dbPTM

SPD2A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SPD2A_MOUSE
UniProt AC	O89032
Protein Name	SH3 and PX domain-containing protein 2A
Gene Name	Sh3pxd2a
Organism	Mus musculus (Mouse).
Sequence Length	1124
Subcellular Localization	Cytoplasm. Cell projection, podosome. Cytoplasmic in normal cells and localizes to podosomes in Src-transformed cells..
Protein Description	Adapter protein involved in invadopodia and podosome formation, extracellular matrix degradation and invasiveness of some cancer cells. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. In association with ADAM12, mediates the neurotoxic effect of amyloid-beta peptide (By similarity)..
Protein Sequence	MLAYCVQDATVVDVEKRRSPSKHYVYIINVTWSDSTSQTIYRRYSKFFDLQMQLLDKFPIEGGQKDPKQRIIPFLPGKILFRRSHIRDVAVKRLKPIDEYCRALVRLPPHISQCDEVFRFFEARPEDVNPPKEDYGSSKRKSVWLSSWAESPKKDVTGADTNAEPMILEQYVVVSNYKKQENSELSLQAGEVVDVIEKNESGWWFVSTSEEQGWVPATYLEAQNGTRDDSDINTSKTGEVSKRRKAHLRRLDRRWTLGGMVNRQHSREEKYVTVQPYTSQSKDEIGFEKGVTVEVIRKNLEGWWYIRYLGKEGWAPASYLKKAKDDLPTRKKNLAGPVEIIGNIMEISNLLNKKASGDKEAPAEGEGSEAPITKKEISLPILCNASNGSALAIPERTTSKLAQGSPAVARIAPQRAQISSPNLRTRPPPRRESSLGFQLPKPPEPPSVEVEYYTIAEFQSCISDGISFRGGQKAEVIDKNSGGWWYVQIGEKEGWAPASYIDKRKKPNLSRRTSTLTRPKVPPPAPPSKPKEAEENPVGACESQGSPLKVKYEEPEYDVPAFGFDSEPEMNEEPSGDRGSGDKHPAQPRRISPASSLQRAHFKVGESSEDVALEEETIYENEGFRPYTEDTLSARGSSGDSDSPGSSSLSLAVKNSPKSDSPKSSSLLKLKAEKNAQAELGKNQSNISFSSSVTISTTCSSSSSSSSLSKNNGDLKPRSASDAGIRDTPKVGTKKDPDVKAGLASCARAKPSVRPKPVLNRAESQSQEKMDISSLRRQLRPTGQLRGGLKGSRSEDSELPPQMASEGSRRGSADIIPLTATTPPCVPKKEWEGQGATYVTCSAYQKVQDSEISFPEGAEVHVLEKAESGWWYVRFGELEGWAPSHYLVAEENQQPDTASKEGDTGKSSQNEGKSDSLEKIEKRVQALNTVNQSKRATPPIPSKPPGGFGKTSGTVAVKMRNGVRQVAVRPQSVFVSPPPKDNNLSCALRRNESLTATDSLRGVRRNSSFSTARSAAAEAKGRLAERAASQGSESPLLPTQRKGIPVSPVRPKPIEKSQFIHNNLKDVYISIADYEGDEETAGFQEGVSMEVLEKNPNGWWYCQILDEVKPFKGWVPSNYLEKKN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
84	Phosphorylation	GKILFRRSHIRDVAV CCEEEECHHHHHHHH	21.00	20531401
137	Phosphorylation	PPKEDYGSSKRKSVW CCHHHCCCCCCCEEE	26.85	29514104
137 (in isoform 3)	Phosphorylation	-	26.85	29514104
228 (in isoform 3)	Phosphorylation	-	60.65	29514104
234	Phosphorylation	RDDSDINTSKTGEVS CCCCCCCCCCCCCHH	31.75	-
235	Phosphorylation	DDSDINTSKTGEVSK CCCCCCCCCCCCHHH	24.59	-
237	Phosphorylation	SDINTSKTGEVSKRR CCCCCCCCCCHHHHH	38.04	-
241	Phosphorylation	TSKTGEVSKRRKAHL CCCCCCHHHHHHHHH	19.01	-
243 (in isoform 2)	Phosphorylation	-	37.51	29514104
256	Phosphorylation	RRLDRRWTLGGMVNR HHHHHHCHHHHCCCC	17.45	26824392
271	Phosphorylation	QHSREEKYVTVQPYT CCCCCCCEEEEECCC	12.48	29514104
378	Phosphorylation	PITKKEISLPILCNA CCCCCEECCCEEEEC	29.23	26824392
405	Phosphorylation	TSKLAQGSPAVARIA CCHHHCCCHHHHHHC	9.52	24899341
419	Phosphorylation	APQRAQISSPNLRTR CCCCCCCCCCCCCCC	27.88	22942356
420	Phosphorylation	PQRAQISSPNLRTRP CCCCCCCCCCCCCCC	21.31	25521595
510	Phosphorylation	KRKKPNLSRRTSTLT CCCCCCCCCCCCCCC	26.76	22942356
513	Phosphorylation	KPNLSRRTSTLTRPK CCCCCCCCCCCCCCC	25.59	22817900
514	Phosphorylation	PNLSRRTSTLTRPKV CCCCCCCCCCCCCCC	21.43	24899341
515	Phosphorylation	NLSRRTSTLTRPKVP CCCCCCCCCCCCCCC	31.38	24899341
517	Phosphorylation	SRRTSTLTRPKVPPP CCCCCCCCCCCCCCC	45.04	29550500
543	Phosphorylation	NPVGACESQGSPLKV CCCCCCCCCCCCCEE	39.46	27742792
546	Phosphorylation	GACESQGSPLKVKYE CCCCCCCCCCEEEEC	21.30	25521595
552	Phosphorylation	GSPLKVKYEEPEYDV CCCCEEEECCCCCCC	28.63	25619855
557	Phosphorylation	VKYEEPEYDVPAFGF EEECCCCCCCCCCCC	32.72	25619855
566	Phosphorylation	VPAFGFDSEPEMNEE CCCCCCCCCCCCCCC	53.44	18515860
592	Phosphorylation	PAQPRRISPASSLQR CCCCCCCCCCHHHHH	16.77	26824392
595	Phosphorylation	PRRISPASSLQRAHF CCCCCCCHHHHHHHE	34.66	25159016
596	Phosphorylation	RRISPASSLQRAHFK CCCCCCHHHHHHHEE	30.54	21082442
607	Phosphorylation	AHFKVGESSEDVALE HHEECCCCCHHCCCC	32.85	26643407
608	Phosphorylation	HFKVGESSEDVALEE HEECCCCCHHCCCCE	33.25	26643407
617	Phosphorylation	DVALEEETIYENEGF HCCCCEEEEECCCCC	31.94	26643407
619	Phosphorylation	ALEEETIYENEGFRP CCCEEEEECCCCCCC	21.81	22817900
627	Phosphorylation	ENEGFRPYTEDTLSA CCCCCCCCCCCCCCC	20.64	30635358
628	Phosphorylation	NEGFRPYTEDTLSAR CCCCCCCCCCCCCCC	30.02	30635358
631	Phosphorylation	FRPYTEDTLSARGSS CCCCCCCCCCCCCCC	19.17	30635358
633	Phosphorylation	PYTEDTLSARGSSGD CCCCCCCCCCCCCCC	20.29	30635358
637	Phosphorylation	DTLSARGSSGDSDSP CCCCCCCCCCCCCCC	26.12	25619855
638	Phosphorylation	TLSARGSSGDSDSPG CCCCCCCCCCCCCCC	49.82	25619855
641	Phosphorylation	ARGSSGDSDSPGSSS CCCCCCCCCCCCCCC	43.44	25619855
643	Phosphorylation	GSSGDSDSPGSSSLS CCCCCCCCCCCCCEE	34.80	25521595
646	Phosphorylation	GDSDSPGSSSLSLAV CCCCCCCCCCEEEEE	21.82	25619855
647	Phosphorylation	DSDSPGSSSLSLAVK CCCCCCCCCEEEEEE	41.01	25619855
648	Phosphorylation	SDSPGSSSLSLAVKN CCCCCCCCEEEEEEC	24.55	25619855
650	Phosphorylation	SPGSSSLSLAVKNSP CCCCCCEEEEEECCC	19.07	25619855
656	Phosphorylation	LSLAVKNSPKSDSPK EEEEEECCCCCCCCC	28.17	25619855
659	Phosphorylation	AVKNSPKSDSPKSSS EEECCCCCCCCCCHH	46.86	26160508
661	Phosphorylation	KNSPKSDSPKSSSLL ECCCCCCCCCCHHHH	41.12	26160508
666	Phosphorylation	SDSPKSSSLLKLKAE CCCCCCHHHHHHHHH	44.82	24453211
719	Phosphorylation	NGDLKPRSASDAGIR CCCCCCCCHHHCCCC	40.42	27742792
721	Phosphorylation	DLKPRSASDAGIRDT CCCCCCHHHCCCCCC	29.28	26824392
728	Phosphorylation	SDAGIRDTPKVGTKK HHCCCCCCCCCCCCC	18.37	-
764	Phosphorylation	PVLNRAESQSQEKMD CCCCHHHHHCHHHCC	33.86	26824392
766	Phosphorylation	LNRAESQSQEKMDIS CCHHHHHCHHHCCHH	49.97	26824392
773	Phosphorylation	SQEKMDISSLRRQLR CHHHCCHHHHHHHHC	21.03	25159016
774	Phosphorylation	QEKMDISSLRRQLRP HHHCCHHHHHHHHCC	26.65	29514104
786	Methylation	LRPTGQLRGGLKGSR HCCCCCCCCCCCCCC	29.28	18958345
792	Phosphorylation	LRGGLKGSRSEDSEL CCCCCCCCCCCCCCC	30.92	26239621
794	Phosphorylation	GGLKGSRSEDSELPP CCCCCCCCCCCCCCH	47.67	26239621
797	Phosphorylation	KGSRSEDSELPPQMA CCCCCCCCCCCHHHH	36.66	26239621
805	Phosphorylation	ELPPQMASEGSRRGS CCCHHHHCCCCCCCC	36.83	22817900
812	Phosphorylation	SEGSRRGSADIIPLT CCCCCCCCCCEEECC	22.43	25521595
819	Phosphorylation	SADIIPLTATTPPCV CCCEEECCCCCCCCC	19.32	27742792
821	Phosphorylation	DIIPLTATTPPCVPK CEEECCCCCCCCCCC	34.30	25619855
822	Phosphorylation	IIPLTATTPPCVPKK EEECCCCCCCCCCCC	23.83	27742792
916	Phosphorylation	QNEGKSDSLEKIEKR CCCCCCHHHHHHHHH	45.58	27681418
933	Phosphorylation	ALNTVNQSKRATPPI HHHHHCHHCCCCCCC	20.93	29514104
937	Phosphorylation	VNQSKRATPPIPSKP HCHHCCCCCCCCCCC	33.36	23684622
972	Phosphorylation	QVAVRPQSVFVSPPP EEEECCCEEEECCCC	21.87	26824392
976	Phosphorylation	RPQSVFVSPPPKDNN CCCEEEECCCCCCCC	21.89	23608596
985	Phosphorylation	PPKDNNLSCALRRNE CCCCCCCHHHHHCCC	10.24	26643407
993	Phosphorylation	CALRRNESLTATDSL HHHHCCCCCCHHHHC	34.27	25521595
995	Phosphorylation	LRRNESLTATDSLRG HHCCCCCCHHHHCCC	36.47	25619855
997	Phosphorylation	RNESLTATDSLRGVR CCCCCCHHHHCCCHH	22.38	25619855
999	Phosphorylation	ESLTATDSLRGVRRN CCCCHHHHCCCHHCC	18.66	25619855
1001	Methylation	LTATDSLRGVRRNSS CCHHHHCCCHHCCCC	45.58	58860119
1007	Phosphorylation	LRGVRRNSSFSTARS CCCHHCCCCHHHHHH	30.83	23684622
1008	Phosphorylation	RGVRRNSSFSTARSA CCHHCCCCHHHHHHH	27.11	25521595
1010	Phosphorylation	VRRNSSFSTARSAAA HHCCCCHHHHHHHHH	24.09	22324799
1011	Phosphorylation	RRNSSFSTARSAAAE HCCCCHHHHHHHHHH	24.87	23684622
1029	Phosphorylation	RLAERAASQGSESPL HHHHHHHHCCCCCCC	33.80	25521595
1032	Phosphorylation	ERAASQGSESPLLPT HHHHHCCCCCCCCCC	27.54	22942356
1034	Phosphorylation	AASQGSESPLLPTQR HHHCCCCCCCCCCCC	23.65	26824392
1039	Phosphorylation	SESPLLPTQRKGIPV CCCCCCCCCCCCCCC	40.76	25619855
1047	Phosphorylation	QRKGIPVSPVRPKPI CCCCCCCCCCCCCCC	16.60	26824392

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
557	Y	Phosphorylation	Kinase	SRC	P12931	PSP
619	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SPD2A_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 SPD2A_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of SPD2A_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of SPD2A_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566 AND SER-993, ANDMASS SPECTROMETRY.	19367708 [Abstract]
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, AND MASSSPECTROMETRY.	17114649 [Abstract]