ASHWN_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ASHWN_HUMAN
• UniProt AC: Q9BVC5
• Protein Name: Ashwin
• Gene Name: C2orf49
• Organism: Homo sapiens (Human).
• Sequence Length: 232
• Protein Sequence: MAGDVGGRSCTDSELLLHPELLSQEFLLLTLEQKNIAVETDVRVNKDSLTDLYVQHAIPLPQRDLPKNRWGKMMEKKREQHEIKNETKRSSTVDGLRKRPLIVFDGSSTSTSIKVKKTENGDNDRLKPPPQASFTSNAFRKLSNSSSSVSPLILSSNLPVNNKTEHNNNDAKQNHDLTHRKSPSGPVKSPPLSPVGTTPVKLKRAAPKEEAEAMNNLKPPQAKRKIQHVTWP

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
11	Phosphorylation	DVGGRSCTDSELLLH CCCCCCCCCHHHHHC	43.75	22817900
23	Phosphorylation	LLHPELLSQEFLLLT HHCHHHHCHHHHHHH	40.04	-
50	Phosphorylation	RVNKDSLTDLYVQHA CCCHHHHHHHHHHHC	28.10	29978859
53	Phosphorylation	KDSLTDLYVQHAIPL HHHHHHHHHHHCCCC	10.81	27642862
72	Acetylation	LPKNRWGKMMEKKRE CCCCHHHHHHHHHHH	28.28	25953088
90	Phosphorylation	IKNETKRSSTVDGLR HCHHHHCCCCCCCCC	31.73	25394399
91	Phosphorylation	KNETKRSSTVDGLRK CHHHHCCCCCCCCCC	36.16	23186163
92	Phosphorylation	NETKRSSTVDGLRKR HHHHCCCCCCCCCCC	24.70	23186163
107	Phosphorylation	PLIVFDGSSTSTSIK CEEEECCCCCCCEEE	32.08	23312004
108	Phosphorylation	LIVFDGSSTSTSIKV EEEECCCCCCCEEEE	31.72	24117733
109	Phosphorylation	IVFDGSSTSTSIKVK EEECCCCCCCEEEEE	37.41	24117733
110	Phosphorylation	VFDGSSTSTSIKVKK EECCCCCCCEEEEEE	23.31	24117733
111	Phosphorylation	FDGSSTSTSIKVKKT ECCCCCCCEEEEEEC	34.26	23401153
112	Phosphorylation	DGSSTSTSIKVKKTE CCCCCCCEEEEEECC	21.85	24117733
143	Phosphorylation	SNAFRKLSNSSSSVS HHHHHHHCCCCCCCC	37.39	30278072
145	Phosphorylation	AFRKLSNSSSSVSPL HHHHHCCCCCCCCCE	28.37	30278072
146	Phosphorylation	FRKLSNSSSSVSPLI HHHHCCCCCCCCCEE	30.77	30278072
147	Phosphorylation	RKLSNSSSSVSPLIL HHHCCCCCCCCCEEE	34.28	25159151
148	Phosphorylation	KLSNSSSSVSPLILS HHCCCCCCCCCEEEC	28.67	23401153
150	Phosphorylation	SNSSSSVSPLILSSN CCCCCCCCCEEECCC	18.88	25159151
155	Phosphorylation	SVSPLILSSNLPVNN CCCCEEECCCCCCCC	15.36	29978859
156	Phosphorylation	VSPLILSSNLPVNNK CCCEEECCCCCCCCC	38.65	23663014
164	Phosphorylation	NLPVNNKTEHNNNDA CCCCCCCCCCCCCCH	44.60	23186163
178 (in isoform 2)	Phosphorylation	-	26.20	29743597
178	Phosphorylation	AKQNHDLTHRKSPSG HHHHCCCCCCCCCCC	26.20	20068231
182	Phosphorylation	HDLTHRKSPSGPVKS CCCCCCCCCCCCCCC	25.02	29255136
184	Phosphorylation	LTHRKSPSGPVKSPP CCCCCCCCCCCCCCC	63.92	29255136
189	Phosphorylation	SPSGPVKSPPLSPVG CCCCCCCCCCCCCCC	31.80	29255136
193	Phosphorylation	PVKSPPLSPVGTTPV CCCCCCCCCCCCCCC	24.26	29255136
197	Phosphorylation	PPLSPVGTTPVKLKR CCCCCCCCCCCCCCC	28.32	22167270
198	Phosphorylation	PLSPVGTTPVKLKRA CCCCCCCCCCCCCCC	21.84	22167270
201	Acetylation	PVGTTPVKLKRAAPK CCCCCCCCCCCCCCH	49.87	25953088
218	Acetylation	AEAMNNLKPPQAKRK HHHHHCCCCCHHHHH	57.69	26051181
230	Phosphorylation	KRKIQHVTWP----- HHHCCCCCCC-----	29.87	23917254

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ASHWN_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 ASHWN_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
CN166_HUMAN	C14orf166	physical	22939629
RTCB_HUMAN	RTCB	physical	22939629
DDX1_HUMAN	DDX1	physical	22939629
FA98B_HUMAN	FAM98B	physical	22939629
HNRPD_HUMAN	HNRNPD	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.

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-182; SER-189; SER-193;THR-197 AND THR-198, AND MASS SPECTROMETRY.
PubMed: 19690332

"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; SER-193; THR-197AND THR-198, AND MASS SPECTROMETRY.
PubMed: 19413330

"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-189; SER-193 ANDTHR-198, AND MASS SPECTROMETRY.
PubMed: 18669648

"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND SER-193, ANDMASS SPECTROMETRY.
PubMed: 18187866

"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; SER-193 ANDTHR-197, AND MASS SPECTROMETRY.
PubMed: 17287340

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND SER-193, ANDMASS SPECTROMETRY.
PubMed: 17081983