dbPTM

S10AB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	S10AB_HUMAN
UniProt AC	P31949
Protein Name	Protein S100-A11
Gene Name	S100A11
Organism	Homo sapiens (Human).
Sequence Length	105
Subcellular Localization	Cytoplasm . Nucleus .
Protein Description	Facilitates the differentiation and the cornification of keratinocytes..
Protein Sequence	MAKISSPTETERCIESLIAVFQKYAGKDGYNYTLSKTEFLSFMNTELAAFTKNQKDPGVLDRMMKKLDTNSDGQLDFSEFLNLIGGLAMACHDSFLKAVPSQKRT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MAKISSPT -------CCCCCCCH	8.49	22814378
2	Acetylation	------MAKISSPTE ------CCCCCCCHH	20.21	22814378
3	Ubiquitination	-----MAKISSPTET -----CCCCCCCHHH	41.65	19608861
3	Acetylation	-----MAKISSPTET -----CCCCCCCHHH	41.65	19608861
3	2-Hydroxyisobutyrylation	-----MAKISSPTET -----CCCCCCCHHH	41.65	-
5	Phosphorylation	---MAKISSPTETER ---CCCCCCCHHHHH	29.56	29255136
6	Phosphorylation	--MAKISSPTETERC --CCCCCCCHHHHHH	39.04	29255136
8	Phosphorylation	MAKISSPTETERCIE CCCCCCCHHHHHHHH	58.44	23927012
10	Phosphorylation	KISSPTETERCIESL CCCCCHHHHHHHHHH	31.07	23927012
13	S-nitrosocysteine	SPTETERCIESLIAV CCHHHHHHHHHHHHH	3.09	-
13	S-nitrosylation	SPTETERCIESLIAV CCHHHHHHHHHHHHH	3.09	18335467
16	Phosphorylation	ETERCIESLIAVFQK HHHHHHHHHHHHHHH	12.74	23090842
23	Ubiquitination	SLIAVFQKYAGKDGY HHHHHHHHHCCCCCC	26.13	21906983
23	Acetylation	SLIAVFQKYAGKDGY HHHHHHHHHCCCCCC	26.13	26051181
24	Phosphorylation	LIAVFQKYAGKDGYN HHHHHHHHCCCCCCC	15.14	26356563
27	Malonylation	VFQKYAGKDGYNYTL HHHHHCCCCCCCEEE	39.55	32601280
27	Ubiquitination	VFQKYAGKDGYNYTL HHHHHCCCCCCCEEE	39.55	21890473
27	Acetylation	VFQKYAGKDGYNYTL HHHHHCCCCCCCEEE	39.55	23954790
27	Succinylation	VFQKYAGKDGYNYTL HHHHHCCCCCCCEEE	39.55	23954790
30	Phosphorylation	KYAGKDGYNYTLSKT HHCCCCCCCEEECHH	18.35	25159151
32	Phosphorylation	AGKDGYNYTLSKTEF CCCCCCCEEECHHHH	10.69	25159151
33	Phosphorylation	GKDGYNYTLSKTEFL CCCCCCEEECHHHHH	22.40	28152594
35	Phosphorylation	DGYNYTLSKTEFLSF CCCCEEECHHHHHHH	29.72	21815630
37	Phosphorylation	YNYTLSKTEFLSFMN CCEEECHHHHHHHHH	28.70	25159151
41	Phosphorylation	LSKTEFLSFMNTELA ECHHHHHHHHHHHHH	27.98	24719451
43	Sulfoxidation	KTEFLSFMNTELAAF HHHHHHHHHHHHHHH	5.65	30846556
51	Phosphorylation	NTELAAFTKNQKDPG HHHHHHHHCCCCCCH	25.10	28348404
52	Acetylation	TELAAFTKNQKDPGV HHHHHHHCCCCCCHH	51.43	26051181
52	Ubiquitination	TELAAFTKNQKDPGV HHHHHHHCCCCCCHH	51.43	-
55	2-Hydroxyisobutyrylation	AAFTKNQKDPGVLDR HHHHCCCCCCHHHHH	75.24	-
55	Malonylation	AAFTKNQKDPGVLDR HHHHCCCCCCHHHHH	75.24	26320211
55	Ubiquitination	AAFTKNQKDPGVLDR HHHHCCCCCCHHHHH	75.24	20972266
62	Methylation	KDPGVLDRMMKKLDT CCCHHHHHHHHHCCC	23.96	115493061
65	Ubiquitination	GVLDRMMKKLDTNSD HHHHHHHHHCCCCCC	40.62	-
65	Acetylation	GVLDRMMKKLDTNSD HHHHHHHHHCCCCCC	40.62	19822915
66	Acetylation	VLDRMMKKLDTNSDG HHHHHHHHCCCCCCC	33.43	19822925
69	Phosphorylation	RMMKKLDTNSDGQLD HHHHHCCCCCCCCCC	47.24	22617229
71	Phosphorylation	MKKLDTNSDGQLDFS HHHCCCCCCCCCCHH	45.25	25159151
78	Phosphorylation	SDGQLDFSEFLNLIG CCCCCCHHHHHHHHH	27.40	23090842
89	Sulfoxidation	NLIGGLAMACHDSFL HHHHHHHHHHHHHHH	5.00	30846556
94	Phosphorylation	LAMACHDSFLKAVPS HHHHHHHHHHHHCCC	14.60	14623863
97	Ubiquitination	ACHDSFLKAVPSQKR HHHHHHHHHCCCCCC	45.38	-
101	Phosphorylation	SFLKAVPSQKRT--- HHHHHCCCCCCC---	41.56	30576142
105	Phosphorylation	AVPSQKRT------- HCCCCCCC-------	50.42	26270265

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 S10AB_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
10	T	Phosphorylation		18618420
Phosphorylation at Thr-10 by PRKCA significantly suppresses homodimerization and promotes association with NCL/nucleolin which induces nuclear translocation.

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 S10AB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
S10AB_HUMAN	S100A11	physical	10673436
VIGLN_HUMAN	HDLBP	physical	22939629
STAM1_HUMAN	STAM	physical	22939629
TACC1_HUMAN	TACC1	physical	22939629
UBE2F_HUMAN	UBE2F	physical	22939629
ANXA1_HUMAN	ANXA1	physical	17932043
PA24A_HUMAN	PLA2G4A	physical	17932043

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 S10AB_HUMAN

Related Literatures of Post-Translational Modification

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-3, AND MASS SPECTROMETRY.	19608861 [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 SER-6, AND MASSSPECTROMETRY.	18669648 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND MASSSPECTROMETRY.	15302935 [Abstract]
"The structure of S100A11 fragment explains a local structural changeinduced by phosphorylation."; Kouno T., Mizuguchi M., Sakaguchi M., Makino E., Mori Y., Shinoda H.,Aizawa T., Demura M., Huh N.H., Kawano K.; J. Pept. Sci. 14:1129-1138(2008). Cited for: STRUCTURE BY NMR OF 1-19, DISULFIDE BOND, PHOSPHORYLATION AT THR-10,FUNCTION, AND SUBCELLULAR LOCATION.	18618420 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-30, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-30 AND TYR-32, AND MASSSPECTROMETRY.	18083107 [Abstract]

show