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P67936

- TPM4_HUMAN

UniProt

P67936 - TPM4_HUMAN

Protein

Tropomyosin alpha-4 chain

Gene

TPM4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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. Binds calcium.1 Publication

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. structural constituent of muscle Source: ProtInc

    GO - Biological processi

    1. cellular component movement Source: UniProtKB
    2. muscle contraction Source: Reactome
    3. muscle filament sliding Source: Reactome
    4. osteoblast differentiation Source: UniProt

    Keywords - Molecular functioni

    Muscle protein

    Keywords - Ligandi

    Actin-binding, Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_16969. Striated Muscle Contraction.
    REACT_20558. Smooth Muscle Contraction.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tropomyosin alpha-4 chain
    Alternative name(s):
    TM30p1
    Tropomyosin-4
    Gene namesi
    Name:TPM4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:12013. TPM4.

    Subcellular locationi

    GO - Cellular componenti

    1. cortical cytoskeleton Source: Ensembl
    2. cytoskeleton Source: UniProtKB
    3. cytosol Source: Reactome
    4. extracellular vesicular exosome Source: UniProt
    5. filamentous actin Source: Ensembl
    6. membrane Source: UniProt
    7. muscle thin filament tropomyosin Source: ProtInc
    8. podosome Source: Ensembl
    9. stress fiber Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti178342. Inflammatory myofibroblastic tumor.
    PharmGKBiPA36693.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed5 Publications
    Chaini2 – 248247Tropomyosin alpha-4 chainPRO_0000205635Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei177 – 1771N6-acetyllysine1 Publication
    Modified residuei215 – 2151N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP67936.
    PaxDbiP67936.
    PeptideAtlasiP67936.
    PRIDEiP67936.

    2D gel databases

    DOSAC-COBS-2DPAGEP67936.
    OGPiP07226.

    PTM databases

    PhosphoSiteiP67936.

    Expressioni

    Tissue specificityi

    Detected in cardiac tissue and platelets, the form found in cardiac tissue is a higher molecular weight than the form found in platelets. Expressed at higher levels in the platelets of hypertensive patients with cardiac hypertrophy than in the platelets of hypertensive patients without cardiac hypertrophy (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiP67936.
    BgeeiP67936.
    CleanExiHS_TPM4.
    GenevestigatoriP67936.

    Organism-specific databases

    HPAiCAB004685.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta chain.By similarity

    Protein-protein interaction databases

    BioGridi113024. 45 interactions.
    IntActiP67936. 6 interactions.
    MINTiMINT-4138291.

    Structurei

    3D structure databases

    ProteinModelPortaliP67936.
    SMRiP67936. Positions 5-248.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili2 – 248247By 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.
    HOVERGENiHBG107404.
    KOiK10375.
    OMAiEKCKQVE.
    PhylomeDBiP67936.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P67936-1) [UniParc]FASTAAdd to Basket

    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

    MAGLNSLEAV KRKIQALQQQ ADEAEDRAQG LQRELDGERE RREKAEGDVA    50
    ALNRRIQLVE EELDRAQERL ATALQKLEEA EKAADESERG MKVIENRAMK 100
    DEEKMEIQEM QLKEAKHIAE EADRKYEEVA RKLVILEGEL ERAEERAEVS 150
    ELKCGDLEEE LKNVTNNLKS LEAASEKYSE KEDKYEEEIK LLSDKLKEAE 200
    TRAEFAERTV AKLEKTIDDL EEKLAQAKEE NVGLHQTLDQ TLNELNCI 248
    Length:248
    Mass (Da):28,522
    Last modified:January 23, 2007 - v3
    Checksum:i5D5CDF6BF76552A8
    GO
    Isoform 2 (identifier: P67936-2) [UniParc] [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-44: MAGLNSLEAV...LDGERERREK → MEAIKKKMQM...LELTEKKASD

    Show »
    Length:284
    Mass (Da):32,723
    Checksum:i29C0F6ADF4C87F0C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti59 – 591V → F in AAH02827. (PubMed:15489334)Curated
    Sequence conflicti152 – 1521L → S in AAA36774. (PubMed:3865200)Curated
    Sequence conflicti162 – 1632KN → RT in AAA36774. (PubMed:3865200)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti204 – 2041E → Q in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036535

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4444MAGLN…ERREK → MEAIKKKMQMLKLDKENAID RAEQAEADKKAAEDKCKQVE EELTHLQKKLKGTEDELDKY SEDLKDAQEKLELTEKKASD in isoform 2. 1 PublicationVSP_006611Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05276 mRNA. Translation: CAA28888.1.
    AK023385 mRNA. Translation: BAB14554.1.
    AK315076 mRNA. Translation: BAG37545.1.
    BT019634 mRNA. Translation: AAV38440.1.
    CH471106 Genomic DNA. Translation: EAW84521.1.
    BC002827 mRNA. Translation: AAH02827.1.
    BC037576 mRNA. Translation: AAH37576.1.
    BC067225 mRNA. Translation: AAH67225.1.
    M12127 mRNA. Translation: AAA36774.1.
    CCDSiCCDS12338.1.
    CCDS46007.1. [P67936-2]
    PIRiS07282.
    RefSeqiNP_001138632.1. NM_001145160.1. [P67936-2]
    NP_003281.1. NM_003290.2. [P67936-1]
    UniGeneiHs.631618.

    Genome annotation databases

    EnsembliENST00000300933; ENSP00000300933; ENSG00000167460. [P67936-1]
    ENST00000344824; ENSP00000345230; ENSG00000167460. [P67936-2]
    GeneIDi7171.
    KEGGihsa:7171.
    UCSCiuc002ndi.2. human. [P67936-2]
    uc002ndj.2. human.

    Polymorphism databases

    DMDMi54039751.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05276 mRNA. Translation: CAA28888.1 .
    AK023385 mRNA. Translation: BAB14554.1 .
    AK315076 mRNA. Translation: BAG37545.1 .
    BT019634 mRNA. Translation: AAV38440.1 .
    CH471106 Genomic DNA. Translation: EAW84521.1 .
    BC002827 mRNA. Translation: AAH02827.1 .
    BC037576 mRNA. Translation: AAH37576.1 .
    BC067225 mRNA. Translation: AAH67225.1 .
    M12127 mRNA. Translation: AAA36774.1 .
    CCDSi CCDS12338.1.
    CCDS46007.1. [P67936-2 ]
    PIRi S07282.
    RefSeqi NP_001138632.1. NM_001145160.1. [P67936-2 ]
    NP_003281.1. NM_003290.2. [P67936-1 ]
    UniGenei Hs.631618.

    3D structure databases

    ProteinModelPortali P67936.
    SMRi P67936. Positions 5-248.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113024. 45 interactions.
    IntActi P67936. 6 interactions.
    MINTi MINT-4138291.

    PTM databases

    PhosphoSitei P67936.

    Polymorphism databases

    DMDMi 54039751.

    2D gel databases

    DOSAC-COBS-2DPAGE P67936.
    OGPi P07226.

    Proteomic databases

    MaxQBi P67936.
    PaxDbi P67936.
    PeptideAtlasi P67936.
    PRIDEi P67936.

    Protocols and materials databases

    DNASUi 7171.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000300933 ; ENSP00000300933 ; ENSG00000167460 . [P67936-1 ]
    ENST00000344824 ; ENSP00000345230 ; ENSG00000167460 . [P67936-2 ]
    GeneIDi 7171.
    KEGGi hsa:7171.
    UCSCi uc002ndi.2. human. [P67936-2 ]
    uc002ndj.2. human.

    Organism-specific databases

    CTDi 7171.
    GeneCardsi GC19P017322.
    H-InvDB HIX0022609.
    HGNCi HGNC:12013. TPM4.
    HPAi CAB004685.
    MIMi 600317. gene.
    neXtProti NX_P67936.
    Orphaneti 178342. Inflammatory myofibroblastic tumor.
    PharmGKBi PA36693.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG304012.
    HOVERGENi HBG107404.
    KOi K10375.
    OMAi EKCKQVE.
    PhylomeDBi P67936.
    TreeFami TF351519.

    Enzyme and pathway databases

    Reactomei REACT_16969. Striated Muscle Contraction.
    REACT_20558. Smooth Muscle Contraction.

    Miscellaneous databases

    ChiTaRSi TPM4. human.
    GeneWikii TPM4.
    GenomeRNAii 7171.
    NextBioi 28104.
    PROi P67936.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P67936.
    Bgeei P67936.
    CleanExi HS_TPM4.
    Genevestigatori P67936.

    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. "Characterization of a cDNA defining a gene family encoding TM30p1, a human fibroblast tropomyosin."
      McLeod A.R., Talbot K., Smillie L.B., Houlker C.
      J. Mol. Biol. 194:1-10(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fibroblast.
    2. "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] (ISOFORMS 1 AND 2).
      Tissue: Ovarian carcinoma and Tongue.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. 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] (ISOFORM 1).
      Tissue: Eye, Placenta and Testis.
    6. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-12.
      Tissue: Platelet.
    7. Bienvenut W.V., Claeys D.
      Submitted (NOV-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-11; 45-54; 56-69; 77-89; 133-146 AND 216-223, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Platelet.
    8. "The calcium binding protein tropomyosin in human platelets and cardiac tissue: elevation in hypertensive cardiac hypertrophy."
      Crabos M., Yamakado T., Heizmann C.W., Cerletti N., Buehler F.R., Erne P.
      Eur. J. Clin. Invest. 21:472-478(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 9-31; 44-61; 89-95; 205-214 AND 231-243 (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Platelet.
    9. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 13-27; 45-82; 132-142; 154-169 AND 216-228, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    10. "A muscle-type tropomyosin in human fibroblasts: evidence for expression by an alternative RNA splicing mechanism."
      MacLeod A.R., Houlker C., Reinach F.C., Smillie L.B., Talbot K., Modi G., Walsh F.S.
      Proc. Natl. Acad. Sci. U.S.A. 82:7835-7839(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 118-248.
      Tissue: Fibroblast.
    11. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
      Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
      Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 177-189 AND 228-247.
      Tissue: Keratinocyte.
    12. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-177 AND LYS-215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-204.

    Entry informationi

    Entry nameiTPM4_HUMAN
    AccessioniPrimary (citable) accession number: P67936
    Secondary accession number(s): P07226
    , Q15659, Q5U0D9, Q9BU85, Q9H8Q3, Q9UCS1, Q9UCS2, Q9UCS3, Q9UCS4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 110 of the entry and version 3 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 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3