UniProt ID | TYB4_HUMAN | |
---|---|---|
UniProt AC | P62328 | |
Protein Name | Thymosin beta-4 | |
Gene Name | TMSB4X | |
Organism | Homo sapiens (Human). | |
Sequence Length | 44 | |
Subcellular Localization | Cytoplasm, cytoskeleton. | |
Protein Description | 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.. | |
Protein Sequence | MSDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSDKPDMAE ------CCCCCCHHH | 55.10 | 29255136 | |
2 | Acetylation | ------MSDKPDMAE ------CCCCCCHHH | 55.10 | 20068231 | |
4 | Methylation | ----MSDKPDMAEIE ----CCCCCCHHHHH | 35.29 | 19608861 | |
4 | Acetylation | ----MSDKPDMAEIE ----CCCCCCHHHHH | 35.29 | 19608861 | |
4 | Trimethylation | ----MSDKPDMAEIE ----CCCCCCHHHHH | 35.29 | - | |
4 | Ubiquitination | ----MSDKPDMAEIE ----CCCCCCHHHHH | 35.29 | 19608861 | |
12 | Acetylation | PDMAEIEKFDKSKLK CCHHHHHHHCHHHHC | 65.60 | 19608861 | |
12 | Ubiquitination | PDMAEIEKFDKSKLK CCHHHHHHHCHHHHC | 65.60 | 19608861 | |
12 | Succinylation | PDMAEIEKFDKSKLK CCHHHHHHHCHHHHC | 65.60 | 23954790 | |
12 | Sumoylation | PDMAEIEKFDKSKLK CCHHHHHHHCHHHHC | 65.60 | 28112733 | |
15 | Acetylation | AEIEKFDKSKLKKTE HHHHHHCHHHHCCCC | 53.26 | 12433517 | |
15 | Ubiquitination | AEIEKFDKSKLKKTE HHHHHHCHHHHCCCC | 53.26 | - | |
16 | Phosphorylation | EIEKFDKSKLKKTET HHHHHCHHHHCCCCC | 45.10 | 28464451 | |
17 | Acetylation | IEKFDKSKLKKTETQ HHHHCHHHHCCCCCC | 70.80 | 19809627 | |
19 | Acetylation | KFDKSKLKKTETQEK HHCHHHHCCCCCCCC | 62.48 | - | |
20 | Ubiquitination | FDKSKLKKTETQEKN HCHHHHCCCCCCCCC | 63.13 | - | |
21 | Phosphorylation | DKSKLKKTETQEKNP CHHHHCCCCCCCCCC | 42.55 | 30266825 | |
23 | Phosphorylation | SKLKKTETQEKNPLP HHHCCCCCCCCCCCC | 47.46 | 23401153 | |
26 | Acetylation | KKTETQEKNPLPSKE CCCCCCCCCCCCCHH | 54.79 | 19608861 | |
26 | Ubiquitination | KKTETQEKNPLPSKE CCCCCCCCCCCCCHH | 54.79 | 21906983 | |
31 | Phosphorylation | QEKNPLPSKETIEQE CCCCCCCCHHHHHHH | 51.29 | 23401153 | |
32 | Ubiquitination | EKNPLPSKETIEQEK CCCCCCCHHHHHHHH | 57.86 | 19608861 | |
32 | Acetylation | EKNPLPSKETIEQEK CCCCCCCHHHHHHHH | 57.86 | 19608861 | |
32 | Succinylation | EKNPLPSKETIEQEK CCCCCCCHHHHHHHH | 57.86 | 23954790 | |
34 | Phosphorylation | NPLPSKETIEQEKQA CCCCCHHHHHHHHHH | 33.28 | 29255136 | |
39 | Acetylation | KETIEQEKQAGES-- HHHHHHHHHHCCC-- | 45.18 | 19608861 | |
39 | Ubiquitination | KETIEQEKQAGES-- HHHHHHHHHHCCC-- | 45.18 | 21906983 | |
44 | Phosphorylation | QEKQAGES------- HHHHHCCC------- | 44.60 | 23401153 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of TYB4_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TYB4_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of TYB4_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ACTS_HUMAN | ACTA1 | physical | 11812134 | |
ACTG_HUMAN | ACTG1 | physical | 8617195 | |
MLH1_HUMAN | MLH1 | physical | 20706999 | |
TRIP6_HUMAN | TRIP6 | physical | 25416956 | |
PNMA1_HUMAN | PNMA1 | physical | 25416956 | |
RBPMS_HUMAN | RBPMS | physical | 25416956 | |
K1C40_HUMAN | KRT40 | physical | 25416956 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-4; LYS-12; LYS-26; LYS-32AND LYS-39, AND MASS SPECTROMETRY. |