dbPTM

TYB10_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TYB10_HUMAN
UniProt AC	P63313
Protein Name	Thymosin beta-10
Gene Name	TMSB10
Organism	Homo sapiens (Human).
Sequence Length	44
Subcellular Localization	Cytoplasm, cytoskeleton.
Protein Description	Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization (By similarity)..
Protein Sequence	MADKPDMGEIASFDKAKLKKTETQEKNTLPTKETIEQEKRSEIS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADKPDMGE ------CCCCCCHHH	33.27	19413330
4	Acetylation	----MADKPDMGEIA ----CCCCCCHHHHC	33.12	19608861
4	Trimethylation	----MADKPDMGEIA ----CCCCCCHHHHC	33.12	-
4	Ubiquitination	----MADKPDMGEIA ----CCCCCCHHHHC	33.12	33845483
4	Methylation	----MADKPDMGEIA ----CCCCCCHHHHC	33.12	-
7	Sulfoxidation	-MADKPDMGEIASFD -CCCCCCHHHHCCCC	7.62	28183972
12	Phosphorylation	PDMGEIASFDKAKLK CCHHHHCCCCHHHHC	39.37	29255136
15	Acetylation	GEIASFDKAKLKKTE HHHCCCCHHHHCCCC	45.47	19608861
15	Ubiquitination	GEIASFDKAKLKKTE HHHCCCCHHHHCCCC	45.47	21906983
15	Methylation	GEIASFDKAKLKKTE HHHCCCCHHHHCCCC	45.47	12433529
17	Acetylation	IASFDKAKLKKTETQ HCCCCHHHHCCCCCC	67.58	21466224
17	Ubiquitination	IASFDKAKLKKTETQ HCCCCHHHHCCCCCC	67.58	22817900
19	Ubiquitination	SFDKAKLKKTETQEK CCCHHHHCCCCCCCC	57.87	22817900
20	Ubiquitination	FDKAKLKKTETQEKN CCHHHHCCCCCCCCC	63.13	22817900
21	Phosphorylation	DKAKLKKTETQEKNT CHHHHCCCCCCCCCC	42.55	19664994
23	Phosphorylation	AKLKKTETQEKNTLP HHHCCCCCCCCCCCC	47.46	23911959
26	Acetylation	KKTETQEKNTLPTKE CCCCCCCCCCCCCHH	45.47	23236377
26	Ubiquitination	KKTETQEKNTLPTKE CCCCCCCCCCCCCHH	45.47	27667366
28	O-linked_Glycosylation	TETQEKNTLPTKETI CCCCCCCCCCCHHHH	45.22	30831877
28	Phosphorylation	TETQEKNTLPTKETI CCCCCCCCCCCHHHH	45.22	23403867
31	Phosphorylation	QEKNTLPTKETIEQE CCCCCCCCHHHHHHH	44.62	19664994
31	O-linked_Glycosylation	QEKNTLPTKETIEQE CCCCCCCCHHHHHHH	44.62	19664994
32	Ubiquitination	EKNTLPTKETIEQEK CCCCCCCHHHHHHHH	51.42	21890473
32	Ubiquitination	EKNTLPTKETIEQEK CCCCCCCHHHHHHHH	51.42	27667366
32	Acetylation	EKNTLPTKETIEQEK CCCCCCCHHHHHHHH	51.42	23954790
34	Phosphorylation	NTLPTKETIEQEKRS CCCCCHHHHHHHHHH	31.22	30243723
39	Ubiquitination	KETIEQEKRSEIS-- HHHHHHHHHHHCC--	62.00	32015554
39	Acetylation	KETIEQEKRSEIS-- HHHHHHHHHHHCC--	62.00	19608861
41	Phosphorylation	TIEQEKRSEIS---- HHHHHHHHHCC----	50.80	25159151
44	Phosphorylation	QEKRSEIS------- HHHHHHCC-------	30.07	23403867

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 TYB10_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TYB10_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 TYB10_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
YRDC_HUMAN	YRDC	physical	22939629
KRA92_HUMAN	KRTAP9-2	physical	25416956
LEG3_HUMAN	LGALS3	physical	26344197
PROF1_HUMAN	PFN1	physical	26344197

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 TYB10_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-15; LYS-26 ANDLYS-39, AND MASS SPECTROMETRY.	19608861 [Abstract]
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-4, AND MASS SPECTROMETRY.	16916647 [Abstract]
Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-23, AND MASSSPECTROMETRY.	18669648 [Abstract]