TLN1_MOUSE
ID TLN1_MOUSE Reviewed; 2541 AA.
AC P26039; A2AIM8; Q8VEF0;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Talin-1;
GN Name=Tln1; Synonyms=Tln;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Fibroblast;
RX PubMed=2120593; DOI=10.1038/347685a0;
RA Rees D.J.G., Ades S.A., Singer S.J., Hynes R.O.;
RT "Sequence and domain structure of talin.";
RL Nature 347:685-689(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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 [4]
RP INTERACTION WITH PTK2.
RX PubMed=7622520; DOI=10.1074/jbc.270.28.16995;
RA Chen H.C., Appeddu P.A., Parsons J.T., Hildebrand J.D., Schaller M.D.,
RA Guan J.L.;
RT "Interaction of focal adhesion kinase with cytoskeletal protein talin.";
RL J. Biol. Chem. 270:16995-16999(1995).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1116, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1116, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425; SER-446; SER-620;
RP SER-729; SER-1328; SER-1878 AND SER-2040, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP SUBCELLULAR LOCATION.
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 [10]
RP INTERACTION WITH APBB1IP AND VCL.
RX PubMed=23389036; DOI=10.1074/jbc.m112.438119;
RA Goult B.T., Zacharchenko T., Bate N., Tsang R., Hey F., Gingras A.R.,
RA Elliott P.R., Roberts G.C., Ballestrem C., Critchley D.R., Barsukov I.L.;
RT "RIAM and vinculin binding to talin are mutually exclusive and regulate
RT adhesion assembly and turnover.";
RL J. Biol. Chem. 288:8238-8249(2013).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1544, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 482-789 IN COMPLEX WITH VCL.
RX PubMed=15272303; DOI=10.1038/sj.emboj.7600285;
RA Papagrigoriou E., Gingras A.R., Barsukov I.L., Bate N., Fillingham I.J.,
RA Patel B., Frank R., Ziegler W.H., Roberts G.C.K., Critchley D.R.,
RA Emsley J.;
RT "Activation of a vinculin-binding site in the talin rod involves
RT rearrangement of a five-helix bundle.";
RL EMBO J. 23:2942-2951(2004).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 209-410 IN COMPLEX WITH PIP5K1C.
RX PubMed=15623515; DOI=10.1074/jbc.m413180200;
RA de Pereda J.M., Wegener K.L., Santelli E., Bate N., Ginsberg M.H.,
RA Critchley D.R., Campbell I.D., Liddington R.C.;
RT "Structural basis for phosphatidylinositol phosphate kinase type Igamma
RT binding to talin at focal adhesions.";
RL J. Biol. Chem. 280:8381-8386(2005).
RN [14]
RP STRUCTURE BY NMR OF 755-889, AND INTERACTION WITH VCL.
RX PubMed=15642262; DOI=10.1016/j.str.2004.11.006;
RA Fillingham I., Gingras A.R., Papagrigoriou E., Patel B., Emsley J.,
RA Critchley D.R., Roberts G.C.K., Barsukov I.L.;
RT "A vinculin binding domain from the talin rod unfolds to form a complex
RT with the vinculin head.";
RL Structure 13:65-74(2005).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1359-1659, AND INTERACTION WITH
RP F-ACTIN AND VCL.
RX PubMed=20610383; DOI=10.1074/jbc.m109.095455;
RA Gingras A.R., Bate N., Goult B.T., Patel B., Kopp P.M., Emsley J.,
RA Barsukov I.L., Roberts G.C., Critchley D.R.;
RT "Central region of talin has a unique fold that binds vinculin and actin.";
RL J. Biol. Chem. 285:29577-29587(2010).
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.
CC -!- SUBUNIT: Part of a complex composed of THSD1, PTK2/FAK1, TLN1 and VCL
CC (By similarity). Interacts with THSD1; this promotes interaction with
CC PTK2/FAK1 and VCL (By similarity). Interacts with NRAP and LAYN (By
CC similarity). Interacts with SYNM (By similarity). Interacts with ITGB1;
CC the interaction is prevented by competitive binding of ITGB1BP1 (By
CC similarity). Binds with high affinity to VCL and with low affinity to
CC integrins (PubMed:23389036, PubMed:20610383, PubMed:15642262,
CC PubMed:15272303). Interacts with APBB1IP; this inhibits VCL binding
CC (PubMed:23389036). Interacts with PTK2/FAK1 (PubMed:7622520). Interacts
CC with PIP5K1C (PubMed:15623515). Interacts with F-actin
CC (PubMed:20610383). {ECO:0000250|UniProtKB:P54939,
CC ECO:0000250|UniProtKB:Q9Y490, ECO:0000269|PubMed:15272303,
CC ECO:0000269|PubMed:15623515, ECO:0000269|PubMed:15642262,
CC ECO:0000269|PubMed:20610383, ECO:0000269|PubMed:23389036,
CC ECO:0000269|PubMed:7622520}.
CC -!- INTERACTION:
CC P26039; Q8R5A3: Apbb1ip; NbExp=8; IntAct=EBI-1039593, EBI-7450496;
CC P26039; Q64727: Vcl; NbExp=2; IntAct=EBI-1039593, EBI-432047;
CC P26039; P05556: ITGB1; Xeno; NbExp=2; IntAct=EBI-1039593, EBI-703066;
CC P26039; P05106: ITGB3; Xeno; NbExp=7; IntAct=EBI-1039593, EBI-702847;
CC P26039; P12003: VCL; Xeno; NbExp=5; IntAct=EBI-1039593, EBI-1039563;
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:0000269|PubMed:21768292}. Cell junction, focal adhesion
CC {ECO:0000269|PubMed:21768292}. Note=Colocalizes with LAYN at the
CC membrane ruffles (By similarity). Localized preferentially in focal
CC adhesions than fibrillar adhesions. {ECO:0000250}.
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DR EMBL; X56123; CAA39588.1; -; mRNA.
DR EMBL; AL732506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018557; AAH18557.1; -; mRNA.
DR EMBL; BC150810; AAI50811.1; -; mRNA.
DR CCDS; CCDS18101.1; -.
DR PIR; S11661; S11661.
DR RefSeq; NP_035732.2; NM_011602.5.
DR RefSeq; XP_006537832.2; XM_006537769.3.
DR PDB; 1SJ7; X-ray; 2.50 A; A/B/C=482-655.
DR PDB; 1SJ8; X-ray; 2.60 A; A=482-789.
DR PDB; 1T01; X-ray; 2.06 A; B=605-628.
DR PDB; 1U89; NMR; -; A=755-889.
DR PDB; 1Y19; X-ray; 2.60 A; B/D/F/H/J/L=209-410.
DR PDB; 1ZW3; X-ray; 3.30 A; B=1628-1652.
DR PDB; 2B0H; NMR; -; A=1843-1973.
DR PDB; 2G35; NMR; -; A=305-404.
DR PDB; 2JSW; NMR; -; A=2300-2482.
DR PDB; 2KBB; NMR; -; A=1655-1822.
DR PDB; 2KC1; NMR; -; A=1-85.
DR PDB; 2KC2; NMR; -; A=86-202.
DR PDB; 2KGX; NMR; -; A=1655-1822, B=311-401.
DR PDB; 2KMA; NMR; -; A=1-202.
DR PDB; 2KVP; NMR; -; A=1815-1973.
DR PDB; 2L10; NMR; -; A=1206-1357.
DR PDB; 2L7A; NMR; -; A=787-911.
DR PDB; 2L7N; NMR; -; A=1046-1207.
DR PDB; 2LQG; NMR; -; A=913-1044.
DR PDB; 2QDQ; X-ray; 2.20 A; A/B=2494-2541.
DR PDB; 2X0C; X-ray; 2.00 A; A=1359-1659.
DR PDB; 3DYJ; X-ray; 1.85 A; A/B=1974-2293.
DR PDB; 3IVF; X-ray; 1.94 A; A=1-400.
DR PDB; 3S90; X-ray; 1.97 A; C/D=1512-1546.
DR PDB; 4F7G; X-ray; 2.05 A; A=206-405, B=1654-1847.
DR PDB; 4W8P; X-ray; 1.50 A; A=1357-1657.
DR PDB; 5FZT; X-ray; 2.10 A; A=1359-1659.
DR PDB; 5IC0; X-ray; 1.97 A; A=1357-1822.
DR PDB; 5IC1; X-ray; 2.20 A; A=1357-1822.
DR PDB; 5NL1; X-ray; 2.50 A; A/B/C/D/E/F=480-635.
DR PDB; 6BA6; NMR; -; A=1-86.
DR PDB; 6MFS; X-ray; 2.85 A; A=1-136, A=169-400.
DR PDB; 6TWN; X-ray; 2.28 A; A/B=1359-1659.
DR PDB; 6VGU; X-ray; 2.78 A; A=1-430.
DR PDBsum; 1SJ7; -.
DR PDBsum; 1SJ8; -.
DR PDBsum; 1T01; -.
DR PDBsum; 1U89; -.
DR PDBsum; 1Y19; -.
DR PDBsum; 1ZW3; -.
DR PDBsum; 2B0H; -.
DR PDBsum; 2G35; -.
DR PDBsum; 2JSW; -.
DR PDBsum; 2KBB; -.
DR PDBsum; 2KC1; -.
DR PDBsum; 2KC2; -.
DR PDBsum; 2KGX; -.
DR PDBsum; 2KMA; -.
DR PDBsum; 2KVP; -.
DR PDBsum; 2L10; -.
DR PDBsum; 2L7A; -.
DR PDBsum; 2L7N; -.
DR PDBsum; 2LQG; -.
DR PDBsum; 2QDQ; -.
DR PDBsum; 2X0C; -.
DR PDBsum; 3DYJ; -.
DR PDBsum; 3IVF; -.
DR PDBsum; 3S90; -.
DR PDBsum; 4F7G; -.
DR PDBsum; 4W8P; -.
DR PDBsum; 5FZT; -.
DR PDBsum; 5IC0; -.
DR PDBsum; 5IC1; -.
DR PDBsum; 5NL1; -.
DR PDBsum; 6BA6; -.
DR PDBsum; 6MFS; -.
DR PDBsum; 6TWN; -.
DR PDBsum; 6VGU; -.
DR AlphaFoldDB; P26039; -.
DR BMRB; P26039; -.
DR SMR; P26039; -.
DR BioGRID; 204222; 28.
DR DIP; DIP-647N; -.
DR IntAct; P26039; 18.
DR MINT; P26039; -.
DR STRING; 10090.ENSMUSP00000030187; -.
DR iPTMnet; P26039; -.
DR PhosphoSitePlus; P26039; -.
DR SwissPalm; P26039; -.
DR CPTAC; non-CPTAC-3676; -.
DR EPD; P26039; -.
DR jPOST; P26039; -.
DR MaxQB; P26039; -.
DR PaxDb; P26039; -.
DR PeptideAtlas; P26039; -.
DR PRIDE; P26039; -.
DR ProteomicsDB; 259514; -.
DR Antibodypedia; 1497; 702 antibodies from 42 providers.
DR DNASU; 21894; -.
DR Ensembl; ENSMUST00000030187; ENSMUSP00000030187; ENSMUSG00000028465.
DR GeneID; 21894; -.
DR KEGG; mmu:21894; -.
DR UCSC; uc008sqe.2; mouse.
DR CTD; 7094; -.
DR MGI; MGI:1099832; Tln1.
DR VEuPathDB; HostDB:ENSMUSG00000028465; -.
DR eggNOG; KOG4261; Eukaryota.
DR GeneTree; ENSGT00940000157006; -.
DR HOGENOM; CLU_000364_1_1_1; -.
DR InParanoid; P26039; -.
DR OMA; VDMTQHY; -.
DR OrthoDB; 9839at2759; -.
DR PhylomeDB; P26039; -.
DR TreeFam; TF314677; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-354192; Integrin signaling.
DR Reactome; R-MMU-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-MMU-372708; p130Cas linkage to MAPK signaling for integrins.
DR Reactome; R-MMU-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-MMU-445355; Smooth Muscle Contraction.
DR Reactome; R-MMU-5674135; MAP2K and MAPK activation.
DR BioGRID-ORCS; 21894; 10 hits in 72 CRISPR screens.
DR ChiTaRS; Tln1; mouse.
DR EvolutionaryTrace; P26039; -.
DR PRO; PR:P26039; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P26039; protein.
DR Bgee; ENSMUSG00000028465; Expressed in granulocyte and 266 other tissues.
DR ExpressionAtlas; P26039; baseline and differential.
DR Genevisible; P26039; MM.
DR GO; GO:0005912; C:adherens junction; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IDA:MGI.
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:0005178; F:integrin binding; IMP:CAFA.
DR GO; GO:0030274; F:LIM domain binding; ISO:MGI.
DR GO; GO:0035091; F:phosphatidylinositol binding; IMP:CAFA.
DR GO; GO:0001786; F:phosphatidylserine binding; IMP:CAFA.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0017166; F:vinculin binding; ISO:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007044; P:cell-substrate junction assembly; IMP:MGI.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:MGI.
DR GO; GO:0033622; P:integrin activation; IMP:CAFA.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:CAFA.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd12150; talin-RS; 1.
DR DisProt; DP00653; -.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR IDEAL; IID50205; -.
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; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..2541
FT /note="Talin-1"
FT /id="PRO_0000219429"
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:0000250|UniProtKB:P54939"
FT REGION 1359..1659
FT /note="Interaction with VCL and F-actin"
FT /evidence="ECO:0000269|PubMed:20610383"
FT MOD_RES 167
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y490"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y490"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1021
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y490"
FT MOD_RES 1116
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455,
FT ECO:0007744|PubMed:18034455"
FT MOD_RES 1142
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y490"
FT MOD_RES 1201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y490"
FT MOD_RES 1225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y490"
FT MOD_RES 1263
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y490"
FT MOD_RES 1323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y490"
FT MOD_RES 1328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1544
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1849
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y490"
FT MOD_RES 1855
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y490"
FT MOD_RES 1878
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2031
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y490"
FT MOD_RES 2040
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2115
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y490"
FT VARIANT 1105
FT /note="L -> P"
FT VARIANT 2180
FT /note="K -> M"
FT CONFLICT 673
FT /note="K -> N (in Ref. 1; CAA39588)"
FT /evidence="ECO:0000305"
FT CONFLICT 1227
FT /note="S -> L (in Ref. 1; CAA39588)"
FT /evidence="ECO:0000305"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:3IVF"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:3IVF"
FT HELIX 25..33
FT /evidence="ECO:0007829|PDB:3IVF"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:3IVF"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:3IVF"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:3IVF"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:3IVF"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:2KC1"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:6BA6"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:3IVF"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:3IVF"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:3IVF"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:6VGU"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:3IVF"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:3IVF"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:3IVF"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:3IVF"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:2KMA"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:2KC2"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:2KC2"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:2KC2"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:3IVF"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:3IVF"
FT HELIX 209..224
FT /evidence="ECO:0007829|PDB:3IVF"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:3IVF"
FT HELIX 232..247
FT /evidence="ECO:0007829|PDB:3IVF"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:3IVF"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:3IVF"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:3IVF"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:3IVF"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:3IVF"
FT HELIX 291..304
FT /evidence="ECO:0007829|PDB:3IVF"
FT TURN 306..309
FT /evidence="ECO:0007829|PDB:3IVF"
FT STRAND 311..318
FT /evidence="ECO:0007829|PDB:3IVF"
FT STRAND 325..332
FT /evidence="ECO:0007829|PDB:3IVF"
FT STRAND 334..341
FT /evidence="ECO:0007829|PDB:3IVF"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:3IVF"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:3IVF"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:3IVF"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:3IVF"
FT STRAND 365..369
FT /evidence="ECO:0007829|PDB:3IVF"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:3IVF"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:3IVF"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:3IVF"
FT HELIX 385..397
FT /evidence="ECO:0007829|PDB:3IVF"
FT HELIX 493..512
FT /evidence="ECO:0007829|PDB:1SJ7"
FT HELIX 526..560
FT /evidence="ECO:0007829|PDB:1SJ7"
FT STRAND 565..567
FT /evidence="ECO:0007829|PDB:1SJ7"
FT HELIX 570..600
FT /evidence="ECO:0007829|PDB:1SJ7"
FT HELIX 606..626
FT /evidence="ECO:0007829|PDB:1T01"
FT HELIX 634..652
FT /evidence="ECO:0007829|PDB:1SJ7"
FT HELIX 664..690
FT /evidence="ECO:0007829|PDB:1SJ8"
FT STRAND 696..699
FT /evidence="ECO:0007829|PDB:1SJ8"
FT HELIX 700..723
FT /evidence="ECO:0007829|PDB:1SJ8"
FT TURN 724..726
FT /evidence="ECO:0007829|PDB:1SJ8"
FT HELIX 730..756
FT /evidence="ECO:0007829|PDB:1SJ8"
FT HELIX 762..780
FT /evidence="ECO:0007829|PDB:1SJ8"
FT STRAND 787..790
FT /evidence="ECO:0007829|PDB:2L7A"
FT STRAND 792..794
FT /evidence="ECO:0007829|PDB:1U89"
FT HELIX 799..814
FT /evidence="ECO:0007829|PDB:1U89"
FT TURN 815..817
FT /evidence="ECO:0007829|PDB:1U89"
FT HELIX 820..843
FT /evidence="ECO:0007829|PDB:1U89"
FT HELIX 844..846
FT /evidence="ECO:0007829|PDB:1U89"
FT HELIX 850..876
FT /evidence="ECO:0007829|PDB:1U89"
FT STRAND 878..880
FT /evidence="ECO:0007829|PDB:1U89"
FT HELIX 884..907
FT /evidence="ECO:0007829|PDB:2L7A"
FT HELIX 914..938
FT /evidence="ECO:0007829|PDB:2LQG"
FT STRAND 943..946
FT /evidence="ECO:0007829|PDB:2LQG"
FT HELIX 951..975
FT /evidence="ECO:0007829|PDB:2LQG"
FT HELIX 980..1007
FT /evidence="ECO:0007829|PDB:2LQG"
FT HELIX 1008..1010
FT /evidence="ECO:0007829|PDB:2LQG"
FT HELIX 1014..1042
FT /evidence="ECO:0007829|PDB:2LQG"
FT HELIX 1049..1073
FT /evidence="ECO:0007829|PDB:2L7N"
FT HELIX 1084..1105
FT /evidence="ECO:0007829|PDB:2L7N"
FT HELIX 1115..1141
FT /evidence="ECO:0007829|PDB:2L7N"
FT HELIX 1147..1172
FT /evidence="ECO:0007829|PDB:2L7N"
FT STRAND 1174..1177
FT /evidence="ECO:0007829|PDB:2L7N"
FT HELIX 1179..1201
FT /evidence="ECO:0007829|PDB:2L7N"
FT HELIX 1207..1223
FT /evidence="ECO:0007829|PDB:2L10"
FT TURN 1224..1226
FT /evidence="ECO:0007829|PDB:2L10"
FT HELIX 1235..1260
FT /evidence="ECO:0007829|PDB:2L10"
FT HELIX 1264..1289
FT /evidence="ECO:0007829|PDB:2L10"
FT HELIX 1295..1324
FT /evidence="ECO:0007829|PDB:2L10"
FT HELIX 1329..1353
FT /evidence="ECO:0007829|PDB:2L10"
FT HELIX 1360..1373
FT /evidence="ECO:0007829|PDB:4W8P"
FT HELIX 1374..1377
FT /evidence="ECO:0007829|PDB:4W8P"
FT STRAND 1384..1386
FT /evidence="ECO:0007829|PDB:5IC0"
FT HELIX 1389..1416
FT /evidence="ECO:0007829|PDB:4W8P"
FT HELIX 1419..1450
FT /evidence="ECO:0007829|PDB:4W8P"
FT HELIX 1464..1480
FT /evidence="ECO:0007829|PDB:4W8P"
FT HELIX 1488..1515
FT /evidence="ECO:0007829|PDB:4W8P"
FT HELIX 1519..1548
FT /evidence="ECO:0007829|PDB:4W8P"
FT HELIX 1552..1576
FT /evidence="ECO:0007829|PDB:4W8P"
FT HELIX 1579..1581
FT /evidence="ECO:0007829|PDB:4W8P"
FT HELIX 1590..1622
FT /evidence="ECO:0007829|PDB:4W8P"
FT HELIX 1627..1653
FT /evidence="ECO:0007829|PDB:4W8P"
FT HELIX 1658..1683
FT /evidence="ECO:0007829|PDB:5IC0"
FT HELIX 1695..1722
FT /evidence="ECO:0007829|PDB:5IC0"
FT HELIX 1724..1751
FT /evidence="ECO:0007829|PDB:5IC0"
FT HELIX 1755..1782
FT /evidence="ECO:0007829|PDB:5IC0"
FT HELIX 1786..1788
FT /evidence="ECO:0007829|PDB:5IC1"
FT HELIX 1790..1818
FT /evidence="ECO:0007829|PDB:5IC0"
FT STRAND 1822..1824
FT /evidence="ECO:0007829|PDB:2KVP"
FT HELIX 1827..1840
FT /evidence="ECO:0007829|PDB:2KVP"
FT HELIX 1847..1874
FT /evidence="ECO:0007829|PDB:2B0H"
FT TURN 1875..1877
FT /evidence="ECO:0007829|PDB:2B0H"
FT HELIX 1879..1881
FT /evidence="ECO:0007829|PDB:2KVP"
FT HELIX 1882..1904
FT /evidence="ECO:0007829|PDB:2B0H"
FT STRAND 1907..1909
FT /evidence="ECO:0007829|PDB:2KVP"
FT HELIX 1910..1939
FT /evidence="ECO:0007829|PDB:2B0H"
FT HELIX 1944..1968
FT /evidence="ECO:0007829|PDB:2B0H"
FT HELIX 1969..1971
FT /evidence="ECO:0007829|PDB:2B0H"
FT HELIX 1976..2000
FT /evidence="ECO:0007829|PDB:3DYJ"
FT HELIX 2012..2014
FT /evidence="ECO:0007829|PDB:3DYJ"
FT HELIX 2016..2036
FT /evidence="ECO:0007829|PDB:3DYJ"
FT STRAND 2037..2039
FT /evidence="ECO:0007829|PDB:3DYJ"
FT HELIX 2041..2068
FT /evidence="ECO:0007829|PDB:3DYJ"
FT HELIX 2074..2100
FT /evidence="ECO:0007829|PDB:3DYJ"
FT TURN 2101..2103
FT /evidence="ECO:0007829|PDB:3DYJ"
FT HELIX 2109..2161
FT /evidence="ECO:0007829|PDB:3DYJ"
FT STRAND 2162..2164
FT /evidence="ECO:0007829|PDB:3DYJ"
FT HELIX 2172..2195
FT /evidence="ECO:0007829|PDB:3DYJ"
FT HELIX 2198..2223
FT /evidence="ECO:0007829|PDB:3DYJ"
FT HELIX 2230..2259
FT /evidence="ECO:0007829|PDB:3DYJ"
FT HELIX 2263..2288
FT /evidence="ECO:0007829|PDB:3DYJ"
FT HELIX 2301..2324
FT /evidence="ECO:0007829|PDB:2JSW"
FT STRAND 2332..2334
FT /evidence="ECO:0007829|PDB:2JSW"
FT HELIX 2341..2373
FT /evidence="ECO:0007829|PDB:2JSW"
FT HELIX 2380..2382
FT /evidence="ECO:0007829|PDB:2JSW"
FT HELIX 2383..2416
FT /evidence="ECO:0007829|PDB:2JSW"
FT HELIX 2421..2442
FT /evidence="ECO:0007829|PDB:2JSW"
FT TURN 2443..2445
FT /evidence="ECO:0007829|PDB:2JSW"
FT HELIX 2451..2476
FT /evidence="ECO:0007829|PDB:2JSW"
FT HELIX 2497..2528
FT /evidence="ECO:0007829|PDB:2QDQ"
SQ SEQUENCE 2541 AA; 269821 MW; 78832388E2392B8E CRC64;
MVALSLKISI GNVVKTMQFE PSTMVYDACR MIRERIPEAL AGPPNDFGLF LSDDDPKKGI
WLEAGKALDY YMLRNGDTME YRKKQRPLKI RMLDGTVKTI MVDDSKTVTD MLMTICARIG
ITNHDEYSLV RELMEEKKDE GTGTLRKDKT LLRDEKKMEK LKQKLHTDDE LNWLDHGRTL
REQGVEEHET LLLRRKFFYS DQNVDSRDPV QLNLLYVQAR DDILNGSHPV SFDKACEFAG
FQCQIQFGPH NEQKHKAGFL DLKDFLPKEY VKQKGERKIF QAHKNCGQMS EIEAKVRYVK
LARSLKTYGV SFFLVKEKMK GKNKLVPRLL GITKECVMRV DEKTKEVIQE WSLTNIKRWA
ASPKSFTLDF GDYQDGYYSV QTTEGEQIAQ LIAGYIDIIL KKKKSKDHFG LEGDEESTML
EDSVSPKKST VLQQQYNRVG KVEHGSVALP AIMRSGASGP ENFQVGSMPP AQQQITSGQM
HRGHMPPLTS AQQALTGTIN SSMQAVQAAQ ATLDDFETLP PLGQDAASKA WRKNKMDESK
HEIHSQVDAI TAGTASVVNL TAGDPAETDY TAVGCAVTTI SSNLTEMSRG VKLLAALLED
EGGNGRPLLQ AAKGLAGAVS ELLRSAQPAS AEPRQNLLQA AGNVGQASGE LLQQIGESDT
DPHFQDVLMQ 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 APKASAGPQP LLVQSCKAVA
EQIPLLVQGV RGSQAQPDSP SAQLALIAAS QSFLQPGGKM VAAAKASVPT IQDQASAMQL
SQCAKNLGTA LAELRTAAQK AQEACGPLEM DSALSVVQNL EKDLQEIKAA ARDGKLKPLP
GETMEKCTQD LGNSTKAVSS AIAKLLGEIA QGNENYAGIA ARDVAGGLRS LAQAARGVAA
LTSDPAVQAI VLDTASDVLD KASSLIEEAK KASGHPGDPE SQQRLAQVAK AVTQALNRCV
SCLPGQRDVD NALRAVGDAS KRLLSDSLPP STGTFQEAQS RLNEAAAGLN QAATELVQAS
RGTPQDLARA SGRFGQDFST FLEAGVEMAG QAPSQEDRAQ VVSNLKGISM SSSKLLLAAK
ALSTDPASPN LKSQLAAAAR AVTDSINQLI TMCTQQAPGQ KECDNALRQL ETVRELLENP
VQPINDMSYF GCLDSVMENS KVLGEAMTGI SQNAKNGNLP EFGDAIATAS KALCGFTEAA
AQAAYLVGVS DPNSQAGQQG LVEPTQFARA NQAIQMACQS LGEPGCTQAQ VLSAATIVAK
HTSALCNSCR LASARTANPT AKRQFVQSAK EVANSTANLV KTIKALDGDF TEENRAQCRA
ATAPLLEAVD NLSAFASNPE FSSVPAQISP EGRAAMEPIV ISAKTMLESA GGLIQTARAL
AVNPRDPPRW SVLAGHSRTV SDSIKKLITS MRDKAPGQLE CETAIAALNS CLRDLDQASL
AAVSQQLAPR EGISQEALHT QMLTAVQEIS HLIEPLASAA RAEASQLGHK VSQMAQYFEP
LTLAAVGAAS KTLSHPQQMA LLDQTKTLAE SALQLLYTAK EAGGNPKQAA HTQEALEEAV
QMMTEAVEDL TTTLNEAASA AGVVGGMVDS ITQAINQLDE GPMGDPEGSF VDYQTTMVRT
AKAIAVTVQE MVTKSNTSPE ELGPLANQLT SDYGRLASQA KPAAVAAENE EIGAHIKHRV
QELGHGCSAL VTKAGALQCS PSDVYTKKEL IECARRVSEK VSHVLAALQA GNRGTQACIT
AASAVSGIIA DLDTTIMFAT AGTLNREGAE TFADHREGIL KTAKVLVEDT KVLVQNAAGS
QEKLAQAAQS SVATITRLAD VVKLGAASLG AEDPETQVVL INAVKDVAKA LGDLISATKA
AAGKVGDDPA VWQLKNSAKV MVTNVTSLLK TVKAVEDEAT KGTRALEATT EHIRQELAVF
CSPEPPAKTS TPEDFIRMTK GITMATAKAV AAGNSCRQED VIATANLSRR AIADMLRACK
EAAFHPEVAP DVRLRALHYG RECANGYLEL LDHVLLTLQK PNPDLKQQLT GHSKRVAGSV
TELIQAAEAM KGTEWVDPED PTVIAENELL GAAAAIEAAA KKLEQLKPRA KPKEADESLN
FEEQILEAAK SIAAATSALV KAASAAQREL VAQGKVGAIP ANALDDGQWS QGLISAARMV
AAATNNLCEA ANAAVQGHAS QEKLISSAKQ VAASTAQLLV ACKVKADQDS EAMKRLQAAG
NAVKRASDNL VKAAQKAAAF EDQENETVVV KEKMVGGIAQ IIAAQEEMLR KERELEEARK
KLAQIRQQQY KFLPSELRDE H
