LYSM2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LYSM2_HUMAN
• UniProt AC: Q8IV50
• Protein Name: LysM and putative peptidoglycan-binding domain-containing protein 2
• Gene Name: LYSMD2
• Organism: Homo sapiens (Human).
• Sequence Length: 215
• Protein Sequence: MADSSPALSLREGGPRAPRPSAPSPPPRSRSGSESEEAELSLSLARTKTRSYGSTASVRAPLGAGVIERHVEHRVRAGDTLQGIALKYGVTMEQIKRANKLFTNDCIFLKKTLNIPVISEKPLLFNGLNSIDSPENETADNSFSQEEEPVVAGEDLPPPSPQESDVQPVQPEEVSARDFLQRLDLQIKLSTQAAKKLKEESRDEESPYATSLYHS

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
2	Acetylation	------MADSSPALS ------CCCCCCCCC	25.95	22814378
4	Phosphorylation	----MADSSPALSLR ----CCCCCCCCCCC	28.78	29255136
5	Phosphorylation	---MADSSPALSLRE ---CCCCCCCCCCCC	18.10	23401153
9	Phosphorylation	ADSSPALSLREGGPR CCCCCCCCCCCCCCC	27.73	22199227
21	Phosphorylation	GPRAPRPSAPSPPPR CCCCCCCCCCCCCCC	54.83	30266825
24	Phosphorylation	APRPSAPSPPPRSRS CCCCCCCCCCCCCCC	50.16	29255136
29	Phosphorylation	APSPPPRSRSGSESE CCCCCCCCCCCCHHH	36.25	29255136
31	Phosphorylation	SPPPRSRSGSESEEA CCCCCCCCCCHHHHH	48.17	30278072
33	Phosphorylation	PPRSRSGSESEEAEL CCCCCCCCHHHHHHH	38.91	30278072
35	Phosphorylation	RSRSGSESEEAELSL CCCCCCHHHHHHHHH	42.29	25159151
41	Phosphorylation	ESEEAELSLSLARTK HHHHHHHHHHHHHHC	13.86	30301811
43	Phosphorylation	EEAELSLSLARTKTR HHHHHHHHHHHHCCC	19.33	30301811
49	Phosphorylation	LSLARTKTRSYGSTA HHHHHHCCCCCCCCE	25.00	27251275
51	Phosphorylation	LARTKTRSYGSTASV HHHHCCCCCCCCEEE	38.79	28555341
52	Phosphorylation	ARTKTRSYGSTASVR HHHCCCCCCCCEEEE	16.29	-
54	Phosphorylation	TKTRSYGSTASVRAP HCCCCCCCCEEEECC	16.74	27251275
55	Phosphorylation	KTRSYGSTASVRAPL CCCCCCCCEEEECCC	20.70	29214152
57	Phosphorylation	RSYGSTASVRAPLGA CCCCCCEEEECCCCC	16.54	23401153
103	Phosphorylation	KRANKLFTNDCIFLK HHHHHHCCCCEEEEE	40.35	25599653
110	Ubiquitination	TNDCIFLKKTLNIPV CCCEEEEECCCCCCC	32.72	-
110	Acetylation	TNDCIFLKKTLNIPV CCCEEEEECCCCCCC	32.72	27452117
195	Acetylation	KLSTQAAKKLKEESR HHHHHHHHHHHHHHC	62.75	25953088
201	Phosphorylation	AKKLKEESRDEESPY HHHHHHHHCCCCCCC	46.23	22199227
206	Phosphorylation	EESRDEESPYATSLY HHHCCCCCCCHHHCC	22.59	28796482
208	Phosphorylation	SRDEESPYATSLYHS HCCCCCCCHHHCCCC	31.61	25159151
210	Phosphorylation	DEESPYATSLYHS-- CCCCCCHHHCCCC--	17.27	28796482
211	Phosphorylation	EESPYATSLYHS--- CCCCCHHHCCCC---	20.82	28796482
213	Phosphorylation	SPYATSLYHS----- CCCHHHCCCC-----	10.36	28796482
215	Phosphorylation	YATSLYHS------- CHHHCCCC-------	28.49	28796482

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

Oops, there are no upstream regulatory protein records of LYSM2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LYSM2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of LYSM2_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of LYSM2_HUMAN !!

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND MASSSPECTROMETRY.
PubMed: 19690332

"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-208 AND TYR-213, ANDMASS SPECTROMETRY.
PubMed: 15592455