Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P06753

- TPM3_HUMAN

UniProt

P06753 - TPM3_HUMAN

Protein

Tropomyosin alpha-3 chain

Gene

TPM3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 172 (01 Oct 2014)
      Sequence version 2 (26 Jun 2013)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. cellular component movement Source: UniProtKB
    2. muscle contraction Source: Reactome
    3. muscle filament sliding Source: Reactome

    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: UniProt
    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

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Involvement in diseasei

    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti9 – 91M → R in NEM1; decrease in the sensitivity of contraction to activating calcium. 1 Publication
    VAR_013460
    Natural varianti168 – 1681R → H in NEM1 and CAPM1. 3 Publications
    VAR_070069
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti100 – 1001L → M in CFTD. 1 Publication
    VAR_070066
    Natural varianti168 – 1681R → C in CFTD and CAPM1. 2 Publications
    VAR_070067
    Natural varianti168 – 1681R → G in CFTD. 1 Publication
    VAR_070068
    Natural varianti169 – 1691K → E in CFTD. 1 Publication
    VAR_070070
    Natural varianti245 – 2451R → G in CFTD. 1 Publication
    VAR_070071
    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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti168 – 1681R → C in CFTD and CAPM1. 2 Publications
    VAR_070067
    Natural varianti168 – 1681R → H in NEM1 and CAPM1. 3 Publications
    VAR_070069

    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
    Chaini1 – 285285Tropomyosin alpha-3 chainPRO_0000205632Add
    BLAST

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP06753.
    PaxDbiP06753.
    PRIDEiP06753.

    2D gel databases

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

    PTM databases

    PhosphoSiteiP06753.

    Expressioni

    Gene expression databases

    ArrayExpressiP06753.
    BgeeiP06753.
    CleanExiHS_TPM3.
    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. 46 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.
    HOGENOMiHOG000231522.
    HOVERGENiHBG107404.
    InParanoidiP06753.
    KOiK09290.
    OMAiNIPKCED.
    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.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    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

    MMEAIKKKMQ MLKLDKENAL DRAEQAEAEQ KQAEERSKQL EDELAAMQKK    50
    LKGTEDELDK YSEALKDAQE KLELAEKKAA DAEAEVASLN RRIQLVEEEL 100
    DRAQERLATA LQKLEEAEKA ADESERGMKV IENRALKDEE KMELQEIQLK 150
    EAKHIAEEAD RKYEEVARKL VIIEGDLERT EERAELAESK CSELEEELKN 200
    VTNNLKSLEA QAEKYSQKED KYEEEIKILT DKLKEAETRA EFAERSVAKL 250
    EKTIDDLEDE LYAQKLKYKA ISEELDHALN DMTSI 285
    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.Curated 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.Curated

    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.

    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.

    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.

    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.

    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)Curated
    Sequence conflicti43 – 431E → K in ABC40673. (PubMed:16201836)Curated
    Sequence conflicti66 – 661A → P in ABC40673. (PubMed:16201836)Curated
    Sequence conflicti85 – 851D → G in ABC40673. (PubMed:16201836)Curated
    Sequence conflicti110 – 1101I → L in ABC40673. (PubMed:16201836)Curated
    Sequence conflicti135 – 1351I → T in ABC40673. (PubMed:16201836)Curated
    Sequence conflicti150 – 1501A → T in ABC40673. (PubMed:16201836)Curated
    Sequence conflicti192 – 1921L → F in ABC40673. (PubMed:16201836)Curated
    Sequence conflicti196 – 1961L → P in ABC40673. (PubMed:16201836)Curated
    Sequence conflicti202 – 2021R → C in ABC40673. (PubMed:16201836)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti9 – 91M → R in NEM1; decrease in the sensitivity of contraction to activating calcium. 1 Publication
    VAR_013460
    Natural varianti100 – 1001L → M in CFTD. 1 Publication
    VAR_070066
    Natural varianti168 – 1681R → C in CFTD and CAPM1. 2 Publications
    VAR_070067
    Natural varianti168 – 1681R → G in CFTD. 1 Publication
    VAR_070068
    Natural varianti168 – 1681R → H in NEM1 and CAPM1. 3 Publications
    VAR_070069
    Natural varianti169 – 1691K → E in CFTD. 1 Publication
    VAR_070070
    Natural varianti245 – 2451R → G in CFTD. 1 Publication
    VAR_070071

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS1060.1. [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 ]
    PIRi A25530.
    S06210. A24199.
    RefSeqi NP_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 ]
    UniGenei Hs.535581.
    Hs.578978.
    Hs.644306.
    Hs.654421.

    3D structure databases

    ProteinModelPortali P06753.
    SMRi P06753. Positions 9-285.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113023. 46 interactions.
    IntActi P06753. 14 interactions.
    MINTi MINT-1142638.
    STRINGi 9606.ENSP00000357513.

    PTM databases

    PhosphoSitei P06753.

    Polymorphism databases

    DMDMi 519668659.

    2D gel databases

    DOSAC-COBS-2DPAGE P06753.
    SWISS-2DPAGE P06753.

    Proteomic databases

    MaxQBi P06753.
    PaxDbi P06753.
    PRIDEi P06753.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000302206 ; 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 ]
    GeneIDi 7170.
    KEGGi hsa:7170.
    UCSCi uc001fdz.1. human.
    uc001fea.1. human. [P06753-2 ]
    uc001feb.1. human. [P06753-3 ]
    uc001fec.2. human. [P06753-1 ]
    uc001fed.2. human.

    Organism-specific databases

    CTDi 7170.
    GeneCardsi GC01M154127.
    GeneReviewsi TPM3.
    HGNCi HGNC:12012. TPM3.
    HPAi HPA000261.
    HPA009066.
    MIMi 164970. gene.
    188550. phenotype.
    191030. gene.
    255310. phenotype.
    609284. phenotype.
    neXtProti NX_P06753.
    Orphaneti 171881. Cap myopathy.
    171439. Childhood-onset nemaline myopathy.
    2020. Congenital fiber-type disproportion myopathy.
    178342. Inflammatory myofibroblastic tumor.
    171433. Intermediate nemaline myopathy.
    PharmGKBi PA36692.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG304012.
    HOGENOMi HOG000231522.
    HOVERGENi HBG107404.
    InParanoidi P06753.
    KOi K09290.
    OMAi NIPKCED.
    OrthoDBi EOG7673C8.
    PhylomeDBi P06753.
    TreeFami TF351519.

    Enzyme and pathway databases

    Reactomei REACT_16969. Striated Muscle Contraction.
    REACT_20558. Smooth Muscle Contraction.

    Miscellaneous databases

    ChiTaRSi TPM3. human.
    GeneWikii Tropomyosin_3.
    GenomeRNAii 7170.
    NextBioi 28092.
    PROi P06753.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P06753.
    Bgeei P06753.
    CleanExi HS_TPM3.
    Genevestigatori P06753.

    Family and domain databases

    InterProi IPR000533. Tropomyosin.
    [Graphical view ]
    Pfami PF00261. Tropomyosin. 1 hit.
    [Graphical view ]
    PRINTSi PR00194. TROPOMYOSIN.
    PROSITEi PS00326. TROPOMYOSIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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 AND 3), ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215 (ISOFORMS 2 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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.
    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. 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. Cited for: VARIANT CAPM1 HIS-168.

    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: October 1, 2014
    This is version 172 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