TPM1_HUMAN
ID TPM1_HUMAN Reviewed; 284 AA.
AC P09493; B7Z5T7; D9YZV2; D9YZV3; D9YZV8; P09494; P10469; Q6DV89; Q6DV90;
AC Q7Z6L8; Q86W64; Q96IK2; Q9UCI1; Q9UCI2; Q9UCY9; Q9Y427;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 227.
DE RecName: Full=Tropomyosin alpha-1 chain;
DE AltName: Full=Alpha-tropomyosin;
DE AltName: Full=Tropomyosin-1;
GN Name=TPM1; Synonyms=C15orf13, TMSA;
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 PROTEIN SEQUENCE (ISOFORM 1), AND ACETYLATION AT MET-1.
RX PubMed=3548719; DOI=10.1016/0006-291x(87)91486-0;
RA Mische S.M., Manjula B.N., Fischetti V.A.;
RT "Relation of streptococcal M protein with human and rabbit tropomyosin: the
RT complete amino acid sequence of human cardiac alpha tropomyosin, a highly
RT conserved contractile protein.";
RL Biochem. Biophys. Res. Commun. 142:813-818(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Fibroblast;
RX PubMed=3336357; DOI=10.1128/mcb.8.1.160-168.1988;
RA Lin C.-S., Leavitt J.;
RT "Cloning and characterization of a cDNA encoding transformation-sensitive
RT tropomyosin isoform 3 from tumorigenic human fibroblasts.";
RL Mol. Cell. Biol. 8:160-168(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RX PubMed=3336363; DOI=10.1128/mcb.8.1.433-440.1988;
RA McLeod A.R., Gooding C.;
RT "Human hTM alpha gene: expression in muscle and nonmuscle tissue.";
RL Mol. Cell. Biol. 8:433-440(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 6), AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=15249230; DOI=10.1016/j.bbrc.2004.06.084;
RA Denz C.R., Narshi A., Zajdel R.W., Dube D.K.;
RT "Expression of a novel cardiac-specific tropomyosin isoform in humans.";
RL Biochem. Biophys. Res. Commun. 320:1291-1297(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [9]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC TISSUE=Brain, Hippocampus, and Placenta;
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 [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 58-284 (ISOFORM 2).
RC TISSUE=Liver;
RX PubMed=3138425; DOI=10.1007/bf02100079;
RA Colote S., Widada J.S., Ferraz C., Bonhomme F., Marti J., Liautard J.-P.;
RT "Evolution of tropomyosin functional domains: differential splicing and
RT genomic constraints.";
RL J. Mol. Evol. 27:228-235(1988).
RN [12]
RP PROTEIN SEQUENCE OF 134-149 AND 153-167.
RC TISSUE=Colon;
RX PubMed=8450225;
RA Das K.M., Dasgupta A., Mandal A., Geng X.;
RT "Autoimmunity to cytoskeletal protein tropomyosin. A clue to the
RT pathogenetic mechanism for ulcerative colitis.";
RL J. Immunol. 150:2487-2493(1993).
RN [13]
RP MASS SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=11840567;
RX DOI=10.1002/1615-9861(200202)2:2<212::aid-prot212>3.0.co;2-h;
RA Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A.,
RA Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J.,
RA Zvelebil M.J.;
RT "Cluster analysis of an extensive human breast cancer cell line protein
RT expression map database.";
RL Proteomics 2:212-223(2002).
RN [14]
RP PHOSPHORYLATION AT SER-283, AND MUTAGENESIS OF SER-283.
RX PubMed=17895359; DOI=10.1242/jcs.003251;
RA Houle F., Poirier A., Dumaresq J., Huot J.;
RT "DAP kinase mediates the phosphorylation of tropomyosin-1 downstream of the
RT ERK pathway, which regulates the formation of stress fibers in response to
RT oxidative stress.";
RL J. Cell Sci. 120:3666-3677(2007).
RN [15]
RP TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Ahamed M.E.;
RL Submitted (APR-2007) to UniProtKB.
RN [16]
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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-213 (ISOFORMS 10; 3; 4 AND 8),
RP AND 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 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 [19]
RP FUNCTION, CHARACTERIZATION OF VARIANTS CMH3 ASN-175 AND GLY-180, AND
RP SUBUNIT.
RX PubMed=23170982; DOI=10.1021/bi301323n;
RA Janco M., Kalyva A., Scellini B., Piroddi N., Tesi C., Poggesi C.,
RA Geeves M.A.;
RT "alpha-Tropomyosin with a D175N or E180G mutation in only one chain differs
RT from tropomyosin with mutations in both chains.";
RL Biochemistry 51:9880-9890(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-31 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-51 (ISOFORM 5), AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [21]
RP INTERACTION WITH LMOD2.
RX PubMed=26873245; DOI=10.1016/j.bbapap.2016.02.009;
RA Colpan M., Tolkatchev D., Grover S., Helms G.L., Cort J.R., Moroz N.,
RA Kostyukova A.S.;
RT "Localization of the binding interface between leiomodin-2 and alpha-
RT tropomyosin.";
RL Biochim. Biophys. Acta 1864:523-530(2016).
RN [22]
RP VARIANTS CMH3 ASN-175 AND GLY-180.
RX PubMed=8205619; DOI=10.1016/0092-8674(94)90054-x;
RA Thierfelder L., Watkins H., Macrae C., Lamas R., McKenna W.J.,
RA Vosberg H.-P., Seidman J.G., Seidman C.E.;
RT "Alpha-tropomyosin and cardiac troponin T mutations cause familial
RT hypertrophic cardiomyopathy: a disease of the sarcomere.";
RL Cell 77:701-712(1994).
RN [23]
RP VARIANTS CMH3 VAL-63 AND ASN-175.
RX PubMed=8523464; DOI=10.1016/0022-2828(95)90026-8;
RA Nakajima-Taniguchi C., Matsui H., Nagata S., Kishimoto T.,
RA Yamauchi-Takihara K.;
RT "Novel missense mutation in alpha-tropomyosin gene found in Japanese
RT patients with hypertrophic cardiomyopathy.";
RL J. Mol. Cell. Cardiol. 27:2053-2058(1995).
RN [24]
RP VARIANT CMH3 ASN-175.
RX PubMed=7898523; DOI=10.1056/nejm199504203321603;
RA Watkins H., McKenna W.J., Thierfelder L., Suk H.J., Anan R., O'Donoghue A.,
RA Spirito P., Matsumori A., Moravec C.S., Seidman J.G., Seidman C.E.;
RT "Mutations in the genes for cardiac troponin T and alpha-tropomyosin in
RT hypertrophic cardiomyopathy.";
RL N. Engl. J. Med. 332:1058-1064(1995).
RN [25]
RP VARIANT CMH3 ASN-175.
RX PubMed=9822100; DOI=10.1016/s0735-1097(98)00448-3;
RA Jaeaeskelaeinen P., Soranta M., Miettinen R., Saarinen L., Pihlajamaeki J.,
RA Silvennoinen K., Tikanoja T., Laakso M., Kuusisto J.;
RT "The cardiac beta-myosin heavy chain gene is not the predominant gene for
RT hypertrophic cardiomyopathy in the Finnish population.";
RL J. Am. Coll. Cardiol. 32:1709-1716(1998).
RN [26]
RP VARIANTS CMD1Y LYS-40 AND LYS-54.
RX PubMed=11273725; DOI=10.1006/jmcc.2000.1339;
RA Olson T.M., Kishimoto N.Y., Whitby F.G., Michels V.V.;
RT "Mutations that alter the surface charge of alpha-tropomyosin are
RT associated with dilated cardiomyopathy.";
RL J. Mol. Cell. Cardiol. 33:723-732(2001).
RN [27]
RP VARIANT CMH3 VAL-180.
RX PubMed=12974739; DOI=10.1034/j.1399-0004.2003.00151.x;
RA Erdmann J., Daehmlow S., Wischke S., Senyuva M., Werner U., Raible J.,
RA Tanis N., Dyachenko S., Hummel M., Hetzer R., Regitz-Zagrosek V.;
RT "Mutation spectrum in a large cohort of unrelated consecutive patients with
RT hypertrophic cardiomyopathy.";
RL Clin. Genet. 64:339-349(2003).
RN [28]
RP VARIANTS LVNC9 LYS-192 AND GLU-248.
RX PubMed=21551322; DOI=10.1161/circgenetics.110.959270;
RA Probst S., Oechslin E., Schuler P., Greutmann M., Boye P., Knirsch W.,
RA Berger F., Thierfelder L., Jenni R., Klaassen S.;
RT "Sarcomere gene mutations in isolated left ventricular noncompaction
RT cardiomyopathy do not predict clinical phenotype.";
RL Circ. Cardiovasc. Genet. 4:367-374(2011).
CC -!- FUNCTION: Binds to actin filaments in muscle and non-muscle cells
CC (PubMed:23170982). Plays a central role, in association with the
CC troponin complex, in the calcium dependent regulation of vertebrate
CC striated muscle contraction (PubMed:23170982). Smooth muscle
CC contraction is regulated by interaction with caldesmon. In non-muscle
CC cells is implicated in stabilizing cytoskeleton actin filaments.
CC -!- SUBUNIT: Homodimer (PubMed:23170982). Heterodimer of an alpha (TPM1,
CC TPM3 or TPM4) and a beta (TPM2) chain (By similarity). Interacts with
CC HRG (via the HRR domain); the interaction contributes to the
CC antiangiogenic properties of the histidine/proline-rich region (HRR) of
CC HRG (By similarity). Interacts (via N-terminus) with LMOD2 (via N-
CC terminus) and TMOD1 (via N-terminus) (PubMed:26873245). {ECO:0000250,
CC ECO:0000250|UniProtKB:P04268, ECO:0000250|UniProtKB:P04692,
CC ECO:0000269|PubMed:23170982, ECO:0000269|PubMed:26873245}.
CC -!- INTERACTION:
CC P09493; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-351158, EBI-747505;
CC P09493; Q8TC20: CAGE1; NbExp=3; IntAct=EBI-351158, EBI-10196469;
CC P09493; Q08379: GOLGA2; NbExp=3; IntAct=EBI-351158, EBI-618309;
CC P09493; Q9BQD3: KXD1; NbExp=4; IntAct=EBI-351158, EBI-739657;
CC P09493; Q9Y6D9: MAD1L1; NbExp=6; IntAct=EBI-351158, EBI-742610;
CC P09493; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-351158, EBI-6872807;
CC P09493; P13805: TNNT1; NbExp=4; IntAct=EBI-351158, EBI-726527;
CC P09493-5; Q08379: GOLGA2; NbExp=3; IntAct=EBI-10196387, EBI-618309;
CC P09493-5; V9HW56: HEL-S-108; NbExp=3; IntAct=EBI-10196387, EBI-10330141;
CC P09493-5; Q9BQD3: KXD1; NbExp=3; IntAct=EBI-10196387, EBI-739657;
CC P09493-5; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-10196387, EBI-6872807;
CC P09493-5; P0C1Z6-2: TFPT; NbExp=3; IntAct=EBI-10196387, EBI-10178002;
CC P09493-10; Q9UL45: BLOC1S6; NbExp=5; IntAct=EBI-12123928, EBI-465781;
CC P09493-10; Q8TC20-4: CAGE1; NbExp=4; IntAct=EBI-12123928, EBI-11522698;
CC P09493-10; Q2M329: CCDC96; NbExp=3; IntAct=EBI-12123928, EBI-12382974;
CC P09493-10; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-12123928, EBI-10175300;
CC P09493-10; Q8IZT9: FAM9C; NbExp=3; IntAct=EBI-12123928, EBI-2870039;
CC P09493-10; P02671-2: FGA; NbExp=3; IntAct=EBI-12123928, EBI-9640259;
CC P09493-10; Q08379: GOLGA2; NbExp=3; IntAct=EBI-12123928, EBI-618309;
CC P09493-10; O14879: IFIT3; NbExp=4; IntAct=EBI-12123928, EBI-745127;
CC P09493-10; Q9BQD3: KXD1; NbExp=7; IntAct=EBI-12123928, EBI-739657;
CC P09493-10; Q9Y6D9: MAD1L1; NbExp=6; IntAct=EBI-12123928, EBI-742610;
CC P09493-10; P62195: PSMC5; NbExp=3; IntAct=EBI-12123928, EBI-357745;
CC P09493-10; Q8N0S2: SYCE1; NbExp=4; IntAct=EBI-12123928, EBI-6872807;
CC P09493-10; P0C1Z6: TFPT; NbExp=3; IntAct=EBI-12123928, EBI-1245626;
CC P09493-10; P13805-3: TNNT1; NbExp=4; IntAct=EBI-12123928, EBI-12151635;
CC P09493-10; O95619: YEATS4; NbExp=3; IntAct=EBI-12123928, EBI-399269;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P04692}. Note=Associates with F-actin stress
CC fibers. {ECO:0000250|UniProtKB:P04692}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Skeletal muscle, TPM1alpha;
CC IsoId=P09493-1; Sequence=Displayed;
CC Name=2; Synonyms=Smooth muscle;
CC IsoId=P09493-2; Sequence=VSP_006576, VSP_006578, VSP_006579;
CC Name=3; Synonyms=Fibroblast, TM3;
CC IsoId=P09493-3; Sequence=VSP_006577, VSP_006579;
CC Name=4;
CC IsoId=P09493-4; Sequence=VSP_006577;
CC Name=5;
CC IsoId=P09493-5; Sequence=VSP_017498, VSP_017499;
CC Name=6; Synonyms=10, TPM1kappa;
CC IsoId=P09493-6; Sequence=VSP_036064;
CC Name=7;
CC IsoId=P09493-7; Sequence=VSP_036064, VSP_006579;
CC Name=8;
CC IsoId=P09493-8; Sequence=VSP_047297, VSP_047298, VSP_047299,
CC VSP_047300, VSP_006579;
CC Name=9;
CC IsoId=P09493-9; Sequence=VSP_006579;
CC Name=10;
CC IsoId=P09493-10; Sequence=VSP_047299, VSP_047300, VSP_047301;
CC -!- TISSUE SPECIFICITY: Detected in primary breast cancer tissues but
CC undetectable in normal breast tissues in Sudanese patients. Isoform 1
CC is expressed in adult and fetal skeletal muscle and cardiac tissues,
CC with higher expression levels in the cardiac tissues. Isoform 10 is
CC expressed in adult and fetal cardiac tissues, but not in skeletal
CC muscle. {ECO:0000269|PubMed:15249230, ECO:0000269|Ref.15}.
CC -!- DOMAIN: The molecule is in a coiled coil structure that is formed by 2
CC polypeptide chains. The sequence exhibits a prominent seven-residues
CC periodicity.
CC -!- PTM: Phosphorylated at Ser-283 by DAPK1 in response to oxidative stress
CC and this phosphorylation enhances stress fiber formation in endothelial
CC cells. {ECO:0000269|PubMed:17895359}.
CC -!- MASS SPECTROMETRY: [Isoform 3]: Mass=32875.93; Method=MALDI; Note=The
CC measured range is 1-284.; Evidence={ECO:0000269|PubMed:11840567};
CC -!- DISEASE: Cardiomyopathy, familial hypertrophic 3 (CMH3) [MIM:115196]: A
CC hereditary heart disorder characterized by ventricular hypertrophy,
CC which is usually asymmetric and often involves the interventricular
CC septum. The symptoms include dyspnea, syncope, collapse, palpitations,
CC and chest pain. They can be readily provoked by exercise. The disorder
CC has inter- and intrafamilial variability ranging from benign to
CC malignant forms with high risk of cardiac failure and sudden cardiac
CC death. {ECO:0000269|PubMed:12974739, ECO:0000269|PubMed:23170982,
CC ECO:0000269|PubMed:7898523, ECO:0000269|PubMed:8205619,
CC ECO:0000269|PubMed:8523464, ECO:0000269|PubMed:9822100}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Cardiomyopathy, dilated 1Y (CMD1Y) [MIM:611878]: A disorder
CC characterized by ventricular dilation and impaired systolic function,
CC resulting in congestive heart failure and arrhythmia. Patients are at
CC risk of premature death. {ECO:0000269|PubMed:11273725}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Left ventricular non-compaction 9 (LVNC9) [MIM:611878]: A form
CC of left ventricular non-compaction, a cardiomyopathy due to myocardial
CC morphogenesis arrest and characterized by a hypertrophic left
CC ventricle, a severely thickened 2-layered myocardium, numerous
CC prominent trabeculations, deep intertrabecular recesses, and poor
CC systolic function. Clinical manifestations are variable. Some affected
CC individuals experience no symptoms at all, others develop heart
CC failure. In some cases, left ventricular non-compaction is associated
CC with other congenital heart anomalies. LVNC9 is an autosomal dominant
CC condition. {ECO:0000269|PubMed:21551322}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: Incomplete sequence. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
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DR EMBL; M19267; AAA36771.1; -; mRNA.
DR EMBL; M19713; AAA61225.1; -; mRNA.
DR EMBL; M19714; AAA61226.1; -; mRNA.
DR EMBL; M19715; AAA61227.1; -; mRNA.
DR EMBL; AY640414; AAT68294.1; -; mRNA.
DR EMBL; AY640415; AAT68295.1; -; mRNA.
DR EMBL; AK299387; BAH13023.1; -; mRNA.
DR EMBL; AL050179; CAB43309.2; -; mRNA.
DR EMBL; GU324929; ADL14500.1; -; Genomic_DNA.
DR EMBL; GU324930; ADL14501.1; -; Genomic_DNA.
DR EMBL; GU324933; ADL14504.1; -; Genomic_DNA.
DR EMBL; GU324935; ADL14506.1; -; Genomic_DNA.
DR EMBL; AC079328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471082; EAW77619.1; -; Genomic_DNA.
DR EMBL; CH471082; EAW77622.1; -; Genomic_DNA.
DR EMBL; CH471082; EAW77623.1; -; Genomic_DNA.
DR EMBL; CH471082; EAW77627.1; -; Genomic_DNA.
DR EMBL; CH471082; EAW77628.1; -; Genomic_DNA.
DR EMBL; BC007433; AAH07433.1; -; mRNA.
DR EMBL; BC050473; AAH50473.1; -; mRNA.
DR EMBL; BC053545; AAH53545.1; -; mRNA.
DR EMBL; X12369; CAA30930.1; -; mRNA.
DR CCDS; CCDS10181.1; -. [P09493-10]
DR CCDS; CCDS32262.1; -. [P09493-7]
DR CCDS; CCDS32263.1; -. [P09493-3]
DR CCDS; CCDS32264.1; -. [P09493-5]
DR CCDS; CCDS45273.1; -. [P09493-1]
DR CCDS; CCDS58368.1; -. [P09493-8]
DR CCDS; CCDS58369.1; -. [P09493-9]
DR CCDS; CCDS86459.1; -. [P09493-6]
DR PIR; A27674; A27674.
DR PIR; A27678; A25825.
DR PIR; S05585; S05585.
DR RefSeq; NP_000357.3; NM_000366.5. [P09493-10]
DR RefSeq; NP_001018004.1; NM_001018004.1. [P09493-9]
DR RefSeq; NP_001018005.1; NM_001018005.1. [P09493-1]
DR RefSeq; NP_001018006.1; NM_001018006.1. [P09493-3]
DR RefSeq; NP_001018007.1; NM_001018007.1. [P09493-7]
DR RefSeq; NP_001018008.1; NM_001018008.1. [P09493-5]
DR RefSeq; NP_001018020.1; NM_001018020.1. [P09493-8]
DR RefSeq; NP_001288173.1; NM_001301244.1. [P09493-6]
DR RefSeq; NP_001317273.1; NM_001330344.1.
DR RefSeq; NP_001317275.1; NM_001330346.1.
DR RefSeq; NP_001317280.1; NM_001330351.1.
DR RefSeq; XP_016878027.1; XM_017022538.1. [P09493-10]
DR PDB; 3MUD; X-ray; 2.20 A; C/D=1-29.
DR PDB; 5KHT; X-ray; 1.50 A; A/B/C/D=1-28.
DR PDB; 6UT2; NMR; -; B/C=1-14.
DR PDB; 6X5Z; EM; 4.24 A; O/P=1-284.
DR PDBsum; 3MUD; -.
DR PDBsum; 5KHT; -.
DR PDBsum; 6UT2; -.
DR PDBsum; 6X5Z; -.
DR AlphaFoldDB; P09493; -.
DR BMRB; P09493; -.
DR SMR; P09493; -.
DR BioGRID; 113021; 234.
DR IntAct; P09493; 98.
DR MINT; P09493; -.
DR STRING; 9606.ENSP00000351022; -.
DR ChEMBL; CHEMBL4295705; -.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR GlyGen; P09493; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P09493; -.
DR MetOSite; P09493; -.
DR PhosphoSitePlus; P09493; -.
DR SwissPalm; P09493; -.
DR BioMuta; TPM1; -.
DR DMDM; 136092; -.
DR UCD-2DPAGE; P09493; -.
DR CPTAC; CPTAC-1462; -.
DR CPTAC; CPTAC-1463; -.
DR CPTAC; CPTAC-1464; -.
DR EPD; P09493; -.
DR jPOST; P09493; -.
DR MassIVE; P09493; -.
DR MaxQB; P09493; -.
DR PeptideAtlas; P09493; -.
DR PRIDE; P09493; -.
DR ProteomicsDB; 15181; -.
DR ProteomicsDB; 15182; -.
DR ProteomicsDB; 15183; -.
DR ProteomicsDB; 52229; -. [P09493-1]
DR ProteomicsDB; 52230; -. [P09493-2]
DR ProteomicsDB; 52231; -. [P09493-3]
DR ProteomicsDB; 52232; -. [P09493-4]
DR ProteomicsDB; 52233; -. [P09493-5]
DR ProteomicsDB; 52234; -. [P09493-6]
DR ProteomicsDB; 52235; -. [P09493-7]
DR Antibodypedia; 635; 332 antibodies from 39 providers.
DR DNASU; 7168; -.
DR Ensembl; ENST00000267996.11; ENSP00000267996.7; ENSG00000140416.23. [P09493-7]
DR Ensembl; ENST00000288398.10; ENSP00000288398.6; ENSG00000140416.23. [P09493-10]
DR Ensembl; ENST00000334895.10; ENSP00000334624.4; ENSG00000140416.23. [P09493-5]
DR Ensembl; ENST00000358278.7; ENSP00000351022.3; ENSG00000140416.23. [P09493-3]
DR Ensembl; ENST00000403994.9; ENSP00000385107.4; ENSG00000140416.23. [P09493-1]
DR Ensembl; ENST00000559397.6; ENSP00000452879.1; ENSG00000140416.23. [P09493-8]
DR Ensembl; ENST00000559556.5; ENSP00000453941.1; ENSG00000140416.23. [P09493-9]
DR Ensembl; ENST00000561266.6; ENSP00000453955.2; ENSG00000140416.23. [P09493-6]
DR GeneID; 7168; -.
DR KEGG; hsa:7168; -.
DR MANE-Select; ENST00000403994.9; ENSP00000385107.4; NM_001018005.2; NP_001018005.1.
DR UCSC; uc002alg.4; human. [P09493-1]
DR CTD; 7168; -.
DR DisGeNET; 7168; -.
DR GeneCards; TPM1; -.
DR GeneReviews; TPM1; -.
DR HGNC; HGNC:12010; TPM1.
DR HPA; ENSG00000140416; Group enriched (heart muscle, skeletal muscle, tongue).
DR MalaCards; TPM1; -.
DR MIM; 115196; phenotype.
DR MIM; 191010; gene.
DR MIM; 611878; phenotype.
DR neXtProt; NX_P09493; -.
DR OpenTargets; ENSG00000140416; -.
DR Orphanet; 154; Familial isolated dilated cardiomyopathy.
DR Orphanet; 54260; Left ventricular noncompaction.
DR Orphanet; 155; NON RARE IN EUROPE: Familial isolated hypertrophic cardiomyopathy.
DR PharmGKB; PA36690; -.
DR VEuPathDB; HostDB:ENSG00000140416; -.
DR GeneTree; ENSGT01030000234542; -.
DR HOGENOM; CLU_055027_0_0_1; -.
DR InParanoid; P09493; -.
DR PhylomeDB; P09493; -.
DR TreeFam; TF351519; -.
DR PathwayCommons; P09493; -.
DR Reactome; R-HSA-390522; Striated Muscle Contraction.
DR Reactome; R-HSA-445355; Smooth Muscle Contraction.
DR SignaLink; P09493; -.
DR SIGNOR; P09493; -.
DR BioGRID-ORCS; 7168; 14 hits in 1089 CRISPR screens.
DR ChiTaRS; TPM1; human.
DR GeneWiki; TPM1; -.
DR GenomeRNAi; 7168; -.
DR Pharos; P09493; Tbio.
DR PRO; PR:P09493; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P09493; protein.
DR Bgee; ENSG00000140416; Expressed in left ventricle myocardium and 214 other tissues.
DR ExpressionAtlas; P09493; baseline and differential.
DR Genevisible; P09493; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0032059; C:bleb; IMP:BHF-UCL.
DR GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005862; C:muscle thin filament tropomyosin; TAS:ProtInc.
DR GO; GO:0032587; C:ruffle membrane; IDA:BHF-UCL.
DR GO; GO:0030017; C:sarcomere; TAS:BHF-UCL.
DR GO; GO:0001725; C:stress fiber; IDA:BHF-UCL.
DR GO; GO:0003779; F:actin binding; TAS:BHF-UCL.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0008092; F:cytoskeletal protein binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:BHF-UCL.
DR GO; GO:0008307; F:structural constituent of muscle; TAS:ProtInc.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0060048; P:cardiac muscle contraction; IMP:BHF-UCL.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IEP:BHF-UCL.
DR GO; GO:0007010; P:cytoskeleton organization; TAS:BHF-UCL.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0030049; P:muscle filament sliding; ISS:BHF-UCL.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:BHF-UCL.
DR GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; IMP:BHF-UCL.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IMP:BHF-UCL.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISS:BHF-UCL.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISS:BHF-UCL.
DR GO; GO:0003065; P:positive regulation of heart rate by epinephrine; ISS:BHF-UCL.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISS:BHF-UCL.
DR GO; GO:0008360; P:regulation of cell shape; IMP:BHF-UCL.
DR GO; GO:0008016; P:regulation of heart contraction; TAS:ProtInc.
DR GO; GO:0006937; P:regulation of muscle contraction; TAS:ProtInc.
DR GO; GO:0031529; P:ruffle organization; ISS:BHF-UCL.
DR GO; GO:0045214; P:sarcomere organization; IMP:BHF-UCL.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
DR GO; GO:0042060; P:wound healing; ISS:BHF-UCL.
DR InterPro; IPR000533; Tropomyosin.
DR Pfam; PF00261; Tropomyosin; 1.
DR PRINTS; PR00194; TROPOMYOSIN.
DR PROSITE; PS00326; TROPOMYOSIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW Cardiomyopathy; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Disease variant; Muscle protein; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..284
FT /note="Tropomyosin alpha-1 chain"
FT /id="PRO_0000205620"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..284
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:3548719"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04692"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58771"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58771"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58771"
FT MOD_RES 261
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P04692"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58771"
FT MOD_RES 283
FT /note="Phosphoserine; by DAPK1"
FT /evidence="ECO:0000269|PubMed:17895359"
FT VAR_SEQ 1..80
FT /note="MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKG
FT TEDELDKYSEALKDAQEKLELAEKKATD -> MCRLRIFLRTASSEHLHERKLRET
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:3138425"
FT /id="VSP_006576"
FT VAR_SEQ 1..80
FT /note="MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKG
FT TEDELDKYSEALKDAQEKLELAEKKATD -> MAGSSSLEAVRRKIRSLQEQADAAEER
FT AGTLQRELDHERKLRET (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017498"
FT VAR_SEQ 41..80
FT /note="DELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATD -> EDIAAKEK
FT LLRVSEDERDRVLEELHKAEDSLLAAEEAAAK (in isoform 6 and isoform
FT 7)"
FT /evidence="ECO:0000303|PubMed:15249230,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_036064"
FT VAR_SEQ 41..53
FT /note="DELVSLQKKLKGT -> EDIAAKEKLLRVS (in isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_047297"
FT VAR_SEQ 57..80
FT /note="LDKYSEALKDAQEKLELAEKKATD -> RDRVLEELHKAEDSLLAAEEAAAK
FT (in isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_047298"
FT VAR_SEQ 189..212
FT /note="KCAELEEELKTVTNNLKSLEAQAE -> QVRQLEEQLRIMDSDLESINAAED
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:3138425"
FT /id="VSP_006578"
FT VAR_SEQ 189..212
FT /note="KCAELEEELKTVTNNLKSLEAQAE -> QVRQLEEQLRIMDQTLKALMAAED
FT (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:3336357, ECO:0000303|PubMed:3336363"
FT /id="VSP_006577"
FT VAR_SEQ 189..192
FT /note="KCAE -> QVRQ (in isoform 8 and isoform 10)"
FT /evidence="ECO:0000305"
FT /id="VSP_047299"
FT VAR_SEQ 196..212
FT /note="ELKTVTNNLKSLEAQAE -> QLRIMDQTLKALMAAED (in isoform 8
FT and isoform 10)"
FT /evidence="ECO:0000305"
FT /id="VSP_047300"
FT VAR_SEQ 258..284
FT /note="DELYAQKLKYKAISEELDHALNDMTSI -> EKVAHAKEENLSMHQMLDQTL
FT LELNNM (in isoform 2, isoform 3, isoform 7, isoform 8 and
FT isoform 9)"
FT /evidence="ECO:0000303|PubMed:17974005,
FT ECO:0000303|PubMed:3138425, ECO:0000303|PubMed:3336357,
FT ECO:0000303|PubMed:3336363"
FT /id="VSP_006579"
FT VAR_SEQ 259..284
FT /note="ELYAQKLKYKAISEELDHALNDMTSI -> QLYQQLEQNRRLTNELKLALNE
FT D (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017499"
FT VAR_SEQ 284
FT /note="I -> M (in isoform 10)"
FT /evidence="ECO:0000305"
FT /id="VSP_047301"
FT VARIANT 40
FT /note="E -> K (in CMD1Y; dbSNP:rs104894501)"
FT /evidence="ECO:0000269|PubMed:11273725"
FT /id="VAR_043986"
FT VARIANT 54
FT /note="E -> K (in CMD1Y; dbSNP:rs104894505)"
FT /evidence="ECO:0000269|PubMed:11273725"
FT /id="VAR_043987"
FT VARIANT 63
FT /note="A -> V (in CMH3; dbSNP:rs199476306)"
FT /evidence="ECO:0000269|PubMed:8523464"
FT /id="VAR_013135"
FT VARIANT 175
FT /note="D -> N (in CMH3; no change in homodimerization; no
FT change in homodimer thermal stability; decreased actin
FT binding; recessive effect in the homodimer; increased
FT calcium-dependent regulation of myosin binding to actin
FT filaments; dominant effect in the homodimer;
FT dbSNP:rs104894503)"
FT /evidence="ECO:0000269|PubMed:23170982,
FT ECO:0000269|PubMed:7898523, ECO:0000269|PubMed:8205619,
FT ECO:0000269|PubMed:8523464, ECO:0000269|PubMed:9822100"
FT /id="VAR_007601"
FT VARIANT 180
FT /note="E -> G (in CMH3; no change in homodimerization;
FT decreased in hom odimer thermal stability; decreased in
FT actin binding; increased calcium-dependent regulation of
FT myosin binding to actin filaments; dominant effect in the
FT homodimer; dbSNP:rs104894502)"
FT /evidence="ECO:0000269|PubMed:23170982,
FT ECO:0000269|PubMed:8205619"
FT /id="VAR_007602"
FT VARIANT 180
FT /note="E -> V (in CMH3; dbSNP:rs104894502)"
FT /evidence="ECO:0000269|PubMed:12974739"
FT /id="VAR_029452"
FT VARIANT 192
FT /note="E -> K (in LVNC9; dbSNP:rs199476315)"
FT /evidence="ECO:0000269|PubMed:21551322"
FT /id="VAR_070121"
FT VARIANT 248
FT /note="K -> E (in LVNC9; dbSNP:rs199476319)"
FT /evidence="ECO:0000269|PubMed:21551322"
FT /id="VAR_070122"
FT MUTAGEN 15
FT /note="K->N: Impairs interaction with LMOD2 and TMOD1."
FT /evidence="ECO:0000269|PubMed:26873245"
FT MUTAGEN 283
FT /note="S->A: Loss of phosphorylation and decreased
FT formation of actin stress fibers."
FT /evidence="ECO:0000269|PubMed:17895359"
FT MUTAGEN 283
FT /note="S->E: Increased formation of actin stress fibers."
FT /evidence="ECO:0000269|PubMed:17895359"
FT CONFLICT 109
FT /note="A -> V (in Ref. 11; CAA30930)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="N -> D (in Ref. 4; AAT68294/AAT68295)"
FT /evidence="ECO:0000305"
FT HELIX 1..28
FT /evidence="ECO:0007829|PDB:5KHT"
FT MOD_RES P09493-2:31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES P09493-3:213
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES P09493-4:213
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES P09493-5:51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES P09493-8:213
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES P09493-10:213
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
SQ SEQUENCE 284 AA; 32709 MW; F57139E2B0972F4D CRC64;
MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL KGTEDELDKY
SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA
DESERGMKVI ESRAQKDEEK MEIQEIQLKE AKHIAEDADR KYEEVARKLV IIESDLERAE
ERAELSEGKC AELEEELKTV TNNLKSLEAQ AEKYSQKEDR YEEEIKVLSD KLKEAETRAE
FAERSVTKLE KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI
