TYB4_HUMAN - dbPTM
TYB4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSDKPDMAE
------CCCCCCHHH
55.1029255136
2Acetylation------MSDKPDMAE
------CCCCCCHHH
55.1020068231
4Methylation----MSDKPDMAEIE
----CCCCCCHHHHH
35.2919608861
4Acetylation----MSDKPDMAEIE
----CCCCCCHHHHH
35.2919608861
4Trimethylation----MSDKPDMAEIE
----CCCCCCHHHHH
35.29-
4Ubiquitination----MSDKPDMAEIE
----CCCCCCHHHHH
35.2919608861
12AcetylationPDMAEIEKFDKSKLK
CCHHHHHHHCHHHHC
65.6019608861
12UbiquitinationPDMAEIEKFDKSKLK
CCHHHHHHHCHHHHC
65.6019608861
12SuccinylationPDMAEIEKFDKSKLK
CCHHHHHHHCHHHHC
65.6023954790
12SumoylationPDMAEIEKFDKSKLK
CCHHHHHHHCHHHHC
65.6028112733
15AcetylationAEIEKFDKSKLKKTE
HHHHHHCHHHHCCCC
53.2612433517
15UbiquitinationAEIEKFDKSKLKKTE
HHHHHHCHHHHCCCC
53.26-
16PhosphorylationEIEKFDKSKLKKTET
HHHHHCHHHHCCCCC
45.1028464451
17AcetylationIEKFDKSKLKKTETQ
HHHHCHHHHCCCCCC
70.8019809627
19AcetylationKFDKSKLKKTETQEK
HHCHHHHCCCCCCCC
62.48-
20UbiquitinationFDKSKLKKTETQEKN
HCHHHHCCCCCCCCC
63.13-
21PhosphorylationDKSKLKKTETQEKNP
CHHHHCCCCCCCCCC
42.5530266825
23PhosphorylationSKLKKTETQEKNPLP
HHHCCCCCCCCCCCC
47.4623401153
26AcetylationKKTETQEKNPLPSKE
CCCCCCCCCCCCCHH
54.7919608861
26UbiquitinationKKTETQEKNPLPSKE
CCCCCCCCCCCCCHH
54.7921906983
31PhosphorylationQEKNPLPSKETIEQE
CCCCCCCCHHHHHHH
51.2923401153
32UbiquitinationEKNPLPSKETIEQEK
CCCCCCCHHHHHHHH
57.8619608861
32AcetylationEKNPLPSKETIEQEK
CCCCCCCHHHHHHHH
57.8619608861
32SuccinylationEKNPLPSKETIEQEK
CCCCCCCHHHHHHHH
57.8623954790
34PhosphorylationNPLPSKETIEQEKQA
CCCCCHHHHHHHHHH
33.2829255136
39AcetylationKETIEQEKQAGES--
HHHHHHHHHHCCC--
45.1819608861
39UbiquitinationKETIEQEKQAGES--
HHHHHHHHHHCCC--
45.1821906983
44PhosphorylationQEKQAGES-------
HHHHHCCC-------
44.6023401153

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TYB4_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACTS_HUMANACTA1physical
11812134
ACTG_HUMANACTG1physical
8617195
MLH1_HUMANMLH1physical
20706999
TRIP6_HUMANTRIP6physical
25416956
PNMA1_HUMANPNMA1physical
25416956
RBPMS_HUMANRBPMSphysical
25416956
K1C40_HUMANKRT40physical
25416956

Drug and Disease Associations
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.
Regulatory Network of TYB4_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.

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