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P62328 (TYB4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thymosin beta-4

Short name=T beta-4
Alternative name(s):
Fx

Cleaved into the following chain:

  1. Hematopoietic system regulatory peptide
    Alternative name(s):
    Seraspenide
Gene names
Name:TMSB4X
Synonyms:TB4X, THYB4, TMSB4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length44 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Seraspenide inhibits the entry of hematopoietic pluripotent stem cells into the S-phase By similarity.

Subunit structure

Interacts with SERPINB1 By similarity. Identified in a complex composed of ACTA1, COBL, GSN AND TMSB4X. Ref.4 Ref.10

Subcellular location

Cytoplasmcytoskeleton.

Tissue specificity

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

Induction

By alpha interferons. Decreased levels in THP-1 cells after treatment with recombinant interferon-lambda. Ref.1 Ref.5

Sequence similarities

Belongs to the thymosin beta family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MLH1P4069216EBI-712598,EBI-744248

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 4443Thymosin beta-4
PRO_0000045920
Peptide2 – 54Hematopoietic system regulatory peptide By similarity
PRO_0000034295

Amino acid modifications

Modified residue21N-acetylserine
Modified residue261N6-acetyllysine Ref.7
Modified residue391N6-acetyllysine Ref.7

Experimental info

Mutagenesis121K → P: Very weak actin binding; no inhibition of actin polymerization.
Mutagenesis161S → A: Binds actin 2.5-fold less than wild-type; little change in inhibition of actin polymerization.
Mutagenesis161S → AS: Very weak actin binding; no inhibition of actin polymerization.
Mutagenesis181L → A or P: Very weak actin binding; no inhibition of actin polymerization.

Sequences

Sequence LengthMass (Da)Tools
P62328 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 440C6158482DAAD0

FASTA445,053
        10         20         30         40 
MSDKPDMAEI EKFDKSKLKK TETQEKNPLP SKETIEQEKQ AGES 

« Hide

References

« Hide 'large scale' references
[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.
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Structural states and dynamics of the D-loop in actin."
Durer Z.A., Kudryashov D.S., Sawaya M.R., Altenbach C., Hubbell W., Reisler E.
Biophys. J. 103:930-939(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 21-44 IN COMPLEX WITH ACTA1; GSN AND COBL, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17733 mRNA. Translation: AAA36745.1.
AJ295158 Genomic DNA. Translation: CAC43317.1.
BT007090 mRNA. Translation: AAP35753.1.
X02493 mRNA. Translation: CAA26323.1.
PIRA38682. I56000.
RefSeqNP_066932.1. NM_021109.3.
UniGeneHs.437277.
Hs.703237.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UY5model-T2-44[»]
3TU5X-ray3.00B21-44[»]
DisProtDP00357.
ProteinModelPortalP62328.
SMRP62328. Positions 2-42.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112969. 13 interactions.
IntActP62328. 22 interactions.
MINTMINT-6542280.
STRING9606.ENSP00000370007.

PTM databases

PhosphoSiteP62328.

Polymorphism databases

DMDM78103211.

2D gel databases

DOSAC-COBS-2DPAGEP62328.

Proteomic databases

PaxDbP62328.
PRIDEP62328.

Protocols and materials databases

DNASU7114.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000380633; ENSP00000370007; ENSG00000205542.
ENST00000380635; ENSP00000370009; ENSG00000205542.
ENST00000380636; ENSP00000370010; ENSG00000205542.
ENST00000451311; ENSP00000414376; ENSG00000205542.
GeneID7114.
KEGGhsa:7114.
UCSCuc004cvf.3. human.

Organism-specific databases

CTD7114.
GeneCardsGC0XP012993.
HGNCHGNC:11881. TMSB4X.
HPACAB033806.
MIM300159. gene.
neXtProtNX_P62328.
PharmGKBPA36581.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG126035.
HOVERGENHBG012534.
InParanoidP62328.
KOK05764.
OrthoDBEOG7TJ3MT.
PhylomeDBP62328.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

BgeeP62328.
CleanExHS_TMSB4X.
GenevestigatorP62328.

Family and domain databases

Gene3D1.20.5.520. 1 hit.
InterProIPR001152. Thymosin_b4.
IPR016323. Thymosin_b4_metazoa.
[Graphical view]
PANTHERPTHR12021. PTHR12021. 1 hit.
PfamPF01290. Thymosin. 1 hit.
[Graphical view]
PIRSFPIRSF001828. Thymosin_beta. 1 hit.
ProDomPD005116. Thymosin_b4. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00152. THY. 1 hit.
[Graphical view]
PROSITEPS00500. THYMOSIN_B4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTMSB4X. human.
GeneWikiThymosin_beta-4.
GenomeRNAi7114.
NextBio27851.
PROP62328.
SOURCESearch...

Entry information

Entry nameTYB4_HUMAN
AccessionPrimary (citable) accession number: P62328
Secondary accession number(s): P01253 expand/collapse secondary AC list , P01254, Q546P5, Q63576, Q9UE55
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM