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P09493

- TPM1_HUMAN

UniProt

P09493 - TPM1_HUMAN

Protein

Tropomyosin alpha-1 chain

Gene

TPM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 2 (01 Nov 1990)
      Previous versions | rss
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    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 - Molecular functioni

    1. actin binding Source: BHF-UCL
    2. cytoskeletal protein binding Source: UniProtKB
    3. structural constituent of cytoskeleton Source: BHF-UCL
    4. structural constituent of muscle Source: ProtInc

    GO - Biological processi

    1. cardiac muscle contraction Source: BHF-UCL
    2. cellular component movement Source: UniProtKB
    3. cellular response to reactive oxygen species Source: BHF-UCL
    4. cytoskeleton organization Source: BHF-UCL
    5. in utero embryonic development Source: Ensembl
    6. muscle contraction Source: Reactome
    7. muscle filament sliding Source: BHF-UCL
    8. negative regulation of cell migration Source: BHF-UCL
    9. positive regulation of ATPase activity Source: BHF-UCL
    10. positive regulation of cell adhesion Source: BHF-UCL
    11. positive regulation of heart rate by epinephrine Source: BHF-UCL
    12. positive regulation of stress fiber assembly Source: BHF-UCL
    13. regulation of heart contraction Source: ProtInc
    14. regulation of muscle contraction Source: ProtInc
    15. ruffle organization Source: BHF-UCL
    16. sarcomere organization Source: BHF-UCL
    17. ventricular cardiac muscle tissue morphogenesis Source: BHF-UCL
    18. wound healing Source: BHF-UCL

    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-1 chain
    Alternative name(s):
    Alpha-tropomyosin
    Tropomyosin-1
    Gene namesi
    Name:TPM1
    Synonyms:C15orf13, TMSA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:12010. TPM1.

    Subcellular locationi

    GO - Cellular componenti

    1. bleb Source: BHF-UCL
    2. cytoskeleton Source: UniProtKB
    3. cytosol Source: Reactome
    4. filamentous actin Source: Ensembl
    5. muscle thin filament tropomyosin Source: ProtInc
    6. ruffle membrane Source: BHF-UCL
    7. sarcomere Source: BHF-UCL
    8. stress fiber Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Involvement in diseasei

    Cardiomyopathy, familial hypertrophic 3 (CMH3) [MIM:115196]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti63 – 631A → V in CMH3. 1 Publication
    VAR_013135
    Natural varianti175 – 1751D → N in CMH3. 4 Publications
    Corresponds to variant rs28934270 [ dbSNP | Ensembl ].
    VAR_007601
    Natural varianti180 – 1801E → G in CMH3. 1 Publication
    Corresponds to variant rs28934269 [ dbSNP | Ensembl ].
    VAR_007602
    Natural varianti180 – 1801E → V in CMH3. 1 Publication
    VAR_029452
    Cardiomyopathy, dilated 1Y (CMD1Y) [MIM:611878]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti40 – 401E → K in CMD1Y. 1 Publication
    VAR_043986
    Natural varianti54 – 541E → K in CMD1Y. 1 Publication
    VAR_043987
    Left ventricular non-compaction 9 (LVNC9) [MIM:611878]: A disease due to an arrest of myocardial morphogenesis. It is characterized by a hypertrophic left ventricle with deep trabeculations and with poor systolic function, with or without associated left ventricular dilation. In some cases, it is associated with other congenital heart anomalies.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti192 – 1921E → K in LVNC9. 1 Publication
    VAR_070121
    Natural varianti248 – 2481K → E in LVNC9. 1 Publication
    VAR_070122

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi283 – 2831S → A: Loss of phosphorylation and decreased formation of actin stress fibers. 1 Publication
    Mutagenesisi283 – 2831S → E: Increased formation of actin stress fibers. 1 Publication

    Keywords - Diseasei

    Cardiomyopathy, Disease mutation

    Organism-specific databases

    MIMi115196. phenotype.
    611878. phenotype.
    Orphaneti154. Familial isolated dilated cardiomyopathy.
    155. Familial isolated hypertrophic cardiomyopathy.
    54260. Left ventricular noncompaction.
    PharmGKBiPA36690.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 284284Tropomyosin alpha-1 chainPRO_0000205620Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Cross-linki77 – 77Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei283 – 2831Phosphoserine; by DAPK11 Publication

    Post-translational modificationi

    Phosphorylated at Ser-283 by DAPK1 in response to oxidative stress and this phosphorylation enhances stress fiber formation in endothelial cells.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP09493.
    PaxDbiP09493.
    PRIDEiP09493.

    2D gel databases

    UCD-2DPAGEP09493.

    PTM databases

    PhosphoSiteiP09493.

    Expressioni

    Tissue specificityi

    Detected in primary breast cancer tissues but undetectable in normal breast tissues in Sudanese patients. Isoform 1 is expressed in adult and fetal skeletal muscle and cardiac tissues, with higher expression levels in the cardiac tissues. Isoform 10 is expressed in adult and fetal cardiac tissues, but not in skeletal muscle.2 Publications

    Gene expression databases

    ArrayExpressiP09493.
    BgeeiP09493.
    GenevestigatoriP09493.

    Organism-specific databases

    HPAiCAB017698.
    HPA000261.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta chain. Interacts with HRG (via the HRR domain); the interaction contributes to the antiangiogenic properties of the histidine/proline-rich region (HRR) of HRG.By similarity

    Protein-protein interaction databases

    BioGridi113021. 60 interactions.
    IntActiP09493. 14 interactions.
    MINTiMINT-1458755.

    Structurei

    3D structure databases

    ProteinModelPortaliP09493.
    SMRiP09493. Positions 1-284.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1 – 284284By 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.
    HOGENOMiHOG000231521.
    HOVERGENiHBG107404.
    KOiK10373.
    OMAiRDICNTI.
    OrthoDBiEOG7673C8.
    PhylomeDBiP09493.
    TreeFamiTF351519.

    Family and domain databases

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

    Sequences (10)i

    Sequence statusi: Complete.

    This entry describes 10 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: P09493-1) [UniParc]FASTAAdd to Basket

    Also known as: Skeletal muscle, TPM1alpha

    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

    MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL    50
    KGTEDELDKY SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD 100
    RAQERLATAL QKLEEAEKAA DESERGMKVI ESRAQKDEEK MEIQEIQLKE 150
    AKHIAEDADR KYEEVARKLV IIESDLERAE ERAELSEGKC AELEEELKTV 200
    TNNLKSLEAQ AEKYSQKEDR YEEEIKVLSD KLKEAETRAE FAERSVTKLE 250
    KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI 284
    Length:284
    Mass (Da):32,709
    Last modified:November 1, 1990 - v2
    Checksum:iF57139E2B0972F4D
    GO
    Isoform 2 (identifier: P09493-2) [UniParc]FASTAAdd to Basket

    Also known as: Smooth muscle

    The sequence of this isoform differs from the canonical sequence as follows:
         1-80: MDAIKKKMQM...LELAEKKATD → MCRLRIFLRTASSEHLHERKLRET
         189-212: KCAELEEELKTVTNNLKSLEAQAE → QVRQLEEQLRIMDSDLESINAAED
         258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLSMHQMLDQTLLELNNM

    Note: Incomplete sequence.

    Show »
    Length:228
    Mass (Da):26,680
    Checksum:iA6770D102A359A7B
    GO
    Isoform 3 (identifier: P09493-3) [UniParc]FASTAAdd to Basket

    Also known as: Fibroblast, TM3

    The sequence of this isoform differs from the canonical sequence as follows:
         189-212: KCAELEEELKTVTNNLKSLEAQAE → QVRQLEEQLRIMDQTLKALMAAED
         258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLSMHQMLDQTLLELNNM

    Note: Contains a N6-acetyllysine at position 213.

    Show »
    Length:284
    Mass (Da):32,876
    Checksum:iFDBEEFE342C4ACE3
    GO
    Isoform 4 (identifier: P09493-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         189-212: KCAELEEELKTVTNNLKSLEAQAE → QVRQLEEQLRIMDQTLKALMAAED

    Note: Contains a N6-acetyllysine at position 213.

    Show »
    Length:284
    Mass (Da):32,848
    Checksum:iD29DBCA97BC3C6EE
    GO
    Isoform 5 (identifier: P09493-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-80: MDAIKKKMQM...LELAEKKATD → MAGSSSLEAV...LDHERKLRET
         259-284: ELYAQKLKYKAISEELDHALNDMTSI → QLYQQLEQNRRLTNELKLALNED

    Show »
    Length:245
    Mass (Da):28,385
    Checksum:i1255A14D9F26E29F
    GO
    Isoform 6 (identifier: P09493-6) [UniParc]FASTAAdd to Basket

    Also known as: 10, TPM1kappa

    The sequence of this isoform differs from the canonical sequence as follows:
         41-80: DELVSLQKKL...LELAEKKATD → EDIAAKEKLL...LLAAEEAAAK

    Show »
    Length:284
    Mass (Da):32,649
    Checksum:i1610BB50FB8EB0F5
    GO
    Isoform 7 (identifier: P09493-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         41-80: DELVSLQKKL...LELAEKKATD → EDIAAKEKLL...LLAAEEAAAK
         258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLSMHQMLDQTLLELNNM

    Note: No experimental confirmation available.

    Show »
    Length:284
    Mass (Da):32,678
    Checksum:i3933E81AC289DAF8
    GO
    Isoform 8 (identifier: P09493-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         41-53: DELVSLQKKLKGT → EDIAAKEKLLRVS
         57-80: LDKYSEALKDAQEKLELAEKKATD → RDRVLEELHKAEDSLLAAEEAAAK
         189-192: KCAE → QVRQ
         196-212: ELKTVTNNLKSLEAQAE → QLRIMDQTLKALMAAED
         258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLSMHQMLDQTLLELNNM

    Note: Gene prediction based on EST data. Contains a N6-acetyllysine at position 213.

    Show »
    Length:284
    Mass (Da):32,817
    Checksum:i1EDF6D5109DD335B
    GO
    Isoform 9 (identifier: P09493-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLSMHQMLDQTLLELNNM

    Note: Gene prediction based on EST data.

    Show »
    Length:284
    Mass (Da):32,737
    Checksum:iDA526AA889904540
    GO
    Isoform 10 (identifier: P09493-10) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         189-192: KCAE → QVRQ
         196-212: ELKTVTNNLKSLEAQAE → QLRIMDQTLKALMAAED
         284-284: I → M

    Note: No experimental confirmation available. Contains a N6-acetyllysine at position 213.

    Show »
    Length:284
    Mass (Da):32,866
    Checksum:iD45DBCA97BC3C6EE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti109 – 1091A → V in CAA30930. (PubMed:3138425)Curated
    Sequence conflicti203 – 2031N → D in AAT68294. (PubMed:15249230)Curated
    Sequence conflicti203 – 2031N → D in AAT68295. (PubMed:15249230)Curated

    Mass spectrometryi

    Isoform 3 : Molecular mass is 32875.93 Da from positions 1 - 284. Determined by MALDI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti40 – 401E → K in CMD1Y. 1 Publication
    VAR_043986
    Natural varianti54 – 541E → K in CMD1Y. 1 Publication
    VAR_043987
    Natural varianti63 – 631A → V in CMH3. 1 Publication
    VAR_013135
    Natural varianti175 – 1751D → N in CMH3. 4 Publications
    Corresponds to variant rs28934270 [ dbSNP | Ensembl ].
    VAR_007601
    Natural varianti180 – 1801E → G in CMH3. 1 Publication
    Corresponds to variant rs28934269 [ dbSNP | Ensembl ].
    VAR_007602
    Natural varianti180 – 1801E → V in CMH3. 1 Publication
    VAR_029452
    Natural varianti192 – 1921E → K in LVNC9. 1 Publication
    VAR_070121
    Natural varianti248 – 2481K → E in LVNC9. 1 Publication
    VAR_070122

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8080MDAIK…KKATD → MCRLRIFLRTASSEHLHERK LRET in isoform 2. 1 PublicationVSP_006576Add
    BLAST
    Alternative sequencei1 – 8080MDAIK…KKATD → MAGSSSLEAVRRKIRSLQEQ ADAAEERAGTLQRELDHERK LRET in isoform 5. 1 PublicationVSP_017498Add
    BLAST
    Alternative sequencei41 – 8040DELVS…KKATD → EDIAAKEKLLRVSEDERDRV LEELHKAEDSLLAAEEAAAK in isoform 6 and isoform 7. 2 PublicationsVSP_036064Add
    BLAST
    Alternative sequencei41 – 5313DELVS…KLKGT → EDIAAKEKLLRVS in isoform 8. CuratedVSP_047297Add
    BLAST
    Alternative sequencei57 – 8024LDKYS…KKATD → RDRVLEELHKAEDSLLAAEE AAAK in isoform 8. CuratedVSP_047298Add
    BLAST
    Alternative sequencei189 – 21224KCAEL…EAQAE → QVRQLEEQLRIMDSDLESIN AAED in isoform 2. 1 PublicationVSP_006578Add
    BLAST
    Alternative sequencei189 – 21224KCAEL…EAQAE → QVRQLEEQLRIMDQTLKALM AAED in isoform 3 and isoform 4. 3 PublicationsVSP_006577Add
    BLAST
    Alternative sequencei189 – 1924KCAE → QVRQ in isoform 8 and isoform 10. CuratedVSP_047299
    Alternative sequencei196 – 21217ELKTV…EAQAE → QLRIMDQTLKALMAAED in isoform 8 and isoform 10. CuratedVSP_047300Add
    BLAST
    Alternative sequencei258 – 28427DELYA…DMTSI → EKVAHAKEENLSMHQMLDQT LLELNNM in isoform 2, isoform 3, isoform 7, isoform 8 and isoform 9. 4 PublicationsVSP_006579Add
    BLAST
    Alternative sequencei259 – 28426ELYAQ…DMTSI → QLYQQLEQNRRLTNELKLAL NED in isoform 5. 1 PublicationVSP_017499Add
    BLAST
    Alternative sequencei284 – 2841I → M in isoform 10. CuratedVSP_047301

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19267 mRNA. Translation: AAA36771.1.
    M19713 mRNA. Translation: AAA61225.1.
    M19714 mRNA. Translation: AAA61226.1.
    M19715 mRNA. Translation: AAA61227.1.
    AY640414 mRNA. Translation: AAT68294.1.
    AY640415 mRNA. Translation: AAT68295.1.
    AK299387 mRNA. Translation: BAH13023.1.
    AL050179 mRNA. Translation: CAB43309.2.
    GU324929 Genomic DNA. Translation: ADL14500.1.
    GU324930 Genomic DNA. Translation: ADL14501.1.
    GU324933 Genomic DNA. Translation: ADL14504.1.
    GU324935 Genomic DNA. Translation: ADL14506.1.
    AC079328 Genomic DNA. No translation available.
    CH471082 Genomic DNA. Translation: EAW77619.1.
    CH471082 Genomic DNA. Translation: EAW77622.1.
    CH471082 Genomic DNA. Translation: EAW77623.1.
    CH471082 Genomic DNA. Translation: EAW77627.1.
    CH471082 Genomic DNA. Translation: EAW77628.1.
    BC007433 mRNA. Translation: AAH07433.1.
    BC050473 mRNA. Translation: AAH50473.1.
    BC053545 mRNA. Translation: AAH53545.1.
    X12369 mRNA. Translation: CAA30930.1.
    CCDSiCCDS10181.1. [P09493-10]
    CCDS32262.1. [P09493-7]
    CCDS32263.1. [P09493-3]
    CCDS32264.1. [P09493-5]
    CCDS45273.1. [P09493-1]
    CCDS58368.1. [P09493-8]
    CCDS58369.1. [P09493-9]
    PIRiA27674.
    A27678. A25825.
    S05585.
    RefSeqiNP_000357.3. NM_000366.5. [P09493-10]
    NP_001018004.1. NM_001018004.1. [P09493-9]
    NP_001018005.1. NM_001018005.1. [P09493-1]
    NP_001018006.1. NM_001018006.1. [P09493-3]
    NP_001018007.1. NM_001018007.1. [P09493-7]
    NP_001018008.1. NM_001018008.1. [P09493-5]
    NP_001018020.1. NM_001018020.1. [P09493-8]
    XP_005254700.1. XM_005254643.1. [P09493-6]
    XP_006720730.1. XM_006720667.1. [P09493-4]
    XP_006720731.1. XM_006720668.1. [P09493-10]
    UniGeneiHs.133892.
    Hs.602995.

    Genome annotation databases

    EnsembliENST00000267996; ENSP00000267996; ENSG00000140416. [P09493-7]
    ENST00000288398; ENSP00000288398; ENSG00000140416. [P09493-10]
    ENST00000334895; ENSP00000334624; ENSG00000140416. [P09493-5]
    ENST00000358278; ENSP00000351022; ENSG00000140416. [P09493-3]
    ENST00000403994; ENSP00000385107; ENSG00000140416. [P09493-1]
    ENST00000559397; ENSP00000452879; ENSG00000140416. [P09493-8]
    ENST00000559556; ENSP00000453941; ENSG00000140416. [P09493-9]
    GeneIDi7168.
    KEGGihsa:7168.
    UCSCiuc002alg.3. human. [P09493-1]
    uc002alh.3. human.
    uc002ali.3. human.
    uc002alj.3. human. [P09493-7]
    uc002all.3. human.
    uc010uie.2. human. [P09493-6]

    Polymorphism databases

    DMDMi136092.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19267 mRNA. Translation: AAA36771.1 .
    M19713 mRNA. Translation: AAA61225.1 .
    M19714 mRNA. Translation: AAA61226.1 .
    M19715 mRNA. Translation: AAA61227.1 .
    AY640414 mRNA. Translation: AAT68294.1 .
    AY640415 mRNA. Translation: AAT68295.1 .
    AK299387 mRNA. Translation: BAH13023.1 .
    AL050179 mRNA. Translation: CAB43309.2 .
    GU324929 Genomic DNA. Translation: ADL14500.1 .
    GU324930 Genomic DNA. Translation: ADL14501.1 .
    GU324933 Genomic DNA. Translation: ADL14504.1 .
    GU324935 Genomic DNA. Translation: ADL14506.1 .
    AC079328 Genomic DNA. No translation available.
    CH471082 Genomic DNA. Translation: EAW77619.1 .
    CH471082 Genomic DNA. Translation: EAW77622.1 .
    CH471082 Genomic DNA. Translation: EAW77623.1 .
    CH471082 Genomic DNA. Translation: EAW77627.1 .
    CH471082 Genomic DNA. Translation: EAW77628.1 .
    BC007433 mRNA. Translation: AAH07433.1 .
    BC050473 mRNA. Translation: AAH50473.1 .
    BC053545 mRNA. Translation: AAH53545.1 .
    X12369 mRNA. Translation: CAA30930.1 .
    CCDSi CCDS10181.1. [P09493-10 ]
    CCDS32262.1. [P09493-7 ]
    CCDS32263.1. [P09493-3 ]
    CCDS32264.1. [P09493-5 ]
    CCDS45273.1. [P09493-1 ]
    CCDS58368.1. [P09493-8 ]
    CCDS58369.1. [P09493-9 ]
    PIRi A27674.
    A27678. A25825.
    S05585.
    RefSeqi NP_000357.3. NM_000366.5. [P09493-10 ]
    NP_001018004.1. NM_001018004.1. [P09493-9 ]
    NP_001018005.1. NM_001018005.1. [P09493-1 ]
    NP_001018006.1. NM_001018006.1. [P09493-3 ]
    NP_001018007.1. NM_001018007.1. [P09493-7 ]
    NP_001018008.1. NM_001018008.1. [P09493-5 ]
    NP_001018020.1. NM_001018020.1. [P09493-8 ]
    XP_005254700.1. XM_005254643.1. [P09493-6 ]
    XP_006720730.1. XM_006720667.1. [P09493-4 ]
    XP_006720731.1. XM_006720668.1. [P09493-10 ]
    UniGenei Hs.133892.
    Hs.602995.

    3D structure databases

    ProteinModelPortali P09493.
    SMRi P09493. Positions 1-284.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113021. 60 interactions.
    IntActi P09493. 14 interactions.
    MINTi MINT-1458755.

    PTM databases

    PhosphoSitei P09493.

    Polymorphism databases

    DMDMi 136092.

    2D gel databases

    UCD-2DPAGE P09493.

    Proteomic databases

    MaxQBi P09493.
    PaxDbi P09493.
    PRIDEi P09493.

    Protocols and materials databases

    DNASUi 7168.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000267996 ; ENSP00000267996 ; ENSG00000140416 . [P09493-7 ]
    ENST00000288398 ; ENSP00000288398 ; ENSG00000140416 . [P09493-10 ]
    ENST00000334895 ; ENSP00000334624 ; ENSG00000140416 . [P09493-5 ]
    ENST00000358278 ; ENSP00000351022 ; ENSG00000140416 . [P09493-3 ]
    ENST00000403994 ; ENSP00000385107 ; ENSG00000140416 . [P09493-1 ]
    ENST00000559397 ; ENSP00000452879 ; ENSG00000140416 . [P09493-8 ]
    ENST00000559556 ; ENSP00000453941 ; ENSG00000140416 . [P09493-9 ]
    GeneIDi 7168.
    KEGGi hsa:7168.
    UCSCi uc002alg.3. human. [P09493-1 ]
    uc002alh.3. human.
    uc002ali.3. human.
    uc002alj.3. human. [P09493-7 ]
    uc002all.3. human.
    uc010uie.2. human. [P09493-6 ]

    Organism-specific databases

    CTDi 7168.
    GeneCardsi GC15P063334.
    GeneReviewsi TPM1.
    HGNCi HGNC:12010. TPM1.
    HPAi CAB017698.
    HPA000261.
    MIMi 115196. phenotype.
    191010. gene.
    611878. phenotype.
    neXtProti NX_P09493.
    Orphaneti 154. Familial isolated dilated cardiomyopathy.
    155. Familial isolated hypertrophic cardiomyopathy.
    54260. Left ventricular noncompaction.
    PharmGKBi PA36690.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG304012.
    HOGENOMi HOG000231521.
    HOVERGENi HBG107404.
    KOi K10373.
    OMAi RDICNTI.
    OrthoDBi EOG7673C8.
    PhylomeDBi P09493.
    TreeFami TF351519.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi TPM1. human.
    GeneWikii TPM1.
    GenomeRNAii 7168.
    NextBioi 28070.
    PROi P09493.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09493.
    Bgeei P09493.
    Genevestigatori P09493.

    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. "Relation of streptococcal M protein with human and rabbit tropomyosin: the complete amino acid sequence of human cardiac alpha tropomyosin, a highly conserved contractile protein."
      Mische S.M., Manjula B.N., Fischetti V.A.
      Biochem. Biophys. Res. Commun. 142:813-818(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE (ISOFORM 1), ACETYLATION AT MET-1.
    2. "Cloning and characterization of a cDNA encoding transformation-sensitive tropomyosin isoform 3 from tumorigenic human fibroblasts."
      Lin C.-S., Leavitt J.
      Mol. Cell. Biol. 8:160-168(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Fibroblast.
    3. "Human hTM alpha gene: expression in muscle and nonmuscle tissue."
      McLeod A.R., Gooding C.
      Mol. Cell. Biol. 8:433-440(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
    4. "Expression of a novel cardiac-specific tropomyosin isoform in humans."
      Denz C.R., Narshi A., Zajdel R.W., Dube D.K.
      Biochem. Biophys. Res. Commun. 320:1291-1297(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 6), TISSUE SPECIFICITY.
      Tissue: Heart.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Tongue.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
      Tissue: Uterus.
    7. NHLBI resequencing and genotyping service (RS&G)
      Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    8. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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 4 AND 5).
      Tissue: Brain, Hippocampus and Placenta.
    11. "Evolution of tropomyosin functional domains: differential splicing and genomic constraints."
      Colote S., Widada J.S., Ferraz C., Bonhomme F., Marti J., Liautard J.-P.
      J. Mol. Evol. 27:228-235(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 58-284 (ISOFORM 2).
      Tissue: Liver.
    12. "Autoimmunity to cytoskeletal protein tropomyosin. A clue to the pathogenetic mechanism for ulcerative colitis."
      Das K.M., Dasgupta A., Mandal A., Geng X.
      J. Immunol. 150:2487-2493(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 134-149 AND 153-167.
      Tissue: Colon.
    13. "Cluster analysis of an extensive human breast cancer cell line protein expression map database."
      Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.
      Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY.
      Tissue: Mammary cancer.
    14. "DAP kinase mediates the phosphorylation of tropomyosin-1 downstream of the ERK pathway, which regulates the formation of stress fibers in response to oxidative stress."
      Houle F., Poirier A., Dumaresq J., Huot J.
      J. Cell Sci. 120:3666-3677(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-283, MUTAGENESIS OF SER-283.
    15. Ahamed M.E.
      Submitted (APR-2007) to UniProtKB
      Cited for: TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
    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-213 (ISOFORMS 10; 3; 4 AND 8), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Alpha-tropomyosin and cardiac troponin T mutations cause familial hypertrophic cardiomyopathy: a disease of the sarcomere."
      Thierfelder L., Watkins H., Macrae C., Lamas R., McKenna W.J., Vosberg H.-P., Seidman J.G., Seidman C.E.
      Cell 77:701-712(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CMH3 ASN-175 AND GLY-180.
    20. "Novel missense mutation in alpha-tropomyosin gene found in Japanese patients with hypertrophic cardiomyopathy."
      Nakajima-Taniguchi C., Matsui H., Nagata S., Kishimoto T., Yamauchi-Takihara K.
      J. Mol. Cell. Cardiol. 27:2053-2058(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CMH3 VAL-63 AND ASN-175.
    21. "Mutations in the genes for cardiac troponin T and alpha-tropomyosin in hypertrophic cardiomyopathy."
      Watkins H., McKenna W.J., Thierfelder L., Suk H.J., Anan R., O'Donoghue A., Spirito P., Matsumori A., Moravec C.S., Seidman J.G., Seidman C.E.
      N. Engl. J. Med. 332:1058-1064(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CMH3 ASN-175.
    22. "The cardiac beta-myosin heavy chain gene is not the predominant gene for hypertrophic cardiomyopathy in the Finnish population."
      Jaeaeskelaeinen P., Soranta M., Miettinen R., Saarinen L., Pihlajamaeki J., Silvennoinen K., Tikanoja T., Laakso M., Kuusisto J.
      J. Am. Coll. Cardiol. 32:1709-1716(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CMH3 ASN-175.
    23. "Mutations that alter the surface charge of alpha-tropomyosin are associated with dilated cardiomyopathy."
      Olson T.M., Kishimoto N.Y., Whitby F.G., Michels V.V.
      J. Mol. Cell. Cardiol. 33:723-732(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CMD1Y LYS-40 AND LYS-54.
    24. "Mutation spectrum in a large cohort of unrelated consecutive patients with hypertrophic cardiomyopathy."
      Erdmann J., Daehmlow S., Wischke S., Senyuva M., Werner U., Raible J., Tanis N., Dyachenko S., Hummel M., Hetzer R., Regitz-Zagrosek V.
      Clin. Genet. 64:339-349(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CMH3 VAL-180.
    25. "Sarcomere gene mutations in isolated left ventricular noncompaction cardiomyopathy do not predict clinical phenotype."
      Probst S., Oechslin E., Schuler P., Greutmann M., Boye P., Knirsch W., Berger F., Thierfelder L., Jenni R., Klaassen S.
      Circ. Cardiovasc. Genet. 4:367-374(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS LVNC9 LYS-192 AND GLU-248.

    Entry informationi

    Entry nameiTPM1_HUMAN
    AccessioniPrimary (citable) accession number: P09493
    Secondary accession number(s): B7Z5T7
    , D9YZV2, D9YZV3, D9YZV8, P09494, P10469, Q6DV89, Q6DV90, Q7Z6L8, Q86W64, Q96IK2, Q9UCI1, Q9UCI2, Q9UCY9, Q9Y427
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 160 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 15
      Human chromosome 15: 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