dbPTM

SKAP2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SKAP2_MOUSE
UniProt AC	Q3UND0
Protein Name	Src kinase-associated phosphoprotein 2
Gene Name	Skap2
Organism	Mus musculus (Mouse).
Sequence Length	358
Subcellular Localization	Cytoplasm . Membrane ruffles of macrophages. Perikarya and dendrites from neurons.
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	MPNPSCTSSPGPLPEEIRNLLADVETFVADTLKGENLSKKAKEKRESLIKKIKDVKSVYLQEFQDKGDAEDGDEYDDPFAGPADTISLASERYDKDDDGPSDGNQFPPIAAQDLPFVIKAGYLEKRRKDHSFLGFEWQKRWCALSKTVFYYYGSDKDKQQKGEFAIDGYDVRMNNTLRKDGKKDCCFEICAPDKRIYQFTAASPKDAEEWVQQLKFILQDLGSDVIPEDDEERGELYDDVDHPAAVSSPQRSQPIDDEIYEELPEEEEDTASVKMDEQGKGSRDSVHHTSGDKSTDYANFYQGLWDCTGALSDELSFKRGDVIYILSKEYNRYGWWVGEMKGAIGLVPKAYLMEMYDI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MPNPSCTSSPGP ---CCCCCCCCCCCC	36.35	22345495
7	Phosphorylation	-MPNPSCTSSPGPLP -CCCCCCCCCCCCCH	36.26	30387612
8	Phosphorylation	MPNPSCTSSPGPLPE CCCCCCCCCCCCCHH	38.57	22345495
9 (in isoform 2)	Phosphorylation	-	18.74	27566939
9	Phosphorylation	PNPSCTSSPGPLPEE CCCCCCCCCCCCHHH	18.74	30352176
42	Acetylation	ENLSKKAKEKRESLI CCCHHHHHHHHHHHH	73.06	7712145
47	Phosphorylation	KAKEKRESLIKKIKD HHHHHHHHHHHHHHH	39.15	26824392
57	Phosphorylation	KKIKDVKSVYLQEFQ HHHHHHHHHHHHHHH	18.82	25619855
59	Phosphorylation	IKDVKSVYLQEFQDK HHHHHHHHHHHHHCC	15.12	25619855
75	Phosphorylation	DAEDGDEYDDPFAGP CCCCCCCCCCCCCCC	30.31	25619855
85	Phosphorylation	PFAGPADTISLASER CCCCCCCCEEEEHHC	17.99	25619855
87	Phosphorylation	AGPADTISLASERYD CCCCCCEEEEHHCCC	21.70	25619855
90	Phosphorylation	ADTISLASERYDKDD CCCEEEEHHCCCCCC	28.09	25619855
93	Phosphorylation	ISLASERYDKDDDGP EEEEHHCCCCCCCCC	24.24	25293948
101	Phosphorylation	DKDDDGPSDGNQFPP CCCCCCCCCCCCCCC	64.77	25293948
122	Phosphorylation	PFVIKAGYLEKRRKD CEEEEECCHHHHCCC	19.29	25367039
131	Phosphorylation	EKRRKDHSFLGFEWQ HHHCCCCCCCCCHHH	32.09	19854140
150	Phosphorylation	ALSKTVFYYYGSDKD HHHCEEEEEECCCHH	7.46	21454597
151	Phosphorylation	LSKTVFYYYGSDKDK HHCEEEEEECCCHHH	7.01	21454597
152	Phosphorylation	SKTVFYYYGSDKDKQ HCEEEEEECCCHHHH	9.97	29472430
154	Phosphorylation	TVFYYYGSDKDKQQK EEEEEECCCHHHHCC	25.93	22345495
169	Phosphorylation	GEFAIDGYDVRMNNT CCEEECCCEEECCCE	13.91	-
197	Phosphorylation	CAPDKRIYQFTAASP ECCCCCEEEEECCCC	11.12	28725479
200	Phosphorylation	DKRIYQFTAASPKDA CCCEEEEECCCCCCH	13.04	23737553
203	Phosphorylation	IYQFTAASPKDAEEW EEEEECCCCCCHHHH	29.98	23737553
223	Phosphorylation	FILQDLGSDVIPEDD HHHHHHCCCCCCCCH	35.68	30635358
237	Phosphorylation	DEERGELYDDVDHPA HHHCCCCCCCCCCHH	13.04	19144319
247	Phosphorylation	VDHPAAVSSPQRSQP CCCHHHCCCCCCCCC	31.41	30635358
248	Phosphorylation	DHPAAVSSPQRSQPI CCHHHCCCCCCCCCC	20.60	26026062
252	Phosphorylation	AVSSPQRSQPIDDEI HCCCCCCCCCCCHHH	34.75	25619855
260	Phosphorylation	QPIDDEIYEELPEEE CCCCHHHHHHCCCCC	10.99	24723360
270	Phosphorylation	LPEEEEDTASVKMDE CCCCCCCCCCEEECC	24.90	25619855
272	Phosphorylation	EEEEDTASVKMDEQG CCCCCCCCEEECCCC	25.10	25521595
282	Phosphorylation	MDEQGKGSRDSVHHT ECCCCCCCCCCCCCC	36.08	25159016
285	Phosphorylation	QGKGSRDSVHHTSGD CCCCCCCCCCCCCCC	23.41	25159016
289	Phosphorylation	SRDSVHHTSGDKSTD CCCCCCCCCCCCCCC	21.37	25159016
290	Phosphorylation	RDSVHHTSGDKSTDY CCCCCCCCCCCCCCH	40.41	30635358
297	Phosphorylation	SGDKSTDYANFYQGL CCCCCCCHHHHHHHH	11.97	-
324	Phosphorylation	FKRGDVIYILSKEYN CCCCCEEEEEECCHH	8.82	25367039
333	Phosphorylation	LSKEYNRYGWWVGEM EECCHHHCCCCCHHC	17.29	25367039

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
260	Y	Phosphorylation	Kinase	FYN	P06241	PSP
260	Y	Phosphorylation	Kinase	FYN	P39688	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SKAP2_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of SKAP2_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SKAP2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling."; Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.; J. Immunol. 179:5864-5876(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-75; TYR-151 AND TYR-260,AND MASS SPECTROMETRY.	17947660 [Abstract]
"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 AT TYR-75; TYR-197 AND TYR-260, AND MASS SPECTROMETRY.	15592455 [Abstract]
"Adaptor protein SKAP55R is associated with myeloid differentiationand growth arrest."; Curtis D.J., Jane S.M., Hilton D.J., Dougherty L., Bodine D.M.,Begley C.G.; Exp. Hematol. 28:1250-1259(2000). Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,SUBCELLULAR LOCATION, INDUCTION, POSSIBLE INTERACTION WITH FYN; HCKAND LYN, PHOSPHORYLATION AT TYR-260, MUTAGENESIS OF TYR-260, ANDFUNCTION.	11063873 [Abstract]