TLN1_HUMAN
ID TLN1_HUMAN Reviewed; 2541 AA.
AC Q9Y490; A6NMY0; Q86YD0; Q9NZQ2; Q9UHH8; Q9UPX3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 3.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Talin-1;
GN Name=TLN1; Synonyms=KIAA1027, TLN;
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], AND VARIANT LEU-1227.
RA Mao L., Fan Y.H.;
RT "Complete cDNA sequence of human talin.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=10610730; DOI=10.1006/geno.1999.6019;
RA Ben-Yosef T., Francomano C.A.;
RT "Characterization of the human talin (TLN) gene: genomic structure,
RT chromosomal localization, and expression pattern.";
RL Genomics 62:316-319(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TRP-1919.
RC TISSUE=Embryonic carcinoma;
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 [8]
RP PROTEIN SEQUENCE OF 8-15; 34-82; 99-106; 119-131; 138-146; 148-156;
RP 165-178; 182-194; 197-234; 257-268; 307-316; 344-358; 428-438; 442-454;
RP 593-634; 674-685; 722-741; 766-824; 828-854; 862-869; 876-910; 923-943;
RP 958-999; 1026-1035; 1076-1086; 1097-1122; 1130-1184; 1191-1198; 1208-1214;
RP 1223-1269; 1274-1306; 1321-1340; 1362-1368; 1402-1431; 1531-1541;
RP 1560-1646; 1674-1780; 1863-1917; 1961-1973; 2007-2016; 2025-2057;
RP 2064-2085; 2090-2099; 2105-2115; 2120-2130; 2134-2141; 2145-2154;
RP 2169-2177; 2198-2209; 2221-2233; 2267-2274; 2276-2321; 2322-2329;
RP 2334-2361; 2369-2398; 2430-2443; 2456-2472; 2477-2491; 2494-2510 AND
RP 2512-2519, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [9]
RP INTERACTION WITH NRAP.
RX PubMed=10320340; DOI=10.1021/bi982395t;
RA Luo G., Herrera A.H., Horowits R.;
RT "Molecular interactions of N-RAP, a nebulin-related protein of striated
RT muscle myotendon junctions and intercalated disks.";
RL Biochemistry 38:6135-6143(1999).
RN [10]
RP INTERACTION WITH PIP5K1C.
RX PubMed=12422220; DOI=10.1038/nature01082;
RA Ling K., Doughman R.L., Firestone A.J., Bunce M.W., Anderson R.A.;
RT "Type I gamma phosphatidylinositol phosphate kinase targets and regulates
RT focal adhesions.";
RL Nature 420:89-93(2002).
RN [11]
RP INTERACTION WITH ITGB1.
RX PubMed=12473654; DOI=10.1074/jbc.m211258200;
RA Bouvard D., Vignoud L., Dupe-Manet S., Abed N., Fournier H.N.,
RA Vincent-Monegat C., Retta S.F., Fassler R., Block M.R.;
RT "Disruption of focal adhesions by integrin cytoplasmic domain-associated
RT protein-1 alpha.";
RL J. Biol. Chem. 278:6567-6574(2003).
RN [12]
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 [13]
RP INTERACTION WITH SYNM.
RX PubMed=18342854; DOI=10.1016/j.yexcr.2008.01.034;
RA Sun N., Critchley D.R., Paulin D., Li Z., Robson R.M.;
RT "Identification of a repeated domain within mammalian alpha-synemin that
RT interacts directly with talin.";
RL Exp. Cell Res. 314:1839-1849(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, AND IDENTIFICATION BY
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, AND IDENTIFICATION BY
RP 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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2031 AND LYS-2115, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, AND IDENTIFICATION BY
RP 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 [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP INTERACTION WITH ITGB1.
RX PubMed=21768292; DOI=10.1083/jcb.201007108;
RA Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A., Mosher D.,
RA Block M.R., Albiges-Rizo C., Bouvard D.;
RT "Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent
RT fibronectin deposition.";
RL J. Cell Biol. 194:307-322(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2040, 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-167 AND SER-425, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [23]
RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL135.
RX PubMed=25121749; DOI=10.1016/j.chom.2014.07.005;
RA Stanton R.J., Prod'homme V., Purbhoo M.A., Moore M., Aicheler R.J.,
RA Heinzmann M., Bailer S.M., Haas J., Antrobus R., Weekes M.P., Lehner P.J.,
RA Vojtesek B., Miners K.L., Man S., Wilkie G.S., Davison A.J., Wang E.C.,
RA Tomasec P., Wilkinson G.W.;
RT "HCMV pUL135 remodels the actin cytoskeleton to impair immune recognition
RT of infected cells.";
RL Cell Host Microbe 16:201-214(2014).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-1021; THR-1142;
RP SER-1201; SER-1225; THR-1263; SER-1323; SER-1849; THR-1855 AND SER-2040,
RP AND 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).
RN [25]
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 [26]
RP INTERACTION WITH THSD1.
RX PubMed=27895300; DOI=10.1161/strokeaha.116.014161;
RA Santiago-Sim T., Fang X., Hennessy M.L., Nalbach S.V., DePalma S.R.,
RA Lee M.S., Greenway S.C., McDonough B., Hergenroeder G.W., Patek K.J.,
RA Colosimo S.M., Qualmann K.J., Hagan J.P., Milewicz D.M., MacRae C.A.,
RA Dymecki S.M., Seidman C.E., Seidman J.G., Kim D.H.;
RT "THSD1 (thrombospondin type 1 domain containing protein 1) mutation in the
RT pathogenesis of intracranial aneurysm and subarachnoid emorrhage.";
RL Stroke 47:3005-3013(2016).
RN [27]
RP ERRATUM OF PUBMED:27895300.
RA Santiago-Sim T., Fang X., Hennessy M.L., Nalbach S.V., DePalma S.R.,
RA Lee M.S., Greenway S.C., McDonough B., Hergenroeder G.W., Patek K.J.,
RA Colosimo S.M., Qualmann K.J., Hagan J.P., Milewicz D.M., MacRae C.A.,
RA Dymecki S.M., Seidman C.E., Seidman J.G., Kim D.H.;
RT "THSD1 (thrombospondin type 1 domain containing protein 1) mutation in the
RT pathogenesis of intracranial aneurysm and subarachnoid emorrhage.";
RL Stroke 48:e240-e240(2016).
RN [28]
RP INTERACTION WITH THSD1.
RX PubMed=29069646; DOI=10.1159/000484298;
RA Rui Y.N., Xu Z., Fang X., Menezes M.R., Balzeau J., Niu A., Hagan J.P.,
RA Kim D.H.;
RT "The Intracranial Aneurysm Gene THSD1 Connects Endosome Dynamics to Nascent
RT Focal Adhesion Assembly.";
RL Cell. Physiol. Biochem. 43:2200-2211(2017).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 607-631 IN COMPLEX WITH VCL.
RX PubMed=15070891; DOI=10.1074/jbc.m403076200;
RA Izard T., Vonrhein C.;
RT "Structural basis for amplifying vinculin activation by talin.";
RL J. Biol. Chem. 279:27667-27678(2004).
CC -!- FUNCTION: Probably involved in connections of major cytoskeletal
CC structures to the plasma membrane. High molecular weight cytoskeletal
CC protein concentrated at regions of cell-substratum contact and, in
CC lymphocytes, at cell-cell contacts (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of a complex composed of THSD1, PTK2/FAK1, TLN1 and VCL
CC (PubMed:29069646). Interacts with THSD1 (PubMed:27895300,
CC PubMed:29069646); this promotes interaction with PTK2/FAK1 and VCL.
CC Binds with high affinity to VCL and with low affinity to integrins
CC (PubMed:15070891). Interacts with APBB1IP; this inhibits VCL binding.
CC Interacts with PTK2/FAK1 (By similarity). Interacts with PIP5K1C and
CC NRAP (PubMed:10320340, PubMed:12422220). Interacts with LAYN (By
CC similarity). Interacts with SYNM (PubMed:18342854). Interacts with
CC ITGB1; the interaction is prevented by competitive binding of ITGB1BP1
CC (PubMed:21768292, PubMed:12473654). {ECO:0000250|UniProtKB:P26039,
CC ECO:0000250|UniProtKB:P54939, ECO:0000269|PubMed:10320340,
CC ECO:0000269|PubMed:12422220, ECO:0000269|PubMed:12473654,
CC ECO:0000269|PubMed:15070891, ECO:0000269|PubMed:18342854,
CC ECO:0000269|PubMed:21768292, ECO:0000269|PubMed:25121749,
CC ECO:0000269|PubMed:27895300, ECO:0000269|PubMed:29069646}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus
CC protein UL135. {ECO:0000269|PubMed:25121749}.
CC -!- INTERACTION:
CC Q9Y490; Q2M1Z3: ARHGAP31; NbExp=2; IntAct=EBI-2462036, EBI-2803146;
CC Q9Y490; P00533: EGFR; NbExp=2; IntAct=EBI-2462036, EBI-297353;
CC Q9Y490; P04626: ERBB2; NbExp=3; IntAct=EBI-2462036, EBI-641062;
CC Q9Y490; P05556: ITGB1; NbExp=2; IntAct=EBI-2462036, EBI-703066;
CC Q9Y490; P05106: ITGB3; NbExp=6; IntAct=EBI-2462036, EBI-702847;
CC Q9Y490; Q6ZVC0: NYAP1; NbExp=2; IntAct=EBI-2462036, EBI-20847847;
CC Q9Y490; O60331: PIP5K1C; NbExp=3; IntAct=EBI-2462036, EBI-8869029;
CC Q9Y490; P56180: TPTE; NbExp=3; IntAct=EBI-2462036, EBI-3914809;
CC -!- SUBCELLULAR LOCATION: Cell projection, ruffle membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell surface
CC {ECO:0000250|UniProtKB:P26039}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:P26039}. Note=Colocalizes with LAYN at the
CC membrane ruffles. Localized preferentially in focal adhesions than
CC fibrillar adhesions (By similarity). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA82979.2; Type=Erroneous initiation; Note=Extended N-terminus.; 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; AF078828; AAD13152.1; -; mRNA.
DR EMBL; AF177198; AAF23322.1; -; mRNA.
DR EMBL; AF178534; AAF27330.1; -; Genomic_DNA.
DR EMBL; AF178081; AAF27330.1; JOINED; Genomic_DNA.
DR EMBL; AB028950; BAA82979.2; ALT_INIT; mRNA.
DR EMBL; AL133410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58352.1; -; Genomic_DNA.
DR EMBL; BC042923; AAH42923.1; -; mRNA.
DR CCDS; CCDS35009.1; -.
DR RefSeq; NP_006280.3; NM_006289.3.
DR PDB; 1SYQ; X-ray; 2.42 A; B=607-631.
DR PDB; 2MWN; NMR; -; B=308-400.
DR PDB; 4DJ9; X-ray; 2.25 A; B=2075-2103.
DR PDB; 6R9T; EM; 6.20 A; A=1-2541.
DR PDBsum; 1SYQ; -.
DR PDBsum; 2MWN; -.
DR PDBsum; 4DJ9; -.
DR PDBsum; 6R9T; -.
DR AlphaFoldDB; Q9Y490; -.
DR BMRB; Q9Y490; -.
DR SASBDB; Q9Y490; -.
DR SMR; Q9Y490; -.
DR BioGRID; 112949; 162.
DR ComplexPortal; CPX-791; Talin-1-Vinculin focal adhesion activation complex.
DR CORUM; Q9Y490; -.
DR ELM; Q9Y490; -.
DR IntAct; Q9Y490; 72.
DR MINT; Q9Y490; -.
DR STRING; 9606.ENSP00000316029; -.
DR CarbonylDB; Q9Y490; -.
DR GlyGen; Q9Y490; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9Y490; -.
DR MetOSite; Q9Y490; -.
DR PhosphoSitePlus; Q9Y490; -.
DR SwissPalm; Q9Y490; -.
DR BioMuta; TLN1; -.
DR DMDM; 81175200; -.
DR OGP; Q9Y490; -.
DR CPTAC; CPTAC-282; -.
DR CPTAC; CPTAC-283; -.
DR EPD; Q9Y490; -.
DR jPOST; Q9Y490; -.
DR MassIVE; Q9Y490; -.
DR MaxQB; Q9Y490; -.
DR PaxDb; Q9Y490; -.
DR PeptideAtlas; Q9Y490; -.
DR PRIDE; Q9Y490; -.
DR ProteomicsDB; 86131; -.
DR Antibodypedia; 1497; 702 antibodies from 42 providers.
DR DNASU; 7094; -.
DR Ensembl; ENST00000314888.10; ENSP00000316029.9; ENSG00000137076.21.
DR GeneID; 7094; -.
DR KEGG; hsa:7094; -.
DR MANE-Select; ENST00000314888.10; ENSP00000316029.9; NM_006289.4; NP_006280.3.
DR UCSC; uc003zxt.3; human.
DR CTD; 7094; -.
DR DisGeNET; 7094; -.
DR GeneCards; TLN1; -.
DR HGNC; HGNC:11845; TLN1.
DR HPA; ENSG00000137076; Low tissue specificity.
DR MIM; 186745; gene.
DR neXtProt; NX_Q9Y490; -.
DR OpenTargets; ENSG00000137076; -.
DR PharmGKB; PA36547; -.
DR VEuPathDB; HostDB:ENSG00000137076; -.
DR eggNOG; KOG4261; Eukaryota.
DR GeneTree; ENSGT00940000157006; -.
DR HOGENOM; CLU_000364_1_1_1; -.
DR InParanoid; Q9Y490; -.
DR OMA; VDMTQHY; -.
DR OrthoDB; 9839at2759; -.
DR PhylomeDB; Q9Y490; -.
DR TreeFam; TF314677; -.
DR PathwayCommons; Q9Y490; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-354192; Integrin signaling.
DR Reactome; R-HSA-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-HSA-372708; p130Cas linkage to MAPK signaling for integrins.
DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR Reactome; R-HSA-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-HSA-445355; Smooth Muscle Contraction.
DR Reactome; R-HSA-5674135; MAP2K and MAPK activation.
DR Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
DR Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions.
DR Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
DR Reactome; R-HSA-9649948; Signaling downstream of RAS mutants.
DR Reactome; R-HSA-9656223; Signaling by RAF1 mutants.
DR SignaLink; Q9Y490; -.
DR SIGNOR; Q9Y490; -.
DR BioGRID-ORCS; 7094; 419 hits in 1092 CRISPR screens.
DR ChiTaRS; TLN1; human.
DR EvolutionaryTrace; Q9Y490; -.
DR GeneWiki; TLN1; -.
DR GenomeRNAi; 7094; -.
DR Pharos; Q9Y490; Tbio.
DR PRO; PR:Q9Y490; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9Y490; protein.
DR Bgee; ENSG00000137076; Expressed in popliteal artery and 178 other tissues.
DR Genevisible; Q9Y490; HS.
DR GO; GO:0005912; C:adherens junction; IMP:ARUK-UCL.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; ISS:HGNC-UCL.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
DR GO; GO:0030274; F:LIM domain binding; IPI:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:Ensembl.
DR GO; GO:0001786; F:phosphatidylserine binding; IEA:Ensembl.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0017166; F:vinculin binding; IPI:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; TAS:UniProtKB.
DR GO; GO:0007044; P:cell-substrate junction assembly; IEA:Ensembl.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0033622; P:integrin activation; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0070527; P:platelet aggregation; HMP:UniProtKB.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; IC:ComplexPortal.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd12150; talin-RS; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR032425; FERM_f0.
DR InterPro; IPR035964; I/LWEQ_dom_sf.
DR InterPro; IPR002558; ILWEQ_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR037438; Talin1/2-RS.
DR InterPro; IPR015224; Talin_cent.
DR InterPro; IPR036476; Talin_cent_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR015009; Vinculin-bd_dom.
DR Pfam; PF16511; FERM_f0; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF01608; I_LWEQ; 1.
DR Pfam; PF09141; Talin_middle; 1.
DR Pfam; PF08913; VBS; 1.
DR SMART; SM00295; B41; 1.
DR SMART; SM00307; ILWEQ; 1.
DR SUPFAM; SSF109880; SSF109880; 1.
DR SUPFAM; SSF109885; SSF109885; 4.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF47220; SSF47220; 5.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS50945; I_LWEQ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell junction; Cell membrane; Cell projection;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Host-virus interaction;
KW Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..2541
FT /note="Talin-1"
FT /id="PRO_0000219428"
FT DOMAIN 86..403
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 2293..2533
FT /note="I/LWEQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00292"
FT REGION 280..435
FT /note="Interaction with LAYN"
FT /evidence="ECO:0000250|UniProtKB:P54939"
FT REGION 1327..1948
FT /note="Interaction with SYNM"
FT /evidence="ECO:0000269|PubMed:18342854"
FT REGION 1359..1659
FT /note="Interaction with VCL and F-actin"
FT /evidence="ECO:0000250|UniProtKB:P26039"
FT MOD_RES 167
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26039"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26039"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26039"
FT MOD_RES 1021
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1116
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P26039"
FT MOD_RES 1142
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1263
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1544
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26039"
FT MOD_RES 1849
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1855
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1878
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26039"
FT MOD_RES 2031
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 2040
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 2115
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 1227
FT /note="S -> L (in dbSNP:rs2295795)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_023751"
FT VARIANT 1919
FT /note="R -> W (in dbSNP:rs17854239)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_023752"
FT VARIANT 1984
FT /note="A -> T (in dbSNP:rs35642290)"
FT /id="VAR_055538"
FT CONFLICT 824
FT /note="R -> G (in Ref. 1; AAD13152 and 2; AAF23322)"
FT /evidence="ECO:0000305"
FT CONFLICT 1549
FT /note="A -> P (in Ref. 1; AAD13152 and 2; AAF23322)"
FT /evidence="ECO:0000305"
FT CONFLICT 1604
FT /note="K -> Q (in Ref. 1; AAD13152 and 2; AAF23322)"
FT /evidence="ECO:0000305"
FT CONFLICT 1701
FT /note="Q -> E (in Ref. 1; AAD13152 and 2; AAF23322)"
FT /evidence="ECO:0000305"
FT CONFLICT 1718
FT /note="N -> H (in Ref. 1; AAD13152 and 2; AAF23322)"
FT /evidence="ECO:0000305"
FT CONFLICT 1966
FT /note="A -> R (in Ref. 1; AAD13152)"
FT /evidence="ECO:0000305"
FT CONFLICT 2256
FT /note="Missing (in Ref. 2; AAF27330)"
FT /evidence="ECO:0000305"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:2MWN"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:2MWN"
FT STRAND 320..327
FT /evidence="ECO:0007829|PDB:2MWN"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:2MWN"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:2MWN"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:2MWN"
FT STRAND 363..369
FT /evidence="ECO:0007829|PDB:2MWN"
FT STRAND 377..381
FT /evidence="ECO:0007829|PDB:2MWN"
FT HELIX 385..399
FT /evidence="ECO:0007829|PDB:2MWN"
FT HELIX 608..625
FT /evidence="ECO:0007829|PDB:1SYQ"
FT HELIX 2079..2098
FT /evidence="ECO:0007829|PDB:4DJ9"
SQ SEQUENCE 2541 AA; 269767 MW; E21575E9199BBC5C CRC64;
MVALSLKISI GNVVKTMQFE PSTMVYDACR IIRERIPEAP AGPPSDFGLF LSDDDPKKGI
WLEAGKALDY YMLRNGDTME YRKKQRPLKI RMLDGTVKTI MVDDSKTVTD MLMTICARIG
ITNHDEYSLV RELMEEKKEE ITGTLRKDKT LLRDEKKMEK LKQKLHTDDE LNWLDHGRTL
REQGVEEHET LLLRRKFFYS DQNVDSRDPV QLNLLYVQAR DDILNGSHPV SFDKACEFAG
FQCQIQFGPH NEQKHKAGFL DLKDFLPKEY VKQKGERKIF QAHKNCGQMS EIEAKVRYVK
LARSLKTYGV SFFLVKEKMK GKNKLVPRLL GITKECVMRV DEKTKEVIQE WNLTNIKRWA
ASPKSFTLDF GDYQDGYYSV QTTEGEQIAQ LIAGYIDIIL KKKKSKDHFG LEGDEESTML
EDSVSPKKST VLQQQYNRVG KVEHGSVALP AIMRSGASGP ENFQVGSMPP AQQQITSGQM
HRGHMPPLTS AQQALTGTIN SSMQAVQAAQ ATLDDFDTLP PLGQDAASKA WRKNKMDESK
HEIHSQVDAI TAGTASVVNL TAGDPAETDY TAVGCAVTTI SSNLTEMSRG VKLLAALLED
EGGSGRPLLQ AAKGLAGAVS ELLRSAQPAS AEPRQNLLQA AGNVGQASGE LLQQIGESDT
DPHFQDALMQ LAKAVASAAA ALVLKAKSVA QRTEDSGLQT QVIAAATQCA LSTSQLVACT
KVVAPTISSP VCQEQLVEAG RLVAKAVEGC VSASQAATED GQLLRGVGAA ATAVTQALNE
LLQHVKAHAT GAGPAGRYDQ ATDTILTVTE NIFSSMGDAG EMVRQARILA QATSDLVNAI
KADAEGESDL ENSRKLLSAA KILADATAKM VEAAKGAAAH PDSEEQQQRL REAAEGLRMA
TNAAAQNAIK KKLVQRLEHA AKQAAASATQ TIAAAQHAAS TPKASAGPQP LLVQSCKAVA
EQIPLLVQGV RGSQAQPDSP SAQLALIAAS QSFLQPGGKM VAAAKASVPT IQDQASAMQL
SQCAKNLGTA LAELRTAAQK AQEACGPLEM DSALSVVQNL EKDLQEVKAA ARDGKLKPLP
GETMEKCTQD LGNSTKAVSS AIAQLLGEVA QGNENYAGIA ARDVAGGLRS LAQAARGVAA
LTSDPAVQAI VLDTASDVLD KASSLIEEAK KAAGHPGDPE SQQRLAQVAK AVTQALNRCV
SCLPGQRDVD NALRAVGDAS KRLLSDSLPP STGTFQEAQS RLNEAAAGLN QAATELVQAS
RGTPQDLARA SGRFGQDFST FLEAGVEMAG QAPSQEDRAQ VVSNLKGISM SSSKLLLAAK
ALSTDPAAPN LKSQLAAAAR AVTDSINQLI TMCTQQAPGQ KECDNALREL ETVRELLENP
VQPINDMSYF GCLDSVMENS KVLGEAMTGI SQNAKNGNLP EFGDAISTAS KALCGFTEAA
AQAAYLVGVS DPNSQAGQQG LVEPTQFARA NQAIQMACQS LGEPGCTQAQ VLSAATIVAK
HTSALCNSCR LASARTTNPT AKRQFVQSAK EVANSTANLV KTIKALDGAF TEENRAQCRA
ATAPLLEAVD NLSAFASNPE FSSIPAQISP EGRAAMEPIV ISAKTMLESA GGLIQTARAL
AVNPRDPPSW SVLAGHSRTV SDSIKKLITS MRDKAPGQLE CETAIAALNS CLRDLDQASL
AAVSQQLAPR EGISQEALHT QMLTAVQEIS HLIEPLANAA RAEASQLGHK VSQMAQYFEP
LTLAAVGAAS KTLSHPQQMA LLDQTKTLAE SALQLLYTAK EAGGNPKQAA HTQEALEEAV
QMMTEAVEDL TTTLNEAASA AGVVGGMVDS ITQAINQLDE GPMGEPEGSF VDYQTTMVRT
AKAIAVTVQE MVTKSNTSPE ELGPLANQLT SDYGRLASEA KPAAVAAENE EIGSHIKHRV
QELGHGCAAL VTKAGALQCS PSDAYTKKEL IECARRVSEK VSHVLAALQA GNRGTQACIT
AASAVSGIIA DLDTTIMFAT AGTLNREGTE TFADHREGIL KTAKVLVEDT KVLVQNAAGS
QEKLAQAAQS SVATITRLAD VVKLGAASLG AEDPETQVVL INAVKDVAKA LGDLISATKA
AAGKVGDDPA VWQLKNSAKV MVTNVTSLLK TVKAVEDEAT KGTRALEATT EHIRQELAVF
CSPEPPAKTS TPEDFIRMTK GITMATAKAV AAGNSCRQED VIATANLSRR AIADMLRACK
EAAYHPEVAP DVRLRALHYG RECANGYLEL LDHVLLTLQK PSPELKQQLT GHSKRVAGSV
TELIQAAEAM KGTEWVDPED PTVIAENELL GAAAAIEAAA KKLEQLKPRA KPKEADESLN
FEEQILEAAK SIAAATSALV KAASAAQREL VAQGKVGAIP ANALDDGQWS QGLISAARMV
AAATNNLCEA ANAAVQGHAS QEKLISSAKQ VAASTAQLLV ACKVKADQDS EAMKRLQAAG
NAVKRASDNL VKAAQKAAAF EEQENETVVV KEKMVGGIAQ IIAAQEEMLR KERELEEARK
KLAQIRQQQY KFLPSELRDE H
