TARA_HUMAN
ID TARA_HUMAN Reviewed; 2365 AA.
AC Q9H2D6; B1AHD4; B1AHD7; F2Z2W0; F8W6V6; O94797; Q2PZW8; Q2Q3Z9; Q2Q400;
AC Q5R3M6; Q96DW1; Q9BT77; Q9BTL7; Q9BY98; Q9Y3L4;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=TRIO and F-actin-binding protein;
DE AltName: Full=Protein Tara;
DE AltName: Full=Trio-associated repeat on actin;
GN Name=TRIOBP; Synonyms=KIAA1662, TARA; ORFNames=HRIHFB2122;
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 INTERACTION WITH TRIO AND
RP ACTIN.
RX PubMed=11148140; DOI=10.1242/jcs.114.2.389;
RA Seipel K., O'Brien S.P., Iannotti E., Medley Q.G., Streuli M.;
RT "Tara, a novel F-actin binding protein, associates with the Trio guanine
RT nucleotide exchange factor and regulates actin cytoskeletal organization.";
RL J. Cell Sci. 114:389-399(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4 AND 5), AND INVOLVEMENT IN
RP DFNB28.
RC TISSUE=Inner ear;
RX PubMed=16385457; DOI=10.1086/499164;
RA Riazuddin S., Khan S.N., Ahmed Z.M., Ghosh M., Caution K., Nazli S.,
RA Kabra M., Zafar A.U., Chen K., Naz S., Antonellis A., Pavan W.J.,
RA Green E.D., Wilcox E.R., Friedman P.L., Morell R.J., Riazuddin S.,
RA Friedman T.B.;
RT "Mutations in TRIOBP, which encodes a putative cytoskeletal-organizing
RT protein, are associated with nonsyndromic recessive deafness.";
RL Am. J. Hum. Genet. 78:137-143(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, AND VARIANTS
RP DFNB28 ARG-1019 AND ARG-1377.
RC TISSUE=Brain;
RX PubMed=16385458; DOI=10.1086/499495;
RA Shahin H., Walsh T., Sobe T., Abu Sa'ed J., Abu Rayan A., Lynch E.D.,
RA Lee M.K., Avraham K.B., King M.-C., Kanaan M.;
RT "Mutations in a novel isoform of TRIOBP that encodes a filamentous-actin
RT binding protein are responsible for DFNB28 recessive nonsyndromic hearing
RT loss.";
RL Am. J. Hum. Genet. 78:144-152(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 2-431 (ISOFORM 6).
RC TISSUE=Colon, and Pancreas;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 340-563, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Fetal brain;
RX PubMed=9853615; DOI=10.1038/4315;
RA Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.;
RT "Selection system for genes encoding nuclear-targeted proteins.";
RL Nat. Biotechnol. 16:1338-1342(1998).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 713-2365, AND VARIANT ARG-1377.
RC TISSUE=Brain;
RX PubMed=11258795; DOI=10.1093/dnares/8.1.1;
RA Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O.;
RT "Identification of novel transcribed sequences on human chromosome 22 by
RT expressed sequence tag mapping.";
RL DNA Res. 8:1-9(2001).
RN [8]
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 [9]
RP FUNCTION, INTERACTION WITH HECTD3, AND UBIQUITINATION.
RX PubMed=18194665; DOI=10.1016/j.bbrc.2008.01.022;
RA Yu J., Lan J., Zhu Y., Li X., Lai X., Xue Y., Jin C., Huang H.;
RT "The E3 ubiquitin ligase HECTD3 regulates ubiquitination and degradation of
RT Tara.";
RL Biochem. Biophys. Res. Commun. 367:805-812(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1949 AND SER-1955, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1955, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1949 AND SER-1955, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [13]
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 [14]
RP PHOSPHORYLATION AT THR-457 (ISOFORM 1), AND SUBCELLULAR LOCATION (ISOFORM
RP 1).
RX PubMed=22820163; DOI=10.1016/j.yexcr.2012.07.001;
RA Zhu Y., Wang C., Lan J., Yu J., Jin C., Huang H.;
RT "Phosphorylation of Tara by Plk1 is essential for faithful chromosome
RT segregation in mitosis.";
RL Exp. Cell Res. 318:2344-2352(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1955, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1796, AND IDENTIFICATION BY
RP 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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: May regulate actin cytoskeletal organization, cell spreading
CC and cell contraction by directly binding and stabilizing filamentous F-
CC actin. The localized formation of TARA and TRIO complexes coordinates
CC the amount of F-actin present in stress fibers. May also serve as a
CC linker protein to recruit proteins required for F-actin formation and
CC turnover. {ECO:0000269|PubMed:18194665}.
CC -!- SUBUNIT: Binds to TRIO and F-actin (PubMed:11148140). May also interact
CC with myosin II (PubMed:11148140). Interacts with HECTD3
CC (PubMed:18194665). Interacts with PJVK (By similarity).
CC {ECO:0000250|UniProtKB:Q99KW3, ECO:0000269|PubMed:11148140,
CC ECO:0000269|PubMed:18194665}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9853615}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:9853615}. Note=Localized to F-actin in
CC a periodic pattern. {ECO:0000269|PubMed:9853615}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
CC {ECO:0000269|PubMed:22820163}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:22820163}. Midbody
CC {ECO:0000269|PubMed:22820163}. Note=Centrosomal localization occurs
CC upon phosphorylation by PLK1 at Thr-457 and lasts from prophase to
CC anaphase. At telophase, relocalizes to midbody.
CC {ECO:0000269|PubMed:22820163}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=2; Synonyms=TRIOBP-6;
CC IsoId=Q9H2D6-1; Sequence=Displayed;
CC Name=3; Synonyms=Long isoform;
CC IsoId=Q9H2D6-2; Sequence=VSP_017714, VSP_017715, VSP_017717;
CC Name=4; Synonyms=TRIOBP-3;
CC IsoId=Q9H2D6-3; Sequence=VSP_017712;
CC Name=5; Synonyms=TRIOBP-4;
CC IsoId=Q9H2D6-4; Sequence=VSP_017712, VSP_017713;
CC Name=1; Synonyms=TRIOBP-1;
CC IsoId=Q9H2D6-5; Sequence=VSP_017711, VSP_017716;
CC Name=6;
CC IsoId=Q9H2D6-6; Sequence=VSP_047498, VSP_047499, VSP_047500,
CC VSP_047501;
CC Name=7;
CC IsoId=Q9H2D6-7; Sequence=VSP_047498, VSP_047499;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in heart and
CC placenta. Isoform 3 is expressed in fetal brain, retina and cochlea but
CC is not detectable in the other tissues. {ECO:0000269|PubMed:16385458}.
CC -!- DOMAIN: Contains at least 2 actin-binding sites per coiled-coil dimer.
CC -!- PTM: Ubiquitinated by HECTD3, leading to its degradation by the
CC proteasome. {ECO:0000269|PubMed:18194665}.
CC -!- PTM: [Isoform 1]: Phosphorylation at Thr-457 by PLK1 ensures mitotic
CC progression and is essential for accurate chromosome segregation.
CC {ECO:0000269|PubMed:22820163}.
CC -!- DISEASE: Deafness, autosomal recessive, 28 (DFNB28) [MIM:609823]: A
CC form of non-syndromic sensorineural hearing loss. Sensorineural
CC deafness results from damage to the neural receptors of the inner ear,
CC the nerve pathways to the brain, or the area of the brain that receives
CC sound information. {ECO:0000269|PubMed:16385457,
CC ECO:0000269|PubMed:16385458}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Has been identified by a selection system for genes
CC encoding nuclear-targeted protein. {ECO:0000269|PubMed:9853615}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34800.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF281030; AAG44841.1; -; mRNA.
DR EMBL; DQ228003; ABB59559.1; -; mRNA.
DR EMBL; DQ228004; ABB59560.1; -; mRNA.
DR EMBL; DQ228005; ABB59561.1; -; mRNA.
DR EMBL; DQ278603; ABB77204.1; -; mRNA.
DR EMBL; Z83844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003618; AAH03618.1; -; mRNA.
DR EMBL; BC004303; AAH04303.1; -; mRNA.
DR EMBL; BC013278; AAH13278.2; -; mRNA.
DR EMBL; BC022200; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB015343; BAA34800.1; ALT_FRAME; mRNA.
DR EMBL; AB051449; BAB33332.2; -; mRNA.
DR CCDS; CCDS33644.1; -. [Q9H2D6-6]
DR CCDS; CCDS43015.1; -. [Q9H2D6-1]
DR CCDS; CCDS43016.1; -. [Q9H2D6-7]
DR RefSeq; NP_001034230.1; NM_001039141.2. [Q9H2D6-1]
DR RefSeq; NP_008963.3; NM_007032.5. [Q9H2D6-7]
DR RefSeq; NP_619538.2; NM_138632.2. [Q9H2D6-6]
DR AlphaFoldDB; Q9H2D6; -.
DR SMR; Q9H2D6; -.
DR BioGRID; 116261; 117.
DR IntAct; Q9H2D6; 56.
DR MINT; Q9H2D6; -.
DR STRING; 9606.ENSP00000384312; -.
DR iPTMnet; Q9H2D6; -.
DR PhosphoSitePlus; Q9H2D6; -.
DR BioMuta; TRIOBP; -.
DR DMDM; 90110075; -.
DR EPD; Q9H2D6; -.
DR jPOST; Q9H2D6; -.
DR MassIVE; Q9H2D6; -.
DR MaxQB; Q9H2D6; -.
DR PaxDb; Q9H2D6; -.
DR PeptideAtlas; Q9H2D6; -.
DR PRIDE; Q9H2D6; -.
DR ProteomicsDB; 23821; -.
DR ProteomicsDB; 29844; -.
DR ProteomicsDB; 80531; -. [Q9H2D6-1]
DR ProteomicsDB; 80532; -. [Q9H2D6-2]
DR ProteomicsDB; 80533; -. [Q9H2D6-3]
DR ProteomicsDB; 80534; -. [Q9H2D6-4]
DR ProteomicsDB; 80535; -. [Q9H2D6-5]
DR Antibodypedia; 288; 117 antibodies from 25 providers.
DR DNASU; 11078; -.
DR Ensembl; ENST00000403663.6; ENSP00000386026.2; ENSG00000100106.22. [Q9H2D6-7]
DR Ensembl; ENST00000407319.7; ENSP00000383913.2; ENSG00000100106.22. [Q9H2D6-6]
DR Ensembl; ENST00000644935.1; ENSP00000496394.1; ENSG00000100106.22. [Q9H2D6-1]
DR GeneID; 11078; -.
DR KEGG; hsa:11078; -.
DR MANE-Select; ENST00000644935.1; ENSP00000496394.1; NM_001039141.3; NP_001034230.1.
DR UCSC; uc003atr.4; human. [Q9H2D6-1]
DR CTD; 11078; -.
DR DisGeNET; 11078; -.
DR GeneCards; TRIOBP; -.
DR GeneReviews; TRIOBP; -.
DR HGNC; HGNC:17009; TRIOBP.
DR HPA; ENSG00000100106; Low tissue specificity.
DR MalaCards; TRIOBP; -.
DR MIM; 609761; gene.
DR MIM; 609823; phenotype.
DR neXtProt; NX_Q9H2D6; -.
DR OpenTargets; ENSG00000100106; -.
DR Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR PharmGKB; PA142670699; -.
DR VEuPathDB; HostDB:ENSG00000100106; -.
DR eggNOG; KOG4807; Eukaryota.
DR GeneTree; ENSGT00940000157340; -.
DR HOGENOM; CLU_231134_0_0_1; -.
DR InParanoid; Q9H2D6; -.
DR OMA; QRDNPGT; -.
DR OrthoDB; 428862at2759; -.
DR PhylomeDB; Q9H2D6; -.
DR TreeFam; TF343361; -.
DR PathwayCommons; Q9H2D6; -.
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea.
DR SignaLink; Q9H2D6; -.
DR SIGNOR; Q9H2D6; -.
DR BioGRID-ORCS; 11078; 16 hits in 1082 CRISPR screens.
DR ChiTaRS; TRIOBP; human.
DR GeneWiki; TRIOBP; -.
DR GenomeRNAi; 11078; -.
DR Pharos; Q9H2D6; Tbio.
DR PRO; PR:Q9H2D6; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9H2D6; protein.
DR Bgee; ENSG00000100106; Expressed in lower lobe of lung and 206 other tissues.
DR ExpressionAtlas; Q9H2D6; baseline and differential.
DR Genevisible; Q9H2D6; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0120044; C:stereocilium base; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR GO; GO:0045159; F:myosin II binding; NAS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; NAS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030047; P:actin modification; NAS:UniProtKB.
DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; IEA:Ensembl.
DR GO; GO:0051016; P:barbed-end actin filament capping; NAS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IDA:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR CDD; cd13275; PH_M-RIP; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR039597; M-RIP_PH.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell cycle; Cell division;
KW Coiled coil; Cytoplasm; Cytoskeleton; Deafness; Disease variant;
KW Methylation; Mitosis; Non-syndromic deafness; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..2365
FT /note="TRIO and F-actin-binding protein"
FT /id="PRO_0000072433"
FT DOMAIN 1778..1887
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 48..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1168..1554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1593..1667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1679..1751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1889..2017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2174..2194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2062..2247
FT /evidence="ECO:0000255"
FT COILED 2281..2361
FT /evidence="ECO:0000255"
FT COMPBIAS 120..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1488..1507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1519..1534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1594..1608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1641..1667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1682..1698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1724..1738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1891..1915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1946..1960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1964..1994
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1796
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1930
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q99KW3"
FT MOD_RES 1949
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 1955
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..1772
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:11148140,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_017711"
FT VAR_SEQ 1..172
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16385457"
FT /id="VSP_017712"
FT VAR_SEQ 1..61
FT /note="MEEVPGDALCEHFEANILTQNRCQNCFHPEEAHGARYQELRSPSGAEVPYCD
FT LPRCPPAPE -> MGGWKGPGQRRGKEGPEARRRAAERGGGGGGGGVPAPRSPAREPRP
FT RSCLLLPPPWGAAMT (in isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047498"
FT VAR_SEQ 62..1774
FT /note="Missing (in isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047499"
FT VAR_SEQ 1317..2365
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16385457"
FT /id="VSP_017713"
FT VAR_SEQ 1317..1355
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16385458"
FT /id="VSP_017714"
FT VAR_SEQ 1729..1774
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16385458"
FT /id="VSP_017715"
FT VAR_SEQ 1773..1774
FT /note="RR -> MT (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:11148140,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_017716"
FT VAR_SEQ 1794..1806
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16385458"
FT /id="VSP_017717"
FT VAR_SEQ 2109..2144
FT /note="EACERSLAEMESSHQQVMEELQRHHERELQRLQQEK -> LVGVITVPVLQT
FT RPLSSERLCDLPKVTPPAGLKGGI (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047500"
FT VAR_SEQ 2145..2365
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047501"
FT VARIANT 217
FT /note="S -> N (in dbSNP:rs12628603)"
FT /id="VAR_059725"
FT VARIANT 493
FT /note="S -> N (in dbSNP:rs4821700)"
FT /id="VAR_059726"
FT VARIANT 817
FT /note="T -> S (in dbSNP:rs41302575)"
FT /id="VAR_061708"
FT VARIANT 863
FT /note="N -> K (in dbSNP:rs9610841)"
FT /id="VAR_051412"
FT VARIANT 1019
FT /note="G -> R (in DFNB28; dbSNP:rs549095193)"
FT /evidence="ECO:0000269|PubMed:16385458"
FT /id="VAR_025719"
FT VARIANT 1187
FT /note="F -> L (in dbSNP:rs5756795)"
FT /id="VAR_059727"
FT VARIANT 1300
FT /note="H -> R (in dbSNP:rs739138)"
FT /id="VAR_059728"
FT VARIANT 1372
FT /note="E -> D (in dbSNP:rs8140207)"
FT /id="VAR_051413"
FT VARIANT 1377
FT /note="W -> R (in dbSNP:rs8140958)"
FT /evidence="ECO:0000269|PubMed:11258795,
FT ECO:0000269|PubMed:16385458"
FT /id="VAR_051414"
FT CONFLICT 713..719
FT /note="RTTQQEN -> KSTFGCL (in Ref. 7; BAB33332)"
FT /evidence="ECO:0000305"
FT CONFLICT 1421
FT /note="R -> S (in Ref. 3; ABB77204)"
FT /evidence="ECO:0000305"
FT CONFLICT 1689
FT /note="S -> G (in Ref. 3; ABB77204)"
FT /evidence="ECO:0000305"
FT CONFLICT 1896
FT /note="Missing (in Ref. 3; ABB77204)"
FT /evidence="ECO:0000305"
FT CONFLICT 1904
FT /note="N -> D (in Ref. 3; ABB77204)"
FT /evidence="ECO:0000305"
FT CONFLICT 2114
FT /note="S -> T (in Ref. 1; AAG44841)"
FT /evidence="ECO:0000305"
FT CONFLICT 2141
FT /note="Q -> L (in Ref. 5; AAH04303)"
FT /evidence="ECO:0000305"
FT CONFLICT 2274
FT /note="S -> T (in Ref. 1; AAG44841)"
FT /evidence="ECO:0000305"
FT CONFLICT 2283
FT /note="E -> EHLYPQ (in Ref. 5; AAH04303)"
FT /evidence="ECO:0000305"
FT CONFLICT 2359
FT /note="M -> I (in Ref. 1; AAG44841)"
FT /evidence="ECO:0000305"
FT MOD_RES Q9H2D6-5:457
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22820163"
SQ SEQUENCE 2365 AA; 261376 MW; B2CF9AD57E930283 CRC64;
MEEVPGDALC EHFEANILTQ NRCQNCFHPE EAHGARYQEL RSPSGAEVPY CDLPRCPPAP
EDPLSASTSG CQSVVDPGLR PGPKRGPSPS AGLPEEGPTA APRSRSRELE AVPYLEGLTT
SLCGSCNEDP GSDPTSSPDS ATPDDTSNSS SVDWDTVERQ EEEAPSWDEL AVMIPRRPRE
GPRADSSQRA PSLLTRSPVG GDAAGQKKED TGGGGRSAGQ HWARLRGESG LSLERHRSTL
TQASSMTPHS GPRSTTSQAS PAQRDTAQAA STREIPRASS PHRITQRDTS RASSTQQEIS
RASSTQQETS RASSTQEDTP RASSTQEDTP RASSTQWNTP RASSPSRSTQ LDNPRTSSTQ
QDNPQTSFPT CTPQRENPRT PCVQQDDPRA SSPNRTTQRE NSRTSCAQRD NPKASRTSSP
NRATRDNPRT SCAQRDNPRA SSPSRATRDN PTTSCAQRDN PRASRTSSPN RATRDNPRTS
CAQRDNPRAS SPSRATRDNP TTSCAQRDNP RASRTSSPNR ATRDNPRTSC AQRDNPRASS
PNRAARDNPT TSCAQRDNPR ASRTSSPNRA TRDNPRTSCA QRDNPRASSP NRATRDNPTT
SCAQRDNPRA SRTSSPNRAT RDNPRTSCAQ RDNPRASSPN RTTQQDSPRT SCARRDDPRA
SSPNRTIQQE NPRTSCALRD NPRASSPSRT IQQENPRTSC AQRDDPRASS PNRTTQQENP
RTSCARRDNP RASSRNRTIQ RDNPRTSCAQ RDNPRASSPN RTIQQENLRT SCTRQDNPRT
SSPNRATRDN PRTSCAQRDN LRASSPIRAT QQDNPRTCIQ QNIPRSSSTQ QDNPKTSCTK
RDNLRPTCTQ RDRTQSFSFQ RDNPGTSSSQ CCTQKENLRP SSPHRSTQWN NPRNSSPHRT
NKDIPWASFP LRPTQSDGPR TSSPSRSKQS EVPWASIALR PTQGDRPQTS SPSRPAQHDP
PQSSFGPTQY NLPSRATSSS HNPGHQSTSR TSSPVYPAAY GAPLTSPEPS QPPCAVCIGH
RDAPRASSPP RYLQHDPFPF FPEPRAPESE PPHHEPPYIP PAVCIGHRDA PRASSPPRHT
QFDPFPFLPD TSDAEHQCQS PQHEPLQLPA PVCIGYRDAP RASSPPRQAP EPSLLFQDLP
RASTESLVPS MDSLHECPHI PTPVCIGHRD APSFSSPPRQ APEPSLFFQD PPGTSMESLA
PSTDSLHGSP VLIPQVCIGH RDAPRASSPP RHPPSDLAFL APSPSPGSSG GSRGSAPPGE
TRHNLEREEY TVLADLPPPR RLAQRQPGPQ AQCSSGGRTH SPGRAEVERL FGQERRKSEA
AGAFQAQDEG RSQQPSQGQS QLLRRQSSPA PSRQVTMLPA KQAELTRRSQ AEPPHPWSPE
KRPEGDRQLQ GSPLPPRTSA RTPERELRTQ RPLESGQAGP RQPLGVWQSQ EEPPGSQGPH
RHLERSWSSQ EGGLGPGGWW GCGEPSLGAA KAPEGAWGGT SREYKESWGQ PEAWEEKPTH
ELPRELGKRS PLTSPPENWG GPAESSQSWH SGTPTAVGWG AEGACPYPRG SERRPELDWR
DLLGLLRAPG EGVWARVPSL DWEGLLELLQ ARLPRKDPAG HRDDLARALG PELGPPGTND
VPEQESHSQP EGWAEATPVN GHSPALQSQS PVQLPSPACT STQWPKIKVT RGPATATLAG
LEQTGPLGSR STAKGPSLPE LQFQPEEPEE SEPSRGQDPL TDQKQADSAD KRPAEGKAGS
PLKGRLVTSW RMPGDRPTLF NPFLLSLGVL RWRRPDLLNF KKGWMSILDE PGEPPSPSLT
TTSTSQWKKH WFVLTDSSLK YYRDSTAEEA DELDGEIDLR SCTDVTEYAV QRNYGFQIHT
KDAVYTLSAM TSGIRRNWIE ALRKTVRPTS APDVTKLSDS NKENALHSYS TQKGPLKAGE
QRAGSEVISR GGPRKADGQR QALDYVELSP LTQASPQRAR TPARTPDRLA KQEELERDLA
QRSEERRKWF EATDSRTPEV PAGEGPRRGL GAPLTEDQQN RLSEEIEKKW QELEKLPLRE
NKRVPLTALL NQSRGERRGP PSDGHEALEK EVQALRAQLE AWRLQGEAPQ SALRSQEDGH
IPPGYISQEA CERSLAEMES SHQQVMEELQ RHHERELQRL QQEKEWLLAE ETAATASAIE
AMKKAYQEEL SRELSKTRSL QQGPDGLRKQ HQSDVEALKR ELQVLSEQYS QKCLEIGALM
RQAEEREHTL RRCQQEGQEL LRHNQELHGR LSEEIDQLRG FIASQGMGNG CGRSNERSSC
ELEVLLRVKE NELQYLKKEV QCLRDELQMM QKDKRFTSGK YQDVYVELSH IKTRSEREIE
QLKEHLRLAM AALQEKESMR NSLAE
