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P58776

- TPM2_RABIT

UniProt

P58776 - TPM2_RABIT

Protein

Tropomyosin beta chain

Gene

TPM2

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 57 (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. The non-muscle isoform may have a role in agonist-mediated receptor internalization By similarity.By similarity

    Keywords - Molecular functioni

    Muscle protein

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tropomyosin beta chain
    Alternative name(s):
    Beta-tropomyosin
    Tropomyosin-2
    Gene namesi
    Name:TPM2
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Chromosome 1

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. cytoskeleton Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 284284Tropomyosin beta chainPRO_0000205630Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    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

    PRIDEiP58776.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta chain.

    Protein-protein interaction databases

    IntActiP58776. 1 interaction.
    MINTiMINT-7966042.
    STRINGi9986.ENSOCUP00000008788.

    Structurei

    3D structure databases

    ProteinModelPortaliP58776.
    SMRiP58776. 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.
    GeneTreeiENSGT00550000074494.
    HOGENOMiHOG000231521.
    HOVERGENiHBG107404.
    OMAiFLEVIIE.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    P58776-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDAIKKKMQM LKLDKENAID RAEQAEADKK QAEDRCKQLE EEQQALQKKL    50
    KGTEDEVEKY SESVKDAQEK 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):32,837
    Last modified:July 21, 1986 - v1
    Checksum:iF95D2BF6250F40AE
    GO

    Sequence databases

    PIRiA02980. TMRBB.

    Genome annotation databases

    EnsembliENSOCUT00000022879; ENSOCUP00000022333; ENSOCUG00000010198.

    Cross-referencesi

    Sequence databases

    PIRi A02980. TMRBB.

    3D structure databases

    ProteinModelPortali P58776.
    SMRi P58776. Positions 1-284.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P58776. 1 interaction.
    MINTi MINT-7966042.
    STRINGi 9986.ENSOCUP00000008788.

    Proteomic databases

    PRIDEi P58776.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSOCUT00000022879 ; ENSOCUP00000022333 ; ENSOCUG00000010198 .

    Phylogenomic databases

    eggNOGi NOG304012.
    GeneTreei ENSGT00550000074494.
    HOGENOMi HOG000231521.
    HOVERGENi HBG107404.
    OMAi FLEVIIE.

    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 comparison of the amino acid sequences of rabbit skeletal muscle alpha- and beta-tropomyosins."
      Mak A.S., Smillie L.B., Steward G.R.
      J. Biol. Chem. 255:3647-3655(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.

    Entry informationi

    Entry nameiTPM2_RABIT
    AccessioniPrimary (citable) accession number: P58776
    Secondary accession number(s): P02560
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 57 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3