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Thymosin beta-4 (T beta-4) (Fx) [Cleaved into: Hematopoietic system regulatory peptide (Seraspenide)]

 TYB4_HUMAN              Reviewed;          44 AA.
P62328; P01253; P01254; Q546P5; Q63576; Q9UE55;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
12-SEP-2018, entry version 146.
RecName: Full=Thymosin beta-4;
Short=T beta-4;
AltName: Full=Fx;
Contains:
RecName: Full=Hematopoietic system regulatory peptide;
AltName: Full=Seraspenide;
Name=TMSB4X; Synonyms=TB4X, THYB4, TMSB4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND TISSUE SPECIFICITY.
TISSUE=Peripheral blood leukocyte;
PubMed=3500230;
Gondo H., Kudo J., White J.W., Barr C., Selvanayagam P.,
Saunders G.F.;
"Differential expression of the human thymosin-beta 4 gene in
lymphocytes, macrophages, and granulocytes.";
J. Immunol. 139:3840-3848(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=16010977; DOI=10.1007/s11010-005-7642-4;
Yang S.P., Lee H.J., Su Y.;
"Molecular cloning and structural characterization of the functional
human thymosin beta4 gene.";
Mol. Cell. Biochem. 272:97-105(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 2-44, INTERACTION WITH ACTIN, CLEAVAGE OF
INITIATOR METHIONINE, AND ACETYLATION AT SER-2.
PubMed=1999398;
Safer D., Elzinga M., Nachmias V.T.;
"Thymosin beta 4 and Fx, an actin-sequestering peptide, are
indistinguishable.";
J. Biol. Chem. 266:4029-4032(1991).
[5]
PROTEIN SEQUENCE OF 2-44, IDENTIFICATION BY MASS SPECTROMETRY, AND
ACETYLATION AT SER-2.
TISSUE=Tear;
PubMed=25946035; DOI=10.1021/acs.jproteome.5b00179;
Azkargorta M., Soria J., Ojeda C., Guzman F., Acera A., Iloro I.,
Suarez T., Elortza F.;
"Human basal tear peptidome characterization by CID, HCD, and ETD
followed by in silico and in vitro analyses for antimicrobial peptide
identification.";
J. Proteome Res. 14:2649-2658(2015).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 8-44, AND INDUCTION.
PubMed=6548414; DOI=10.1016/0092-8674(84)90270-8;
Friedman R.L., Manly S.P., McMahon M., Kerr I.M., Stark G.R.;
"Transcriptional and posttranscriptional regulation of interferon-
induced gene expression in human cells.";
Cell 38:745-755(1984).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-4; LYS-12; LYS-26; LYS-32
AND LYS-39, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE
SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE
SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-23; SER-31 AND
THR-34, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-12, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[15]
STRUCTURE BY NMR OF WILD-TYPE AND OF MUTANTS LYS-12; SER-16 AND LEU-18
IN COMPLEX WITH ACTIN.
PubMed=10848969; DOI=10.1046/j.1432-1327.2000.01380.x;
Simenel C., Van Troys M., Vandekerckhove J., Ampe C., Delepierre M.;
"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.";
Eur. J. Biochem. 267:3530-3538(2000).
[16]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 21-44 IN COMPLEX WITH ACTA1;
GSN AND COBL, AND SUBUNIT.
PubMed=23009842; DOI=10.1016/j.bpj.2012.07.030;
Durer Z.A., Kudryashov D.S., Sawaya M.R., Altenbach C., Hubbell W.,
Reisler E.;
"Structural states and dynamics of the D-loop in actin.";
Biophys. J. 103:930-939(2012).
-!- FUNCTION: 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.
{ECO:0000250}.
-!- FUNCTION: Seraspenide inhibits the entry of hematopoietic
pluripotent stem cells into the S-phase. {ECO:0000250}.
-!- SUBUNIT: Interacts with SERPINB1 (By similarity). Identified in a
complex composed of ACTA1, COBL, GSN AND TMSB4X. {ECO:0000250,
ECO:0000269|PubMed:10848969, ECO:0000269|PubMed:1999398,
ECO:0000269|PubMed:23009842}.
-!- INTERACTION:
P40692:MLH1; NbExp=16; IntAct=EBI-712598, EBI-744248;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
-!- TISSUE SPECIFICITY: Expressed in several hemopoietic cell lines
and lymphoid malignant cells. Decreased levels in myeloma cells.
{ECO:0000269|PubMed:3500230}.
-!- INDUCTION: By alpha interferons. Decreased levels in THP-1 cells
after treatment with recombinant interferon-lambda.
{ECO:0000269|PubMed:3500230, ECO:0000269|PubMed:6548414}.
-!- SIMILARITY: Belongs to the thymosin beta family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M17733; AAA36745.1; -; mRNA.
EMBL; AJ295158; CAC43317.1; -; Genomic_DNA.
EMBL; BT007090; AAP35753.1; -; mRNA.
EMBL; X02493; CAA26323.1; -; mRNA.
CCDS; CCDS35202.1; -.
PIR; I56000; A38682.
RefSeq; NP_066932.1; NM_021109.3.
UniGene; Hs.437277; -.
UniGene; Hs.703237; -.
PDB; 1UY5; Model; -; T=2-44.
PDB; 3TU5; X-ray; 3.00 A; B=21-44.
PDB; 4PL7; X-ray; 2.30 A; A/B=2-44.
PDB; 4PL8; X-ray; 2.00 A; H=2-44.
PDBsum; 1UY5; -.
PDBsum; 3TU5; -.
PDBsum; 4PL7; -.
PDBsum; 4PL8; -.
DisProt; DP00357; -.
ProteinModelPortal; P62328; -.
SMR; P62328; -.
BioGrid; 112969; 28.
IntAct; P62328; 39.
MINT; P62328; -.
STRING; 9606.ENSP00000370007; -.
MoonDB; P62328; Curated.
MoonProt; P62328; -.
iPTMnet; P62328; -.
PhosphoSitePlus; P62328; -.
BioMuta; TMSB4X; -.
DMDM; 78103211; -.
DOSAC-COBS-2DPAGE; P62328; -.
EPD; P62328; -.
MaxQB; P62328; -.
PaxDb; P62328; -.
PeptideAtlas; P62328; -.
PRIDE; P62328; -.
ProteomicsDB; 57395; -.
TopDownProteomics; P62328; -.
DNASU; 7114; -.
Ensembl; ENST00000380633; ENSP00000370007; ENSG00000205542.
Ensembl; ENST00000380635; ENSP00000370009; ENSG00000205542.
Ensembl; ENST00000380636; ENSP00000370010; ENSG00000205542.
Ensembl; ENST00000451311; ENSP00000414376; ENSG00000205542.
GeneID; 7114; -.
KEGG; hsa:7114; -.
UCSC; uc004cvf.4; human.
CTD; 7114; -.
DisGeNET; 7114; -.
EuPathDB; HostDB:ENSG00000205542.10; -.
GeneCards; TMSB4X; -.
HGNC; HGNC:11881; TMSB4X.
HPA; CAB033806; -.
MIM; 300159; gene.
neXtProt; NX_P62328; -.
OpenTargets; ENSG00000205542; -.
PharmGKB; PA36581; -.
eggNOG; KOG4794; Eukaryota.
eggNOG; ENOG410Y3I4; LUCA.
GeneTree; ENSGT00390000007040; -.
HOVERGEN; HBG012534; -.
InParanoid; P62328; -.
KO; K05764; -.
OrthoDB; EOG091G1AVI; -.
PhylomeDB; P62328; -.
Reactome; R-HSA-114608; Platelet degranulation.
ChiTaRS; TMSB4X; human.
GeneWiki; Thymosin_beta-4; -.
GenomeRNAi; 7114; -.
PRO; PR:P62328; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000205542; Expressed in 91 organ(s), highest expression level in blood.
CleanEx; HS_TMSB4X; -.
ExpressionAtlas; P62328; baseline and differential.
Genevisible; P62328; HS.
GO; GO:0005737; C:cytoplasm; IDA:CAFA.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:CAFA.
GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
GO; GO:0005622; C:intracellular; IDA:CAFA.
GO; GO:0005634; C:nucleus; IDA:CAFA.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0003785; F:actin monomer binding; IDA:CAFA.
GO; GO:0019899; F:enzyme binding; IPI:CAFA.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0007015; P:actin filament organization; IEA:InterPro.
GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; IMP:CAFA.
GO; GO:2000483; P:negative regulation of interleukin-8 secretion; IDA:CAFA.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:CAFA.
GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; IMP:CAFA.
GO; GO:1903026; P:negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding; IDA:CAFA.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IDA:CAFA.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IDA:CAFA.
GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; IDA:CAFA.
GO; GO:1905273; P:positive regulation of proton-transporting ATP synthase activity, rotational mechanism; IDA:CAFA.
GO; GO:0050727; P:regulation of inflammatory response; IMP:CAFA.
GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; IGI:CAFA.
GO; GO:0042989; P:sequestering of actin monomers; IDA:CAFA.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:CAFA.
Gene3D; 1.20.5.520; -; 1.
InterPro; IPR001152; Beta-thymosin.
InterPro; IPR038386; Beta-thymosin_sf.
PANTHER; PTHR12021; PTHR12021; 1.
Pfam; PF01290; Thymosin; 1.
PIRSF; PIRSF001828; Thymosin_beta; 1.
ProDom; PD005116; Thymosin_b4; 1.
SMART; SM00152; THY; 1.
PROSITE; PS00500; THYMOSIN_B4; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Actin-binding; Complete proteome;
Cytoplasm; Cytoskeleton; Direct protein sequencing; Isopeptide bond;
Phosphoprotein; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000269|PubMed:1999398,
ECO:0000269|PubMed:25946035}.
CHAIN 2 44 Thymosin beta-4.
{ECO:0000269|PubMed:25946035}.
/FTId=PRO_0000045920.
PEPTIDE 2 5 Hematopoietic system regulatory peptide.
{ECO:0000250}.
/FTId=PRO_0000034295.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000269|PubMed:1999398,
ECO:0000269|PubMed:25946035}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 4 4 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 12 12 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 23 23 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 26 26 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 31 31 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 32 32 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 34 34 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 39 39 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
CROSSLNK 12 12 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
MUTAGEN 12 12 K->P: Very weak actin binding; no
inhibition of actin polymerization.
MUTAGEN 16 16 S->A: Binds actin 2.5-fold less than
wild-type; little change in inhibition of
actin polymerization.
MUTAGEN 16 16 S->AS: Very weak actin binding; no
inhibition of actin polymerization.
MUTAGEN 18 18 L->A,P: Very weak actin binding; no
inhibition of actin polymerization.
HELIX 6 11 {ECO:0000244|PDB:4PL8}.
HELIX 15 17 {ECO:0000244|PDB:4PL8}.
HELIX 32 39 {ECO:0000244|PDB:4PL7}.
SEQUENCE 44 AA; 5053 MW; 440C6158482DAAD0 CRC64;
MSDKPDMAEI EKFDKSKLKK TETQEKNPLP SKETIEQEKQ AGES


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