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P70566

- TMOD2_RAT

UniProt

P70566 - TMOD2_RAT

Protein

Tropomodulin-2

Gene

Tmod2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    Functioni

    Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton By similarity.By similarity

    GO - Molecular functioni

    1. actin binding Source: RGD
    2. tropomyosin binding Source: RGD

    GO - Biological processi

    1. actin filament organization Source: RGD
    2. learning or memory Source: Ensembl
    3. neuron-neuron synaptic transmission Source: Ensembl
    4. positive regulation of G-protein coupled receptor protein signaling pathway Source: Ensembl

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tropomodulin-2
    Alternative name(s):
    Neuronal tropomodulin
    Short name:
    N-Tmod
    Gene namesi
    Name:Tmod2
    Synonyms:Ntmod
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 8

    Organism-specific databases

    RGDi61948. Tmod2.

    Subcellular locationi

    Cytoplasmcytoskeleton By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. cytoskeleton Source: UniProtKB-SubCell
    3. growth cone Source: RGD
    4. neuron projection Source: RGD

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 351351Tropomodulin-2PRO_0000186133Add
    BLAST

    Proteomic databases

    PaxDbiP70566.
    PRIDEiP70566.

    2D gel databases

    World-2DPAGE0004:P70566.

    Expressioni

    Tissue specificityi

    Neuronal-tissue specific.

    Gene expression databases

    GenevestigatoriP70566.

    Interactioni

    Subunit structurei

    Binds to the N-terminus of tropomyosin and to actin. Binds to TMBr3 as well as to other low molecular mass tropomyosins (TM5a or TM5), but not to high molecular mass tropomyosins (TM2 or TMBr1).

    Protein-protein interaction databases

    BioGridi248623. 1 interaction.
    STRINGi10116.ENSRNOP00000014124.

    Structurei

    3D structure databases

    ProteinModelPortaliP70566.
    SMRiP70566. Positions 181-346.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tropomodulin family.Curated

    Phylogenomic databases

    eggNOGiNOG329422.
    GeneTreeiENSGT00740000115178.
    HOGENOMiHOG000261624.
    HOVERGENiHBG056172.
    InParanoidiP70566.
    KOiK10370.
    OMAiVNNPKFD.
    OrthoDBiEOG7D59Q1.
    PhylomeDBiP70566.
    TreeFamiTF315841.

    Family and domain databases

    InterProiIPR004934. Tropomodulin.
    [Graphical view]
    PANTHERiPTHR10901. PTHR10901. 1 hit.
    PfamiPF03250. Tropomodulin. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P70566-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALPFQKGLE KYKNIDEDEL LGKLSEEELK QLENVLDDLD PESATLPAGF    50
    RQKDQTQKAA TGPFDREHLL MYLEKEALEQ KDREDFVPFT GEKKGRVFIP 100
    KEKPVETRKE EKVTLDPELE EALASASDTE LYDLAAVLGV HNLLNNPKFD 150
    EETTNGQGRK GPVRNVVKGE KAKPVFEEPP NPTNVEASLQ QMKANDPSLQ 200
    EVNLNNIKNI PIPTLKEFAK ALETNTHVRK FSLAATRSND PVALAFAEML 250
    KVNKTLKSLN VESNFITGAG ILALVEALRE NDTLTEIKID NQRQQLGTAV 300
    EMEIAQMLEE NSRILKFGYQ FTKQGPRTRV AAAITKNNDL VRKKRVEGDR 350
    R 351
    Length:351
    Mass (Da):39,492
    Last modified:February 1, 1997 - v1
    Checksum:i24F5C67EA897983E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59240 mRNA. Translation: AAC52854.1.
    RefSeqiNP_113801.1. NM_031613.1.
    XP_006243469.1. XM_006243407.1.
    XP_006243470.1. XM_006243408.1.
    UniGeneiRn.74047.

    Genome annotation databases

    EnsembliENSRNOT00000014124; ENSRNOP00000014124; ENSRNOG00000010447.
    GeneIDi58814.
    KEGGirno:58814.
    UCSCiRGD:61948. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59240 mRNA. Translation: AAC52854.1 .
    RefSeqi NP_113801.1. NM_031613.1.
    XP_006243469.1. XM_006243407.1.
    XP_006243470.1. XM_006243408.1.
    UniGenei Rn.74047.

    3D structure databases

    ProteinModelPortali P70566.
    SMRi P70566. Positions 181-346.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 248623. 1 interaction.
    STRINGi 10116.ENSRNOP00000014124.

    2D gel databases

    World-2DPAGE 0004:P70566.

    Proteomic databases

    PaxDbi P70566.
    PRIDEi P70566.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000014124 ; ENSRNOP00000014124 ; ENSRNOG00000010447 .
    GeneIDi 58814.
    KEGGi rno:58814.
    UCSCi RGD:61948. rat.

    Organism-specific databases

    CTDi 29767.
    RGDi 61948. Tmod2.

    Phylogenomic databases

    eggNOGi NOG329422.
    GeneTreei ENSGT00740000115178.
    HOGENOMi HOG000261624.
    HOVERGENi HBG056172.
    InParanoidi P70566.
    KOi K10370.
    OMAi VNNPKFD.
    OrthoDBi EOG7D59Q1.
    PhylomeDBi P70566.
    TreeFami TF315841.

    Miscellaneous databases

    NextBioi 611346.
    PROi P70566.

    Gene expression databases

    Genevestigatori P70566.

    Family and domain databases

    InterProi IPR004934. Tropomodulin.
    [Graphical view ]
    PANTHERi PTHR10901. PTHR10901. 1 hit.
    Pfami PF03250. Tropomodulin. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "N-tropomodulin: a novel isoform of tropomodulin identified as the major binding protein to brain tropomyosin."
      Watakabe A., Kobayashi R., Helfman D.M.
      J. Cell Sci. 109:2299-2310(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Brain.
    2. Lubec G., Chen W.-Q.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 82-93 AND 238-251, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Hippocampus.

    Entry informationi

    Entry nameiTMOD2_RAT
    AccessioniPrimary (citable) accession number: P70566
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 85 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