Reviewed, UniProtKB/Swiss-Prot P62328 (TYB4_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	44 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 hematopoeitic pluripotent stem cells into the S-phase By similarity.
Subcellular location	Cytoplasm › cytoskeleton.
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.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Ligand	Actin-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	actin cytoskeleton organization Inferred from electronic annotation. Source: InterPro sequestering of actin monomers Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	actin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MLH1	P40692	1	EBI-712598,EBI-744248

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.4
	Peptide	2 – 44	43	Thymosin beta-4 Ref.4		PRO_0000045920
	Peptide	2 – 5	4	Hematopoietic system regulatory peptide By similarity		PRO_0000034295
Amino acid modifications
	Modified residue	2	1	N-acetylserine
	Modified residue	4	1	N6-acetyllysine Ref.6
	Modified residue	12	1	N6-acetyllysine Ref.6
	Modified residue	23	1	Phosphothreonine By similarity
	Modified residue	26	1	N6-acetyllysine Ref.6
	Modified residue	32	1	N6-acetyllysine Ref.6
	Modified residue	39	1	N6-acetyllysine Ref.6
Experimental info
	Mutagenesis	12	1	K → P: Very weak actin binding; no inhibition of actin polymerization.
	Mutagenesis	16	1	S → A: Binds actin 2.5-fold less than wild-type; little change in inhibition of actin polymerization.
	Mutagenesis	16	1	S → AS: Very weak actin binding; no inhibition of actin polymerization.
	Mutagenesis	18	1	L → A or P: Very weak actin binding; no inhibition of actin polymerization.

Sequences

	Sequence		Length	Mass (Da)
	P62328-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 440C6158482DAAD0	FASTA	44	5,053
	10 20 30 40 MSDKPDMAEI EKFDKSKLKK TETQEKNPLP SKETIEQEKQ AGES

References

	« Hide 'large scale' referencesShow '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: 3500230] [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: 16010977] [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: 1999398] [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: 6548414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-44, INDUCTION.
[6]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-4; LYS-12; LYS-26; LYS-32 AND LYS-39, MASS SPECTROMETRY.
[7]	"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: 10848969] [Abstract] Cited for: STRUCTURE BY NMR OF WILD-TYPE AND OF MUTANTS LYS-12; SER-16 AND LEU-18 IN COMPLEX WITH ACTIN.
+	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.

IPI

IPI00220828.

PIR

A38682. I56000.

RefSeq

NP_066932.1.

UniGene

Hs.522584
Hs.703237

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UY5	model	-	T	2-44	[»]

SMR

P62328. Positions 2-41.

DisProt

DP00357.

ModBase

Search...

Protein-protein interaction databases

IntAct

P62328. 8 interactions.

STRING

P62328.

PTM databases

PhosphoSite

P62328.

2-D gel databases

DOSAC-COBS-2DPAGE

P62328.

Proteomic databases

PRIDE

P62328.

Genome annotation databases

Ensembl

ENST00000380633; ENSP00000370007; ENSG00000205542; Homo sapiens. [Genome view]
ENST00000380635; ENSP00000370009; ENSG00000205542; Homo sapiens. [Genome view]
ENST00000380636; ENSP00000370010; ENSG00000205542; Homo sapiens. [Genome view]
ENST00000380638; ENSP00000370012; ENSG00000205542; Homo sapiens. [Genome view]
ENST00000451311; ENSP00000414376; ENSG00000205542; Homo sapiens. [Genome view]

GeneID

7114.

KEGG

hsa:7114.

UCSC

uc004cvf.1. human.

Organism-specific databases

CTD

7114.

GeneCards

GC0XP012903.

H-InvDB

HIX0016658.
HIX0030597.
HIX0031489.
HIX0040813.

HGNC

HGNC:11881. TMSB4X.

MIM

300159. gene.

PharmGKB

PA36581.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

HBG012534.

InParanoid

P62328.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P62328.

Bgee

P62328.

CleanEx

HS_TMSB4X.

Genevestigator

P62328.

GermOnline

ENSG00000205542. Homo sapiens.

Family and domain databases

InterPro

IPR001152. Thymosin_b4.
IPR016323. Thymosin_b4_chordata.
[Graphical view]

Gene3D

G3DSA:1.20.5.520. Thymosin_b4. 1 hit.

Pfam

PF01290. Thymosin. 1 hit.
[Graphical view]

PIRSF

PIRSF001828. Thymosin_beta. 1 hit.

ProDom

PD005116. Thymosin_b4. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00152. THY. 1 hit.
[Graphical view]

PROSITE

PS00500. THYMOSIN_B4. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

27851.

SOURCE

Search...

Entry information

Entry name

TYB4_HUMAN

Accession

Primary (citable) accession number: P62328
Secondary accession number(s): P01253 , P01254, Q546P5, Q63576, Q9UE55

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	March 2, 2010
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.