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P06753 (TPM3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 167. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tropomyosin alpha-3 chain
Alternative name(s):
Gamma-tropomyosin
Tropomyosin-3
Tropomyosin-5
Short name=hTM5
Gene names
Name:TPM3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length285 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subunit structure

Heterodimer of an alpha and a beta chain. Binds to TMOD1. Ref.13

Subcellular location

Cytoplasmcytoskeleton.

Domain

The molecule is in a coiled coil structure that is formed by 2 polypeptide chains. The sequence exhibits a prominent seven-residues periodicity.

Involvement in disease

Nemaline myopathy 1 (NEM1) [MIM:609284]: A form of nemaline myopathy with autosomal dominant or recessive inheritance. Nemaline myopathies are disorders characterized by muscle weakness of varying onset and severity, and abnormal thread-like or rod-shaped structures in muscle fibers on histologic examination. Autosomal dominant NEM1 is characterized by a moderate phenotype with onset between birth and early second decade of life. Weakness is diffuse and symmetric with slow progression often with need for a wheelchair in adulthood. The autosomal recessive form has onset at birth with moderate to severe hypotonia and diffuse weakness. In the most severe cases, death can occur before 2 years. Less severe cases have delayed major motor milestones, and these patients may walk, but often need a wheelchair before 10 years.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 Ref.20 Ref.21

Thyroid papillary carcinoma (TPC) [MIM:188550]: A common tumor of the thyroid that typically arises as an irregular, solid or cystic mass from otherwise normal thyroid tissue. Papillary carcinomas are malignant neoplasm characterized by the formation of numerous, irregular, finger-like projections of fibrous stroma that is covered with a surface layer of neoplastic epithelial cells.
Note: The disease is caused by mutations affecting the gene represented in this entry. A chromosomal aberration involving TPM3 is found in thyroid papillary carcinomas. A rearrangement with NTRK1 generates the TRK fusion transcript by fusing the amino end of isoform 2 of TPM3 to the 3'-end of NTRK1.

Myopathy, congenital, with fiber-type disproportion (CFTD) [MIM:255310]: A genetically heterogeneous disorder in which there is relative hypotrophy of type 1 muscle fibers compared to type 2 fibers on skeletal muscle biopsy. However, these findings are not specific and can be found in many different myopathic and neuropathic conditions.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22

Cap myopathy 1 (CAPM1) [MIM:609284]: 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 slowly progressive muscle weakness. Respiratory problems are common.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22 Ref.23 Ref.24

Sequence similarities

Belongs to the tropomyosin family.

Caution

It is uncertain whether Met-1 or Met-2 is the initiator.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P06753-1)

Also known as: Skeletal muscle;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P06753-2)

Also known as: Cytoskeletal; TM30nm;

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: MMEAIKKKMQ...LELAEKKAAD → MAGITTIEAV...VEGERRAREQ
     190-212: KCSELEEELKNVTNNLKSLEAQA → RCREMDEQIRLMDQNLKCLSAAE
     260-285: ELYAQKLKYKAISEELDHALNDMTSI → KLKCTKEEHLCTQRMLDQTLLDLNEM
Note: Peptides 2-27, 41-55, 132-153, 163-169, 216-225 and 237-248 have been identified and sequenced by MS. Initiator Met-1 is removed. Contains a N-acetylalanine at position 2. Ref.8 (ABC40673) sequence corresponds to a TPM3 retrocopy (rcTPM3) on chromosome 16 that is generated by retroposition of reversed transcribed mRNA back to the genome. rcTPM3 functionality is uncertain. It has been detected by MS in primary breast cancer tissues. Contains a N6-acetyllysine at position 215. Contains a N6-acetyllysine at position 177.
Isoform 3 (identifier: P06753-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: MMEAIKKKMQ...LELAEKKAAD → MAGITTIEAV...VEGERRAREQ
     190-212: KCSELEEELKNVTNNLKSLEAQA → RCREMDEQIRLMDQNLKCLSAAE
     259-285: DELYAQKLKYKAISEELDHALNDMTSI → ERLYSQLERNRLLSNELKLTLHDLCD
Note: Peptides 2-27, 41-55, 132-153 and 163-169 have been identified and sequenced by MS. Initiator Met-1 is removed. Contains a N-acetylalanine at position 2. Contains a N6-acetyllysine at position 177.
Isoform 4 (identifier: P06753-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: MM → MAGITTI
     5-21: IKKKMQMLKLDKENALD → VKRKIQVLQQQADDAEE
     25-81: QAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAAD → RLQREVEGERRAREQ
     259-260: DE → ER
     263-285: AQKLKYKAISEELDHALNDMTSI → SQLERNRLLSNELKLTLHDLCD
Note: Gene prediction based on EST data.
Isoform 5 (identifier: P06753-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: MM → MAGITTI
     5-21: IKKKMQMLKLDKENALD → VKRKIQVLQQQADDAEE
     25-81: QAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAAD → RLQREVEGERRAREQ
     260-285: ELYAQKLKYKAISEELDHALNDMTSI → KLKCTKEEHLCTQRMLDQTLLDLNEM
Note: Gene prediction based on EST data. Contains a N6-acetyllysine at position 215.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 285285Tropomyosin alpha-3 chain
PRO_0000205632

Regions

Coiled coil1 – 285285 By similarity

Natural variations

Alternative sequence1 – 8181MMEAI…KKAAD → MAGITTIEAVKRKIQVLQQQ ADDAEERAERLQREVEGERR AREQ in isoform 2 and isoform 3.
VSP_006604
Alternative sequence1 – 22MM → MAGITTI in isoform 4 and isoform 5.
VSP_047302
Alternative sequence5 – 2117IKKKM…ENALD → VKRKIQVLQQQADDAEE in isoform 4 and isoform 5.
VSP_047303
Alternative sequence25 – 8157QAEAE…KKAAD → RLQREVEGERRAREQ in isoform 4 and isoform 5.
VSP_047304
Alternative sequence190 – 21223KCSEL…LEAQA → RCREMDEQIRLMDQNLKCLS AAE in isoform 2 and isoform 3.
VSP_006605
Alternative sequence259 – 28527DELYA…DMTSI → ERLYSQLERNRLLSNELKLT LHDLCD in isoform 3.
VSP_006607
Alternative sequence259 – 2602DE → ER in isoform 4.
VSP_047305
Alternative sequence260 – 28526ELYAQ…DMTSI → KLKCTKEEHLCTQRMLDQTL LDLNEM in isoform 2 and isoform 5.
VSP_006606
Alternative sequence263 – 28523AQKLK…DMTSI → SQLERNRLLSNELKLTLHDL CD in isoform 4.
VSP_047306
Natural variant91M → R in NEM1; decrease in the sensitivity of contraction to activating calcium. Ref.18 Ref.20
VAR_013460
Natural variant1001L → M in CFTD. Ref.22
VAR_070066
Natural variant1681R → C in CFTD and CAPM1. Ref.22 Ref.23
VAR_070067
Natural variant1681R → G in CFTD. Ref.22
VAR_070068
Natural variant1681R → H in NEM1 and CAPM1. Ref.21 Ref.22 Ref.24
VAR_070069
Natural variant1691K → E in CFTD. Ref.22
VAR_070070
Natural variant2451R → G in CFTD. Ref.22
VAR_070071

Experimental info

Sequence conflict1501K → E in CAA27243. Ref.3
Isoform 2:
Sequence conflict331R → Q in ABC40673. Ref.8
Sequence conflict431E → K in ABC40673. Ref.8
Sequence conflict661A → P in ABC40673. Ref.8
Sequence conflict851D → G in ABC40673. Ref.8
Sequence conflict1101I → L in ABC40673. Ref.8
Sequence conflict1351I → T in ABC40673. Ref.8
Sequence conflict1501A → T in ABC40673. Ref.8
Sequence conflict1921L → F in ABC40673. Ref.8
Sequence conflict1961L → P in ABC40673. Ref.8
Sequence conflict2021R → C in ABC40673. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Skeletal muscle) [UniParc].

Last modified June 26, 2013. Version 2.
Checksum: 99EAD24C45460A14

FASTA28532,950
        10         20         30         40         50         60 
MMEAIKKKMQ MLKLDKENAL DRAEQAEAEQ KQAEERSKQL EDELAAMQKK LKGTEDELDK 

        70         80         90        100        110        120 
YSEALKDAQE KLELAEKKAA DAEAEVASLN RRIQLVEEEL DRAQERLATA LQKLEEAEKA 

       130        140        150        160        170        180 
ADESERGMKV IENRALKDEE KMELQEIQLK EAKHIAEEAD RKYEEVARKL VIIEGDLERT 

       190        200        210        220        230        240 
EERAELAESK CSELEEELKN VTNNLKSLEA QAEKYSQKED KYEEEIKILT DKLKEAETRA 

       250        260        270        280 
EFAERSVAKL EKTIDDLEDE LYAQKLKYKA ISEELDHALN DMTSI 

« Hide

Isoform 2 (Cytoskeletal) (TM30nm) [UniParc].

Checksum: 5C049312A337BC19
Show »

FASTA24829,033
Isoform 3 [UniParc].

Checksum: 4929E6D4591374D3
Show »

FASTA24728,955
Isoform 4 [UniParc].

Checksum: 239796CBE73C98AE
Show »

FASTA24728,793
Isoform 5 [UniParc].

Checksum: 179E2D62BC8993F5
Show »

FASTA24828,870

References

« Hide 'large scale' references
[1]"Tissue-specific expression of the human tropomyosin gene involved in the generation of the trk oncogene."
Reinach F.C., McLeod A.R.
Nature 322:648-650(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"The mRNA and RNA-copy pseudogenes encoding TM30nm, a human cytoskeletal tropomyosin."
McLeod A.R., Houlker C., Talbot K.
Nucleic Acids Res. 14:8413-8426(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"Organization of the hTMnm gene. Implications for the evolution of muscle and non-muscle tropomyosins."
Clayton L., Reinach F.C., Chumbley G.M., MacLeod A.R.
J. Mol. Biol. 201:507-515(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2).
[4]"Identification and characterization of a novel tropomyosin isoform from a colon cancer cell line T84."
Lin J.J.-C., Lin J.L.-C., Geng X., Das K.M.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 3).
Tissue: Colon cancer.
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Bone, Kidney, Skeletal muscle and Uterus.
[8]"Emergence of young human genes after a burst of retroposition in primates."
Marques A.C., Dupanloup I., Vinckenbosch N., Reymond A., Kaessmann H.
PLoS Biol. 3:E357-E357(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-248 (ISOFORM 2), IDENTIFICATION OF RCTPM3.
[9]Bienvenut W.V., Claeys D.
Submitted (DEC-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 93-126; 135-150; 154-168 AND 215-245, PARTIAL PROTEIN SEQUENCE (ISOFORMS 2/3), CLEAVAGE OF INITIATOR METHIONINE (ISOFORMS 2/3), ACETYLATION AT ALA-2 (ISOFORMS 2/3), IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma and Platelet.
[10]Bienvenut W.V., Glen H., Brunton V.G., Frame M.C.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 93-119, PARTIAL PROTEIN SEQUENCE (ISOFORMS 2/3), CLEAVAGE OF INITIATOR METHIONINE (ISOFORMS 2/3), ACETYLATION AT ALA-2 (ISOFORMS 2/3), IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Osteosarcoma.
[11]"A human oncogene formed by the fusion of truncated tropomyosin and protein tyrosine kinase sequences."
Martin-Zanca D., Hughes S.H., Barbacid M.
Nature 319:743-748(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CHROMOSOMAL TRANSLOCATION WITH NTRK1.
[12]"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
Tissue: Keratinocyte.
[13]"Erythrocyte tropomodulin binds to the N-terminus of hTM5, a tropomyosin isoform encoded by the gamma-tropomyosin gene."
Sung L.A., Lin J.J.-C.
Biochem. Biophys. Res. Commun. 201:627-634(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TMOD1.
[14]"Abnormal proteins in primary breast cancer tissues from 25 Sudanese patients."
Ahamed M.E., Ahmed M.E., Eltoum A.M., Altahir G.O., Ahmed K.M., Harbi S.O., Stansalas J., Mohamed A.O.
Eur. J. Inflamm. 6:115-121(2008)
Cited for: IDENTIFICATION OF RCTPM3 BY MASS SPECTROMETRY.
Tissue: Mammary cancer.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-177 (ISOFORMS 2 AND 3), ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215 (ISOFORMS 2 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"A mutation in the alpha tropomyosin gene TPM3 associated with autosomal dominant nemaline myopathy."
Laing N.G., Wilton S.D., Akkari P.A., Dorosz S., Boundy K., Kneebone C., Blumbergs P., White S., Watkins H., Love D.R., Haan E.
Nat. Genet. 9:75-79(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NEM1 ARG-9.
[19]Erratum
Laing N.G., Wilton S.D., Akkari P.A., Dorosz S., Boundy K., Kneebone C., Blumbergs P., White S., Watkins H., Love D.R., Haan E.
Nat. Genet. 10:249-249(1995) [PubMed] [Europe PMC] [Abstract]
[20]"A nemaline myopathy mutation in alpha-tropomyosin causes defective regulation of striated muscle force production."
Michele D.E., Albayya F.P., Metzger J.M.
J. Clin. Invest. 104:1575-1581(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT NEM1 ARG-9.
[21]"A second pedigree with autosomal dominant nemaline myopathy caused by TPM3 mutation: a clinical and pathological study."
Penisson-Besnier I., Monnier N., Toutain A., Dubas F., Laing N.
Neuromuscul. Disord. 17:330-337(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NEM1 HIS-168.
[22]"Mutations in TPM3 are a common cause of congenital fiber type disproportion."
Clarke N.F., Kolski H., Dye D.E., Lim E., Smith R.L., Patel R., Fahey M.C., Bellance R., Romero N.B., Johnson E.S., Labarre-Vila A., Monnier N., Laing N.G., North K.N.
Ann. Neurol. 63:329-337(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CFTD MET-100; CYS-168; GLY-168; GLU-169 AND GLY-245, VARIANT CAPM1 HIS-168.
[23]"TPM3 mutation in one of the original cases of cap disease."
Ohlsson M., Fidzianska A., Tajsharghi H., Oldfors A.
Neurology 72:1961-1963(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CAPM1 CYS-168.
[24]"A TPM3 mutation causing cap myopathy."
De Paula A.M., Franques J., Fernandez C., Monnier N., Lunardi J., Pellissier J.F., Figarella-Branger D., Pouget J.
Neuromuscul. Disord. 19:685-688(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CAPM1 HIS-168.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04201 mRNA. Translation: CAA27798.1.
AY004867 mRNA. Translation: AAF87083.1.
X04588 mRNA. Translation: CAB37185.1.
AL590431 Genomic DNA. Translation: CAH71264.1.
AL590431 Genomic DNA. Translation: CAH71269.1.
CH471121 Genomic DNA. Translation: EAW53229.1.
CH471121 Genomic DNA. Translation: EAW53231.1.
CH471121 Genomic DNA. Translation: EAW53235.1.
BC000771 mRNA. Translation: AAH00771.1.
BC008407 mRNA. Translation: AAH08407.1.
BC008425 mRNA. Translation: AAH08425.1.
BC015403 mRNA. Translation: AAH15403.1.
BC072428 mRNA. Translation: AAH72428.1.
DQ120714 Genomic DNA. Translation: ABC40673.1.
X03541 mRNA. Translation: CAA27243.1. Different termination.
PIRA25530.
A24199. S06210.
RefSeqNP_001036816.1. NM_001043351.1.
NP_001036817.1. NM_001043352.1.
NP_001036818.1. NM_001043353.1.
NP_001265120.1. NM_001278191.1.
NP_689476.2. NM_152263.3.
NP_705935.1. NM_153649.3.
UniGeneHs.535581.
Hs.578978.
Hs.644306.
Hs.654421.

3D structure databases

ProteinModelPortalP06753.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113023. 44 interactions.
IntActP06753. 14 interactions.
MINTMINT-1142638.
STRING9606.ENSP00000357513.

PTM databases

PhosphoSiteP06753.

Polymorphism databases

DMDM519668659.

2D gel databases

DOSAC-COBS-2DPAGEP06753.
SWISS-2DPAGEP06753.

Proteomic databases

PaxDbP06753.
PRIDEP06753.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000323144; ENSP00000357518; ENSG00000143549. [P06753-4]
ENST00000330188; ENSP00000339035; ENSG00000143549. [P06753-5]
ENST00000368530; ENSP00000357516; ENSG00000143549. [P06753-1]
ENST00000368531; ENSP00000357517; ENSG00000143549. [P06753-3]
ENST00000368533; ENSP00000357521; ENSG00000143549. [P06753-2]
GeneID7170.
KEGGhsa:7170.
UCSCuc001fea.1. human. [P06753-2]
uc001feb.1. human. [P06753-3]
uc001fec.2. human. [P06753-1]

Organism-specific databases

CTD7170.
GeneCardsGC01M154127.
HGNCHGNC:12012. TPM3.
HPAHPA000261.
HPA009066.
MIM164970. gene.
188550. phenotype.
191030. gene.
255310. phenotype.
609284. phenotype.
neXtProtNX_P06753.
Orphanet171881. Cap myopathy.
171439. Childhood-onset nemaline myopathy.
2020. Congenital fiber-type disproportion myopathy.
178342. Inflammatory myofibroblastic tumor.
171433. Intermediate nemaline myopathy.
PharmGKBPA36692.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG304012.
HOVERGENHBG107404.
InParanoidP06753.
KOK09290.
OMAELAEAKC.
OrthoDBEOG7673C8.
TreeFamTF351519.

Enzyme and pathway databases

ReactomeREACT_17044. Muscle contraction.

Gene expression databases

ArrayExpressP06753.
BgeeP06753.
CleanExHS_TPM3.
GenevestigatorP06753.

Family and domain databases

InterProIPR000533. Tropomyosin.
[Graphical view]
PfamPF00261. Tropomyosin. 1 hit.
[Graphical view]
PRINTSPR00194. TROPOMYOSIN.
PROSITEPS00326. TROPOMYOSIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTPM3. human.
GeneWikiTropomyosin_3.
GenomeRNAi7170.
NextBio28092.
PROP06753.
SOURCESearch...

Entry information

Entry nameTPM3_HUMAN
AccessionPrimary (citable) accession number: P06753
Secondary accession number(s): D3DV71 expand/collapse secondary AC list , P12324, Q2QD06, Q5VU66, Q5VU71, Q5VU72, Q969Q2, Q9NQH8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: June 26, 2013
Last modified: April 16, 2014
This is version 167 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM