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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

  • actin monomer binding Source: CAFA
  • enzyme binding Source: CAFA
  • RNA binding Source: UniProtKB

GO - Biological processi

  • actin filament organization Source: InterPro
  • cytoplasmic sequestering of NF-kappaB Source: CAFA
  • negative regulation of interleukin-8 secretion Source: CAFA
  • negative regulation of NF-kappaB transcription factor activity Source: CAFA
  • negative regulation of NIK/NF-kappaB signaling Source: CAFA
  • negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding Source: CAFA
  • osteoblast differentiation Source: Ensembl
  • platelet degranulation Source: Reactome
  • positive regulation of ATP biosynthetic process Source: CAFA
  • positive regulation of blood vessel endothelial cell migration Source: CAFA
  • positive regulation of endothelial cell chemotaxis Source: CAFA
  • positive regulation of proton-transporting ATP synthase activity, rotational mechanism Source: CAFA
  • regulation of inflammatory response Source: CAFA
  • regulation of NIK/NF-kappaB signaling Source: CAFA
  • sequestering of actin monomers Source: CAFA
  • tumor necrosis factor-mediated signaling pathway Source: CAFA

Keywordsi

Molecular functionActin-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

EuPathDBiHostDB:ENSG00000205542.10.
HGNCiHGNC:11881. TMSB4X.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi12K → P: Very weak actin binding; no inhibition of actin polymerization. 1
Mutagenesisi16S → A: Binds actin 2.5-fold less than wild-type; little change in inhibition of actin polymerization. 1
Mutagenesisi16S → AS: Very weak actin binding; no inhibition of actin polymerization. 1
Mutagenesisi18L → A or P: Very weak actin binding; no inhibition of actin polymerization. 1

Organism-specific databases

DisGeNETi7114.
OpenTargetsiENSG00000205542.
PharmGKBiPA36581.

Polymorphism and mutation databases

BioMutaiTMSB4X.
DMDMi78103211.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources2 Publications
ChainiPRO_00000459202 – 44Thymosin beta-41 PublicationAdd BLAST43
PeptideiPRO_00000342952 – 5Hematopoietic system regulatory peptideBy similarity4

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources2 Publications1
Modified residuei2PhosphoserineCombined sources1
Modified residuei4N6-acetyllysineCombined sources1
Modified residuei12N6-acetyllysine; alternateCombined sources1
Cross-linki12Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei23PhosphothreonineCombined sources1
Modified residuei26N6-acetyllysineCombined sources1
Modified residuei31PhosphoserineCombined sources1
Modified residuei32N6-acetyllysineCombined sources1
Modified residuei34PhosphothreonineCombined sources1
Modified residuei39N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

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

2D gel databases

DOSAC-COBS-2DPAGEiP62328.

PTM databases

iPTMnetiP62328.
PhosphoSitePlusiP62328.

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

BgeeiENSG00000205542.
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

Show more details

GO - Molecular functioni

  • actin monomer binding Source: CAFA
  • enzyme binding Source: CAFA

Protein-protein interaction databases

BioGridi112969. 28 interactors.
IntActiP62328. 39 interactors.
MINTiMINT-6542280.
STRINGi9606.ENSP00000370007.

Structurei

Secondary structure

144
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 11Combined sources6
Helixi15 – 17Combined sources3
Helixi32 – 39Combined sources8

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the thymosin beta family.Curated

Phylogenomic databases

eggNOGiKOG4794. Eukaryota.
ENOG410Y3I4. LUCA.
GeneTreeiENSGT00390000007040.
HOVERGENiHBG012534.
InParanoidiP62328.
KOiK05764.
OrthoDBiEOG091G1AVI.
PhylomeDBiP62328.

Family and domain databases

InterProiView protein in InterPro
IPR001152. Beta-thymosin.
PANTHERiPTHR12021. PTHR12021. 1 hit.
PfamiView protein in Pfam
PF01290. Thymosin. 1 hit.
PIRSFiPIRSF001828. Thymosin_beta. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD005116. Thymosin_b4. 1 hit.
SMARTiView protein in SMART
SM00152. THY. 1 hit.
PROSITEiView protein in PROSITE
PS00500. THYMOSIN_B4. 1 hit.

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.

Similar proteinsi

Entry informationi

Entry nameiTYB4_HUMAN
AccessioniPrimary (citable) accession number: P62328
Secondary accession number(s): P01253
, P01254, Q546P5, Q63576, Q9UE55
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 22, 2017
This is version 138 of the entry and version 2 of the sequence. See 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