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P58771

- TPM1_MOUSE

UniProt

P58771 - TPM1_MOUSE

Protein

Tropomyosin alpha-1 chain

Gene

Tpm1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      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. structural constituent of cytoskeleton Source: MGI

    GO - Biological processi

    1. cardiac muscle contraction Source: BHF-UCL
    2. cellular response to reactive oxygen species Source: Ensembl
    3. in utero embryonic development Source: MGI
    4. positive regulation of heart rate by epinephrine Source: BHF-UCL
    5. sarcomere organization Source: Ensembl
    6. ventricular cardiac muscle tissue morphogenesis Source: BHF-UCL

    Keywords - Molecular functioni

    Muscle protein

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tropomyosin alpha-1 chain
    Alternative name(s):
    Alpha-tropomyosin
    Tropomyosin-1
    Gene namesi
    Name:Tpm1
    Synonyms:Tpm-1, Tpma
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:98809. Tpm1.

    Subcellular locationi

    GO - Cellular componenti

    1. bleb Source: Ensembl
    2. cytoplasm Source: MGI
    3. muscle thin filament tropomyosin Source: MGI
    4. myofibril Source: MGI
    5. ruffle membrane Source: Ensembl
    6. stress fiber Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 284284Tropomyosin alpha-1 chainPRO_0000205621Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Cross-linki77 – 77Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei283 – 2831Phosphoserine; by DAPK1By similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP58771.
    PaxDbiP58771.
    PRIDEiP58771.

    2D gel databases

    SWISS-2DPAGEP58771.

    PTM databases

    PhosphoSiteiP58771.

    Expressioni

    Inductioni

    Induced in stimulated quiescent cells.1 Publication

    Gene expression databases

    ArrayExpressiP58771.
    BgeeiP58771.
    CleanExiMM_TPM1.
    GenevestigatoriP58771.

    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

    BioGridi204291. 7 interactions.
    DIPiDIP-300N.
    IntActiP58771. 9 interactions.
    MINTiMINT-149814.

    Structurei

    3D structure databases

    ProteinModelPortaliP58771.
    SMRiP58771. Positions 8-284.
    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.
    OrthoDBiEOG7673C8.
    PhylomeDBiP58771.
    TreeFamiTF351519.

    Family and domain databases

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

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: P58771-1) [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 LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL    50
    KGTEDELDKY SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD 100
    RAQERLATAL QKLEEAEKAA DESERGMKVI ESRAQKDEEK MEIQEIQLKE 150
    AKHIAEDADR KYEEVARKLV IIESDLERAE ERAELSEGKC AELEEELKTV 200
    TNNLKSLEAQ AEKYSQKEDK YEEEIKVLSD KLKEAETRAE FAERSVTKLE 250
    KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI 284
    Length:284
    Mass (Da):32,681
    Last modified:July 21, 1986 - v1
    Checksum:iE25609F597A72F4D
    GO
    Isoform 2 (identifier: P58771-2) [UniParc]FASTAAdd to Basket

    Also known as: Fibroblast

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

    Show »
    Length:284
    Mass (Da):32,709
    Checksum:iCD755ABFAEA04540
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei258 – 28427DELYA…DMTSI → EKVAHAKEENLSMHQMLDQT LLELNNM in isoform 2. 1 PublicationVSP_006580Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64831 mRNA. Translation: CAA46043.1.
    M22479 mRNA. Translation: AAA40483.1.
    CCDSiCCDS23311.1. [P58771-2]
    CCDS52845.1. [P58771-1]
    PIRiA31380. A60597.
    RefSeqiNP_001157720.1. NM_001164248.1. [P58771-1]
    NP_077745.2. NM_024427.4. [P58771-2]
    UniGeneiMm.121878.

    Genome annotation databases

    EnsembliENSMUST00000113685; ENSMUSP00000109315; ENSMUSG00000032366. [P58771-1]
    ENSMUST00000113707; ENSMUSP00000109337; ENSMUSG00000032366. [P58771-2]
    GeneIDi22003.
    KEGGimmu:22003.
    UCSCiuc009qfq.2. mouse. [P58771-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64831 mRNA. Translation: CAA46043.1 .
    M22479 mRNA. Translation: AAA40483.1 .
    CCDSi CCDS23311.1. [P58771-2 ]
    CCDS52845.1. [P58771-1 ]
    PIRi A31380. A60597.
    RefSeqi NP_001157720.1. NM_001164248.1. [P58771-1 ]
    NP_077745.2. NM_024427.4. [P58771-2 ]
    UniGenei Mm.121878.

    3D structure databases

    ProteinModelPortali P58771.
    SMRi P58771. Positions 8-284.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204291. 7 interactions.
    DIPi DIP-300N.
    IntActi P58771. 9 interactions.
    MINTi MINT-149814.

    PTM databases

    PhosphoSitei P58771.

    2D gel databases

    SWISS-2DPAGE P58771.

    Proteomic databases

    MaxQBi P58771.
    PaxDbi P58771.
    PRIDEi P58771.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000113685 ; ENSMUSP00000109315 ; ENSMUSG00000032366 . [P58771-1 ]
    ENSMUST00000113707 ; ENSMUSP00000109337 ; ENSMUSG00000032366 . [P58771-2 ]
    GeneIDi 22003.
    KEGGi mmu:22003.
    UCSCi uc009qfq.2. mouse. [P58771-1 ]

    Organism-specific databases

    CTDi 7168.
    MGIi MGI:98809. Tpm1.

    Phylogenomic databases

    eggNOGi NOG304012.
    HOGENOMi HOG000231521.
    HOVERGENi HBG107404.
    KOi K10373.
    OrthoDBi EOG7673C8.
    PhylomeDBi P58771.
    TreeFami TF351519.

    Miscellaneous databases

    ChiTaRSi TPM1. mouse.
    NextBioi 301732.
    PROi P58771.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P58771.
    Bgeei P58771.
    CleanExi MM_TPM1.
    Genevestigatori P58771.

    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. "Subtractive cDNA cloning as a tool to analyse secondary effects of a muscle disease. Characterization of affected genes in the myotonic ADR mouse."
      Schleef M., Zuehlke C., Schoeffl F., Jockusch H.
      Neuromuscul. Disord. 4:205-217(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: A2G.
      Tissue: Fast-twitch skeletal muscle.
    2. "Isolation and characterization of a cDNA that encodes mouse fibroblast tropomyosin isoform 2."
      Takenaga K., Nakamura Y., Tokunaga K., Kageyama H., Sakiyama S.
      Mol. Cell. Biol. 8:5561-5565(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. "Coordinate induction of fibronectin, fibronectin receptor, tropomyosin, and actin genes in serum-stimulated fibroblasts."
      Ryseck R.P., MacDonald-Bravo H., Zerial M., Bravo R.
      Exp. Cell Res. 180:537-545(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    4. "A proteomics approach to identify the ubiquitinated proteins in mouse heart."
      Jeon H.B., Choi E.S., Yoon J.H., Hwang J.H., Chang J.W., Lee E.K., Choi H.W., Park Z.-Y., Yoo Y.J.
      Biochem. Biophys. Res. Commun. 357:731-736(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-77.
      Tissue: Heart.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiTPM1_MOUSE
    AccessioniPrimary (citable) accession number: P58771
    Secondary accession number(s): P02558
    , P19354, P46902, P99034
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 102 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The sequences of cardiac and skeletal muscles are identical.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3