dbPTM

SRC8_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SRC8_MOUSE
UniProt AC	Q60598
Protein Name	Src substrate cortactin
Gene Name	Cttn
Organism	Mus musculus (Mouse).
Sequence Length	546
Subcellular Localization	Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Cell projection, ruffle. Cytoplasm, cell cortex. Cell projection . Cell projection, podosome . Cell projection, dendritic spine. Cell projection, dendrite. Cell membrane Peripheral membrane protei
Protein Description	Contributes to the organization of the actin cytoskeleton and cell shape. [PubMed: 17403031 Plays a role in the formation of lamellipodia and in cell migration (By similarity Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity Through its interaction with CTTNBP2, involved in the regulation of neuronal spine density]
Protein Sequence	MWKASAGHAVSITQDDGGADDWETDPDFVNDVSEKEQRWGAKTVQGSGHQEHINIHKLRENVFQEHQTLKEKELETGPKASHGYGGKFGVEQDRMDRSAVGHEYQSKLSKHCSQVDSVRGFGGKFGVQMDRVDQSAVGFEYQGKTEKHASQKDYSSGFGGKYGVQADRVDKSAVGFDYQGKTEKHESQKDYSKGFGGKYGIDKDKVDKSAVGFEYQGKTEKHESQKDYVKGFGGKFGVQTDRQDKCALGWDHQEKLQLHESQKDYKTGFGGKFGVQSERQDSSAVGFDYKERLAKHESQQDYAKGFGGKYGVQKDRMDKNASTFEEVVQVPSAYQKTVPIEAVTSKTSNIRANFENLAKEREQEDRRKAEAERAQRMAKERQEQEEARRKLEEQARAKKQTPPASPSPQPIEDRPPSSPIYEDAAPFKAEPSYRGSEPEPEYSIEAAGIPEAGSQQGLTYTSEPVYETTEAPGHYQAEDDTYDGYESDLGITAIALYDYQAAGDDEISFDPDDIITNIEMIDDGWWRGVCKGRYGLFPANYVELRQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MWKASAGHAVSI ---CCCCCCCCEEEE	30.93	23984901
11	Phosphorylation	ASAGHAVSITQDDGG CCCCCEEEEECCCCC	22.24	27087446
13	Phosphorylation	AGHAVSITQDDGGAD CCCEEEEECCCCCCC	20.59	26525534
24	Phosphorylation	GGADDWETDPDFVND CCCCCCCCCHHHHHC	48.88	26525534
43	Phosphorylation	EQRWGAKTVQGSGHQ HHHHCCEECCCCCCH	19.96	29899451
47	Phosphorylation	GAKTVQGSGHQEHIN CCEECCCCCCHHHCC	18.93	27742792
68	Phosphorylation	NVFQEHQTLKEKELE HHHHHHHHHHHHHHH	41.53	29514104
76	Phosphorylation	LKEKELETGPKASHG HHHHHHHCCCCCCCC	71.99	22871156
81	Phosphorylation	LETGPKASHGYGGKF HHCCCCCCCCCCCCC	24.46	22871156
84	Phosphorylation	GPKASHGYGGKFGVE CCCCCCCCCCCCCCC	19.79	29514104
87	Acetylation	ASHGYGGKFGVEQDR CCCCCCCCCCCCCCC	34.28	23806337
98	Phosphorylation	EQDRMDRSAVGHEYQ CCCCCCHHHHHHHHH	24.04	29514104
104	Phosphorylation	RSAVGHEYQSKLSKH HHHHHHHHHHHHHHH	16.65	29514104
106	Phosphorylation	AVGHEYQSKLSKHCS HHHHHHHHHHHHHHH	34.36	27841257
107	Acetylation	VGHEYQSKLSKHCSQ HHHHHHHHHHHHHHC	41.05	31600191
107	Malonylation	VGHEYQSKLSKHCSQ HHHHHHHHHHHHHHC	41.05	26320211
109	Phosphorylation	HEYQSKLSKHCSQVD HHHHHHHHHHHHCCC	24.88	29514104
110	Acetylation	EYQSKLSKHCSQVDS HHHHHHHHHHHCCCC	60.10	22826441
110	Malonylation	EYQSKLSKHCSQVDS HHHHHHHHHHHCCCC	60.10	26320211
112	S-nitrosylation	QSKLSKHCSQVDSVR HHHHHHHHHCCCCCC	3.32	22178444
113	Phosphorylation	SKLSKHCSQVDSVRG HHHHHHHHCCCCCCC	32.72	26824392
117	Phosphorylation	KHCSQVDSVRGFGGK HHHHCCCCCCCCCCC	18.17	23375375
119	Methylation	CSQVDSVRGFGGKFG HHCCCCCCCCCCCCC	38.38	24129315
124	Acetylation	SVRGFGGKFGVQMDR CCCCCCCCCCCCCCE	39.05	23806337
124	Malonylation	SVRGFGGKFGVQMDR CCCCCCCCCCCCCCE	39.05	26320211
124	Ubiquitination	SVRGFGGKFGVQMDR CCCCCCCCCCCCCCE	39.05	-
141	Phosphorylation	QSAVGFEYQGKTEKH HHHCCCEEECCCCCC	21.95	29514104
144	Acetylation	VGFEYQGKTEKHASQ CCCEEECCCCCCCCC	37.68	23806337
144	Malonylation	VGFEYQGKTEKHASQ CCCEEECCCCCCCCC	37.68	26320211
150	Phosphorylation	GKTEKHASQKDYSSG CCCCCCCCCCCCCCC	37.17	20139300
152	Acetylation	TEKHASQKDYSSGFG CCCCCCCCCCCCCCC	57.02	31600191
152	Malonylation	TEKHASQKDYSSGFG CCCCCCCCCCCCCCC	57.02	26320211
154	Phosphorylation	KHASQKDYSSGFGGK CCCCCCCCCCCCCCC	16.27	25777480
155	Phosphorylation	HASQKDYSSGFGGKY CCCCCCCCCCCCCCC	33.83	25777480
156	Phosphorylation	ASQKDYSSGFGGKYG CCCCCCCCCCCCCCC	31.73	25777480
161	Acetylation	YSSGFGGKYGVQADR CCCCCCCCCCCCCCE	38.93	23806337
161	Malonylation	YSSGFGGKYGVQADR CCCCCCCCCCCCCCE	38.93	26320211
162	Phosphorylation	SSGFGGKYGVQADRV CCCCCCCCCCCCCEE	26.29	29514104
171	Acetylation	VQADRVDKSAVGFDY CCCCEECHHHCCCCC	37.14	23806337
171	Malonylation	VQADRVDKSAVGFDY CCCCEECHHHCCCCC	37.14	26320211
171	Succinylation	VQADRVDKSAVGFDY CCCCEECHHHCCCCC	37.14	23806337
172	Phosphorylation	QADRVDKSAVGFDYQ CCCEECHHHCCCCCC	24.59	18779572
178	Phosphorylation	KSAVGFDYQGKTEKH HHHCCCCCCCCCCCC	19.53	29514104
181	Acetylation	VGFDYQGKTEKHESQ CCCCCCCCCCCCCCH	37.68	23806337
181	Malonylation	VGFDYQGKTEKHESQ CCCCCCCCCCCCCCH	37.68	26320211
189	Acetylation	TEKHESQKDYSKGFG CCCCCCHHHHHCCCC	68.84	17643370
193	Acetylation	ESQKDYSKGFGGKYG CCHHHHHCCCCCCCC	52.62	31600191
193	Malonylation	ESQKDYSKGFGGKYG CCHHHHHCCCCCCCC	52.62	26320211
198	Acetylation	YSKGFGGKYGIDKDK HHCCCCCCCCCCHHH	40.46	23806337
199	Phosphorylation	SKGFGGKYGIDKDKV HCCCCCCCCCCHHHC	23.69	29514104
203	Acetylation	GGKYGIDKDKVDKSA CCCCCCCHHHCCHHH	58.49	23806337
205	Acetylation	KYGIDKDKVDKSAVG CCCCCHHHCCHHHCC	59.06	23806337
208	Malonylation	IDKDKVDKSAVGFEY CCHHHCCHHHCCCEE	43.21	26320211
215	Phosphorylation	KSAVGFEYQGKTEKH HHHCCCEEECCCCCC	21.95	15592455
224	Phosphorylation	GKTEKHESQKDYVKG CCCCCCHHHHHHHHC	42.10	-
228	Phosphorylation	KHESQKDYVKGFGGK CCHHHHHHHHCCCCC	15.88	29514104
235	Acetylation	YVKGFGGKFGVQTDR HHHCCCCCCCCCCCC	39.05	23806337
235	Malonylation	YVKGFGGKFGVQTDR HHHCCCCCCCCCCCC	39.05	26320211
261	Phosphorylation	EKLQLHESQKDYKTG HHHHHCHHHCCHHCC	31.61	29899451
263	Acetylation	LQLHESQKDYKTGFG HHHCHHHCCHHCCCC	72.76	22902405
265	Phosphorylation	LHESQKDYKTGFGGK HCHHHCCHHCCCCCC	19.93	29514104
272	Acetylation	YKTGFGGKFGVQSER HHCCCCCCCCCCCCC	39.05	23806337
282	Phosphorylation	VQSERQDSSAVGFDY CCCCCCCCCCCCCCH	16.32	26239621
283	Phosphorylation	QSERQDSSAVGFDYK CCCCCCCCCCCCCHH	34.95	26239621
289	Phosphorylation	SSAVGFDYKERLAKH CCCCCCCHHHHHHHH	16.70	29514104
295	Acetylation	DYKERLAKHESQQDY CHHHHHHHHHHHHHH	53.12	23806337
298	Phosphorylation	ERLAKHESQQDYAKG HHHHHHHHHHHHHHC	32.62	29899451
302	Phosphorylation	KHESQQDYAKGFGGK HHHHHHHHHHCCCCC	13.08	29514104
304	Acetylation	ESQQDYAKGFGGKYG HHHHHHHHCCCCCCC	48.85	19608861
309	Acetylation	YAKGFGGKYGVQKDR HHHCCCCCCCCCHHH	38.93	23806337
309	Ubiquitination	YAKGFGGKYGVQKDR HHHCCCCCCCCCHHH	38.93	22790023
310	Phosphorylation	AKGFGGKYGVQKDRM HHCCCCCCCCCHHHC	26.29	29514104
314	Acetylation	GGKYGVQKDRMDKNA CCCCCCCHHHCCCCC	44.91	31600191
314	Malonylation	GGKYGVQKDRMDKNA CCCCCCCHHHCCCCC	44.91	26320211
319	Acetylation	VQKDRMDKNASTFEE CCHHHCCCCCCCHHH	45.10	17643370
322	Phosphorylation	DRMDKNASTFEEVVQ HHCCCCCCCHHHHHC	42.92	26239621
323	Phosphorylation	RMDKNASTFEEVVQV HCCCCCCCHHHHHCC	32.43	26239621
332	Phosphorylation	EEVVQVPSAYQKTVP HHHHCCCHHHCCCCC	40.53	22499769
334	Phosphorylation	VVQVPSAYQKTVPIE HHCCCHHHCCCCCCC	18.19	22499769
336	Ubiquitination	QVPSAYQKTVPIEAV CCCHHHCCCCCCCCC	38.52	22790023
344	Phosphorylation	TVPIEAVTSKTSNIR CCCCCCCCCCCCCHH	31.39	25338131
345	Phosphorylation	VPIEAVTSKTSNIRA CCCCCCCCCCCCHHH	27.60	24719451
346	Acetylation	PIEAVTSKTSNIRAN CCCCCCCCCCCHHHH	46.75	23806337
347	Phosphorylation	IEAVTSKTSNIRANF CCCCCCCCCCHHHHH	27.12	25338131
348	Phosphorylation	EAVTSKTSNIRANFE CCCCCCCCCHHHHHH	33.71	29514104
401	Phosphorylation	QARAKKQTPPASPSP HHHHHHCCCCCCCCC	39.87	24925903
405	Phosphorylation	KKQTPPASPSPQPIE HHCCCCCCCCCCCCC	31.52	24925903
407	Phosphorylation	QTPPASPSPQPIEDR CCCCCCCCCCCCCCC	33.40	24925903
417	Phosphorylation	PIEDRPPSSPIYEDA CCCCCCCCCCCCCCC	51.97	25521595
418	Phosphorylation	IEDRPPSSPIYEDAA CCCCCCCCCCCCCCC	22.53	25521595
421	Phosphorylation	RPPSSPIYEDAAPFK CCCCCCCCCCCCCCC	15.90	24925903
432	Phosphorylation	APFKAEPSYRGSEPE CCCCCCCCCCCCCCC	20.97	25777480
433	Phosphorylation	PFKAEPSYRGSEPEP CCCCCCCCCCCCCCC	29.70	25777480
442	Phosphorylation	GSEPEPEYSIEAAGI CCCCCCCCCEEECCC	26.18	18563927
443	Phosphorylation	SEPEPEYSIEAAGIP CCCCCCCCEEECCCC	16.58	-
460	Phosphorylation	GSQQGLTYTSEPVYE CCCCCCEEECCCEEE	17.20	-
466	Phosphorylation	TYTSEPVYETTEAPG EEECCCEEECCCCCC	20.48	18563927
475	Phosphorylation	TTEAPGHYQAEDDTY CCCCCCCEECCCCCC	18.48	-
482	Phosphorylation	YQAEDDTYDGYESDL EECCCCCCCCCCCCC	17.86	22252131
485	Phosphorylation	EDDTYDGYESDLGIT CCCCCCCCCCCCCEE	14.90	22252131
497	Phosphorylation	GITAIALYDYQAAGD CEEEEEEEEHHHCCC	12.00	-
499	Phosphorylation	TAIALYDYQAAGDDE EEEEEEEHHHCCCCC	6.11	-
541	Phosphorylation	YGLFPANYVELRQ-- CCEEECHHHEECC--	9.45	-

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
24	T	Phosphorylation	Kinase	CK2A1	Q60737	PSP
113	S	Phosphorylation	Kinase	PAK3	Q61036	PSP
150	S	Phosphorylation	Kinase	PAK3	Q61036	PSP
282	S	Phosphorylation	Kinase	PAK3	Q61036	PSP
421	Y	Phosphorylation	Kinase	PTK2	Q05397	GPS
421	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
421	Y	Phosphorylation	Kinase	FAK ISO2	P34152-2	PSP
421	Y	Phosphorylation	Kinase	YES1	Q04736	GPS
421	Y	Phosphorylation	Kinase	FER	P16591	PSP
421	Y	Phosphorylation	Kinase	SRC	P05480	PSP
421	Y	Phosphorylation	Kinase	FER	P70451	PhosphoELM
421	Y	Phosphorylation	Kinase	SRC	P12931	PSP
466	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
466	Y	Phosphorylation	Kinase	YES1	Q04736	GPS
466	Y	Phosphorylation	Kinase	SRC	P05480	PSP
466	Y	Phosphorylation	Kinase	SRC	P12931	PSP
466	Y	Phosphorylation	Kinase	LYN	P25911	PSP
466	Y	Phosphorylation	Kinase	FER	P70451	PhosphoELM
466	Y	Phosphorylation	Kinase	FER	P16591	PSP
466	Y	Phosphorylation	Kinase	FAK ISO2	P34152-2	PSP
466	Y	Phosphorylation	Kinase	FAK1	P34152	Uniprot
466	Y	Phosphorylation	Kinase	PTK2	Q05397	GPS
475	Y	Phosphorylation	Kinase	SRC	P05480	PSP
482	Y	Phosphorylation	Kinase	SRC	P12931	PSP
482	Y	Phosphorylation	Kinase	FER	P70451	PhosphoELM
482	Y	Phosphorylation	Kinase	SRC	P05480	Uniprot
482	Y	Phosphorylation	Kinase	FER	P16591	PSP
482	Y	Phosphorylation	Kinase	PTK2	P34152-2	GPS
482	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
485	Y	Phosphorylation	Kinase	SRC	P05480	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SRC8_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 SRC8_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
MK01_MOUSE	Mapk1	physical	22514278
CASL_MOUSE	Nedd9	physical	24574519

Drug and Disease Associations

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

Regulatory Network of SRC8_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401; SER-405 ANDSER-407, AND MASS SPECTROMETRY.	17242355 [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-418, AND MASSSPECTROMETRY.	17114649 [Abstract]
"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 THR-401, AND MASSSPECTROMETRY.	19367708 [Abstract]