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Protein

Thymosin beta-4

Gene

TMSB4X

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

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

  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-HSA-114608. Platelet degranulation.

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
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:11881. TMSB4X.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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.

Polymorphism and mutation databases

BioMutaiTMSB4X.
DMDMi78103211.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources2 Publications
Chaini2 – 4443Thymosin beta-41 PublicationPRO_0000045920Add
BLAST
Peptidei2 – 54Hematopoietic system regulatory peptideBy similarityPRO_0000034295

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources2 Publications
Modified residuei2 – 21PhosphoserineCombined sources
Modified residuei4 – 41N6-acetyllysineCombined sources
Modified residuei12 – 121N6-acetyllysineCombined sources
Modified residuei23 – 231PhosphothreonineCombined sources
Modified residuei26 – 261N6-acetyllysineCombined sources
Modified residuei31 – 311PhosphoserineCombined sources
Modified residuei32 – 321N6-acetyllysineCombined sources
Modified residuei34 – 341PhosphothreonineCombined sources
Modified residuei39 – 391N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP62328.
MaxQBiP62328.
PaxDbiP62328.
PeptideAtlasiP62328.
PRIDEiP62328.
TopDownProteomicsiP62328.

2D gel databases

DOSAC-COBS-2DPAGEP62328.

PTM databases

iPTMnetiP62328.
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.
ExpressionAtlasiP62328. baseline and differential.
GenevisibleiP62328. HS.

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. 28 interactions.
IntActiP62328. 28 interactions.
MINTiMINT-6542280.
STRINGi9606.ENSP00000370007.

Structurei

Secondary structure

1
44
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 126Combined sources
Helixi15 – 173Combined sources
Helixi32 – 398Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UY5model-T2-44[»]
3TU5X-ray3.00B21-44[»]
4PL7X-ray2.30A/B2-44[»]
4PL8X-ray2.00H2-44[»]
DisProtiDP00357.
ProteinModelPortaliP62328.
SMRiP62328. Positions 6-41.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thymosin beta family.Curated

Phylogenomic databases

eggNOGiKOG4794. Eukaryota.
ENOG410Y3I4. LUCA.
GeneTreeiENSGT00390000007040.
HOVERGENiHBG012534.
InParanoidiP62328.
KOiK05764.
OrthoDBiEOG7TJ3MT.
PhylomeDBiP62328.

Family and domain databases

Gene3Di1.20.5.520. 1 hit.
InterProiIPR001152. Beta-thymosin.
[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

        10         20         30         40 
MSDKPDMAEI EKFDKSKLKK TETQEKNPLP SKETIEQEKQ AGES
Length:44
Mass (Da):5,053
Last modified:January 23, 2007 - v2
Checksum:i440C6158482DAAD0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UY5model-T2-44[»]
3TU5X-ray3.00B21-44[»]
4PL7X-ray2.30A/B2-44[»]
4PL8X-ray2.00H2-44[»]
DisProtiDP00357.
ProteinModelPortaliP62328.
SMRiP62328. Positions 6-41.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112969. 28 interactions.
IntActiP62328. 28 interactions.
MINTiMINT-6542280.
STRINGi9606.ENSP00000370007.

PTM databases

iPTMnetiP62328.
PhosphoSiteiP62328.

Polymorphism and mutation databases

BioMutaiTMSB4X.
DMDMi78103211.

2D gel databases

DOSAC-COBS-2DPAGEP62328.

Proteomic databases

EPDiP62328.
MaxQBiP62328.
PaxDbiP62328.
PeptideAtlasiP62328.
PRIDEiP62328.
TopDownProteomicsiP62328.

Protocols and materials databases

DNASUi7114.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000380633; ENSP00000370007; ENSG00000205542.
ENST00000380635; ENSP00000370009; ENSG00000205542.
ENST00000380636; ENSP00000370010; ENSG00000205542.
ENST00000451311; ENSP00000414376; ENSG00000205542.
GeneIDi7114.
KEGGihsa:7114.
UCSCiuc004cvf.4. human.

Organism-specific databases

CTDi7114.
GeneCardsiTMSB4X.
HGNCiHGNC:11881. TMSB4X.
HPAiCAB033806.
MIMi300159. gene.
neXtProtiNX_P62328.
PharmGKBiPA36581.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4794. Eukaryota.
ENOG410Y3I4. LUCA.
GeneTreeiENSGT00390000007040.
HOVERGENiHBG012534.
InParanoidiP62328.
KOiK05764.
OrthoDBiEOG7TJ3MT.
PhylomeDBiP62328.

Enzyme and pathway databases

ReactomeiR-HSA-114608. Platelet degranulation.

Miscellaneous databases

ChiTaRSiTMSB4X. human.
GeneWikiiThymosin_beta-4.
GenomeRNAii7114.
PROiP62328.
SOURCEiSearch...

Gene expression databases

BgeeiP62328.
CleanExiHS_TMSB4X.
ExpressionAtlasiP62328. baseline and differential.
GenevisibleiP62328. HS.

Family and domain databases

Gene3Di1.20.5.520. 1 hit.
InterProiIPR001152. Beta-thymosin.
[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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "Human basal tear peptidome characterization by CID, HCD, and ETD followed by in silico and in vitro analyses for antimicrobial peptide identification."
    Azkargorta M., Soria J., Ojeda C., Guzman F., Acera A., Iloro I., Suarez T., Elortza F.
    J. Proteome Res. 14:2649-2658(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-44, IDENTIFICATION BY MASS SPECTROMETRY, ACETYLATION AT SER-2.
    Tissue: Tear.
  6. "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.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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-4; LYS-12; LYS-26; LYS-32 AND LYS-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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 SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-23; SER-31 AND THR-34, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  14. "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.
  15. 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: July 6, 2016
This is version 126 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.