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P28289

- TMOD1_HUMAN

UniProt

P28289 - TMOD1_HUMAN

Protein

Tropomodulin-1

Gene

TMOD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      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. May play an important role in regulating the organization of actin filaments by preferentially binding to a specific tropomyosin isoform at its N-terminus.1 Publication

    GO - Biological processi

    1. adult locomotory behavior Source: Ensembl
    2. muscle filament sliding Source: Reactome
    3. myofibril assembly Source: Ensembl

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_16969. Striated Muscle Contraction.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tropomodulin-1
    Alternative name(s):
    Erythrocyte tropomodulin
    Short name:
    E-Tmod
    Gene namesi
    Name:TMOD1
    Synonyms:D9S57E, TMOD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:11871. TMOD1.

    Subcellular locationi

    GO - Cellular componenti

    1. cortical cytoskeleton Source: Ensembl
    2. cytosol Source: Reactome
    3. membrane Source: Ensembl
    4. myofibril Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36572.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 359359Tropomodulin-1PRO_0000186128Add
    BLAST

    Proteomic databases

    MaxQBiP28289.
    PaxDbiP28289.
    PeptideAtlasiP28289.
    PRIDEiP28289.

    PTM databases

    PhosphoSiteiP28289.

    Expressioni

    Tissue specificityi

    Highly expressed in the erythrocyte, heart and skeletal muscle.

    Gene expression databases

    ArrayExpressiP28289.
    BgeeiP28289.
    CleanExiHS_TMOD1.
    GenevestigatoriP28289.

    Organism-specific databases

    HPAiHPA051202.

    Interactioni

    Subunit structurei

    Binds to the N-terminus of isoforms 2/3 of TPM3 and to actin.

    Protein-protein interaction databases

    BioGridi112966. 3 interactions.
    IntActiP28289. 1 interaction.
    STRINGi9606.ENSP00000259365.

    Structurei

    3D structure databases

    ProteinModelPortaliP28289.
    SMRiP28289. Positions 179-344.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni39 – 138100Tropomyosin-bindingSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the tropomodulin family.Curated

    Phylogenomic databases

    eggNOGiNOG329422.
    HOGENOMiHOG000261624.
    HOVERGENiHBG056172.
    InParanoidiP28289.
    KOiK10370.
    OMAiSTIVNKQ.
    OrthoDBiEOG7D59Q1.
    PhylomeDBiP28289.
    TreeFamiTF315841.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    P28289-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSYRRELEKY RDLDEDEILG ALTEEELRTL ENELDELDPD NALLPAGLRQ    50
    KDQTTKAPTG PFKREELLDH LEKQAKEFKD REDLVPYTGE KRGKVWVPKQ 100
    KPLDPVLESV TLEPELEEAL ANASDAELCD IAAILGMHTL MSNQQYYQAL 150
    SSSSIMNKEG LNSVIKPTQY KPVPDEEPNS TDVEETLERI KNNDPKLEEV 200
    NLNNIRNIPI PTLKAYAEAL KENSYVKKFS IVGTRSNDPV AYALAEMLKE 250
    NKVLKTLNVE SNFISGAGIL RLVEALPYNT SLVEMKIDNQ SQPLGNKVEM 300
    EIVSMLEKNA TLLKFGYHFT QQGPRLRASN AMMNNNDLVR KRRLADLTGP 350
    IIPKCRSGV 359
    Length:359
    Mass (Da):40,569
    Last modified:December 1, 1992 - v1
    Checksum:i732B7D7798B88A48
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti17 – 171E → K in AAH02660. (PubMed:15489334)Curated
    Sequence conflicti76 – 761K → E in BAG37124. (PubMed:14702039)Curated
    Sequence conflicti289 – 2891N → S in BAG37124. (PubMed:14702039)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M77016 mRNA. Translation: AAA61224.1.
    AF288155
    , AF288147, AF288148, AF288149, AF288150, AF288151, AF288152, AF288153, AF288154 Genomic DNA. Translation: AAG30124.1.
    AK314533 mRNA. Translation: BAG37124.1.
    AL162385 Genomic DNA. Translation: CAI12854.1.
    BC002660 mRNA. Translation: AAH02660.1.
    CCDSiCCDS6726.1.
    PIRiA42336.
    RefSeqiNP_001159588.1. NM_001166116.1.
    NP_003266.1. NM_003275.3.
    UniGeneiHs.404289.
    Hs.723236.

    Genome annotation databases

    EnsembliENST00000259365; ENSP00000259365; ENSG00000136842.
    ENST00000395211; ENSP00000378637; ENSG00000136842.
    GeneIDi7111.
    KEGGihsa:7111.
    UCSCiuc004axk.2. human.

    Polymorphism databases

    DMDMi135922.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M77016 mRNA. Translation: AAA61224.1 .
    AF288155
    , AF288147 , AF288148 , AF288149 , AF288150 , AF288151 , AF288152 , AF288153 , AF288154 Genomic DNA. Translation: AAG30124.1 .
    AK314533 mRNA. Translation: BAG37124.1 .
    AL162385 Genomic DNA. Translation: CAI12854.1 .
    BC002660 mRNA. Translation: AAH02660.1 .
    CCDSi CCDS6726.1.
    PIRi A42336.
    RefSeqi NP_001159588.1. NM_001166116.1.
    NP_003266.1. NM_003275.3.
    UniGenei Hs.404289.
    Hs.723236.

    3D structure databases

    ProteinModelPortali P28289.
    SMRi P28289. Positions 179-344.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112966. 3 interactions.
    IntActi P28289. 1 interaction.
    STRINGi 9606.ENSP00000259365.

    PTM databases

    PhosphoSitei P28289.

    Polymorphism databases

    DMDMi 135922.

    Proteomic databases

    MaxQBi P28289.
    PaxDbi P28289.
    PeptideAtlasi P28289.
    PRIDEi P28289.

    Protocols and materials databases

    DNASUi 7111.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000259365 ; ENSP00000259365 ; ENSG00000136842 .
    ENST00000395211 ; ENSP00000378637 ; ENSG00000136842 .
    GeneIDi 7111.
    KEGGi hsa:7111.
    UCSCi uc004axk.2. human.

    Organism-specific databases

    CTDi 7111.
    GeneCardsi GC09P100263.
    HGNCi HGNC:11871. TMOD1.
    HPAi HPA051202.
    MIMi 190930. gene.
    neXtProti NX_P28289.
    PharmGKBi PA36572.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG329422.
    HOGENOMi HOG000261624.
    HOVERGENi HBG056172.
    InParanoidi P28289.
    KOi K10370.
    OMAi STIVNKQ.
    OrthoDBi EOG7D59Q1.
    PhylomeDBi P28289.
    TreeFami TF315841.

    Enzyme and pathway databases

    Reactomei REACT_16969. Striated Muscle Contraction.

    Miscellaneous databases

    ChiTaRSi TMOD1. human.
    GeneWikii TMOD1.
    GenomeRNAii 7111.
    NextBioi 27835.
    PROi P28289.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P28289.
    Bgeei P28289.
    CleanExi HS_TMOD1.
    Genevestigatori P28289.

    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. "Molecular cloning and characterization of human fetal liver tropomodulin. A tropomyosin-binding protein."
      Sung L.A., Fowler V.M., Lambert K., Sussman M.A., Karr D., Chien S.
      J. Biol. Chem. 267:2616-2621(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Fetal liver.
    2. "Genomic organization of mouse and human erythrocyte tropomodulin genes encoding the pointed end capping protein for the actin filaments."
      Chu X., Thompson D., Yee L.J., Sung L.A.
      Gene 256:271-281(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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. "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].
    5. "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: Uterus.
    6. "Erythrocyte tropomodulin binds to the N-terminus of hTM5, a tropomyosin isoform encoded by the gamma-tropomyosin gene."
      Sung L.A., Lin J.J.-C.
      Biochem. Biophys. Res. Commun. 201:627-634(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TPM3.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTMOD1_HUMAN
    AccessioniPrimary (citable) accession number: P28289
    Secondary accession number(s): B2RB77, Q9BUF1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 120 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. 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