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P07951

- TPM2_HUMAN

UniProt

P07951 - TPM2_HUMAN

Protein

Tropomyosin beta chain

Gene

TPM2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      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. The non-muscle isoform may have a role in agonist-mediated receptor internalization By similarity.By similarity

    GO - Molecular functioni

    1. actin binding Source: UniProtKB
    2. structural constituent of muscle Source: ProtInc

    GO - Biological processi

    1. muscle contraction Source: Reactome
    2. muscle filament sliding Source: Reactome
    3. regulation of ATPase activity Source: UniProtKB

    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 beta chain
    Alternative name(s):
    Beta-tropomyosin
    Tropomyosin-2
    Gene namesi
    Name:TPM2
    Synonyms:TMSB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:12011. TPM2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. muscle thin filament tropomyosin Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Involvement in diseasei

    Nemaline myopathy 4 (NEM4) [MIM:609285]: A form of nemaline myopathy. Nemaline myopathies are muscular disorders characterized by muscle weakness of varying severity and onset, and abnormal thread-like or rod-shaped structures in muscle fibers on histologic examination. Nemaline myopathy type 4 presents from infancy to childhood with hypotonia and moderate-to-severe proximal weakness with minimal or no progression. Major motor milestones are delayed but independent ambulation is usually achieved, although a wheelchair may be needed in later life.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti41 – 411E → K in NEM4. 1 Publication
    VAR_070978
    Natural varianti117 – 1171E → A in NEM4. 1 Publication
    VAR_013468
    Natural varianti147 – 1471Q → P in NEM4. 1 Publication
    VAR_013469
    Arthrogryposis, distal, 1A (DA1A) [MIM:108120]: A form of distal arthrogryposis, a disease characterized by congenital joint contractures that mainly involve two or more distal parts of the limbs, in the absence of a primary neurological or muscle disease. Distal arthrogryposis type 1 is characterized largely by camptodactyly and clubfoot. Hypoplasia and/or absence of some interphalangeal creases is common. The shoulders and hips are less frequently affected.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti91 – 911R → G in DA1A. 1 Publication
    VAR_016086
    Cap myopathy 2 (CAPM2) [MIM:609285]: A rare congenital skeletal muscle disorder characterized by the presence of cap-like structures which are well demarcated and peripherally located under the sarcolemma and show abnormal accumulation of sarcomeric proteins. Clinical features are early onset of hypotonia and non-progressive or slowly progressive muscle weakness. Respiratory problems are common.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti49 – 491Missing in CAPM2. 1 Publication
    VAR_070979
    Natural varianti52 – 521G → GG in CAPM2. 1 Publication
    VAR_070980
    Natural varianti139 – 1391Missing in CAPM2. 2 Publications
    VAR_070982
    Natural varianti202 – 2021N → K in CAPM2. 1 Publication
    VAR_070983
    Arthrogryposis, distal, 2B (DA2B) [MIM:601680]: A form of distal arthrogryposis, a disease characterized by congenital joint contractures that mainly involve two or more distal parts of the limbs, in the absence of a primary neurological or muscle disease. DA2B is characterized by contractures of the hands and feet, and a distinctive face characterized by prominent nasolabial folds, small mouth and downslanting palpebral fissures.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti133 – 1331R → W in DA2B. 1 Publication
    VAR_070981

    Keywords - Diseasei

    Disease mutation, Nemaline myopathy

    Organism-specific databases

    MIMi108120. phenotype.
    601680. phenotype.
    609285. phenotype.
    Orphaneti171881. Cap myopathy.
    171439. Childhood-onset nemaline myopathy.
    2020. Congenital fiber-type disproportion myopathy.
    1146. Digitotalar dysmorphism.
    1147. Sheldon-Hall syndrome.
    3377. Trismus - pseudocamptodactyly.
    171436. Typical nemaline myopathy.
    PharmGKBiPA36691.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 284284Tropomyosin beta chainPRO_0000205627Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei61 – 611Phosphoserine; by PIK3CGBy similarity

    Post-translational modificationi

    Phosphorylated on Ser-61 by PIK3CG. Phosphorylation on Ser-61 is required for ADRB2 internalization By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP07951.
    PaxDbiP07951.
    PRIDEiP07951.

    2D gel databases

    DOSAC-COBS-2DPAGEP07951.
    REPRODUCTION-2DPAGEIPI00220709.
    UCD-2DPAGEP07951.

    PTM databases

    PhosphoSiteiP07951.

    Expressioni

    Tissue specificityi

    Present in primary breast cancer tissue, absent from normal breast tissue.1 Publication

    Gene expression databases

    ArrayExpressiP07951.
    BgeeiP07951.
    CleanExiHS_TPM2.
    GenevestigatoriP07951.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta chain.

    Protein-protein interaction databases

    BioGridi113022. 31 interactions.
    IntActiP07951. 10 interactions.
    MINTiMINT-94363.
    STRINGi9606.ENSP00000354219.

    Structurei

    3D structure databases

    ProteinModelPortaliP07951.
    SMRiP07951. 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.
    HOVERGENiHBG107404.
    KOiK10374.
    OMAiTEPTHEC.
    PhylomeDBiP07951.
    TreeFamiTF351519.

    Family and domain databases

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

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P07951-1) [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

    MDAIKKKMQM LKLDKENAID RAEQAEADKK QAEDRCKQLE EEQQALQKKL    50
    KGTEDEVEKY SESVKEAQEK LEQAEKKATD AEADVASLNR RIQLVEEELD 100
    RAQERLATAL QKLEEAEKAA DESERGMKVI ENRAMKDEEK MELQEMQLKE 150
    AKHIAEDSDR KYEEVARKLV ILEGELERSE ERAEVAESKC GDLEEELKIV 200
    TNNLKSLEAQ ADKYSTKEDK YEEEIKLLEE KLKEAETRAE FAERSVAKLE 250
    KTIDDLEDEV YAQKMKYKAI SEELDNALND ITSL 284
    Length:284
    Mass (Da):32,851
    Last modified:August 1, 1988 - v1
    Checksum:i18E330568E14E0BE
    GO
    Isoform 2 (identifier: P07951-2) [UniParc]FASTAAdd to Basket

    Also known as: non-muscle, Fibroblast TM36, Epithelial TMe1

    The sequence of this isoform differs from the canonical sequence as follows:
         189-213: KCGDLEEELKIVTNNLKSLEAQADK → RARQLEEELRTMDQALKSLMASEEE
         258-284: DEVYAQKMKYKAISEELDNALNDITSL → ETLASAKEENVEIHQTLDQTLLELNNL

    Show »
    Length:284
    Mass (Da):32,990
    Checksum:i584D60A8A4D6E9CA
    GO
    Isoform 3 (identifier: P07951-3) [UniParc]FASTAAdd to Basket

    Also known as: non-muscle

    The sequence of this isoform differs from the canonical sequence as follows:
         1-80: MDAIKKKMQM...LEQAEKKATD → MAGISSIDAV...ADAERQARER
         189-213: KCGDLEEELKIVTNNLKSLEAQADK → RARQLEEELRTMDQALKSLMASEEE
         258-284: DEVYAQKMKYKAISEELDNALNDITSL → ETLASAKEENVEIHQTLDQTLLELNNL

    Show »
    Length:248
    Mass (Da):28,684
    Checksum:iD89A89A37CF9D026
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti89 – 891N → S in BAD96978. 1 PublicationCurated

    Mass spectrometryi

    Isoform 1 : Molecular mass is 32850.73 Da from positions 1 - 284. Determined by MALDI. 1 Publication
    Isoform 2 : Molecular mass is 32989.81 Da from positions 1 - 284. Determined by MALDI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti41 – 411E → K in NEM4. 1 Publication
    VAR_070978
    Natural varianti49 – 491Missing in CAPM2. 1 Publication
    VAR_070979
    Natural varianti52 – 521G → GG in CAPM2. 1 Publication
    VAR_070980
    Natural varianti91 – 911R → G in DA1A. 1 Publication
    VAR_016086
    Natural varianti117 – 1171E → A in NEM4. 1 Publication
    VAR_013468
    Natural varianti133 – 1331R → W in DA2B. 1 Publication
    VAR_070981
    Natural varianti139 – 1391Missing in CAPM2. 2 Publications
    VAR_070982
    Natural varianti147 – 1471Q → P in NEM4. 1 Publication
    VAR_013469
    Natural varianti202 – 2021N → K in CAPM2. 1 Publication
    VAR_070983
    Natural varianti273 – 2731E → K.
    Corresponds to variant rs3180843 [ dbSNP | Ensembl ].
    VAR_052402

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8080MDAIK…KKATD → MAGISSIDAVKKKIQSLQQV ADEAEERAEHLQREADAERQ ARER in isoform 3. CuratedVSP_006594Add
    BLAST
    Alternative sequencei189 – 21325KCGDL…AQADK → RARQLEEELRTMDQALKSLM ASEEE in isoform 2 and isoform 3. 4 PublicationsVSP_006595Add
    BLAST
    Alternative sequencei258 – 28427DEVYA…DITSL → ETLASAKEENVEIHQTLDQT LLELNNL in isoform 2 and isoform 3. 4 PublicationsVSP_006596Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12126 mRNA. Translation: AAA61229.1.
    M12125 mRNA. Translation: AAA36773.1.
    X06825 mRNA. Translation: CAA29971.1.
    M75165 mRNA. Translation: AAB59509.1.
    M74817 mRNA. Translation: AAA61230.1.
    AK223258 mRNA. Translation: BAD96978.1.
    AL133410 Genomic DNA. Translation: CAI10974.1.
    AL133410 Genomic DNA. Translation: CAI10977.1.
    CH471071 Genomic DNA. Translation: EAW58354.1.
    BC011776 mRNA. Translation: AAH11776.1.
    AF209746 Genomic DNA. Translation: AAF17621.1.
    J05247 Genomic DNA. Translation: AAA51842.1.
    CCDSiCCDS6586.1. [P07951-2]
    CCDS6587.1. [P07951-1]
    PIRiA23562.
    S00922.
    RefSeqiNP_003280.2. NM_003289.3. [P07951-1]
    NP_998839.1. NM_213674.1. [P07951-2]
    XP_005251625.1. XM_005251568.1. [P07951-1]
    UniGeneiHs.300772.

    Genome annotation databases

    EnsembliENST00000360958; ENSP00000354219; ENSG00000198467. [P07951-1]
    ENST00000378292; ENSP00000367542; ENSG00000198467. [P07951-2]
    GeneIDi7169.
    KEGGihsa:7169.
    UCSCiuc003zxq.3. human. [P07951-2]
    uc003zxs.3. human. [P07951-1]

    Polymorphism databases

    DMDMi136090.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12126 mRNA. Translation: AAA61229.1 .
    M12125 mRNA. Translation: AAA36773.1 .
    X06825 mRNA. Translation: CAA29971.1 .
    M75165 mRNA. Translation: AAB59509.1 .
    M74817 mRNA. Translation: AAA61230.1 .
    AK223258 mRNA. Translation: BAD96978.1 .
    AL133410 Genomic DNA. Translation: CAI10974.1 .
    AL133410 Genomic DNA. Translation: CAI10977.1 .
    CH471071 Genomic DNA. Translation: EAW58354.1 .
    BC011776 mRNA. Translation: AAH11776.1 .
    AF209746 Genomic DNA. Translation: AAF17621.1 .
    J05247 Genomic DNA. Translation: AAA51842.1 .
    CCDSi CCDS6586.1. [P07951-2 ]
    CCDS6587.1. [P07951-1 ]
    PIRi A23562.
    S00922.
    RefSeqi NP_003280.2. NM_003289.3. [P07951-1 ]
    NP_998839.1. NM_213674.1. [P07951-2 ]
    XP_005251625.1. XM_005251568.1. [P07951-1 ]
    UniGenei Hs.300772.

    3D structure databases

    ProteinModelPortali P07951.
    SMRi P07951. Positions 1-284.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113022. 31 interactions.
    IntActi P07951. 10 interactions.
    MINTi MINT-94363.
    STRINGi 9606.ENSP00000354219.

    PTM databases

    PhosphoSitei P07951.

    Polymorphism databases

    DMDMi 136090.

    2D gel databases

    DOSAC-COBS-2DPAGE P07951.
    REPRODUCTION-2DPAGE IPI00220709.
    UCD-2DPAGE P07951.

    Proteomic databases

    MaxQBi P07951.
    PaxDbi P07951.
    PRIDEi P07951.

    Protocols and materials databases

    DNASUi 7169.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360958 ; ENSP00000354219 ; ENSG00000198467 . [P07951-1 ]
    ENST00000378292 ; ENSP00000367542 ; ENSG00000198467 . [P07951-2 ]
    GeneIDi 7169.
    KEGGi hsa:7169.
    UCSCi uc003zxq.3. human. [P07951-2 ]
    uc003zxs.3. human. [P07951-1 ]

    Organism-specific databases

    CTDi 7169.
    GeneCardsi GC09M035672.
    GeneReviewsi TPM2.
    HGNCi HGNC:12011. TPM2.
    MIMi 108120. phenotype.
    190990. gene.
    601680. phenotype.
    609285. phenotype.
    neXtProti NX_P07951.
    Orphaneti 171881. Cap myopathy.
    171439. Childhood-onset nemaline myopathy.
    2020. Congenital fiber-type disproportion myopathy.
    1146. Digitotalar dysmorphism.
    1147. Sheldon-Hall syndrome.
    3377. Trismus - pseudocamptodactyly.
    171436. Typical nemaline myopathy.
    PharmGKBi PA36691.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG304012.
    HOVERGENi HBG107404.
    KOi K10374.
    OMAi TEPTHEC.
    PhylomeDBi P07951.
    TreeFami TF351519.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi TPM2. human.
    GeneWikii TPM2.
    GenomeRNAii 7169.
    NextBioi 28086.
    PROi P07951.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07951.
    Bgeei P07951.
    CleanExi HS_TPM2.
    Genevestigatori P07951.

    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. "A muscle-type tropomyosin in human fibroblasts: evidence for expression by an alternative RNA splicing mechanism."
      MacLeod A.R., Houlker C., Reinach F.C., Smillie L.B., Talbot K., Modi G., Walsh F.S.
      Proc. Natl. Acad. Sci. U.S.A. 82:7835-7839(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Fibroblast.
    2. "Complete nucleotide sequence of the adult skeletal isoform of human skeletal muscle beta-tropomyosin."
      Widada J.S., Ferraz C., Capony J.-P., Liautard J.-P.
      Nucleic Acids Res. 16:3109-3109(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "A cDNA encoding a muscle-type tropomyosin cloned from a human epithelial cell line: identity with human fibroblast tropomyosin TM1."
      Prasad G.L., Meissner S., Sheer D.G., Cooper H.L.
      Biochem. Biophys. Res. Commun. 177:1068-1075(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Colon epithelium.
    4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Gastric mucosa.
    5. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [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] (ISOFORM 2).
      Tissue: Pancreas.
    8. "Nucleotide sequence of the human TPM2 gene."
      Ben-Yosef T., Francomano C.A.
      Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-257 (ISOFORM 2).
    9. "A nonmuscle tropomyosin is encoded by the smooth/skeletal beta-tropomyosin gene and its RNA is transcribed from an internal promoter."
      Libri D., Mouly V., Lemonnier M., Fiszman M.Y.
      J. Biol. Chem. 265:3471-3473(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44 (ISOFORM 3).
    10. "Protein content study revealed the presence of isoform 2 of beta-tropomyosin in primary breast cancer tissues from Sudanese patients."
      Ahamed M.E., Mohamed A.O., Ahmed M.E., Sirinuch B., Surasak J.
      Sudan J. Med. Sci. 2:183-187(2007)
      Cited for: PROTEIN SEQUENCE OF 36-48; 52-65; 141-149 AND 206-217 (ISOFORM 2), TISSUE SPECIFICITY.
      Tissue: Mammary cancer.
    11. "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.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Mutations in the beta-tropomyosin (TPM2) gene -- a rare cause of nemaline myopathy."
      Donner K., Ollikainen M., Ridanpaeae M., Christen H.J., Goebel H.H., de Visser M., Pelin K., Wallgren-Pettersson C.
      Neuromuscul. Disord. 12:151-158(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS NEM4 ALA-117 AND PRO-147.
    14. "Mutations in genes encoding fast-twitch contractile proteins cause distal arthrogryposis syndromes."
      Sung S.S., Brassington A.-M.E., Grannatt K., Rutherford A., Whitby F.G., Krakowiak P.A., Jorde L.B., Carey J.C., Bamshad M.
      Am. J. Hum. Genet. 72:681-690(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DA1A GLY-91.
    15. "Congenital myopathy with nemaline rods and cap structures caused by a mutation in the beta-tropomyosin gene (TPM2)."
      Tajsharghi H., Ohlsson M., Lindberg C., Oldfors A.
      Arch. Neurol. 64:1334-1338(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT NEM4 LYS-41.
    16. "Distal arthrogryposis and muscle weakness associated with a beta-tropomyosin mutation."
      Tajsharghi H., Kimber E., Holmgren D., Tulinius M., Oldfors A.
      Neurology 68:772-775(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DA2B TRP-133.
    17. Cited for: VARIANT CAPM2 GLU-139 DEL.
    18. "New morphologic and genetic findings in cap disease associated with beta-tropomyosin (TPM2) mutations."
      Ohlsson M., Quijano-Roy S., Darin N., Brochier G., Lacene E., Avila-Smirnow D., Fardeau M., Oldfors A., Tajsharghi H.
      Neurology 71:1896-1901(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CAPM2 LYS-49 DEL; GLY-52 INS AND LYS-202.
    19. "Cap disease due to mutation of the beta-tropomyosin gene (TPM2)."
      Clarke N.F., Domazetovska A., Waddell L., Kornberg A., McLean C., North K.N.
      Neuromuscul. Disord. 19:348-351(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CAPM2 GLU-139 DEL.

    Entry informationi

    Entry nameiTPM2_HUMAN
    AccessioniPrimary (citable) accession number: P07951
    Secondary accession number(s): A6NM85
    , P06468, Q13894, Q53FM4, Q5TCU4, Q5TCU7, Q9UH67
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 156 of the entry and version 1 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 9
      Human chromosome 9: 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