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Protein

Tropomyosin alpha-3 chain

Gene

TPM3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Biological processi

  1. movement of cell or subcellular component Source: UniProtKB
  2. muscle contraction Source: Reactome
  3. muscle filament sliding Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_16969. Striated Muscle Contraction.
REACT_20558. Smooth Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Tropomyosin alpha-3 chain
Alternative name(s):
Gamma-tropomyosin
Tropomyosin-3
Tropomyosin-5
Short name:
hTM5
Gene namesi
Name:TPM3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:12012. TPM3.

Subcellular locationi

GO - Cellular componenti

  1. cleavage furrow Source: Ensembl
  2. cortical cytoskeleton Source: Ensembl
  3. cytoskeleton Source: UniProtKB
  4. cytosol Source: Reactome
  5. extracellular vesicular exosome Source: UniProtKB
  6. filamentous actin Source: Ensembl
  7. growth cone Source: Ensembl
  8. muscle thin filament tropomyosin Source: UniProtKB
  9. podosome Source: Ensembl
  10. stress fiber Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Nemaline myopathy 13 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:609284
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91M → R in NEM1; decrease in the sensitivity of contraction to activating calcium. 2 Publications
VAR_013460
Natural varianti88 – 881S → F in NEM1 and CAPM1. 1 Publication
VAR_071500
Natural varianti168 – 1681R → C in CFTD, CAPM1 and NEM1; also found in patients with undefined congenital myopathy. 3 Publications
VAR_070067
Natural varianti168 – 1681R → H in NEM1, CAPM1 and CFTD; also found in patients with undefined congenital myopathy. 6 Publications
VAR_070069
Thyroid papillary carcinoma

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.

Disease descriptionA 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.

See also OMIM:188550
Myopathy, congenital, with fiber-type disproportion4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:255310
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41A → V in CFTD. 1 Publication
VAR_071499
Natural varianti91 – 911R → P in CFTD. 1 Publication
VAR_071502
Natural varianti100 – 1001L → M in CFTD. 1 Publication
VAR_070066
Natural varianti100 – 1001L → V in CFTD. 1 Publication
VAR_071503
Natural varianti168 – 1681R → C in CFTD, CAPM1 and NEM1; also found in patients with undefined congenital myopathy. 3 Publications
VAR_070067
Natural varianti168 – 1681R → G in CFTD. 1 Publication
VAR_070068
Natural varianti168 – 1681R → H in NEM1, CAPM1 and CFTD; also found in patients with undefined congenital myopathy. 6 Publications
VAR_070069
Natural varianti169 – 1691K → E in CFTD. 1 Publication
VAR_070070
Natural varianti174 – 1741E → A in CFTD. 1 Publication
VAR_071506
Natural varianti241 – 2411E → K in CFTD. 1 Publication
VAR_071507
Natural varianti245 – 2451R → G in CFTD. 1 Publication
VAR_070071
Cap myopathy 15 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:609284
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti88 – 881S → F in NEM1 and CAPM1. 1 Publication
VAR_071500
Natural varianti149 – 1491L → I in CAPM1. 1 Publication
VAR_071504
Natural varianti151 – 1511E → A in CAPM1. 1 Publication
VAR_071505
Natural varianti168 – 1681R → C in CFTD, CAPM1 and NEM1; also found in patients with undefined congenital myopathy. 3 Publications
VAR_070067
Natural varianti168 – 1681R → H in NEM1, CAPM1 and CFTD; also found in patients with undefined congenital myopathy. 6 Publications
VAR_070069
Natural varianti245 – 2451R → I in CAPM1. 1 Publication
VAR_071508

Keywords - Diseasei

Disease mutation, Nemaline myopathy, Proto-oncogene

Organism-specific databases

MIMi188550. phenotype.
255310. phenotype.
609284. phenotype.
Orphaneti171881. Cap myopathy.
171439. Childhood-onset nemaline myopathy.
2020. Congenital fiber-type disproportion myopathy.
178342. Inflammatory myofibroblastic tumor.
171433. Intermediate nemaline myopathy.
PharmGKBiPA36692.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 285284Tropomyosin alpha-3 chainPRO_0000205632Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylmethionineBy similarity
Modified residuei54 – 541PhosphothreonineBy similarity
Modified residuei62 – 621PhosphoserineBy similarity
Modified residuei109 – 1091PhosphothreonineBy similarity
Modified residuei207 – 2071PhosphoserineBy similarity
Modified residuei253 – 2531PhosphothreonineBy similarity
Modified residuei283 – 2831PhosphothreonineBy similarity
Modified residuei284 – 2841PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP06753.
PaxDbiP06753.
PRIDEiP06753.

2D gel databases

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

PTM databases

PhosphoSiteiP06753.

Expressioni

Gene expression databases

BgeeiP06753.
CleanExiHS_TPM3.
ExpressionAtlasiP06753. baseline and differential.
GenevestigatoriP06753.

Organism-specific databases

HPAiHPA000261.
HPA009066.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi113023. 79 interactions.
IntActiP06753. 14 interactions.
MINTiMINT-1142638.
STRINGi9606.ENSP00000357513.

Structurei

3D structure databases

ProteinModelPortaliP06753.
SMRiP06753. Positions 9-285.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1 – 285285By similarityAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the tropomyosin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG304012.
GeneTreeiENSGT00550000074494.
HOGENOMiHOG000231522.
HOVERGENiHBG107404.
InParanoidiP06753.
KOiK09290.
OMAiXLEDELA.
OrthoDBiEOG7673C8.
PhylomeDBiP06753.
TreeFamiTF351519.

Family and domain databases

InterProiIPR000533. Tropomyosin.
[Graphical view]
PfamiPF00261. Tropomyosin. 1 hit.
[Graphical view]
PRINTSiPR00194. TROPOMYOSIN.
PROSITEiPS00326. TROPOMYOSIN. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P06753-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MMEAIKKKMQ MLKLDKENAL DRAEQAEAEQ KQAEERSKQL EDELAAMQKK
60 70 80 90 100
LKGTEDELDK YSEALKDAQE KLELAEKKAA DAEAEVASLN RRIQLVEEEL
110 120 130 140 150
DRAQERLATA LQKLEEAEKA ADESERGMKV IENRALKDEE KMELQEIQLK
160 170 180 190 200
EAKHIAEEAD RKYEEVARKL VIIEGDLERT EERAELAESK CSELEEELKN
210 220 230 240 250
VTNNLKSLEA QAEKYSQKED KYEEEIKILT DKLKEAETRA EFAERSVAKL
260 270 280
EKTIDDLEDE LYAQKLKYKA ISEELDHALN DMTSI
Length:285
Mass (Da):32,950
Last modified:June 26, 2013 - v2
Checksum:i99EAD24C45460A14
GO
Isoform 2 (identifier: P06753-2) [UniParc]FASTAAdd to basket

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.Curated1 Publication

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.Curated1 Publication

Show »
Length:248
Mass (Da):29,033
Checksum:i5C049312A337BC19
GO
Isoform 3 (identifier: P06753-3) [UniParc]FASTAAdd to basket

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 177.1 Publication

Show »
Length:247
Mass (Da):28,955
Checksum:i4929E6D4591374D3
GO
Isoform 4 (identifier: P06753-4) [UniParc]FASTAAdd to basket

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.

Show »
Length:247
Mass (Da):28,793
Checksum:i239796CBE73C98AE
GO
Isoform 5 (identifier: P06753-5) [UniParc]FASTAAdd to basket

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 215.1 Publication

Show »
Length:248
Mass (Da):28,870
Checksum:i179E2D62BC8993F5
GO
Isoform 6 (identifier: P06753-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: MMEAIKKKMQ...LELAEKKAAD → MAGITTIEAV...VEGERRAREQ
     190-212: KCSELEEELKNVTNNLKSLEAQA → RCREMDEQIRLMDQNLKCLSAAE

Note: No experimental confirmation available. Contains a N6-acetyllysine at position 177.1 Publication

Show »
Length:248
Mass (Da):28,922
Checksum:i5427F068894BF936
GO
Isoform 7 (identifier: P06753-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-127: Missing.
     260-285: ELYAQKLKYKAISEELDHALNDMTSI → KLKCTKEEHLCTQRMLDQTLLDLNEM

Note: No experimental confirmation available. Gene prediction based on EST data. Contains a N6-acetyllysine at position 125.1 Publication

Show »
Length:158
Mass (Da):18,603
Checksum:iD3F876D8EFC7265F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti150 – 1501K → E in CAA27243 (PubMed:12574106).Curated
Isoform 2 (identifier: P06753-2)
Sequence conflicti33 – 331R → Q in ABC40673 (PubMed:16201836).Curated1 Publication
Sequence conflicti43 – 431E → K in ABC40673 (PubMed:16201836).Curated1 Publication
Sequence conflicti66 – 661A → P in ABC40673 (PubMed:16201836).Curated1 Publication
Sequence conflicti85 – 851D → G in ABC40673 (PubMed:16201836).Curated1 Publication
Sequence conflicti110 – 1101I → L in ABC40673 (PubMed:16201836).Curated1 Publication
Sequence conflicti135 – 1351I → T in ABC40673 (PubMed:16201836).Curated1 Publication
Sequence conflicti150 – 1501A → T in ABC40673 (PubMed:16201836).Curated1 Publication
Sequence conflicti192 – 1921L → F in ABC40673 (PubMed:16201836).Curated1 Publication
Sequence conflicti196 – 1961L → P in ABC40673 (PubMed:16201836).Curated1 Publication
Sequence conflicti202 – 2021R → C in ABC40673 (PubMed:16201836).Curated1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41A → V in CFTD. 1 Publication
VAR_071499
Natural varianti9 – 91M → R in NEM1; decrease in the sensitivity of contraction to activating calcium. 2 Publications
VAR_013460
Natural varianti88 – 881S → F in NEM1 and CAPM1. 1 Publication
VAR_071500
Natural varianti91 – 911R → C Probable disease-associated mutation found in patients with undefined congenital myopathy. 1 Publication
VAR_071501
Natural varianti91 – 911R → P in CFTD. 1 Publication
VAR_071502
Natural varianti100 – 1001L → M in CFTD. 1 Publication
VAR_070066
Natural varianti100 – 1001L → V in CFTD. 1 Publication
VAR_071503
Natural varianti149 – 1491L → I in CAPM1. 1 Publication
VAR_071504
Natural varianti151 – 1511E → A in CAPM1. 1 Publication
VAR_071505
Natural varianti168 – 1681R → C in CFTD, CAPM1 and NEM1; also found in patients with undefined congenital myopathy. 3 Publications
VAR_070067
Natural varianti168 – 1681R → G in CFTD. 1 Publication
VAR_070068
Natural varianti168 – 1681R → H in NEM1, CAPM1 and CFTD; also found in patients with undefined congenital myopathy. 6 Publications
VAR_070069
Natural varianti169 – 1691K → E in CFTD. 1 Publication
VAR_070070
Natural varianti174 – 1741E → A in CFTD. 1 Publication
VAR_071506
Natural varianti241 – 2411E → K in CFTD. 1 Publication
VAR_071507
Natural varianti245 – 2451R → G in CFTD. 1 Publication
VAR_070071
Natural varianti245 – 2451R → I in CAPM1. 1 Publication
VAR_071508
Natural varianti253 – 2531T → K Probable disease-associated mutation found in patients with undefined congenital myopathy. 1 Publication
VAR_071509

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 127127Missing in isoform 7. CuratedVSP_054792Add
BLAST
Alternative sequencei1 – 8181MMEAI…KKAAD → MAGITTIEAVKRKIQVLQQQ ADDAEERAERLQREVEGERR AREQ in isoform 2, isoform 3 and isoform 6. 2 PublicationsVSP_006604Add
BLAST
Alternative sequencei1 – 22MM → MAGITTI in isoform 4 and isoform 5. CuratedVSP_047302
Alternative sequencei5 – 2117IKKKM…ENALD → VKRKIQVLQQQADDAEE in isoform 4 and isoform 5. CuratedVSP_047303Add
BLAST
Alternative sequencei25 – 8157QAEAE…KKAAD → RLQREVEGERRAREQ in isoform 4 and isoform 5. CuratedVSP_047304Add
BLAST
Alternative sequencei190 – 21223KCSEL…LEAQA → RCREMDEQIRLMDQNLKCLS AAE in isoform 2, isoform 3 and isoform 6. 2 PublicationsVSP_006605Add
BLAST
Alternative sequencei259 – 28527DELYA…DMTSI → ERLYSQLERNRLLSNELKLT LHDLCD in isoform 3. CuratedVSP_006607Add
BLAST
Alternative sequencei259 – 2602DE → ER in isoform 4. CuratedVSP_047305
Alternative sequencei260 – 28526ELYAQ…DMTSI → KLKCTKEEHLCTQRMLDQTL LDLNEM in isoform 2, isoform 5 and isoform 7. 2 PublicationsVSP_006606Add
BLAST
Alternative sequencei263 – 28523AQKLK…DMTSI → SQLERNRLLSNELKLTLHDL CD in isoform 4. CuratedVSP_047306Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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: EAW53230.1.
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.
AF474157 mRNA. Translation: AAL84570.1.
CCDSiCCDS1060.1. [P06753-2]
CCDS41400.1. [P06753-5]
CCDS41401.1. [P06753-4]
CCDS41402.1. [P06753-3]
CCDS41403.1. [P06753-1]
CCDS60274.1. [P06753-7]
CCDS60275.1. [P06753-6]
PIRiA25530.
S06210. A24199.
RefSeqiNP_001036816.1. NM_001043351.1. [P06753-5]
NP_001036817.1. NM_001043352.1. [P06753-3]
NP_001036818.1. NM_001043353.1. [P06753-4]
NP_001265118.1. NM_001278189.1. [P06753-6]
NP_001265120.1. NM_001278191.1. [P06753-7]
NP_689476.2. NM_152263.3. [P06753-1]
NP_705935.1. NM_153649.3. [P06753-2]
XP_006711585.1. XM_006711522.1. [P06753-6]
UniGeneiHs.535581.
Hs.578978.
Hs.644306.
Hs.654421.

Genome annotation databases

EnsembliENST00000302206; ENSP00000307712; ENSG00000143549. [P06753-7]
ENST00000323144; ENSP00000357518; ENSG00000143549. [P06753-4]
ENST00000328159; ENSP00000357520; ENSG00000143549. [P06753-6]
ENST00000330188; ENSP00000339035; ENSG00000143549. [P06753-5]
ENST00000368530; ENSP00000357516; ENSG00000143549. [P06753-1]
ENST00000368531; ENSP00000357517; ENSG00000143549. [P06753-3]
ENST00000368533; ENSP00000357521; ENSG00000143549. [P06753-2]
GeneIDi7170.
KEGGihsa:7170.
UCSCiuc001fdz.1. human.
uc001fea.1. human. [P06753-2]
uc001feb.1. human. [P06753-3]
uc001fec.2. human. [P06753-1]
uc001fed.2. human.

Polymorphism databases

DMDMi519668659.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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: EAW53230.1.
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.
AF474157 mRNA. Translation: AAL84570.1.
CCDSiCCDS1060.1. [P06753-2]
CCDS41400.1. [P06753-5]
CCDS41401.1. [P06753-4]
CCDS41402.1. [P06753-3]
CCDS41403.1. [P06753-1]
CCDS60274.1. [P06753-7]
CCDS60275.1. [P06753-6]
PIRiA25530.
S06210. A24199.
RefSeqiNP_001036816.1. NM_001043351.1. [P06753-5]
NP_001036817.1. NM_001043352.1. [P06753-3]
NP_001036818.1. NM_001043353.1. [P06753-4]
NP_001265118.1. NM_001278189.1. [P06753-6]
NP_001265120.1. NM_001278191.1. [P06753-7]
NP_689476.2. NM_152263.3. [P06753-1]
NP_705935.1. NM_153649.3. [P06753-2]
XP_006711585.1. XM_006711522.1. [P06753-6]
UniGeneiHs.535581.
Hs.578978.
Hs.644306.
Hs.654421.

3D structure databases

ProteinModelPortaliP06753.
SMRiP06753. Positions 9-285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113023. 79 interactions.
IntActiP06753. 14 interactions.
MINTiMINT-1142638.
STRINGi9606.ENSP00000357513.

PTM databases

PhosphoSiteiP06753.

Polymorphism databases

DMDMi519668659.

2D gel databases

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

Proteomic databases

MaxQBiP06753.
PaxDbiP06753.
PRIDEiP06753.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302206; ENSP00000307712; ENSG00000143549. [P06753-7]
ENST00000323144; ENSP00000357518; ENSG00000143549. [P06753-4]
ENST00000328159; ENSP00000357520; ENSG00000143549. [P06753-6]
ENST00000330188; ENSP00000339035; ENSG00000143549. [P06753-5]
ENST00000368530; ENSP00000357516; ENSG00000143549. [P06753-1]
ENST00000368531; ENSP00000357517; ENSG00000143549. [P06753-3]
ENST00000368533; ENSP00000357521; ENSG00000143549. [P06753-2]
GeneIDi7170.
KEGGihsa:7170.
UCSCiuc001fdz.1. human.
uc001fea.1. human. [P06753-2]
uc001feb.1. human. [P06753-3]
uc001fec.2. human. [P06753-1]
uc001fed.2. human.

Organism-specific databases

CTDi7170.
GeneCardsiGC01M154127.
GeneReviewsiTPM3.
HGNCiHGNC:12012. TPM3.
HPAiHPA000261.
HPA009066.
MIMi164970. gene.
188550. phenotype.
191030. gene.
255310. phenotype.
609284. phenotype.
neXtProtiNX_P06753.
Orphaneti171881. Cap myopathy.
171439. Childhood-onset nemaline myopathy.
2020. Congenital fiber-type disproportion myopathy.
178342. Inflammatory myofibroblastic tumor.
171433. Intermediate nemaline myopathy.
PharmGKBiPA36692.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG304012.
GeneTreeiENSGT00550000074494.
HOGENOMiHOG000231522.
HOVERGENiHBG107404.
InParanoidiP06753.
KOiK09290.
OMAiXLEDELA.
OrthoDBiEOG7673C8.
PhylomeDBiP06753.
TreeFamiTF351519.

Enzyme and pathway databases

ReactomeiREACT_16969. Striated Muscle Contraction.
REACT_20558. Smooth Muscle Contraction.

Miscellaneous databases

ChiTaRSiTPM3. human.
GeneWikiiTropomyosin_3.
GenomeRNAii7170.
NextBioi28092.
PROiP06753.
SOURCEiSearch...

Gene expression databases

BgeeiP06753.
CleanExiHS_TPM3.
ExpressionAtlasiP06753. baseline and differential.
GenevestigatoriP06753.

Family and domain databases

InterProiIPR000533. Tropomyosin.
[Graphical view]
PfamiPF00261. Tropomyosin. 1 hit.
[Graphical view]
PRINTSiPR00194. TROPOMYOSIN.
PROSITEiPS00326. TROPOMYOSIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. "Altered tropomyosin expression in essential hypertension."
    Dunn S.A., Mohteshamzadeh M., Daly A.K., Thomas T.H.
    Hypertension 41:347-354(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
    Tissue: Skeletal muscle.
  14. "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.
  15. "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.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "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; 3 AND 6), ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215 (ISOFORMS 2 AND 5), ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125 (ISOFORM 7), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  20. "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.
  21. "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.
  22. "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.
  23. Cited for: VARIANTS CFTD MET-100; CYS-168; GLY-168; GLU-169 AND GLY-245, VARIANT CAPM1 HIS-168.
  24. "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.
  25. Cited for: VARIANT CAPM1 HIS-168.
  26. "Mutations of tropomyosin 3 (TPM3) are common and associated with type 1 myofiber hypotrophy in congenital fiber type disproportion."
    Lawlor M.W., Dechene E.T., Roumm E., Geggel A.S., Moghadaszadeh B., Beggs A.H.
    Hum. Mutat. 31:176-183(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CFTD VAL-4; PRO-91; HIS-168 AND LYS-241.
  27. "Congenital fibre type disproportion associated with mutations in the tropomyosin 3 (TPM3) gene mimicking congenital myasthenia."
    Munot P., Lashley D., Jungbluth H., Feng L., Pitt M., Robb S.A., Palace J., Jayawant S., Kennet R., Beeson D., Cullup T., Abbs S., Laing N., Sewry C., Muntoni F.
    Neuromuscul. Disord. 20:796-800(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CFTD HIS-168 AND ALA-174.
  28. Cited for: VARIANTS NEM1 PHE-88 AND CYS-168, VARIANTS CAPM1 PHE-88; ALA-151; CYS-168 AND ILE-245, VARIANTS CFTD VAL-100; CYS-168 AND HIS-168, VARIANTS CYS-91 AND LYS-253.
  29. Cited for: VARIANT CAPM1 ILE-149.

Entry informationi

Entry nameiTPM3_HUMAN
AccessioniPrimary (citable) accession number: P06753
Secondary accession number(s): D3DV71
, P12324, Q2QD06, Q5VU58, Q5VU63, Q5VU66, Q5VU71, Q5VU72, Q8TCG3, Q969Q2, Q9NQH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: June 26, 2013
Last modified: March 4, 2015
This is version 176 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.