TPM2_HUMAN
ID TPM2_HUMAN Reviewed; 284 AA.
AC P07951; A6NM85; P06468; Q13894; Q53FM4; Q5TCU4; Q5TCU7; Q9UH67;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Tropomyosin beta chain;
DE AltName: Full=Beta-tropomyosin;
DE AltName: Full=Tropomyosin-2;
GN Name=TPM2; Synonyms=TMSB;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Fibroblast;
RX PubMed=3865200; DOI=10.1073/pnas.82.23.7835;
RA MacLeod A.R., Houlker C., Reinach F.C., Smillie L.B., Talbot K., Modi G.,
RA Walsh F.S.;
RT "A muscle-type tropomyosin in human fibroblasts: evidence for expression by
RT an alternative RNA splicing mechanism.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:7835-7839(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3368322; DOI=10.1093/nar/16.7.3109;
RA Widada J.S., Ferraz C., Capony J.-P., Liautard J.-P.;
RT "Complete nucleotide sequence of the adult skeletal isoform of human
RT skeletal muscle beta-tropomyosin.";
RL Nucleic Acids Res. 16:3109-3109(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Colon epithelium;
RX PubMed=2059197; DOI=10.1016/0006-291x(91)90647-p;
RA Prasad G.L., Meissner S., Sheer D.G., Cooper H.L.;
RT "A cDNA encoding a muscle-type tropomyosin cloned from a human epithelial
RT cell line: identity with human fibroblast tropomyosin TM1.";
RL Biochem. Biophys. Res. Commun. 177:1068-1075(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Gastric mucosa;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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] (ISOFORM 2).
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-257 (ISOFORM 2).
RA Ben-Yosef T., Francomano C.A.;
RT "Nucleotide sequence of the human TPM2 gene.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44 (ISOFORM 3).
RX PubMed=2303454; DOI=10.1016/s0021-9258(19)39791-1;
RA Libri D., Mouly V., Lemonnier M., Fiszman M.Y.;
RT "A nonmuscle tropomyosin is encoded by the smooth/skeletal beta-tropomyosin
RT gene and its RNA is transcribed from an internal promoter.";
RL J. Biol. Chem. 265:3471-3473(1990).
RN [10]
RP PROTEIN SEQUENCE OF 36-48; 52-65; 141-149 AND 206-217 (ISOFORM 2), AND
RP TISSUE SPECIFICITY.
RC TISSUE=Mammary cancer;
RA Ahamed M.E., Mohamed A.O., Ahmed M.E., Sirinuch B., Surasak J.;
RT "Protein content study revealed the presence of isoform 2 of beta-
RT tropomyosin in primary breast cancer tissues from Sudanese patients.";
RL Sudan J. Med. Sci. 2:183-187(2007).
RN [11]
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 [12]
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 [13]
RP 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 [14]
RP VARIANTS NEM4 ALA-117 AND PRO-147.
RX PubMed=11738357; DOI=10.1016/s0960-8966(01)00252-8;
RA Donner K., Ollikainen M., Ridanpaeae M., Christen H.J., Goebel H.H.,
RA de Visser M., Pelin K., Wallgren-Pettersson C.;
RT "Mutations in the beta-tropomyosin (TPM2) gene -- a rare cause of nemaline
RT myopathy.";
RL Neuromuscul. Disord. 12:151-158(2002).
RN [15]
RP VARIANT DA1A GLY-91.
RX PubMed=12592607; DOI=10.1086/368294;
RA Sung S.S., Brassington A.-M.E., Grannatt K., Rutherford A., Whitby F.G.,
RA Krakowiak P.A., Jorde L.B., Carey J.C., Bamshad M.;
RT "Mutations in genes encoding fast-twitch contractile proteins cause distal
RT arthrogryposis syndromes.";
RL Am. J. Hum. Genet. 72:681-690(2003).
RN [16]
RP VARIANT NEM4 LYS-41.
RX PubMed=17846275; DOI=10.1001/archneur.64.9.1334;
RA Tajsharghi H., Ohlsson M., Lindberg C., Oldfors A.;
RT "Congenital myopathy with nemaline rods and cap structures caused by a
RT mutation in the beta-tropomyosin gene (TPM2).";
RL Arch. Neurol. 64:1334-1338(2007).
RN [17]
RP VARIANT DA2B4 TRP-133.
RX PubMed=17339586; DOI=10.1212/01.wnl.0000256339.40667.fb;
RA Tajsharghi H., Kimber E., Holmgren D., Tulinius M., Oldfors A.;
RT "Distal arthrogryposis and muscle weakness associated with a beta-
RT tropomyosin mutation.";
RL Neurology 68:772-775(2007).
RN [18]
RP VARIANT CAPM2 GLU-139 DEL.
RX PubMed=17434307; DOI=10.1016/j.nmd.2007.02.015;
RA Lehtokari V.L., Ceuterick-de Groote C., de Jonghe P., Marttila M.,
RA Laing N.G., Pelin K., Wallgren-Pettersson C.;
RT "Cap disease caused by heterozygous deletion of the beta-tropomyosin gene
RT TPM2.";
RL Neuromuscul. Disord. 17:433-442(2007).
RN [19]
RP VARIANTS CAPM2 LYS-49 DEL; GLY-52 INS AND LYS-202.
RX PubMed=19047562; DOI=10.1212/01.wnl.0000336654.44814.b8;
RA Ohlsson M., Quijano-Roy S., Darin N., Brochier G., Lacene E.,
RA Avila-Smirnow D., Fardeau M., Oldfors A., Tajsharghi H.;
RT "New morphologic and genetic findings in cap disease associated with beta-
RT tropomyosin (TPM2) mutations.";
RL Neurology 71:1896-1901(2008).
RN [20]
RP VARIANT CAPM2 GLU-139 DEL.
RX PubMed=19345583; DOI=10.1016/j.nmd.2009.03.003;
RA Clarke N.F., Domazetovska A., Waddell L., Kornberg A., McLean C.,
RA North K.N.;
RT "Cap disease due to mutation of the beta-tropomyosin gene (TPM2).";
RL Neuromuscul. Disord. 19:348-351(2009).
RN [21]
RP VARIANT DA2B4 TRP-133.
RX PubMed=23678273; DOI=10.3346/jkms.2013.28.5.780;
RA Ko J.M., Choi I.H., Baek G.H., Kim K.W.;
RT "First Korean family with a mutation in TPM2 associated with Sheldon-Hall
RT syndrome.";
RL J. Korean Med. Sci. 28:780-783(2013).
RN [22]
RP VARIANTS NEM4 GLY-3; LYS-7 DEL; VAL-14; LYS-41; TRP-133; PRO-143 AND
RP PRO-148, VARIANTS DA1A ARG-93; LYS-117; TRP-133 AND CYS-261, VARIANT CAPM2
RP GLU-139 DEL, VARIANTS VAL-2; HIS-93; GLU-128; PRO-133; THR-155 AND GLU-218
RP DEL, AND PHOSPHORYLATION AT THR-53; THR-79; THR-108; SER-158; SER-206;
RP THR-252; THR-282 AND SER-283.
RX PubMed=24692096; DOI=10.1002/humu.22554;
RA Marttila M., Lehtokari V.L., Marston S., Nyman T.A., Barnerias C.,
RA Beggs A.H., Bertini E., Ceyhan-Birsoy O., Cintas P., Gerard M.,
RA Gilbert-Dussardier B., Hogue J.S., Longman C., Eymard B., Frydman M.,
RA Kang P.B., Klinge L., Kolski H., Lochmueller H., Magy L., Manel V.,
RA Mayer M., Mercuri E., North K.N., Peudenier-Robert S., Pihko H.,
RA Probst F.J., Reisin R., Stewart W., Taratuto A.L., de Visser M.,
RA Wilichowski E., Winer J., Nowak K., Laing N.G., Winder T.L., Monnier N.,
RA Clarke N.F., Pelin K., Groenholm M., Wallgren-Pettersson C.;
RT "Mutation update and genotype-phenotype correlations of novel and
RT previously described mutations in TPM2 and TPM3 causing congenital
RT myopathies.";
RL Hum. Mutat. 35:779-790(2014).
RN [23]
RP VARIANT DA2B4 ARG-103.
RX PubMed=30285720; DOI=10.1186/s12881-018-0692-8;
RA Li S., You Y., Gao J., Mao B., Cao Y., Zhao X., Zhang X.;
RT "Novel mutations in TPM2 and PIEZO2 are responsible for distal
RT arthrogryposis (DA) 2B and mild DA in two Chinese families.";
RL BMC Med. Genet. 19:179-179(2018).
CC -!- FUNCTION: Binds to actin filaments in muscle and non-muscle cells.
CC Plays a central role, in association with the troponin complex, in the
CC calcium dependent regulation of vertebrate striated muscle contraction.
CC Smooth muscle contraction is regulated by interaction with caldesmon.
CC In non-muscle cells is implicated in stabilizing cytoskeleton actin
CC filaments. The non-muscle isoform may have a role in agonist-mediated
CC receptor internalization. {ECO:0000250|UniProtKB:P58774,
CC ECO:0000250|UniProtKB:P58775}.
CC -!- SUBUNIT: Homodimer. Heterodimer of an alpha (TPM1, TPM3 or TPM4) and a
CC beta (TPM2) chain. {ECO:0000250|UniProtKB:P04692}.
CC -!- INTERACTION:
CC P07951-2; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-10977815, EBI-11096309;
CC P07951-2; O95363: FARS2; NbExp=3; IntAct=EBI-10977815, EBI-2513774;
CC P07951-2; Q14696: MESD; NbExp=3; IntAct=EBI-10977815, EBI-6165891;
CC P07951-2; Q9Y605: MRFAP1; NbExp=3; IntAct=EBI-10977815, EBI-995714;
CC P07951-2; O95295: SNAPIN; NbExp=3; IntAct=EBI-10977815, EBI-296723;
CC P07951-2; P00441: SOD1; NbExp=3; IntAct=EBI-10977815, EBI-990792;
CC P07951-2; P0C1Z6: TFPT; NbExp=3; IntAct=EBI-10977815, EBI-1245626;
CC P07951-2; P07951-2: TPM2; NbExp=3; IntAct=EBI-10977815, EBI-10977815;
CC P07951-2; Q9UJW7: ZNF229; NbExp=3; IntAct=EBI-10977815, EBI-12068564;
CC P07951-2; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-10977815, EBI-4395669;
CC P07951-2; A8K8V0: ZNF785; NbExp=3; IntAct=EBI-10977815, EBI-3925400;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P58775}. Note=Associates with F-actin stress
CC fibers. {ECO:0000250|UniProtKB:P58775}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Skeletal muscle;
CC IsoId=P07951-1; Sequence=Displayed;
CC Name=2; Synonyms=non-muscle, Fibroblast TM36, Epithelial TMe1;
CC IsoId=P07951-2; Sequence=VSP_006595, VSP_006596;
CC Name=3; Synonyms=non-muscle;
CC IsoId=P07951-3; Sequence=VSP_006594, VSP_006595, VSP_006596;
CC -!- TISSUE SPECIFICITY: Present in primary breast cancer tissue, absent
CC from normal breast tissue. {ECO:0000269|Ref.10}.
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 on Ser-61 by PIK3CG. Phosphorylation on Ser-61 is
CC required for ADRB2 internalization (By similarity). {ECO:0000250}.
CC -!- MASS SPECTROMETRY: [Isoform 1]: Mass=32850.73; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11840567};
CC -!- MASS SPECTROMETRY: [Isoform 2]: Mass=32989.81; Method=MALDI; Note=The
CC measured range is 1-284.; Evidence={ECO:0000269|PubMed:11840567};
CC -!- DISEASE: Nemaline myopathy 4 (NEM4) [MIM:609285]: A form of nemaline
CC myopathy. Nemaline myopathies are muscular disorders characterized by
CC muscle weakness of varying severity and onset, and abnormal thread-like
CC or rod-shaped structures in muscle fibers on histologic examination.
CC Nemaline myopathy type 4 presents from infancy to childhood with
CC hypotonia and moderate-to-severe proximal weakness with minimal or no
CC progression. Major motor milestones are delayed but independent
CC ambulation is usually achieved, although a wheelchair may be needed in
CC later life. {ECO:0000269|PubMed:11738357, ECO:0000269|PubMed:17846275,
CC ECO:0000269|PubMed:24692096}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Arthrogryposis, distal, 1A (DA1A) [MIM:108120]: A form of
CC distal arthrogryposis, a disease characterized by congenital joint
CC contractures that mainly involve two or more distal parts of the limbs,
CC in the absence of a primary neurological or muscle disease. Distal
CC arthrogryposis type 1 is characterized largely by camptodactyly and
CC clubfoot. Hypoplasia and/or absence of some interphalangeal creases is
CC common. The shoulders and hips are less frequently affected.
CC {ECO:0000269|PubMed:12592607, ECO:0000269|PubMed:24692096}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Cap myopathy 2 (CAPM2) [MIM:609285]: A rare congenital
CC skeletal muscle disorder characterized by the presence of cap-like
CC structures which are well demarcated and peripherally located under the
CC sarcolemma and show abnormal accumulation of sarcomeric proteins.
CC Clinical features are early onset of hypotonia and non-progressive or
CC slowly progressive muscle weakness. Respiratory problems are common.
CC {ECO:0000269|PubMed:17434307, ECO:0000269|PubMed:19047562,
CC ECO:0000269|PubMed:19345583, ECO:0000269|PubMed:24692096}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Arthrogryposis, distal, 2B4 (DA2B4) [MIM:108120]: A form of
CC distal arthrogryposis, a disease characterized by congenital joint
CC contractures that mainly involve two or more distal parts of the limbs,
CC in the absence of a primary neurological or muscle disease. Distal
CC arthrogryposis type 2 is characterized by contractures of the hands and
CC feet, and a distinctive face characterized by prominent nasolabial
CC folds, small mouth and downslanting palpebral fissures.
CC {ECO:0000269|PubMed:17339586, ECO:0000269|PubMed:23678273,
CC ECO:0000269|PubMed:30285720}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
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DR EMBL; M12126; AAA61229.1; -; mRNA.
DR EMBL; M12125; AAA36773.1; -; mRNA.
DR EMBL; X06825; CAA29971.1; -; mRNA.
DR EMBL; M75165; AAB59509.1; -; mRNA.
DR EMBL; M74817; AAA61230.1; -; mRNA.
DR EMBL; AK223258; BAD96978.1; -; mRNA.
DR EMBL; AL133410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58354.1; -; Genomic_DNA.
DR EMBL; BC011776; AAH11776.1; -; mRNA.
DR EMBL; AF209746; AAF17621.1; -; Genomic_DNA.
DR EMBL; J05247; AAA51842.1; -; Genomic_DNA.
DR CCDS; CCDS6586.1; -. [P07951-2]
DR CCDS; CCDS6587.1; -. [P07951-1]
DR PIR; A23562; A23562.
DR PIR; S00922; S00922.
DR RefSeq; NP_003280.2; NM_003289.3. [P07951-1]
DR RefSeq; NP_998839.1; NM_213674.1. [P07951-2]
DR RefSeq; XP_016870580.1; XM_017015091.1. [P07951-1]
DR AlphaFoldDB; P07951; -.
DR SMR; P07951; -.
DR BioGRID; 113022; 189.
DR IntAct; P07951; 99.
DR MINT; P07951; -.
DR STRING; 9606.ENSP00000367542; -.
DR GlyGen; P07951; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P07951; -.
DR PhosphoSitePlus; P07951; -.
DR BioMuta; TPM2; -.
DR DMDM; 136090; -.
DR DOSAC-COBS-2DPAGE; P07951; -.
DR REPRODUCTION-2DPAGE; IPI00220709; -.
DR UCD-2DPAGE; P07951; -.
DR CPTAC; CPTAC-286; -.
DR CPTAC; CPTAC-287; -.
DR EPD; P07951; -.
DR jPOST; P07951; -.
DR MassIVE; P07951; -.
DR MaxQB; P07951; -.
DR PaxDb; P07951; -.
DR PeptideAtlas; P07951; -.
DR PRIDE; P07951; -.
DR ProteomicsDB; 52049; -. [P07951-1]
DR ProteomicsDB; 52050; -. [P07951-2]
DR ProteomicsDB; 52051; -. [P07951-3]
DR Antibodypedia; 25944; 318 antibodies from 29 providers.
DR DNASU; 7169; -.
DR Ensembl; ENST00000378292.9; ENSP00000367542.3; ENSG00000198467.16. [P07951-2]
DR Ensembl; ENST00000645482.3; ENSP00000496494.2; ENSG00000198467.16. [P07951-1]
DR GeneID; 7169; -.
DR KEGG; hsa:7169; -.
DR MANE-Select; ENST00000645482.3; ENSP00000496494.2; NM_003289.4; NP_003280.2.
DR UCSC; uc003zxs.4; human. [P07951-1]
DR CTD; 7169; -.
DR DisGeNET; 7169; -.
DR GeneCards; TPM2; -.
DR HGNC; HGNC:12011; TPM2.
DR HPA; ENSG00000198467; Group enriched (skeletal muscle, tongue).
DR MalaCards; TPM2; -.
DR MIM; 108120; phenotype.
DR MIM; 190990; gene.
DR MIM; 609285; phenotype.
DR neXtProt; NX_P07951; -.
DR OpenTargets; ENSG00000198467; -.
DR Orphanet; 171881; Cap myopathy.
DR Orphanet; 171439; Childhood-onset nemaline myopathy.
DR Orphanet; 2020; Congenital fiber-type disproportion myopathy.
DR Orphanet; 1146; Distal arthrogryposis type 1.
DR Orphanet; 1147; Sheldon-Hall syndrome.
DR Orphanet; 171436; Typical nemaline myopathy.
DR PharmGKB; PA36691; -.
DR VEuPathDB; HostDB:ENSG00000198467; -.
DR GeneTree; ENSGT01030000234542; -.
DR HOGENOM; CLU_055027_0_0_1; -.
DR InParanoid; P07951; -.
DR OrthoDB; 1013139at2759; -.
DR PhylomeDB; P07951; -.
DR TreeFam; TF351519; -.
DR PathwayCommons; P07951; -.
DR Reactome; R-HSA-390522; Striated Muscle Contraction.
DR Reactome; R-HSA-445355; Smooth Muscle Contraction.
DR SignaLink; P07951; -.
DR SIGNOR; P07951; -.
DR BioGRID-ORCS; 7169; 36 hits in 1084 CRISPR screens.
DR ChiTaRS; TPM2; human.
DR GeneWiki; TPM2; -.
DR GenomeRNAi; 7169; -.
DR Pharos; P07951; Tbio.
DR PRO; PR:P07951; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P07951; protein.
DR Bgee; ENSG00000198467; Expressed in saphenous vein and 196 other tissues.
DR ExpressionAtlas; P07951; baseline and differential.
DR Genevisible; P07951; HS.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005862; C:muscle thin filament tropomyosin; TAS:ProtInc.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
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:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0043462; P:regulation of ATP-dependent activity; IDA:UniProtKB.
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 Acetylation; Actin-binding; Alternative splicing; Coiled coil; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Disease variant; Muscle protein;
KW Nemaline myopathy; Phosphoprotein; Reference proteome.
FT CHAIN 1..284
FT /note="Tropomyosin beta chain"
FT /id="PRO_0000205627"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..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:0000250|UniProtKB:P58776"
FT MOD_RES 53
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24692096"
FT MOD_RES 61
FT /note="Phosphoserine; by PIK3CG"
FT /evidence="ECO:0000250|UniProtKB:P58774"
FT MOD_RES 79
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24692096"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06753"
FT MOD_RES 108
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24692096"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24692096"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24692096"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58775"
FT MOD_RES 252
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24692096"
FT MOD_RES 261
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P58775"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58775"
FT MOD_RES 282
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24692096"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24692096"
FT VAR_SEQ 1..80
FT /note="MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKG
FT TEDEVEKYSESVKEAQEKLEQAEKKATD -> MAGISSIDAVKKKIQSLQQVADEAEER
FT AEHLQREADAERQARER (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_006594"
FT VAR_SEQ 189..213
FT /note="KCGDLEEELKIVTNNLKSLEAQADK -> RARQLEEELRTMDQALKSLMASE
FT EE (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:2059197, ECO:0000303|PubMed:3865200,
FT ECO:0000303|Ref.4"
FT /id="VSP_006595"
FT VAR_SEQ 258..284
FT /note="DEVYAQKMKYKAISEELDNALNDITSL -> ETLASAKEENVEIHQTLDQTL
FT LELNNL (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:2059197, ECO:0000303|PubMed:3865200,
FT ECO:0000303|Ref.4"
FT /id="VSP_006596"
FT VARIANT 2
FT /note="D -> V (probable disease-associated variant found in
FT patients with undefined congenital myopathy;
FT dbSNP:rs199476145)"
FT /evidence="ECO:0000269|PubMed:24692096"
FT /id="VAR_071485"
FT VARIANT 3
FT /note="A -> G (in NEM4)"
FT /evidence="ECO:0000269|PubMed:24692096"
FT /id="VAR_071486"
FT VARIANT 7
FT /note="Missing (in NEM4)"
FT /evidence="ECO:0000269|PubMed:24692096"
FT /id="VAR_071487"
FT VARIANT 14
FT /note="D -> V (in NEM4)"
FT /evidence="ECO:0000269|PubMed:24692096"
FT /id="VAR_071488"
FT VARIANT 41
FT /note="E -> K (in NEM4; also found in a patient with
FT congenital myopathy with fiber-type disproportion and
FT patients with undefined congenital myopathy;
FT dbSNP:rs137853306)"
FT /evidence="ECO:0000269|PubMed:17846275,
FT ECO:0000269|PubMed:24692096"
FT /id="VAR_070978"
FT VARIANT 49
FT /note="Missing (in CAPM2; dbSNP:rs199476147)"
FT /evidence="ECO:0000269|PubMed:19047562"
FT /id="VAR_070979"
FT VARIANT 52
FT /note="G -> GG (in CAPM2)"
FT /evidence="ECO:0000269|PubMed:19047562"
FT /id="VAR_070980"
FT VARIANT 91
FT /note="R -> G (in DA1A; dbSNP:rs104894127)"
FT /evidence="ECO:0000269|PubMed:12592607"
FT /id="VAR_016086"
FT VARIANT 93
FT /note="Q -> H (probable disease-associated variant found in
FT patients with undefined congenital myopathy;
FT dbSNP:rs727504180)"
FT /evidence="ECO:0000269|PubMed:24692096"
FT /id="VAR_071489"
FT VARIANT 93
FT /note="Q -> R (in DA1A; dbSNP:rs199476151)"
FT /evidence="ECO:0000269|PubMed:24692096"
FT /id="VAR_071490"
FT VARIANT 103
FT /note="Q -> R (in DA2B4; unknown pathological significance;
FT dbSNP:rs1563929383)"
FT /evidence="ECO:0000269|PubMed:30285720"
FT /id="VAR_082273"
FT VARIANT 117
FT /note="E -> A (in NEM4)"
FT /evidence="ECO:0000269|PubMed:11738357"
FT /id="VAR_013468"
FT VARIANT 117
FT /note="E -> K (in DA1A; also found in a patient with
FT congenital myopathy with fiber-type disproportion;
FT dbSNP:rs104894129)"
FT /evidence="ECO:0000269|PubMed:24692096"
FT /id="VAR_071491"
FT VARIANT 128
FT /note="K -> E (probable disease-associated variant found in
FT a patient with congenital myopathy with fiber-type
FT disproportion and patients with undefined congenital
FT myopathy; dbSNP:rs1563929143)"
FT /evidence="ECO:0000269|PubMed:24692096"
FT /id="VAR_071492"
FT VARIANT 133
FT /note="R -> P (probable disease-associated variant found in
FT a patient with congenital myopathy with fiber-type
FT disproportion and patients with undefined congenital
FT myopathy; dbSNP:rs199476152)"
FT /evidence="ECO:0000269|PubMed:24692096"
FT /id="VAR_071493"
FT VARIANT 133
FT /note="R -> W (in DA2B4, NEM4 and DA1A; also found in a
FT patient with congenital myopathy with fiber-type
FT disproportion; dbSNP:rs137853305)"
FT /evidence="ECO:0000269|PubMed:17339586,
FT ECO:0000269|PubMed:23678273, ECO:0000269|PubMed:24692096"
FT /id="VAR_070981"
FT VARIANT 139
FT /note="Missing (in CAPM2; also found in a patient with
FT congenital myopathy with fiber-type disproportion;
FT dbSNP:rs199476153)"
FT /evidence="ECO:0000269|PubMed:17434307,
FT ECO:0000269|PubMed:19345583, ECO:0000269|PubMed:24692096"
FT /id="VAR_070982"
FT VARIANT 143
FT /note="L -> P (in NEM4; also found in a patient with
FT congenital myopathy with fiber-type disproportion)"
FT /evidence="ECO:0000269|PubMed:24692096"
FT /id="VAR_071494"
FT VARIANT 147
FT /note="Q -> P (in NEM4; dbSNP:rs104894128)"
FT /evidence="ECO:0000269|PubMed:11738357"
FT /id="VAR_013469"
FT VARIANT 148
FT /note="L -> P (in NEM4; also found in a patient with
FT congenital myopathy with fiber-type disproportion)"
FT /evidence="ECO:0000269|PubMed:24692096"
FT /id="VAR_071495"
FT VARIANT 155
FT /note="A -> T (probable disease-associated variant found in
FT patients with undefined congenital myopathy;
FT dbSNP:rs1563929039)"
FT /evidence="ECO:0000269|PubMed:24692096"
FT /id="VAR_071496"
FT VARIANT 202
FT /note="N -> K (in CAPM2; dbSNP:rs137853307)"
FT /evidence="ECO:0000269|PubMed:19047562"
FT /id="VAR_070983"
FT VARIANT 218
FT /note="Missing (probable disease-associated variant in
FT patients with undefined congenital myopathy)"
FT /evidence="ECO:0000269|PubMed:24692096"
FT /id="VAR_071497"
FT VARIANT 261
FT /note="Y -> C (in DA1A; also found in patients with
FT undefined congenital myopathy)"
FT /evidence="ECO:0000269|PubMed:24692096"
FT /id="VAR_071498"
FT VARIANT 273
FT /note="E -> K (in dbSNP:rs3180843)"
FT /id="VAR_052402"
FT CONFLICT 89
FT /note="N -> S (in Ref. 4; BAD96978)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 284 AA; 32851 MW; 18E330568E14E0BE CRC64;
MDAIKKKMQM LKLDKENAID RAEQAEADKK QAEDRCKQLE EEQQALQKKL KGTEDEVEKY
SESVKEAQEK LEQAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA
DESERGMKVI ENRAMKDEEK MELQEMQLKE AKHIAEDSDR KYEEVARKLV ILEGELERSE
ERAEVAESKC GDLEEELKIV TNNLKSLEAQ ADKYSTKEDK YEEEIKLLEE KLKEAETRAE
FAERSVAKLE KTIDDLEDEV YAQKMKYKAI SEELDNALND ITSL
