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Q9NYL9

- TMOD3_HUMAN

UniProt

Q9NYL9 - TMOD3_HUMAN

Protein

Tropomodulin-3

Gene

TMOD3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      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. tropomyosin binding Source: ProtInc

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tropomodulin-3
    Alternative name(s):
    Ubiquitous tropomodulin
    Short name:
    U-Tmod
    Gene namesi
    Name:TMOD3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:11873. TMOD3.

    Subcellular locationi

    Cytoplasmcytoskeleton By similarity

    GO - Cellular componenti

    1. striated muscle thin filament Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36574.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 352352Tropomodulin-3PRO_0000186134Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei25 – 251Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9NYL9.
    PaxDbiQ9NYL9.
    PeptideAtlasiQ9NYL9.
    PRIDEiQ9NYL9.

    2D gel databases

    OGPiQ9NYL9.

    PTM databases

    PhosphoSiteiQ9NYL9.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiQ9NYL9.
    BgeeiQ9NYL9.
    CleanExiHS_TMOD3.
    GenevestigatoriQ9NYL9.

    Organism-specific databases

    HPAiHPA001849.

    Interactioni

    Subunit structurei

    Binds to the N-terminus of tropomyosin and to actin.By similarity

    Protein-protein interaction databases

    BioGridi118899. 37 interactions.
    IntActiQ9NYL9. 21 interactions.
    MINTiMINT-1149880.
    STRINGi9606.ENSP00000308753.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NYL9.
    SMRiQ9NYL9. Positions 182-347.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tropomodulin family.Curated

    Phylogenomic databases

    eggNOGiNOG329422.
    HOGENOMiHOG000261624.
    HOVERGENiHBG056172.
    InParanoidiQ9NYL9.
    KOiK10370.
    OMAiNTHVKNF.
    PhylomeDBiQ9NYL9.
    TreeFamiTF315841.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    Q9NYL9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALPFRKDLE KYKDLDEDEL LGNLSETELK QLETVLDDLD PENALLPAGF    50
    RQKNQTSKST TGPFDREHLL SYLEKEALEH KDREDYVPYT GEKKGKIFIP 100
    KQKPVQTFTE EKVSLDPELE EALTSASDTE LCDLAAILGM HNLITNTKFC 150
    NIMGSSNGVD QEHFSNVVKG EKILPVFDEP PNPTNVEESL KRTKENDAHL 200
    VEVNLNNIKN IPIPTLKDFA KALETNTHVK CFSLAATRSN DPVATAFAEM 250
    LKVNKTLKSL NVESNFITGV GILALIDALR DNETLAELKI DNQRQQLGTA 300
    VELEMAKMLE ENTNILKFGY QFTQQGPRTR AANAITKNND LVRKRRVEGD 350
    HQ 352
    Length:352
    Mass (Da):39,595
    Last modified:October 1, 2000 - v1
    Checksum:i8B7F2122C1BE9855
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti27 – 271T → S in AAF31670. (PubMed:10662549)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF237631 mRNA. Translation: AAF45299.1.
    AF177171 mRNA. Translation: AAF31670.1.
    AK312569 mRNA. Translation: BAG35464.1.
    BC020542 mRNA. Translation: AAH20542.1.
    AL137543 mRNA. Translation: CAB70801.1.
    CCDSiCCDS10145.1.
    PIRiT46384.
    RefSeqiNP_055362.1. NM_014547.4.
    XP_006720542.1. XM_006720479.1.
    UniGeneiHs.4998.

    Genome annotation databases

    EnsembliENST00000308580; ENSP00000308753; ENSG00000138594.
    ENST00000544199; ENSP00000438909; ENSG00000138594.
    GeneIDi29766.
    KEGGihsa:29766.
    UCSCiuc002abn.3. human.

    Polymorphism databases

    DMDMi23396884.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF237631 mRNA. Translation: AAF45299.1 .
    AF177171 mRNA. Translation: AAF31670.1 .
    AK312569 mRNA. Translation: BAG35464.1 .
    BC020542 mRNA. Translation: AAH20542.1 .
    AL137543 mRNA. Translation: CAB70801.1 .
    CCDSi CCDS10145.1.
    PIRi T46384.
    RefSeqi NP_055362.1. NM_014547.4.
    XP_006720542.1. XM_006720479.1.
    UniGenei Hs.4998.

    3D structure databases

    ProteinModelPortali Q9NYL9.
    SMRi Q9NYL9. Positions 182-347.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118899. 37 interactions.
    IntActi Q9NYL9. 21 interactions.
    MINTi MINT-1149880.
    STRINGi 9606.ENSP00000308753.

    PTM databases

    PhosphoSitei Q9NYL9.

    Polymorphism databases

    DMDMi 23396884.

    2D gel databases

    OGPi Q9NYL9.

    Proteomic databases

    MaxQBi Q9NYL9.
    PaxDbi Q9NYL9.
    PeptideAtlasi Q9NYL9.
    PRIDEi Q9NYL9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000308580 ; ENSP00000308753 ; ENSG00000138594 .
    ENST00000544199 ; ENSP00000438909 ; ENSG00000138594 .
    GeneIDi 29766.
    KEGGi hsa:29766.
    UCSCi uc002abn.3. human.

    Organism-specific databases

    CTDi 29766.
    GeneCardsi GC15P052121.
    HGNCi HGNC:11873. TMOD3.
    HPAi HPA001849.
    MIMi 605112. gene.
    neXtProti NX_Q9NYL9.
    PharmGKBi PA36574.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG329422.
    HOGENOMi HOG000261624.
    HOVERGENi HBG056172.
    InParanoidi Q9NYL9.
    KOi K10370.
    OMAi NTHVKNF.
    PhylomeDBi Q9NYL9.
    TreeFami TF315841.

    Miscellaneous databases

    ChiTaRSi TMOD3. human.
    GeneWikii TMOD3.
    GenomeRNAii 29766.
    NextBioi 52268.
    PROi Q9NYL9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NYL9.
    Bgeei Q9NYL9.
    CleanExi HS_TMOD3.
    Genevestigatori Q9NYL9.

    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. Conley C.A., Fowler V.M.
      Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Sequencing, expression analysis, and mapping of three unique human tropomodulin genes and their mouse orthologs."
      Cox P.R., Zoghbi H.Y.
      Genomics 63:97-107(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    3. "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].
      Tissue: Brain.
    4. "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].
      Tissue: Adrenal gland.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 264-352.
      Tissue: Testis.
    6. Lubec G., Afjehi-Sadat L.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 318-328, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTMOD3_HUMAN
    AccessioniPrimary (citable) accession number: Q9NYL9
    Secondary accession number(s): B2R6G7, Q9NT43, Q9NZR0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 109 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 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3