GenomeNet

Database: UniProt
Entry: TLN1_HUMAN
LinkDB: TLN1_HUMAN
Original site: 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   16-APR-2014, entry version 145.
DE   RecName: Full=Talin-1;
GN   Name=TLN1; Synonyms=KIAA1027, TLN;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIV.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large 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.,
RA   Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA   Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA   Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA   Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA   Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA   Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA   Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA   Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA   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.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA   Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA   McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA   Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA   Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA   Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA   Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA   Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA   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.,
RA   Rogers J., 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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;
RP   442-454; 593-634; 674-685; 722-741; 766-824; 828-854; 862-869;
RP   876-910; 923-943; 958-999; 1026-1035; 1076-1086; 1097-1122; 1130-1184;
RP   1191-1198; 1208-1214; 1223-1269; 1274-1306; 1321-1340; 1362-1368;
RP   1402-1431; 1531-1541; 1560-1646; 1674-1780; 1863-1917; 1961-1973;
RP   2007-2016; 2025-2057; 2064-2085; 2090-2099; 2105-2115; 2120-2130;
RP   2134-2141; 2145-2154; 2169-2177; 2198-2209; 2221-2233; 2267-2274;
RP   2276-2321; 2322-2329; 2334-2361; 2369-2398; 2430-2443; 2456-2472;
RP   2477-2491; 2494-2510 AND 2512-2519, AND IDENTIFICATION BY MASS
RP   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
RT   striated 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
RT   regulates 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-
RT   associated 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.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling 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
RT   that 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
RP   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   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, AND IDENTIFICATION
RP   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   [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.,
RA   Walther T.C., 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
RP   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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation 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.,
RA   Buerckstuemmer T., 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.,
RA   Mosher D., 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
RP   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.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [22]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [23]
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
CC       cytoskeletal protein concentrated at regions of cell-substratum
CC       contact and, in lymphocytes, at cell-cell contacts (By
CC       similarity).
CC   -!- SUBUNIT: Binds with high affinity to VCL and with low affinity to
CC       integrins. Interacts with APBB1IP; this inhibits VCL binding.
CC       Interacts with PTK2/FAK1 (By similarity). Interacts with PIP5K1C
CC       and NRAP. Interacts with LAYN. Interacts with SYNM. Interacts with
CC       ITGB1; the interaction is prevented by competitive binding of
CC       ITGB1BP1.
CC   -!- INTERACTION:
CC       P00533:EGFR; NbExp=2; IntAct=EBI-2462036, EBI-297353;
CC       P04626:ERBB2; NbExp=3; IntAct=EBI-2462036, EBI-641062;
CC       P05556:ITGB1; NbExp=2; IntAct=EBI-2462036, EBI-703066;
CC       P05106:ITGB3; NbExp=4; IntAct=EBI-2462036, EBI-702847;
CC   -!- SUBCELLULAR LOCATION: Cell projection, ruffle membrane; Peripheral
CC       membrane protein; Cytoplasmic side (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity). Cell surface (By similarity). Cell
CC       junction, focal adhesion (By similarity). Note=Colocalizes with
CC       LAYN at the membrane ruffles. Localized preferentially in focal
CC       adhesions than fibrillar adhesions (By similarity).
CC   -!- SIMILARITY: Contains 1 FERM domain.
CC   -!- SIMILARITY: Contains 1 I/LWEQ domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA82979.2; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs 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   RefSeq; NP_006280.3; NM_006289.3.
DR   UniGene; Hs.471014; -.
DR   PDB; 1SYQ; X-ray; 2.42 A; B=607-631.
DR   PDB; 4DJ9; X-ray; 2.25 A; B=2075-2103.
DR   PDBsum; 1SYQ; -.
DR   PDBsum; 4DJ9; -.
DR   ProteinModelPortal; Q9Y490; -.
DR   SMR; Q9Y490; 1-400, 485-1044, 1046-1357, 1359-1973, 1975-2482, 2496-2529.
DR   BioGrid; 112949; 39.
DR   IntAct; Q9Y490; 10.
DR   MINT; MINT-5002070; -.
DR   STRING; 9606.ENSP00000316029; -.
DR   PhosphoSite; Q9Y490; -.
DR   DMDM; 81175200; -.
DR   OGP; Q9Y490; -.
DR   PaxDb; Q9Y490; -.
DR   PRIDE; Q9Y490; -.
DR   Ensembl; ENST00000314888; ENSP00000316029; ENSG00000137076.
DR   GeneID; 7094; -.
DR   KEGG; hsa:7094; -.
DR   UCSC; uc003zxt.2; human.
DR   CTD; 7094; -.
DR   GeneCards; GC09M035687; -.
DR   HGNC; HGNC:11845; TLN1.
DR   HPA; CAB002006; -.
DR   HPA; HPA004748; -.
DR   MIM; 186745; gene.
DR   neXtProt; NX_Q9Y490; -.
DR   PharmGKB; PA36547; -.
DR   eggNOG; NOG324465; -.
DR   HOGENOM; HOG000006734; -.
DR   HOVERGEN; HBG023870; -.
DR   InParanoid; Q9Y490; -.
DR   KO; K06271; -.
DR   OMA; ITNHEEY; -.
DR   OrthoDB; EOG7TBC1J; -.
DR   PhylomeDB; Q9Y490; -.
DR   TreeFam; TF314677; -.
DR   Reactome; REACT_111045; Developmental Biology.
DR   Reactome; REACT_111102; Signal Transduction.
DR   Reactome; REACT_17015; Metabolism of proteins.
DR   Reactome; REACT_17044; Muscle contraction.
DR   Reactome; REACT_604; Hemostasis.
DR   ChiTaRS; TLN1; human.
DR   EvolutionaryTrace; Q9Y490; -.
DR   GeneWiki; TLN1; -.
DR   GenomeRNAi; 7094; -.
DR   NextBio; 27751; -.
DR   PRO; PR:Q9Y490; -.
DR   ArrayExpress; Q9Y490; -.
DR   Bgee; Q9Y490; -.
DR   CleanEx; HS_TLN1; -.
DR   Genevestigator; Q9Y490; -.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005911; C:cell-cell junction; IC:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; NAS:UniProtKB.
DR   GO; GO:0005815; C:microtubule organizing center; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0001726; C:ruffle; ISS:HGNC.
DR   GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
DR   GO; GO:0030274; F:LIM domain binding; IPI:UniProtKB.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; NAS:UniProtKB.
DR   GO; GO:0017166; F:vinculin binding; IPI:UniProtKB.
DR   GO; GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
DR   GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR   GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
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:0006928; P:cellular component movement; NAS:UniProtKB.
DR   GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:Ensembl.
DR   GO; GO:0007016; P:cytoskeletal anchoring at plasma membrane; NAS:UniProtKB.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; TAS:Reactome.
DR   GO; GO:0006936; P:muscle contraction; TAS:Reactome.
DR   GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR   GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
DR   Gene3D; 1.20.1410.10; -; 3.
DR   Gene3D; 1.20.1420.10; -; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR002558; ILWEQ_dom.
DR   InterPro; IPR002404; Insln_rcpt_S1.
DR   InterPro; IPR011993; PH_like_dom.
DR   InterPro; IPR015710; Talin-1.
DR   InterPro; IPR015224; Talin_cent.
DR   InterPro; IPR015009; Vinculin-bd_dom.
DR   InterPro; IPR006077; Vinculin/catenin.
DR   PANTHER; PTHR19981:SF7; PTHR19981:SF7; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF01608; I_LWEQ; 1.
DR   Pfam; PF02174; IRS; 1.
DR   Pfam; PF09141; Talin_middle; 1.
DR   Pfam; PF08913; VBS; 2.
DR   ProDom; PD011820; ILWEQ; 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   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;
KW   Cell projection; Complete proteome; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Membrane; Phosphoprotein; Polymorphism;
KW   Reference proteome.
FT   CHAIN         1   2541       Talin-1.
FT                                /FTId=PRO_0000219428.
FT   DOMAIN       86    403       FERM.
FT   DOMAIN     2293   2533       I/LWEQ.
FT   REGION      280    435       Interaction with LAYN (By similarity).
FT   REGION     1327   1948       Interaction with SYNM.
FT   MOD_RES     425    425       Phosphoserine.
FT   MOD_RES    1116   1116       Phosphotyrosine (By similarity).
FT   MOD_RES    1544   1544       N6-acetyllysine (By similarity).
FT   MOD_RES    2031   2031       N6-acetyllysine.
FT   MOD_RES    2040   2040       Phosphoserine.
FT   MOD_RES    2115   2115       N6-acetyllysine.
FT   VARIANT    1227   1227       S -> L (in dbSNP:rs2295795).
FT                                /FTId=VAR_023751.
FT   VARIANT    1919   1919       R -> W (in dbSNP:rs17854239).
FT                                /FTId=VAR_023752.
FT   VARIANT    1984   1984       A -> T (in dbSNP:rs35642290).
FT                                /FTId=VAR_055538.
FT   CONFLICT    824    824       R -> G (in Ref. 1; AAD13152 and 2;
FT                                AAF23322).
FT   CONFLICT   1549   1549       A -> P (in Ref. 1; AAD13152 and 2;
FT                                AAF23322).
FT   CONFLICT   1604   1604       K -> Q (in Ref. 1; AAD13152 and 2;
FT                                AAF23322).
FT   CONFLICT   1701   1701       Q -> E (in Ref. 1; AAD13152 and 2;
FT                                AAF23322).
FT   CONFLICT   1718   1718       N -> H (in Ref. 1; AAD13152 and 2;
FT                                AAF23322).
FT   CONFLICT   1966   1966       A -> R (in Ref. 1; AAD13152).
FT   CONFLICT   2256   2256       Missing (in Ref. 2; AAF27330).
FT   HELIX       608    625
FT   HELIX      2079   2098
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
//
DBGET integrated database retrieval system