| General information | | DisProt: | DP00357 | | Name: | Thymosin beta-4 | | Synonym(s): | TYB4_HUMAN
T beta-4
Actin-sequestering peptide Fx
Fx
Hematopoietic system regulatory peptide [cleavage product 1]
Seraspenide
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | P62328 | | UniGene: | Hs.522584 | | SwissProt: | TYB4_HUMAN | | TrEMBL: | | | NCBI (GI): | 78103211 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 44 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MSDKPDMAEI EKFDKSKLKK TETQEKNPLP SKETIEQEKQ AGES
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| Functional narrative |
The widespread beta-thymosin/WH2 actin binding domain has versatile regulatory properties in actin dynamics and motility. Beta-thymosins (isolated WH2 domain) maintain monomeric actin in a "sequestered" nonpolymerizable form. In contrast, when repeated in tandem or inserted in modular proteins, the beta-thymosin/WH2 domain promotes actin assembly at filament barbed ends, like profilin. Plays an important role in the organization of the cytoskeleton. 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.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | | | Location: | 1 - 44 | | Length: | 44 | | Region sequence: |
MSDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Polymerization
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR)
| References:
- Czisch M, Schleicher M, Hörger S, Voelter W, Holak TA. "Conformation of thymosin beta 4 in water determined by NMR spectroscopy." Eur J Biochem. 1993; 218(2): 335-44. PubMed: 8269922
- Domanski M, Hertzog M, Coutant J, Gutsche-Perelroizen I, Bontems F, Carlier MF, Guittet E, van Heijenoort C. "Coupling of folding and binding of thymosin beta4 upon interaction with monomeric actin monitored by nuclear magnetic resonance." J Biol Chem. 2004; 279(22): 23637-45. PubMed: 15039431
| Comments:
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| References |
- Bubb MR. "Thymosin beta 4 interactions." Vitam Horm. 2003; 66: 297-316. PubMed: 12852258
- Hertzog M, van Heijenoort C, Didry D, Gaudier M, Coutant J, Gigant B, Didelot G, Preat T, Knossow M, Guittet E, Carlier MF. "The beta-thymosin/WH2 domain; structural basis for the switch from inhibition to promotion of actin assembly." Cell. 2004; 117(5): 611-23. PubMed: 15163409
- Paunola E, Mattila PK, Lappalainen P. "WH2 domain: a small, versatile adapter for actin monomers." FEBS Letters. ; 513(1): 92-7. PubMed: 11911886
- Safer D, Sosnick TR, Elzinga M. "Thymosin beta 4 binds actin in an extended conformation and contacts both the barbed and pointed ends." Biochemistry. 1997; 36(19): 5806-16. PubMed: 9153421
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| Comments |
Addtional UniGene ID: Hs.703237
An additional entry may be needed for cleavage product 1.
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