ID   TYB4_HUMAN              Reviewed;          44 AA.
AC   P62328; P01253; P01254; Q546P5; Q63576; Q9UE55;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   13-OCT-2009, entry version 58.
DE   RecName: Full=Thymosin beta-4;
DE            Short=T beta-4;
DE   AltName: Full=Fx;
DE   Contains:
DE     RecName: Full=Hematopoietic system regulatory peptide;
DE     AltName: Full=Seraspenide;
GN   Name=TMSB4X; Synonyms=TB4X, THYB4, TMSB4;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Peripheral blood leukocyte;
RX   MEDLINE=88060494; PubMed=3500230;
RA   Gondo H., Kudo J., White J.W., Barr C., Selvanayagam P.,
RA   Saunders G.F.;
RT   "Differential expression of the human thymosin-beta 4 gene in
RT   lymphocytes, macrophages, and granulocytes.";
RL   J. Immunol. 139:3840-3848(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16010977; DOI=10.1007/s11010-005-7642-4;
RA   Yang S.P., Lee H.J., Su Y.;
RT   "Molecular cloning and structural characterization of the functional
RT   human thymosin beta4 gene.";
RL   Mol. Cell. Biochem. 272:97-105(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 2-44, AND INTERACTION WITH ACTIN.
RX   MEDLINE=91154186; PubMed=1999398;
RA   Safer D., Elzinga M., Nachmias V.T.;
RT   "Thymosin beta 4 and Fx, an actin-sequestering peptide, are
RT   indistinguishable.";
RL   J. Biol. Chem. 266:4029-4032(1991).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-44, AND INDUCTION.
RX   MEDLINE=85024867; PubMed=6548414; DOI=10.1016/0092-8674(84)90270-8;
RA   Friedman R.L., Manly S.P., McMahon M., Kerr I.M., Stark G.R.;
RT   "Transcriptional and posttranscriptional regulation of interferon-
RT   induced gene expression in human cells.";
RL   Cell 38:745-755(1984).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-4; LYS-12; LYS-26; LYS-32
RP   AND LYS-39, AND MASS SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [7]
RP   STRUCTURE BY NMR OF WILD-TYPE AND OF MUTANTS LYS-12; SER-16 AND LEU-18
RP   IN COMPLEX WITH ACTIN.
RX   PubMed=10848969; DOI=10.1046/j.1432-1327.2000.01380.x;
RA   Simenel C., Van Troys M., Vandekerckhove J., Ampe C., Delepierre M.;
RT   "Structural requirements for thymosin beta4 in its contact with actin.
RT   An NMR-analysis of thymosin beta4 mutants in solution and correlation
RT   with their biological activity.";
RL   Eur. J. Biochem. 267:3530-3538(2000).
CC   -!- FUNCTION: Plays an important role in the organization of the
CC       cytoskeleton (By similarity). Binds to and sequesters actin
CC       monomers (G actin) and therefore inhibits actin polymerization.
CC   -!- FUNCTION: Seraspenide inhibits the entry of hematopoeitic
CC       pluripotent stem cells into the S-phase (By similarity).
CC   -!- INTERACTION:
CC       P40692:MLH1; NbExp=1; IntAct=EBI-712598, EBI-744248;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Expressed in several hemopoietic cell lines
CC       and lymphoid malignant cells. Decreased levels in myeloma cells.
CC   -!- INDUCTION: By alpha interferons. Decreased levels in THP-1 cells
CC       after treatment with recombinant interferon-lambda.
CC   -!- SIMILARITY: Belongs to the thymosin beta family.
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DR   EMBL; M17733; AAA36745.1; -; mRNA.
DR   EMBL; AJ295158; CAC43317.1; -; Genomic_DNA.
DR   EMBL; BT007090; AAP35753.1; -; mRNA.
DR   EMBL; X02493; CAA26323.1; -; mRNA.
DR   IPI; IPI00220828; -.
DR   PIR; I56000; A38682.
DR   RefSeq; NP_066932.1; -.
DR   UniGene; Hs.522584; -.
DR   UniGene; Hs.703237; -.
DR   PDB; 1UY5; Model; -; T=2-44.
DR   PDBsum; 1UY5; -.
DR   DisProt; DP00357; -.
DR   IntAct; P62328; 8.
DR   STRING; P62328; -.
DR   PhosphoSite; P62328; -.
DR   DOSAC-COBS-2DPAGE; P62328; -.
DR   PRIDE; P62328; -.
DR   Ensembl; ENST00000380633; ENSP00000370007; ENSG00000205542; Homo sapiens.
DR   Ensembl; ENST00000380635; ENSP00000370009; ENSG00000205542; Homo sapiens.
DR   Ensembl; ENST00000380636; ENSP00000370010; ENSG00000205542; Homo sapiens.
DR   Ensembl; ENST00000380638; ENSP00000370012; ENSG00000205542; Homo sapiens.
DR   Ensembl; ENST00000451311; ENSP00000414376; ENSG00000205542; Homo sapiens.
DR   GeneID; 7114; -.
DR   KEGG; hsa:7114; -.
DR   UCSC; uc004cvf.1; human.
DR   CTD; 7114; -.
DR   GeneCards; GC0XP012903; -.
DR   H-InvDB; HIX0016658; -.
DR   HGNC; HGNC:11881; TMSB4X.
DR   MIM; 300159; gene.
DR   PharmGKB; PA36581; -.
DR   HOGENOM; P62328; -.
DR   HOVERGEN; P62328; -.
DR   Reactome; REACT_604; Hemostasis.
DR   NextBio; 27851; -.
DR   ArrayExpress; P62328; -.
DR   Bgee; P62328; -.
DR   CleanEx; HS_TMSB4X; -.
DR   Genevestigator; P62328; -.
DR   GermOnline; ENSG00000205542; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0042989; P:sequestering of actin monomers; IEA:InterPro.
DR   InterPro; IPR001152; Thymosin_b4.
DR   InterPro; IPR016323; Thymosin_b4_chordata.
DR   Gene3D; G3DSA:1.20.5.520; Thymosin_b4; 1.
DR   Pfam; PF01290; Thymosin; 1.
DR   PIRSF; PIRSF001828; Thymosin_beta; 1.
DR   ProDom; PD005116; Thymosin_b4; 1.
DR   SMART; SM00152; THY; 1.
DR   PROSITE; PS00500; THYMOSIN_B4; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Actin-binding; Complete proteome;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing; Phosphoprotein.
FT   INIT_MET      1      1       Removed.
FT   PEPTIDE       2     44       Thymosin beta-4.
FT                                /FTId=PRO_0000045920.
FT   PEPTIDE       2      5       Hematopoietic system regulatory peptide
FT                                (By similarity).
FT                                /FTId=PRO_0000034295.
FT   MOD_RES       2      2       N-acetylserine.
FT   MOD_RES       4      4       N6-acetyllysine.
FT   MOD_RES      12     12       N6-acetyllysine.
FT   MOD_RES      23     23       Phosphothreonine (By similarity).
FT   MOD_RES      26     26       N6-acetyllysine.
FT   MOD_RES      32     32       N6-acetyllysine.
FT   MOD_RES      39     39       N6-acetyllysine.
FT   MUTAGEN      12     12       K->P: Very weak actin binding; no
FT                                inhibition of actin polymerization.
FT   MUTAGEN      16     16       S->A: Binds actin 2.5-fold less than
FT                                wild-type; little change in inhibition of
FT                                actin polymerization.
FT   MUTAGEN      16     16       S->AS: Very weak actin binding; no
FT                                inhibition of actin polymerization.
FT   MUTAGEN      18     18       L->A,P: Very weak actin binding; no
FT                                inhibition of actin polymerization.
SQ   SEQUENCE   44 AA;  5053 MW;  440C6158482DAAD0 CRC64;
     MSDKPDMAEI EKFDKSKLKK TETQEKNPLP SKETIEQEKQ AGES
//