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Tropomyosin beta chain (Beta-tropomyosin) (Tropomyosin-2)

 TPM2_HUMAN              Reviewed;         284 AA.
P07951; A6NM85; P06468; Q13894; Q53FM4; Q5TCU4; Q5TCU7; Q9UH67;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
25-OCT-2017, entry version 183.
RecName: Full=Tropomyosin beta chain;
AltName: Full=Beta-tropomyosin;
AltName: Full=Tropomyosin-2;
Name=TPM2; Synonyms=TMSB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Fibroblast;
PubMed=3865200; DOI=10.1073/pnas.82.23.7835;
MacLeod A.R., Houlker C., Reinach F.C., Smillie L.B., Talbot K.,
Modi G., Walsh F.S.;
"A muscle-type tropomyosin in human fibroblasts: evidence for
expression by an alternative RNA splicing mechanism.";
Proc. Natl. Acad. Sci. U.S.A. 82:7835-7839(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3368322; DOI=10.1093/nar/16.7.3109;
Widada J.S., Ferraz C., Capony J.-P., Liautard J.-P.;
"Complete nucleotide sequence of the adult skeletal isoform of human
skeletal muscle beta-tropomyosin.";
Nucleic Acids Res. 16:3109-3109(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Colon epithelium;
PubMed=2059197; DOI=10.1016/0006-291X(91)90647-P;
Prasad G.L., Meissner S., Sheer D.G., Cooper H.L.;
"A cDNA encoding a muscle-type tropomyosin cloned from a human
epithelial cell line: identity with human fibroblast tropomyosin
TM1.";
Biochem. Biophys. Res. Commun. 177:1068-1075(1991).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Gastric mucosa;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-257 (ISOFORM 2).
Ben-Yosef T., Francomano C.A.;
"Nucleotide sequence of the human TPM2 gene.";
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44 (ISOFORM 3).
PubMed=2303454;
Libri D., Mouly V., Lemonnier M., Fiszman M.Y.;
"A nonmuscle tropomyosin is encoded by the smooth/skeletal beta-
tropomyosin gene and its RNA is transcribed from an internal
promoter.";
J. Biol. Chem. 265:3471-3473(1990).
[10]
PROTEIN SEQUENCE OF 36-48; 52-65; 141-149 AND 206-217 (ISOFORM 2), AND
TISSUE SPECIFICITY.
TISSUE=Mammary cancer;
Ahamed M.E., Mohamed A.O., Ahmed M.E., Sirinuch B., Surasak J.;
"Protein content study revealed the presence of isoform 2 of beta-
tropomyosin in primary breast cancer tissues from Sudanese patients.";
Sudan J. Med. Sci. 2:183-187(2007).
[11]
MASS SPECTROMETRY.
TISSUE=Mammary cancer;
PubMed=11840567;
DOI=10.1002/1615-9861(200202)2:2<212::AID-PROT212>3.0.CO;2-H;
Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A.,
Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J.,
Zvelebil M.J.;
"Cluster analysis of an extensive human breast cancer cell line
protein expression map database.";
Proteomics 2:212-223(2002).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[14]
VARIANTS NEM4 ALA-117 AND PRO-147.
PubMed=11738357; DOI=10.1016/S0960-8966(01)00252-8;
Donner K., Ollikainen M., Ridanpaeae M., Christen H.J., Goebel H.H.,
de Visser M., Pelin K., Wallgren-Pettersson C.;
"Mutations in the beta-tropomyosin (TPM2) gene -- a rare cause of
nemaline myopathy.";
Neuromuscul. Disord. 12:151-158(2002).
[15]
VARIANT DA1A GLY-91.
PubMed=12592607; DOI=10.1086/368294;
Sung S.S., Brassington A.-M.E., Grannatt K., Rutherford A.,
Whitby F.G., Krakowiak P.A., Jorde L.B., Carey J.C., Bamshad M.;
"Mutations in genes encoding fast-twitch contractile proteins cause
distal arthrogryposis syndromes.";
Am. J. Hum. Genet. 72:681-690(2003).
[16]
VARIANT NEM4 LYS-41.
PubMed=17846275; DOI=10.1001/archneur.64.9.1334;
Tajsharghi H., Ohlsson M., Lindberg C., Oldfors A.;
"Congenital myopathy with nemaline rods and cap structures caused by a
mutation in the beta-tropomyosin gene (TPM2).";
Arch. Neurol. 64:1334-1338(2007).
[17]
VARIANT DA2B TRP-133.
PubMed=17339586; DOI=10.1212/01.wnl.0000256339.40667.fb;
Tajsharghi H., Kimber E., Holmgren D., Tulinius M., Oldfors A.;
"Distal arthrogryposis and muscle weakness associated with a beta-
tropomyosin mutation.";
Neurology 68:772-775(2007).
[18]
VARIANT CAPM2 GLU-139 DEL.
PubMed=17434307; DOI=10.1016/j.nmd.2007.02.015;
Lehtokari V.L., Ceuterick-de Groote C., de Jonghe P., Marttila M.,
Laing N.G., Pelin K., Wallgren-Pettersson C.;
"Cap disease caused by heterozygous deletion of the beta-tropomyosin
gene TPM2.";
Neuromuscul. Disord. 17:433-442(2007).
[19]
VARIANTS CAPM2 LYS-49 DEL; GLY-52 INS AND LYS-202.
PubMed=19047562; DOI=10.1212/01.wnl.0000336654.44814.b8;
Ohlsson M., Quijano-Roy S., Darin N., Brochier G., Lacene E.,
Avila-Smirnow D., Fardeau M., Oldfors A., Tajsharghi H.;
"New morphologic and genetic findings in cap disease associated with
beta-tropomyosin (TPM2) mutations.";
Neurology 71:1896-1901(2008).
[20]
VARIANT CAPM2 GLU-139 DEL.
PubMed=19345583; DOI=10.1016/j.nmd.2009.03.003;
Clarke N.F., Domazetovska A., Waddell L., Kornberg A., McLean C.,
North K.N.;
"Cap disease due to mutation of the beta-tropomyosin gene (TPM2).";
Neuromuscul. Disord. 19:348-351(2009).
[21]
VARIANTS NEM4 GLY-3; LYS-7 DEL; VAL-14; LYS-41; TRP-133; PRO-143 AND
PRO-148, VARIANTS DA1A ARG-93; LYS-117; TRP-133 AND CYS-261, VARIANT
CAPM2 GLU-139 DEL, VARIANTS VAL-2; HIS-93; GLU-128; PRO-133; THR-155
AND GLU-218 DEL, AND PHOSPHORYLATION AT THR-53; THR-79; THR-108;
SER-158; SER-206; THR-252; THR-282 AND SER-283.
PubMed=24692096; DOI=10.1002/humu.22554;
Marttila M., Lehtokari V.L., Marston S., Nyman T.A., Barnerias C.,
Beggs A.H., Bertini E., Ceyhan-Birsoy O., Cintas P., Gerard M.,
Gilbert-Dussardier B., Hogue J.S., Longman C., Eymard B., Frydman M.,
Kang P.B., Klinge L., Kolski H., Lochmueller H., Magy L., Manel V.,
Mayer M., Mercuri E., North K.N., Peudenier-Robert S., Pihko H.,
Probst F.J., Reisin R., Stewart W., Taratuto A.L., de Visser M.,
Wilichowski E., Winer J., Nowak K., Laing N.G., Winder T.L.,
Monnier N., Clarke N.F., Pelin K., Groenholm M.,
Wallgren-Pettersson C.;
"Mutation update and genotype-phenotype correlations of novel and
previously described mutations in TPM2 and TPM3 causing congenital
myopathies.";
Hum. Mutat. 35:779-790(2014).
-!- FUNCTION: Binds to actin filaments in muscle and non-muscle cells.
Plays a central role, in association with the troponin complex, in
the calcium dependent regulation of vertebrate striated muscle
contraction. Smooth muscle contraction is regulated by interaction
with caldesmon. In non-muscle cells is implicated in stabilizing
cytoskeleton actin filaments. The non-muscle isoform may have a
role in agonist-mediated receptor internalization.
{ECO:0000250|UniProtKB:P58774, ECO:0000250|UniProtKB:P58775}.
-!- SUBUNIT: Homodimer. Heterodimer of an alpha (TPM1, TPM3 or TPM4)
and a beta (TPM2) chain. {ECO:0000250|UniProtKB:P04692}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:P58775}. Note=Associates with F-actin
stress fibers. {ECO:0000250|UniProtKB:P58775}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Skeletal muscle;
IsoId=P07951-1; Sequence=Displayed;
Name=2; Synonyms=non-muscle, Fibroblast TM36, Epithelial TMe1;
IsoId=P07951-2; Sequence=VSP_006595, VSP_006596;
Name=3; Synonyms=non-muscle;
IsoId=P07951-3; Sequence=VSP_006594, VSP_006595, VSP_006596;
-!- TISSUE SPECIFICITY: Present in primary breast cancer tissue,
absent from normal breast tissue. {ECO:0000269|Ref.10}.
-!- DOMAIN: The molecule is in a coiled coil structure that is formed
by 2 polypeptide chains. The sequence exhibits a prominent seven-
residues periodicity.
-!- PTM: Phosphorylated on Ser-61 by PIK3CG. Phosphorylation on Ser-61
is required for ADRB2 internalization (By similarity).
{ECO:0000250}.
-!- MASS SPECTROMETRY: Mass=32850.73; Method=MALDI; Range=1-284
(P07951-1); Evidence={ECO:0000269|PubMed:11840567};
-!- MASS SPECTROMETRY: Mass=32989.81; Method=MALDI; Range=1-284
(P07951-2); Evidence={ECO:0000269|PubMed:11840567};
-!- DISEASE: Nemaline myopathy 4 (NEM4) [MIM:609285]: A form of
nemaline myopathy. Nemaline myopathies are muscular disorders
characterized by muscle weakness of varying severity and onset,
and abnormal thread-like or rod-shaped structures in muscle fibers
on histologic examination. Nemaline myopathy type 4 presents from
infancy to childhood with hypotonia and moderate-to-severe
proximal weakness with minimal or no progression. Major motor
milestones are delayed but independent ambulation is usually
achieved, although a wheelchair may be needed in later life.
{ECO:0000269|PubMed:11738357, ECO:0000269|PubMed:17846275,
ECO:0000269|PubMed:24692096}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Arthrogryposis, distal, 1A (DA1A) [MIM:108120]: A form of
distal arthrogryposis, a disease characterized by congenital joint
contractures that mainly involve two or more distal parts of the
limbs, in the absence of a primary neurological or muscle disease.
Distal arthrogryposis type 1 is characterized largely by
camptodactyly and clubfoot. Hypoplasia and/or absence of some
interphalangeal creases is common. The shoulders and hips are less
frequently affected. {ECO:0000269|PubMed:12592607,
ECO:0000269|PubMed:24692096}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Cap myopathy 2 (CAPM2) [MIM:609285]: A rare congenital
skeletal muscle disorder characterized by the presence of cap-like
structures which are well demarcated and peripherally located
under the sarcolemma and show abnormal accumulation of sarcomeric
proteins. Clinical features are early onset of hypotonia and non-
progressive or slowly progressive muscle weakness. Respiratory
problems are common. {ECO:0000269|PubMed:17434307,
ECO:0000269|PubMed:19047562, ECO:0000269|PubMed:19345583,
ECO:0000269|PubMed:24692096}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Arthrogryposis, distal, 2B (DA2B) [MIM:601680]: A form of
distal arthrogryposis, a disease characterized by congenital joint
contractures that mainly involve two or more distal parts of the
limbs, in the absence of a primary neurological or muscle disease.
DA2B is characterized by contractures of the hands and feet, and a
distinctive face characterized by prominent nasolabial folds,
small mouth and downslanting palpebral fissures.
{ECO:0000269|PubMed:17339586}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
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EMBL; M12126; AAA61229.1; -; mRNA.
EMBL; M12125; AAA36773.1; -; mRNA.
EMBL; X06825; CAA29971.1; -; mRNA.
EMBL; M75165; AAB59509.1; -; mRNA.
EMBL; M74817; AAA61230.1; -; mRNA.
EMBL; AK223258; BAD96978.1; -; mRNA.
EMBL; AL133410; CAI10974.1; -; Genomic_DNA.
EMBL; AL133410; CAI10977.1; -; Genomic_DNA.
EMBL; CH471071; EAW58354.1; -; Genomic_DNA.
EMBL; BC011776; AAH11776.1; -; mRNA.
EMBL; AF209746; AAF17621.1; -; Genomic_DNA.
EMBL; J05247; AAA51842.1; -; Genomic_DNA.
CCDS; CCDS6586.1; -. [P07951-2]
CCDS; CCDS6587.1; -. [P07951-1]
PIR; A23562; A23562.
PIR; S00922; S00922.
RefSeq; NP_003280.2; NM_003289.3. [P07951-1]
RefSeq; NP_998839.1; NM_213674.1. [P07951-2]
RefSeq; XP_016870580.1; XM_017015091.1. [P07951-1]
UniGene; Hs.300772; -.
ProteinModelPortal; P07951; -.
SMR; P07951; -.
BioGrid; 113022; 129.
IntAct; P07951; 43.
MINT; MINT-94363; -.
STRING; 9606.ENSP00000354219; -.
iPTMnet; P07951; -.
PhosphoSitePlus; P07951; -.
BioMuta; TPM2; -.
DMDM; 136090; -.
DOSAC-COBS-2DPAGE; P07951; -.
REPRODUCTION-2DPAGE; IPI00220709; -.
UCD-2DPAGE; P07951; -.
EPD; P07951; -.
MaxQB; P07951; -.
PaxDb; P07951; -.
PeptideAtlas; P07951; -.
PRIDE; P07951; -.
DNASU; 7169; -.
Ensembl; ENST00000360958; ENSP00000354219; ENSG00000198467. [P07951-1]
Ensembl; ENST00000378292; ENSP00000367542; ENSG00000198467. [P07951-2]
GeneID; 7169; -.
KEGG; hsa:7169; -.
UCSC; uc003zxs.4; human. [P07951-1]
CTD; 7169; -.
DisGeNET; 7169; -.
EuPathDB; HostDB:ENSG00000198467.13; -.
GeneCards; TPM2; -.
GeneReviews; TPM2; -.
HGNC; HGNC:12011; TPM2.
HPA; HPA009066; -.
HPA; HPA047089; -.
HPA; HPA053624; -.
MalaCards; TPM2; -.
MIM; 108120; phenotype.
MIM; 190990; gene.
MIM; 601680; phenotype.
MIM; 609285; phenotype.
neXtProt; NX_P07951; -.
OpenTargets; ENSG00000198467; -.
Orphanet; 171881; Cap myopathy.
Orphanet; 171439; Childhood-onset nemaline myopathy.
Orphanet; 2020; Congenital fiber-type disproportion myopathy.
Orphanet; 1146; Digitotalar dysmorphism.
Orphanet; 1147; Sheldon-Hall syndrome.
Orphanet; 171436; Typical nemaline myopathy.
PharmGKB; PA36691; -.
eggNOG; KOG1003; Eukaryota.
eggNOG; ENOG410XR5K; LUCA.
GeneTree; ENSGT00550000074494; -.
HOVERGEN; HBG107404; -.
InParanoid; P07951; -.
KO; K10374; -.
OMA; CEGQAKD; -.
PhylomeDB; P07951; -.
TreeFam; TF351519; -.
Reactome; R-HSA-390522; Striated Muscle Contraction.
Reactome; R-HSA-445355; Smooth Muscle Contraction.
ChiTaRS; TPM2; human.
GeneWiki; TPM2; -.
GenomeRNAi; 7169; -.
PRO; PR:P07951; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000198467; -.
CleanEx; HS_TPM2; -.
ExpressionAtlas; P07951; baseline and differential.
Genevisible; P07951; HS.
GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
GO; GO:0005884; C:actin filament; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005862; C:muscle thin filament tropomyosin; TAS:ProtInc.
GO; GO:0003779; F:actin binding; IDA:UniProtKB.
GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0008307; F:structural constituent of muscle; TAS:ProtInc.
GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
GO; GO:0030049; P:muscle filament sliding; TAS:Reactome.
GO; GO:0043462; P:regulation of ATPase activity; IDA:UniProtKB.
InterPro; IPR000533; Tropomyosin.
Pfam; PF00261; Tropomyosin; 1.
PRINTS; PR00194; TROPOMYOSIN.
PROSITE; PS00326; TROPOMYOSIN; 1.
1: Evidence at protein level;
Acetylation; Actin-binding; Alternative splicing; Coiled coil;
Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
Disease mutation; Muscle protein; Nemaline myopathy; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 284 Tropomyosin beta chain.
/FTId=PRO_0000205627.
COILED 1 284 {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P58776}.
MOD_RES 53 53 Phosphothreonine.
{ECO:0000269|PubMed:24692096}.
MOD_RES 61 61 Phosphoserine; by PIK3CG.
{ECO:0000250|UniProtKB:P58774}.
MOD_RES 79 79 Phosphothreonine.
{ECO:0000269|PubMed:24692096}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000250|UniProtKB:P06753}.
MOD_RES 108 108 Phosphothreonine.
{ECO:0000269|PubMed:24692096}.
MOD_RES 158 158 Phosphoserine.
{ECO:0000269|PubMed:24692096}.
MOD_RES 206 206 Phosphoserine.
{ECO:0000269|PubMed:24692096}.
MOD_RES 215 215 Phosphoserine.
{ECO:0000250|UniProtKB:P58775}.
MOD_RES 252 252 Phosphothreonine.
{ECO:0000269|PubMed:24692096}.
MOD_RES 261 261 Phosphotyrosine.
{ECO:0000250|UniProtKB:P58775}.
MOD_RES 271 271 Phosphoserine.
{ECO:0000250|UniProtKB:P58775}.
MOD_RES 282 282 Phosphothreonine.
{ECO:0000269|PubMed:24692096}.
MOD_RES 283 283 Phosphoserine.
{ECO:0000269|PubMed:24692096}.
VAR_SEQ 1 80 MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEE
EQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATD
-> MAGISSIDAVKKKIQSLQQVADEAEERAEHLQREADAE
RQARER (in isoform 3). {ECO:0000305}.
/FTId=VSP_006594.
VAR_SEQ 189 213 KCGDLEEELKIVTNNLKSLEAQADK -> RARQLEEELRTM
DQALKSLMASEEE (in isoform 2 and isoform
3). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2059197,
ECO:0000303|PubMed:3865200,
ECO:0000303|Ref.4}.
/FTId=VSP_006595.
VAR_SEQ 258 284 DEVYAQKMKYKAISEELDNALNDITSL -> ETLASAKEEN
VEIHQTLDQTLLELNNL (in isoform 2 and
isoform 3). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2059197,
ECO:0000303|PubMed:3865200,
ECO:0000303|Ref.4}.
/FTId=VSP_006596.
VARIANT 2 2 D -> V (probable disease-associated
mutation found in patients with undefined
congenital myopathy; dbSNP:rs199476145).
{ECO:0000269|PubMed:24692096}.
/FTId=VAR_071485.
VARIANT 3 3 A -> G (in NEM4).
{ECO:0000269|PubMed:24692096}.
/FTId=VAR_071486.
VARIANT 7 7 Missing (in NEM4).
{ECO:0000269|PubMed:24692096}.
/FTId=VAR_071487.
VARIANT 14 14 D -> V (in NEM4).
{ECO:0000269|PubMed:24692096}.
/FTId=VAR_071488.
VARIANT 41 41 E -> K (in NEM4; also found in a patient
with congenital myopathy with fiber-type
disproportion and patients with undefined
congenital myopathy; dbSNP:rs137853306).
{ECO:0000269|PubMed:17846275,
ECO:0000269|PubMed:24692096}.
/FTId=VAR_070978.
VARIANT 49 49 Missing (in CAPM2).
{ECO:0000269|PubMed:19047562}.
/FTId=VAR_070979.
VARIANT 52 52 G -> GG (in CAPM2).
{ECO:0000269|PubMed:19047562}.
/FTId=VAR_070980.
VARIANT 91 91 R -> G (in DA1A; dbSNP:rs104894127).
{ECO:0000269|PubMed:12592607}.
/FTId=VAR_016086.
VARIANT 93 93 Q -> H (probable disease-associated
mutation found in patients with undefined
congenital myopathy; dbSNP:rs727504180).
{ECO:0000269|PubMed:24692096}.
/FTId=VAR_071489.
VARIANT 93 93 Q -> R (in DA1A; dbSNP:rs199476151).
{ECO:0000269|PubMed:24692096}.
/FTId=VAR_071490.
VARIANT 117 117 E -> A (in NEM4).
{ECO:0000269|PubMed:11738357}.
/FTId=VAR_013468.
VARIANT 117 117 E -> K (in DA1A; also found in a patient
with congenital myopathy with fiber-type
disproportion; dbSNP:rs104894129).
{ECO:0000269|PubMed:24692096}.
/FTId=VAR_071491.
VARIANT 128 128 K -> E (probable disease-associated
mutation found in a patient with
congenital myopathy with fiber-type
disproportion and patients with undefined
congenital myopathy).
{ECO:0000269|PubMed:24692096}.
/FTId=VAR_071492.
VARIANT 133 133 R -> P (probable disease-associated
mutation found in a patient with
congenital myopathy with fiber-type
disproportion and patients with undefined
congenital myopathy; dbSNP:rs199476152).
{ECO:0000269|PubMed:24692096}.
/FTId=VAR_071493.
VARIANT 133 133 R -> W (in DA2B, NEM4 and DA1A; also
found in a patient with congenital
myopathy with fiber-type disproportion;
dbSNP:rs137853305).
{ECO:0000269|PubMed:17339586,
ECO:0000269|PubMed:24692096}.
/FTId=VAR_070981.
VARIANT 139 139 Missing (in CAPM2; also found in a
patient with congenital myopathy with
fiber-type disproportion).
{ECO:0000269|PubMed:17434307,
ECO:0000269|PubMed:19345583,
ECO:0000269|PubMed:24692096}.
/FTId=VAR_070982.
VARIANT 143 143 L -> P (in NEM4; also found in a patient
with congenital myopathy with fiber-type
disproportion).
{ECO:0000269|PubMed:24692096}.
/FTId=VAR_071494.
VARIANT 147 147 Q -> P (in NEM4; dbSNP:rs104894128).
{ECO:0000269|PubMed:11738357}.
/FTId=VAR_013469.
VARIANT 148 148 L -> P (in NEM4; also found in a patient
with congenital myopathy with fiber-type
disproportion).
{ECO:0000269|PubMed:24692096}.
/FTId=VAR_071495.
VARIANT 155 155 A -> T (probable disease-associated
mutation found in patients with undefined
congenital myopathy).
{ECO:0000269|PubMed:24692096}.
/FTId=VAR_071496.
VARIANT 202 202 N -> K (in CAPM2; dbSNP:rs137853307).
{ECO:0000269|PubMed:19047562}.
/FTId=VAR_070983.
VARIANT 218 218 Missing (probable disease-associated
mutation in patients with undefined
congenital myopathy).
{ECO:0000269|PubMed:24692096}.
/FTId=VAR_071497.
VARIANT 261 261 Y -> C (in DA1A; also found in patients
with undefined congenital myopathy).
{ECO:0000269|PubMed:24692096}.
/FTId=VAR_071498.
VARIANT 273 273 E -> K (in dbSNP:rs3180843).
/FTId=VAR_052402.
CONFLICT 89 89 N -> S (in Ref. 4; BAD96978).
{ECO:0000305}.
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


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