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P62328

- TYB4_HUMAN

UniProt

P62328 - TYB4_HUMAN

Protein

Thymosin beta-4

Gene

TMSB4X

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Plays an important role in the organization of the cytoskeleton By similarity. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization.By similarity
    Seraspenide inhibits the entry of hematopoietic pluripotent stem cells into the S-phase.By similarity

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. actin cytoskeleton organization Source: InterPro
    2. blood coagulation Source: Reactome
    3. platelet activation Source: Reactome
    4. platelet degranulation Source: Reactome
    5. sequestering of actin monomers Source: InterPro

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thymosin beta-4
    Short name:
    T beta-4
    Alternative name(s):
    Fx
    Cleaved into the following chain:
    Alternative name(s):
    Seraspenide
    Gene namesi
    Name:TMSB4X
    Synonyms:TB4X, THYB4, TMSB4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:11881. TMSB4X.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoskeleton Source: UniProtKB-SubCell
    2. extracellular region Source: Reactome
    3. platelet alpha granule lumen Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi12 – 121K → P: Very weak actin binding; no inhibition of actin polymerization.
    Mutagenesisi16 – 161S → A: Binds actin 2.5-fold less than wild-type; little change in inhibition of actin polymerization.
    Mutagenesisi16 – 161S → AS: Very weak actin binding; no inhibition of actin polymerization.
    Mutagenesisi18 – 181L → A or P: Very weak actin binding; no inhibition of actin polymerization.

    Organism-specific databases

    PharmGKBiPA36581.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 4443Thymosin beta-4PRO_0000045920Add
    BLAST
    Peptidei2 – 54Hematopoietic system regulatory peptideBy similarityPRO_0000034295

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei26 – 261N6-acetyllysine1 Publication
    Modified residuei39 – 391N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP62328.
    PaxDbiP62328.
    PRIDEiP62328.

    2D gel databases

    DOSAC-COBS-2DPAGEP62328.

    PTM databases

    PhosphoSiteiP62328.

    Expressioni

    Tissue specificityi

    Expressed in several hemopoietic cell lines and lymphoid malignant cells. Decreased levels in myeloma cells.1 Publication

    Inductioni

    By alpha interferons. Decreased levels in THP-1 cells after treatment with recombinant interferon-lambda.2 Publications

    Gene expression databases

    BgeeiP62328.
    CleanExiHS_TMSB4X.
    GenevestigatoriP62328.

    Organism-specific databases

    HPAiCAB033806.

    Interactioni

    Subunit structurei

    Interacts with SERPINB1 By similarity. Identified in a complex composed of ACTA1, COBL, GSN AND TMSB4X.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MLH1P4069216EBI-712598,EBI-744248

    Protein-protein interaction databases

    BioGridi112969. 13 interactions.
    IntActiP62328. 22 interactions.
    MINTiMINT-6542280.
    STRINGi9606.ENSP00000370007.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UY5model-T2-44[»]
    3TU5X-ray3.00B21-44[»]
    DisProtiDP00357.
    ProteinModelPortaliP62328.
    SMRiP62328. Positions 2-42.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the thymosin beta family.Curated

    Phylogenomic databases

    eggNOGiNOG126035.
    HOVERGENiHBG012534.
    InParanoidiP62328.
    KOiK05764.
    OMAiQTENRIC.
    OrthoDBiEOG7TJ3MT.
    PhylomeDBiP62328.

    Family and domain databases

    Gene3Di1.20.5.520. 1 hit.
    InterProiIPR001152. Thymosin_b4.
    IPR016323. Thymosin_b4_metazoa.
    [Graphical view]
    PANTHERiPTHR12021. PTHR12021. 1 hit.
    PfamiPF01290. Thymosin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001828. Thymosin_beta. 1 hit.
    ProDomiPD005116. Thymosin_b4. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00152. THY. 1 hit.
    [Graphical view]
    PROSITEiPS00500. THYMOSIN_B4. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P62328-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDKPDMAEI EKFDKSKLKK TETQEKNPLP SKETIEQEKQ AGES         44
    Length:44
    Mass (Da):5,053
    Last modified:January 23, 2007 - v2
    Checksum:i440C6158482DAAD0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17733 mRNA. Translation: AAA36745.1.
    AJ295158 Genomic DNA. Translation: CAC43317.1.
    BT007090 mRNA. Translation: AAP35753.1.
    X02493 mRNA. Translation: CAA26323.1.
    CCDSiCCDS35202.1.
    PIRiI56000. A38682.
    RefSeqiNP_066932.1. NM_021109.3.
    UniGeneiHs.437277.
    Hs.703237.

    Genome annotation databases

    EnsembliENST00000380633; ENSP00000370007; ENSG00000205542.
    ENST00000380635; ENSP00000370009; ENSG00000205542.
    ENST00000380636; ENSP00000370010; ENSG00000205542.
    ENST00000451311; ENSP00000414376; ENSG00000205542.
    GeneIDi7114.
    KEGGihsa:7114.
    UCSCiuc004cvf.3. human.

    Polymorphism databases

    DMDMi78103211.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17733 mRNA. Translation: AAA36745.1 .
    AJ295158 Genomic DNA. Translation: CAC43317.1 .
    BT007090 mRNA. Translation: AAP35753.1 .
    X02493 mRNA. Translation: CAA26323.1 .
    CCDSi CCDS35202.1.
    PIRi I56000. A38682.
    RefSeqi NP_066932.1. NM_021109.3.
    UniGenei Hs.437277.
    Hs.703237.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UY5 model - T 2-44 [» ]
    3TU5 X-ray 3.00 B 21-44 [» ]
    DisProti DP00357.
    ProteinModelPortali P62328.
    SMRi P62328. Positions 2-42.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112969. 13 interactions.
    IntActi P62328. 22 interactions.
    MINTi MINT-6542280.
    STRINGi 9606.ENSP00000370007.

    PTM databases

    PhosphoSitei P62328.

    Polymorphism databases

    DMDMi 78103211.

    2D gel databases

    DOSAC-COBS-2DPAGE P62328.

    Proteomic databases

    MaxQBi P62328.
    PaxDbi P62328.
    PRIDEi P62328.

    Protocols and materials databases

    DNASUi 7114.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000380633 ; ENSP00000370007 ; ENSG00000205542 .
    ENST00000380635 ; ENSP00000370009 ; ENSG00000205542 .
    ENST00000380636 ; ENSP00000370010 ; ENSG00000205542 .
    ENST00000451311 ; ENSP00000414376 ; ENSG00000205542 .
    GeneIDi 7114.
    KEGGi hsa:7114.
    UCSCi uc004cvf.3. human.

    Organism-specific databases

    CTDi 7114.
    GeneCardsi GC0XP012993.
    HGNCi HGNC:11881. TMSB4X.
    HPAi CAB033806.
    MIMi 300159. gene.
    neXtProti NX_P62328.
    PharmGKBi PA36581.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG126035.
    HOVERGENi HBG012534.
    InParanoidi P62328.
    KOi K05764.
    OMAi QTENRIC.
    OrthoDBi EOG7TJ3MT.
    PhylomeDBi P62328.

    Miscellaneous databases

    ChiTaRSi TMSB4X. human.
    GeneWikii Thymosin_beta-4.
    GenomeRNAii 7114.
    NextBioi 27851.
    PROi P62328.
    SOURCEi Search...

    Gene expression databases

    Bgeei P62328.
    CleanExi HS_TMSB4X.
    Genevestigatori P62328.

    Family and domain databases

    Gene3Di 1.20.5.520. 1 hit.
    InterProi IPR001152. Thymosin_b4.
    IPR016323. Thymosin_b4_metazoa.
    [Graphical view ]
    PANTHERi PTHR12021. PTHR12021. 1 hit.
    Pfami PF01290. Thymosin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001828. Thymosin_beta. 1 hit.
    ProDomi PD005116. Thymosin_b4. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00152. THY. 1 hit.
    [Graphical view ]
    PROSITEi PS00500. THYMOSIN_B4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Differential expression of the human thymosin-beta 4 gene in lymphocytes, macrophages, and granulocytes."
      Gondo H., Kudo J., White J.W., Barr C., Selvanayagam P., Saunders G.F.
      J. Immunol. 139:3840-3848(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, TISSUE SPECIFICITY.
      Tissue: Peripheral blood leukocyte.
    2. "Molecular cloning and structural characterization of the functional human thymosin beta4 gene."
      Yang S.P., Lee H.J., Su Y.
      Mol. Cell. Biochem. 272:97-105(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "Thymosin beta 4 and Fx, an actin-sequestering peptide, are indistinguishable."
      Safer D., Elzinga M., Nachmias V.T.
      J. Biol. Chem. 266:4029-4032(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-44, INTERACTION WITH ACTIN, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2.
    5. "Transcriptional and posttranscriptional regulation of interferon-induced gene expression in human cells."
      Friedman R.L., Manly S.P., McMahon M., Kerr I.M., Stark G.R.
      Cell 38:745-755(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-44, INDUCTION.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "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-26 AND LYS-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Structural requirements for thymosin beta4 in its contact with actin. An NMR-analysis of thymosin beta4 mutants in solution and correlation with their biological activity."
      Simenel C., Van Troys M., Vandekerckhove J., Ampe C., Delepierre M.
      Eur. J. Biochem. 267:3530-3538(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF WILD-TYPE AND OF MUTANTS LYS-12; SER-16 AND LEU-18 IN COMPLEX WITH ACTIN.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 21-44 IN COMPLEX WITH ACTA1; GSN AND COBL, SUBUNIT.

    Entry informationi

    Entry nameiTYB4_HUMAN
    AccessioniPrimary (citable) accession number: P62328
    Secondary accession number(s): P01253
    , P01254, Q546P5, Q63576, Q9UE55
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 107 of the entry and version 2 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3