dbPTM

SKAP2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SKAP2_HUMAN
UniProt AC	O75563
Protein Name	Src kinase-associated phosphoprotein 2
Gene Name	SKAP2
Organism	Homo sapiens (Human).
Sequence Length	359
Subcellular Localization	Cytoplasm .
Protein Description	May be involved in B-cell and macrophage adhesion processes. In B-cells, may act by coupling the B-cell receptor (BCR) to integrin activation. May play a role in src signaling pathway..
Protein Sequence	MPNPSSTSSPYPLPEEIRNLLADVETFVADILKGENLSKKAKEKRESLIKKIKDVKSIYLQEFQDKGDAEDGEEYDDPFAGPPDTISLASERYDKDDEAPSDGAQFPPIAAQDLPFVLKAGYLEKRRKDHSFLGFEWQKRWCALSKTVFYYYGSDKDKQQKGEFAIDGYSVRMNNTLRKDGKKDCCFEISAPDKRIYQFTAASPKDAEEWVQQLKFVLQDMESDIIPEDYDERGELYDDVDHPLPISNPLTSSQPIDDEIYEELPEEEEDSAPVKVEEQRKMSQDSVHHTSGDKSTDYANFYQGLWDCTGAFSDELSFKRGDVIYILSKEYNRYGWWVGEMKGAIGLVPKAYIMEMYDI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MPNPSSTSSPYP ---CCCCCCCCCCCC	53.54	23401153
6	Phosphorylation	--MPNPSSTSSPYPL --CCCCCCCCCCCCC	33.30	23401153
7	Phosphorylation	-MPNPSSTSSPYPLP -CCCCCCCCCCCCCC	37.25	25106551
8	Phosphorylation	MPNPSSTSSPYPLPE CCCCCCCCCCCCCCH	31.12	28450419
9	Phosphorylation	PNPSSTSSPYPLPEE CCCCCCCCCCCCCHH	28.65	28450419
11	Phosphorylation	PSSTSSPYPLPEEIR CCCCCCCCCCCHHHH	21.25	28450419
47	Phosphorylation	KAKEKRESLIKKIKD HHHHHHHHHHHHHHH	39.15	24719451
56	Ubiquitination	IKKIKDVKSIYLQEF HHHHHHHHHHHHHHH	41.07	-
57	Phosphorylation	KKIKDVKSIYLQEFQ HHHHHHHHHHHHHHH	19.13	28060719
59	Phosphorylation	IKDVKSIYLQEFQDK HHHHHHHHHHHHHCC	14.93	28060719
66	Ubiquitination	YLQEFQDKGDAEDGE HHHHHHCCCCCCCCC	48.16	21906983
75	Phosphorylation	DAEDGEEYDDPFAGP CCCCCCCCCCCCCCC	22.73	29978859
85	Phosphorylation	PFAGPPDTISLASER CCCCCCCCEEHHHHC	20.45	28060719
87	Phosphorylation	AGPPDTISLASERYD CCCCCCEEHHHHCCC	21.70	26657352
90	Phosphorylation	PDTISLASERYDKDD CCCEEHHHHCCCCCC	28.09	29970186
93	Phosphorylation	ISLASERYDKDDEAP EEHHHHCCCCCCCCC	24.24	28060719
101	Phosphorylation	DKDDEAPSDGAQFPP CCCCCCCCCCCCCCC	56.58	26657352
119	Ubiquitination	QDLPFVLKAGYLEKR HCHHHEEEECCHHHH	34.17	21906983
122	Phosphorylation	PFVLKAGYLEKRRKD HHEEEECCHHHHCCC	19.29	24719451
125	Ubiquitination	LKAGYLEKRRKDHSF EEECCHHHHCCCCCC	55.71	21906983
131	Phosphorylation	EKRRKDHSFLGFEWQ HHHCCCCCCCCCHHH	32.09	28450419
147	Phosphorylation	RWCALSKTVFYYYGS HHHHHHCEEEEEECC	16.69	-
150	Phosphorylation	ALSKTVFYYYGSDKD HHHCEEEEEECCCHH	7.46	28060719
151	Phosphorylation	LSKTVFYYYGSDKDK HHCEEEEEECCCHHH	7.01	28060719
152	Phosphorylation	SKTVFYYYGSDKDKQ HCEEEEEECCCHHHC	9.97	23917254
154	Phosphorylation	TVFYYYGSDKDKQQK EEEEEECCCHHHCCC	25.93	28270605
170	Phosphorylation	EFAIDGYSVRMNNTL CEEECCEEEECCCCC	14.58	24247654
176	Phosphorylation	YSVRMNNTLRKDGKK EEEECCCCCCCCCCC	23.96	27535140
194	Ubiquitination	FEISAPDKRIYQFTA EEEECCCCEEEEEEC	39.37	-
197	Phosphorylation	SAPDKRIYQFTAASP ECCCCEEEEEECCCC	11.12	21082442
200	Phosphorylation	DKRIYQFTAASPKDA CCEEEEEECCCCCCH	13.04	28152594
203	Phosphorylation	IYQFTAASPKDAEEW EEEEECCCCCCHHHH	29.98	28060719
205	Ubiquitination	QFTAASPKDAEEWVQ EEECCCCCCHHHHHH	68.05	21906983
223	Phosphorylation	FVLQDMESDIIPEDY HHHHHCCCCCCCCCC	27.72	-
237	Phosphorylation	YDERGELYDDVDHPL CCCCCCCCCCCCCCC	13.04	23879269
253	Phosphorylation	ISNPLTSSQPIDDEI CCCCCCCCCCCCHHH	34.44	-
261	Phosphorylation	QPIDDEIYEELPEEE CCCCHHHHHHCCCCC	10.99	21253578
275	Ubiquitination	EEDSAPVKVEEQRKM CCCCCCCCHHHHHHH	42.76	-
281	Ubiquitination	VKVEEQRKMSQDSVH CCHHHHHHHCCCCCC	42.47	21906983
283	Phosphorylation	VEEQRKMSQDSVHHT HHHHHHHCCCCCCCC	33.59	26657352
286	Phosphorylation	QRKMSQDSVHHTSGD HHHHCCCCCCCCCCC	18.73	28060719
290	Phosphorylation	SQDSVHHTSGDKSTD CCCCCCCCCCCCCCC	21.37	18669648
291	Phosphorylation	QDSVHHTSGDKSTDY CCCCCCCCCCCCCCH	40.41	27251275
317	Phosphorylation	GAFSDELSFKRGDVI CCCCCCCCCCCCCEE	27.03	24719451
325	Phosphorylation	FKRGDVIYILSKEYN CCCCCEEEEEECCHH	8.82	28270605
328	Phosphorylation	GDVIYILSKEYNRYG CCEEEEEECCHHHCC	17.55	28270605
329	Ubiquitination	DVIYILSKEYNRYGW CEEEEEECCHHHCCC	61.85	21906983
331	Phosphorylation	IYILSKEYNRYGWWV EEEEECCHHHCCCCC	14.53	-
334	Phosphorylation	LSKEYNRYGWWVGEM EECCHHHCCCCCCCC	17.29	-
342	Ubiquitination	GWWVGEMKGAIGLVP CCCCCCCCCCCEECC	40.67	-
350	Ubiquitination	GAIGLVPKAYIMEMY CCCEECCHHHHHHHC	46.47	21906983
357	Phosphorylation	KAYIMEMYDI----- HHHHHHHCCC-----	9.36	-

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 SKAP2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SKAP2_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 SKAP2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
FAK2_HUMAN	PTK2B	physical	12893833
A4_HUMAN	APP	physical	21832049

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 SKAP2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-151 AND TYR-197, ANDMASS SPECTROMETRY.	18083107 [Abstract]
"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 TYR-325, AND MASSSPECTROMETRY.	17081983 [Abstract]