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 24-JAN-2024, entry version 196. DE RecName: Full=TRIO and F-actin-binding protein; DE AltName: Full=Protein Tara; DE AltName: Full=TRF1-associated protein of 68 kDa {ECO:0000303|PubMed:24692559}; DE AltName: Full=Trio-associated repeat on actin; GN Name=TRIOBP; Synonyms=KIAA1662, TARA {ECO:0000303|PubMed:11148140}; GN 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), INTERACTION WITH TRIO AND ACTIN RP (ISOFORM 1), AND TISSUE SPECIFICITY (ISOFORM 1). 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 (ISOFORM 1), INTERACTION WITH HECTD3 (ISOFORM 1), AND RP UBIQUITINATION (ISOFORM 1). 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), SUBCELLULAR LOCATION (ISOFORM 1), RP AND FUNCTION (ISOFORM 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 AT THR-221 AND THR-457 (ISOFORM 1), SUBCELLULAR LOCATION RP (ISOFORM 1), FUNCTION (ISOFORM 1), AND INTERACTION WITH TERF1 (ISOFORM 1). RX PubMed=24692559; DOI=10.1074/jbc.m113.526244; RA Lan J., Zhu Y., Xu L., Yu H., Yu J., Liu X., Fu C., Wang X., Ke Y., RA Huang H., Dou Z.; RT "The 68-kDa telomeric repeat binding factor 1 (TRF1)-associated protein RT (TAP68) interacts with and recruits TRF1 to the spindle pole during RT mitosis."; RL J. Biol. Chem. 289:14145-14156(2014). RN [17] 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 [18] RP SUBUNIT, AND AGGREGATION IN SCHIZOPHRENIA DISEASE. RX PubMed=25333879; DOI=10.1371/journal.pone.0111196; RA Bradshaw N.J., Bader V., Prikulis I., Lueking A., Muellner S., Korth C.; RT "Aggregation of the protein TRIOBP-1 and its potential relevance to RT schizophrenia."; RL PLoS ONE 9:e111196-e111196(2014). RN [19] 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). RN [20] RP FUNCTION (ISOFORM 1), INTERACTION WITH ACTIN (ISOFORM 1), SUBUNIT (ISOFORM RP 1), AND MUTAGENESIS OF THR-221 AND THR-457 (ISOFORM 1). RX PubMed=28438837; DOI=10.1074/jbc.m116.767939; RA Bradshaw N.J., Yerabham A.S.K., Marreiros R., Zhang T., Nagel-Steger L., RA Korth C.; RT "An unpredicted aggregation-critical region of the actin-polymerizing RT protein TRIOBP-1/Tara, determined by elucidation of its domain structure."; RL J. Biol. Chem. 292:9583-9598(2017). CC -!- FUNCTION: [Isoform 1]: Regulates actin cytoskeletal organization, cell CC spreading and cell contraction by directly binding and stabilizing CC filamentous F-actin and prevents its depolymerization (PubMed:18194665, CC PubMed:28438837). May also serve as a linker protein to recruit CC proteins required for F-actin formation and turnover (PubMed:18194665). CC Essential for correct mitotic progression (PubMed:24692559, CC PubMed:22820163). {ECO:0000269|PubMed:18194665, CC ECO:0000269|PubMed:22820163, ECO:0000269|PubMed:24692559, CC ECO:0000269|PubMed:28438837}. CC -!- FUNCTION: [Isoform 5]: Plays a pivotal role in the formation of CC stereocilia rootlets. {ECO:0000250|UniProtKB:Q99KW3}. CC -!- FUNCTION: [Isoform 4]: Plays a pivotal role in the formation of CC stereocilia rootlets. {ECO:0000250|UniProtKB:Q99KW3}. CC -!- SUBUNIT: Isoform 1 forms aggregates (PubMed:28438837, PubMed:25333879). CC Isoform 1 binds to TRIO and F-actin (PubMed:11148140, PubMed:28438837). CC Isoform 1 may also interact with myosin II (PubMed:11148140). Interacts CC with HECTD3 (PubMed:18194665). Interacts with PJVK (By similarity). CC Interacts with TERF1; mediates TERF1 localization to the centrosome CC (PubMed:24692559). {ECO:0000250|UniProtKB:Q99KW3, CC ECO:0000269|PubMed:11148140, ECO:0000269|PubMed:18194665, CC ECO:0000269|PubMed:24692559, ECO:0000269|PubMed:25333879, CC ECO:0000269|PubMed:28438837}. CC -!- SUBCELLULAR LOCATION: Nucleus {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, CC ECO:0000269|PubMed:24692559}. Midbody {ECO:0000269|PubMed:22820163}. CC Chromosome, telomere {ECO:0000269|PubMed:24692559}. Note=Centrosomal CC localization occurs upon phosphorylation by PLK1 at Thr-457 and lasts CC from prophase to anaphase. At telophase, relocalizes to midbody. CC {ECO:0000269|PubMed:22820163}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=7; CC Name=2; Synonyms=TRIOBP-6 {ECO:0000303|PubMed:16385457}; CC IsoId=Q9H2D6-1; Sequence=Displayed; CC Name=3; Synonyms=Long isoform {ECO:0000303|PubMed:16385458}; CC IsoId=Q9H2D6-2; Sequence=VSP_017714, VSP_017715, VSP_017717; CC Name=4; Synonyms=TRIOBP-5 {ECO:0000303|PubMed:16385457}; CC IsoId=Q9H2D6-3; Sequence=VSP_017712; CC Name=5; Synonyms=TRIOBP-4 {ECO:0000303|PubMed:16385457}; CC IsoId=Q9H2D6-4; Sequence=VSP_017712, VSP_017713; CC Name=1; Synonyms=TRIOBP-1 {ECO:0000303|PubMed:11148140}, TAP68 CC {ECO:0000303|PubMed:24692559}, TARA {ECO:0000303|PubMed:28438837}; 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: [Isoform 1]: Widely expressed. Highly expressed in CC heart and placenta. {ECO:0000269|PubMed:11148140}. CC -!- TISSUE SPECIFICITY: [Isoform 3]: Expressed in fetal brain, retina and CC cochlea but is not detectable in the other tissues. CC {ECO:0000269|PubMed:16385458}. CC -!- DOMAIN: Contains at least 2 actin-binding sites per coiled-coil dimer. CC -!- PTM: [Isoform 1]: Ubiquitinated by HECTD3, leading to its degradation CC by the 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 (PubMed:22820163). Phosphorylation at residues Thr-221 and Thr-457 by CC kinase NEK2A and PLK1 coordinates TERF1 translocation from telomere to CC spindle pole (PubMed:24692559). {ECO:0000269|PubMed:22820163, CC ECO:0000269|PubMed:24692559}. 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: [Isoform 1]: Insoluble aggregates is found in the brain CC of schizophrenia patients. {ECO:0000269|PubMed:25333879}. CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative promoter usage. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative splicing of isoform CC 1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing of isoform CC 2. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 5]: Produced by alternative splicing of isoform CC 2. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 6]: Produced by alternative splicing of isoform CC 1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 7]: Produced by alternative splicing of isoform CC 1. {ECO:0000305}. 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; 132. DR IntAct; Q9H2D6; 65. DR MINT; Q9H2D6; -. DR STRING; 9606.ENSP00000496394; -. DR GlyGen; Q9H2D6; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q9H2D6; -. DR PhosphoSitePlus; Q9H2D6; -. DR SwissPalm; Q9H2D6; -. DR BioMuta; TRIOBP; -. DR DMDM; 90110075; -. DR EPD; Q9H2D6; -. DR jPOST; Q9H2D6; -. DR MassIVE; Q9H2D6; -. DR MaxQB; Q9H2D6; -. DR PaxDb; 9606-ENSP00000384312; -. DR PeptideAtlas; 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 Pumba; Q9H2D6; -. DR Antibodypedia; 288; 137 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 AGR; HGNC:17009; -. 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; Rare 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; YIPPAVC; -. DR OrthoDB; 2961037at2759; -. 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; 18 hits in 1161 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 208 other cell types or tissues. DR ExpressionAtlas; Q9H2D6; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI. DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell. DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. 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: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; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR039597; M-RIP_PH. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR PANTHER; PTHR17271; PLECKSTRIN HOMOLOGY PH DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR17271:SF10; TRIO AND F-ACTIN-BINDING PROTEIN; 1. DR Pfam; PF00169; PH; 1. DR SMART; SM00233; PH; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR Genevisible; Q9H2D6; HS. PE 1: Evidence at protein level; KW Actin-binding; Alternative promoter usage; Alternative splicing; KW Cell cycle; Cell division; Chromosome; Coiled coil; Cytoplasm; KW Cytoskeleton; Deafness; Disease variant; Methylation; Mitosis; KW Non-syndromic deafness; Nucleus; Phosphoprotein; Reference proteome; KW Telomere; 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 REGION Q9H2D6-5:324..348 FT /note="Essentiel for its aggregation" FT /evidence="ECO:0000269|PubMed:28438837" FT MOD_RES Q9H2D6-5:221 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:24692559" FT MOD_RES Q9H2D6-5:457 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:22820163" FT MUTAGEN Q9H2D6-5:221 FT /note="T->A: Does not affect interaction with TERF1. FT Remains associated with TERF1 at the telomere in late FT prometaphase cells." FT /evidence="ECO:0000269|PubMed:28438837" FT MUTAGEN Q9H2D6-5:221 FT /note="T->E: Abolishes interaction with TERF1." FT /evidence="ECO:0000269|PubMed:28438837" FT MUTAGEN Q9H2D6-5:457 FT /note="T->A: Prevents the localization of TERF1 to the FT centrosome." FT /evidence="ECO:0000269|PubMed:28438837" FT MUTAGEN Q9H2D6-5:457 FT /note="T->E: Does not affect interaction with TERF1." FT /evidence="ECO:0000269|PubMed:28438837" 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 //