mRNA.
DR EMBL; AL662797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL732442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL845353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX908728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR753328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759873; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR788240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR936878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03318.1; -; Genomic_DNA.
DR EMBL; BC006176; AAH06176.1; -; mRNA.
DR EMBL; BC066644; AAH66644.1; -; mRNA.
DR CCDS; CCDS43444.1; -. [Q6NYC8-1]
DR RefSeq; NP_001128342.1; NM_001134870.1. [Q6NYC8-1]
DR RefSeq; NP_597728.1; NM_133471.3. [Q6NYC8-1]
DR AlphaFoldDB; Q6NYC8; -.
DR SMR; Q6NYC8; -.
DR BioGRID; 128092; 131.
DR IntAct; Q6NYC8; 117.
DR MINT; Q6NYC8; -.
DR STRING; 9606.ENSP00000274853; -.
DR GlyGen; Q6NYC8; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q6NYC8; -.
DR PhosphoSitePlus; Q6NYC8; -.
DR BioMuta; PPP1R18; -.
DR DMDM; 68052323; -.
DR EPD; Q6NYC8; -.
DR jPOST; Q6NYC8; -.
DR MassIVE; Q6NYC8; -.
DR MaxQB; Q6NYC8; -.
DR PaxDb; Q6NYC8; -.
DR PeptideAtlas; Q6NYC8; -.
DR PRIDE; Q6NYC8; -.
DR ProteomicsDB; 66784; -. [Q6NYC8-1]
DR ProteomicsDB; 66785; -. [Q6NYC8-2]
DR Antibodypedia; 55922; 129 antibodies from 25 providers.
DR DNASU; 170954; -.
DR Ensembl; ENST00000274853.8; ENSP00000274853.3; ENSG00000146112.12. [Q6NYC8-1]
DR Ensembl; ENST00000383573.8; ENSP00000373067.4; ENSG00000206485.10.
DR Ensembl; ENST00000399199.7; ENSP00000382150.3; ENSG00000146112.12. [Q6NYC8-1]
DR Ensembl; ENST00000400554.3; ENSP00000383400.3; ENSG00000206485.10.
DR Ensembl; ENST00000437121.2; ENSP00000405234.2; ENSG00000225060.8. [Q6NYC8-1]
DR Ensembl; ENST00000438815.2; ENSP00000413596.2; ENSG00000230341.8. [Q6NYC8-1]
DR Ensembl; ENST00000438945.6; ENSP00000400990.2; ENSG00000234000.8. [Q6NYC8-1]
DR Ensembl; ENST00000443517.2; ENSP00000404066.2; ENSG00000229998.8. [Q6NYC8-1]
DR Ensembl; ENST00000444206.6; ENSP00000416648.2; ENSG00000230341.8. [Q6NYC8-1]
DR Ensembl; ENST00000449705.6; ENSP00000388790.2; ENSG00000229998.8. [Q6NYC8-1]
DR Ensembl; ENST00000451544.6; ENSP00000400129.2; ENSG00000225060.8. [Q6NYC8-1]
DR Ensembl; ENST00000455935.2; ENSP00000412456.2; ENSG00000234000.8. [Q6NYC8-1]
DR Ensembl; ENST00000615527.1; ENSP00000480270.1; ENSG00000146112.12. [Q6NYC8-1]
DR Ensembl; ENST00000615892.4; ENSP00000482578.1; ENSG00000146112.12. [Q6NYC8-4]
DR GeneID; 170954; -.
DR KEGG; hsa:170954; -.
DR MANE-Select; ENST00000274853.8; ENSP00000274853.3; NM_133471.4; NP_597728.1.
DR UCSC; uc003nra.4; human. [Q6NYC8-1]
DR CTD; 170954; -.
DR DisGeNET; 170954; -.
DR GeneCards; PPP1R18; -.
DR HGNC; HGNC:29413; PPP1R18.
DR HPA; ENSG00000146112; Low tissue specificity.
DR MIM; 610990; gene.
DR neXtProt; NX_Q6NYC8; -.
DR OpenTargets; ENSG00000146112; -.
DR PharmGKB; PA134918172; -.
DR VEuPathDB; HostDB:ENSG00000146112; -.
DR eggNOG; ENOG502RY8Q; Eukaryota.
DR GeneTree; ENSGT00530000064035; -.
DR HOGENOM; CLU_1602160_0_0_1; -.
DR InParanoid; Q6NYC8; -.
DR OMA; EWTPRDT; -.
DR PhylomeDB; Q6NYC8; -.
DR TreeFam; TF337604; -.
DR PathwayCommons; Q6NYC8; -.
DR SignaLink; Q6NYC8; -.
DR BioGRID-ORCS; 170954; 27 hits in 1076 CRISPR screens.
DR ChiTaRS; PPP1R18; human.
DR GeneWiki; KIAA1949; -.
DR GenomeRNAi; 170954; -.
DR Pharos; Q6NYC8; Tbio.
DR PRO; PR:Q6NYC8; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q6NYC8; protein.
DR Bgee; ENSG00000146112; Expressed in granulocyte and 96 other tissues.
DR ExpressionAtlas; Q6NYC8; baseline and differential.
DR Genevisible; Q6NYC8; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0019902; F:phosphatase binding; IEA:InterPro.
DR InterPro; IPR025903; Phostensin/Taperin_N_dom.
DR InterPro; IPR025907; Phostensin/Taperin_PP1-bd_dom.
DR InterPro; IPR026671; PPP1R18/Tprn.
DR PANTHER; PTHR21685; PTHR21685; 1.
DR Pfam; PF13914; Phostensin; 1.
DR Pfam; PF13916; Phostensin_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..613
FT /note="Phostensin"
FT /id="PRO_0000050807"
FT REGION 18..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..445
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 199
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BQ30"
FT MOD_RES 457
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BQ30"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BQ30"
FT VAR_SEQ 1..448
FT /note="Missing (in isoform 4)"
FT /id="VSP_057117"
FT VAR_SEQ 1..325
FT /note="Missing (in isoform 3)"
FT /id="VSP_057118"
FT VAR_SEQ 337..377
FT /note="NSGKAREWTPRDIEAQTQKPEPPESAEKLLESPGVEAGEGE -> IMSLAGK
FT GNQHLVTCFPHPVSGGRANCPISTLIQSPWCGWG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014258"
FT VAR_SEQ 378..613
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014259"
FT VAR_SEQ 562..582
FT /note="ELGPEPEVPSAPNPPAAQPDD -> RRRAKLGLSPGEPSPVLGTVEAGPPDP
FT DESAVLLEAIGPVHQNRFIRQERQQQQQQQQRSEELLAERKPGPLEARERRPSPGEMRD
FT QSPKGRESR (in isoform 3)"
FT /id="VSP_057119"
FT VARIANT 222
FT /note="R -> G (in dbSNP:rs9262144)"
FT /evidence="ECO:0000269|PubMed:14574404"
FT /id="VAR_046132"
FT VARIANT 339
FT /note="G -> R (in dbSNP:rs9262143)"
FT /evidence="ECO:0000269|PubMed:14574404,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_046133"
FT VARIANT 356
FT /note="P -> L (in dbSNP:rs2213944)"
FT /id="VAR_034045"
FT MUTAGEN 540
FT /note="I->G: Decrease binding to PP1. Complete inhibition
FT of PP1 binding; when associated with G-542."
FT /evidence="ECO:0000269|PubMed:17374523"
FT MUTAGEN 542
FT /note="F->G: Decrease binding to PP1. Decrease binding to
FT PP1. Complete inhibition of PP1 binding; when associated
FT with G-540."
FT /evidence="ECO:0000269|PubMed:17374523"
FT CONFLICT 81
FT /note="A -> T (in Ref. 4; BAC86229)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="E -> G (in Ref. 4; BAC86229)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="S -> G (in Ref. 3; BAD38640)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 613 AA; 67943 MW; AB1F7C82DD50BB66 CRC64;
MATIPDWKLQ LLARRRQEEA SVRGREKAER ERLSQMPAWK RGLLERRRAK LGLSPGEPSP
VLGTVEAGPP DPDESAVLLE AIGPVHQNRF IRQERQQQQQ QQQRSEELLA ERKPGPLEAR
ERRPSPGEMR DQSPKGRESR EERLSPRETR ERRLGIGGAQ ELSLRPLEAR DWRQSPGEVG
DRSSRLSEAW KWRLSPGETP ERSLRLAESR EQSPRRKEVE SRLSPGESAY QKLGLTEAHK
WRPDSRESQE QSLVQLEATE WRLRSGEERQ DYSEECGRKE EWPVPGVAPK ETAELSETLT
REAQGNSSAG VEAAEQRPVE DGERGMKPTE GWKWTLNSGK AREWTPRDIE AQTQKPEPPE
SAEKLLESPG VEAGEGEAEK EEAGAQGRPL RALQNCCSVP SPLPPEDAGT GGLRQQEEEA
VELQPPPPAP LSPPPPAPTA PQPPGDPLMS RLFYGVKAGP GVGAPRRSGH TFTVNPRRSV
PPATPATPTS PATVDAAVPG AGKKRYPTAE EILVLGGYLR LSRSCLAKGS PERHHKQLKI
SFSETALETT YQYPSESSVL EELGPEPEVP SAPNPPAAQP DDEEDEEELL LLQPELQGGL
RTKALIVDES CRR
