dbPTM

SRC8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SRC8_HUMAN
UniProt AC	Q14247
Protein Name	Src substrate cortactin
Gene Name	CTTN
Organism	Homo sapiens (Human).
Sequence Length	550
Subcellular Localization	Cytoplasm, cytoskeleton . Cell projection, lamellipodium . Cell projection, ruffle. Cell projection, dendrite. Cell projection . Cell membrane Peripheral membrane protein Cytoplasmic side . Cell projection, podosome . Cell junction . Cell junction, fo
Protein Description	Contributes to the organization of the actin cytoskeleton and cell shape. [PubMed: 21296879 Plays a role in the formation of lamellipodia and in cell migration. 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 (By similarity Plays a role in the invasiveness of cancer cells, and the formation of metastases]
Protein Sequence	MWKASAGHAVSIAQDDAGADDWETDPDFVNDVSEKEQRWGAKTVQGSGHQEHINIHKLRENVFQEHQTLKEKELETGPKASHGYGGKFGVEQDRMDKSAVGHEYQSKLSKHCSQVDSVRGFGGKFGVQMDRVDQSAVGFEYQGKTEKHASQKDYSSGFGGKYGVQADRVDKSAVGFDYQGKTEKHESQRDYSKGFGGKYGIDKDKVDKSAVGFEYQGKTEKHESQKDYVKGFGGKFGVQTDRQDKCALGWDHQEKLQLHESQKDYKTGFGGKFGVQSERQDSAAVGFDYKEKLAKHESQQDYSKGFGGKYGVQKDRMDKNASTFEDVTQVSSAYQKTVPVEAVTSKTSNIRANFENLAKEKEQEDRRKAEAERAQRMAKERQEQEEARRKLEEQARAKTQTPPVSPAPQPTEERLPSSPVYEDAASFKAELSYRGPVSGTEPEPVYSMEAADYREASSQQGLAYATEAVYESAEAPGHYPAEDSTYDEYENDLGITAVALYDYQAAGDDEISFDPDDIITNIEMIDDGWWRGVCKGRYGLFPANYVELRQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Methylation	-----MWKASAGHAV -----CCCCCCCCEE	31.03	-
5	Phosphorylation	---MWKASAGHAVSI ---CCCCCCCCEEEE	30.93	25849741
11	Phosphorylation	ASAGHAVSIAQDDAG CCCCCEEEECCCCCC	17.00	25159151
24	Phosphorylation	AGADDWETDPDFVND CCCCCCCCCCCHHHC	48.88	30576142
33	Phosphorylation	PDFVNDVSEKEQRWG CCHHHCCCHHHHHHC	45.90	27251275
35	Ubiquitination	FVNDVSEKEQRWGAK HHHCCCHHHHHHCCE	52.20	-
42	Ubiquitination	KEQRWGAKTVQGSGH HHHHHCCEECCCCCC	45.34	-
43	Phosphorylation	EQRWGAKTVQGSGHQ HHHHCCEECCCCCCH	19.96	27794612
47	Phosphorylation	GAKTVQGSGHQEHIN CCEECCCCCCHHHCC	18.93	25159151
57	Ubiquitination	QEHINIHKLRENVFQ HHHCCHHHHHHHHHH	45.50	-
68	Phosphorylation	NVFQEHQTLKEKELE HHHHHHHHHHHHHHH	41.53	29514088
70	Malonylation	FQEHQTLKEKELETG HHHHHHHHHHHHHCC	70.85	26320211
70	Methylation	FQEHQTLKEKELETG HHHHHHHHHHHHHCC	70.85	-
72	Methylation	EHQTLKEKELETGPK HHHHHHHHHHHCCCC	67.04	-
76	Phosphorylation	LKEKELETGPKASHG HHHHHHHCCCCCCCC	71.99	21601212
79	Methylation	KELETGPKASHGYGG HHHHCCCCCCCCCCC	64.96	-
79	Ubiquitination	KELETGPKASHGYGG HHHHCCCCCCCCCCC	64.96	-
81	Phosphorylation	LETGPKASHGYGGKF HHCCCCCCCCCCCCC	24.46	21601212
84	Phosphorylation	GPKASHGYGGKFGVE CCCCCCCCCCCCCCC	19.79	25394399
87	2-Hydroxyisobutyrylation	ASHGYGGKFGVEQDR CCCCCCCCCCCCCCC	34.28	-
87	Acetylation	ASHGYGGKFGVEQDR CCCCCCCCCCCCCCC	34.28	19608861
87	Methylation	ASHGYGGKFGVEQDR CCCCCCCCCCCCCCC	34.28	19608861
87	Ubiquitination	ASHGYGGKFGVEQDR CCCCCCCCCCCCCCC	34.28	21890473
87	Ubiquitination	ASHGYGGKFGVEQDR CCCCCCCCCCCCCCC	34.28	21890473
87	Ubiquitination	ASHGYGGKFGVEQDR CCCCCCCCCCCCCCC	34.28	21890473
97	2-Hydroxyisobutyrylation	VEQDRMDKSAVGHEY CCCCCCCHHHHHHHH	30.85	-
98	Phosphorylation	EQDRMDKSAVGHEYQ CCCCCCHHHHHHHHH	24.75	25159151
104	Phosphorylation	KSAVGHEYQSKLSKH HHHHHHHHHHHHHHH	16.65	28796482
106	Phosphorylation	AVGHEYQSKLSKHCS HHHHHHHHHHHHHHH	34.36	28796482
107	Acetylation	VGHEYQSKLSKHCSQ HHHHHHHHHHHHHHC	41.05	23236377
107	Methylation	VGHEYQSKLSKHCSQ HHHHHHHHHHHHHHC	41.05	-
107	Ubiquitination	VGHEYQSKLSKHCSQ HHHHHHHHHHHHHHC	41.05	-
109	Phosphorylation	HEYQSKLSKHCSQVD HHHHHHHHHHHHCCC	24.88	25394399
110	Acetylation	EYQSKLSKHCSQVDS HHHHHHHHHHHCCCC	60.10	26051181
110	Ubiquitination	EYQSKLSKHCSQVDS HHHHHHHHHHHCCCC	60.10	-
112	S-nitrosylation	QSKLSKHCSQVDSVR HHHHHHHHHCCCCCC	3.32	2212679
113	Phosphorylation	SKLSKHCSQVDSVRG HHHHHHHHCCCCCCC	32.72	20044836
117	Phosphorylation	KHCSQVDSVRGFGGK HHHHCCCCCCCCCCC	18.17	25159151
119	Methylation	CSQVDSVRGFGGKFG HHCCCCCCCCCCCCC	38.38	-
124	2-Hydroxyisobutyrylation	SVRGFGGKFGVQMDR CCCCCCCCCCCCCCE	39.05	-
124	Acetylation	SVRGFGGKFGVQMDR CCCCCCCCCCCCCCE	39.05	25953088
124	Methylation	SVRGFGGKFGVQMDR CCCCCCCCCCCCCCE	39.05	-
124	Ubiquitination	SVRGFGGKFGVQMDR CCCCCCCCCCCCCCE	39.05	21890473
124	Ubiquitination	SVRGFGGKFGVQMDR CCCCCCCCCCCCCCE	39.05	21890473
124	Ubiquitination	SVRGFGGKFGVQMDR CCCCCCCCCCCCCCE	39.05	21890473
131	Methylation	KFGVQMDRVDQSAVG CCCCCCCEECHHHCC	28.68	-
135	Phosphorylation	QMDRVDQSAVGFEYQ CCCEECHHHCCCEEE	22.06	21945579
141	Phosphorylation	QSAVGFEYQGKTEKH HHHCCCEEECCCCCC	21.95	21945579
144	Sumoylation	VGFEYQGKTEKHASQ CCCEEECCCCCCCCC	37.68	-
144	Acetylation	VGFEYQGKTEKHASQ CCCEEECCCCCCCCC	37.68	23236377
144	Sumoylation	VGFEYQGKTEKHASQ CCCEEECCCCCCCCC	37.68	25114211
144	Ubiquitination	VGFEYQGKTEKHASQ CCCEEECCCCCCCCC	37.68	21890473
144	Ubiquitination	VGFEYQGKTEKHASQ CCCEEECCCCCCCCC	37.68	21890473
144	Ubiquitination	VGFEYQGKTEKHASQ CCCEEECCCCCCCCC	37.68	21890473
145	Phosphorylation	GFEYQGKTEKHASQK CCEEECCCCCCCCCC	58.03	21945579
150	Phosphorylation	GKTEKHASQKDYSSG CCCCCCCCCCCCCCC	37.17	23927012
152	2-Hydroxyisobutyrylation	TEKHASQKDYSSGFG CCCCCCCCCCCCCCC	57.02	-
152	Acetylation	TEKHASQKDYSSGFG CCCCCCCCCCCCCCC	57.02	23236377
152	Ubiquitination	TEKHASQKDYSSGFG CCCCCCCCCCCCCCC	57.02	-
154	Phosphorylation	KHASQKDYSSGFGGK CCCCCCCCCCCCCCC	16.27	27273156
155	Phosphorylation	HASQKDYSSGFGGKY CCCCCCCCCCCCCCC	33.83	25159151
156	Phosphorylation	ASQKDYSSGFGGKYG CCCCCCCCCCCCCCC	31.73	27259358
161	2-Hydroxyisobutyrylation	YSSGFGGKYGVQADR CCCCCCCCCCCCCCE	38.93	-
161	Acetylation	YSSGFGGKYGVQADR CCCCCCCCCCCCCCE	38.93	23954790
161	Malonylation	YSSGFGGKYGVQADR CCCCCCCCCCCCCCE	38.93	26320211
161	Methylation	YSSGFGGKYGVQADR CCCCCCCCCCCCCCE	38.93	-
161	Ubiquitination	YSSGFGGKYGVQADR CCCCCCCCCCCCCCE	38.93	21890473
161	Ubiquitination	YSSGFGGKYGVQADR CCCCCCCCCCCCCCE	38.93	21890473
161	Ubiquitination	YSSGFGGKYGVQADR CCCCCCCCCCCCCCE	38.93	21890473
162	Phosphorylation	SSGFGGKYGVQADRV CCCCCCCCCCCCCEE	26.29	25394399
168	Methylation	KYGVQADRVDKSAVG CCCCCCCEECHHHCC	41.36	-
171	2-Hydroxyisobutyrylation	VQADRVDKSAVGFDY CCCCEECHHHCCCCC	37.14	-
171	Acetylation	VQADRVDKSAVGFDY CCCCEECHHHCCCCC	37.14	30583563
171	Malonylation	VQADRVDKSAVGFDY CCCCEECHHHCCCCC	37.14	26320211
171	Ubiquitination	VQADRVDKSAVGFDY CCCCEECHHHCCCCC	37.14	21890473
171	Ubiquitination	VQADRVDKSAVGFDY CCCCEECHHHCCCCC	37.14	21890473
171	Ubiquitination	VQADRVDKSAVGFDY CCCCEECHHHCCCCC	37.14	21890473
172	Phosphorylation	QADRVDKSAVGFDYQ CCCEECHHHCCCCCC	24.59	21945579
178	Phosphorylation	KSAVGFDYQGKTEKH HHHCCCCCCCCCCCC	19.53	21945579
181	Sumoylation	VGFDYQGKTEKHESQ CCCCCCCCCCCCHHH	37.68	-
181	Acetylation	VGFDYQGKTEKHESQ CCCCCCCCCCCCHHH	37.68	26051181
181	Sumoylation	VGFDYQGKTEKHESQ CCCCCCCCCCCCHHH	37.68	25114211
181	Ubiquitination	VGFDYQGKTEKHESQ CCCCCCCCCCCCHHH	37.68	21890473
181	Ubiquitination	VGFDYQGKTEKHESQ CCCCCCCCCCCCHHH	37.68	21890473
181	Ubiquitination	VGFDYQGKTEKHESQ CCCCCCCCCCCCHHH	37.68	21890473
182	Phosphorylation	GFDYQGKTEKHESQR CCCCCCCCCCCHHHH	58.03	21945579
187	Phosphorylation	GKTEKHESQRDYSKG CCCCCCHHHHCCCCC	30.18	24719451
191	Phosphorylation	KHESQRDYSKGFGGK CCHHHHCCCCCCCCC	17.93	28152594
192	Phosphorylation	HESQRDYSKGFGGKY CHHHHCCCCCCCCCC	30.50	28152594
193	2-Hydroxyisobutyrylation	ESQRDYSKGFGGKYG HHHHCCCCCCCCCCC	52.62	-
193	Acetylation	ESQRDYSKGFGGKYG HHHHCCCCCCCCCCC	52.62	-
193	Ubiquitination	ESQRDYSKGFGGKYG HHHHCCCCCCCCCCC	52.62	-
198	Acetylation	YSKGFGGKYGIDKDK CCCCCCCCCCCCHHH	40.46	19608861
198	Malonylation	YSKGFGGKYGIDKDK CCCCCCCCCCCCHHH	40.46	30639696
198	Ubiquitination	YSKGFGGKYGIDKDK CCCCCCCCCCCCHHH	40.46	21890473
198	Ubiquitination	YSKGFGGKYGIDKDK CCCCCCCCCCCCHHH	40.46	21890473
198	Ubiquitination	YSKGFGGKYGIDKDK CCCCCCCCCCCCHHH	40.46	21890473
199	Phosphorylation	SKGFGGKYGIDKDKV CCCCCCCCCCCHHHC	23.69	25394399
203	Acetylation	GGKYGIDKDKVDKSA CCCCCCCHHHCCHHH	58.49	166221
203	Malonylation	GGKYGIDKDKVDKSA CCCCCCCHHHCCHHH	58.49	26320211
208	Ubiquitination	IDKDKVDKSAVGFEY CCHHHCCHHHCCCEE	43.21	21890473
208	Ubiquitination	IDKDKVDKSAVGFEY CCHHHCCHHHCCCEE	43.21	21890473
208	Ubiquitination	IDKDKVDKSAVGFEY CCHHHCCHHHCCCEE	43.21	21890473
209	Phosphorylation	DKDKVDKSAVGFEYQ CHHHCCHHHCCCEEE	24.59	21945579
215	Phosphorylation	KSAVGFEYQGKTEKH HHHCCCEEECCCCCC	21.95	21945579
218	Sumoylation	VGFEYQGKTEKHESQ CCCEEECCCCCCHHH	37.68	-
218	Acetylation	VGFEYQGKTEKHESQ CCCEEECCCCCCHHH	37.68	110858551
218	Sumoylation	VGFEYQGKTEKHESQ CCCEEECCCCCCHHH	37.68	25114211
219	Phosphorylation	GFEYQGKTEKHESQK CCEEECCCCCCHHHH	58.03	21945579
224	Phosphorylation	GKTEKHESQKDYVKG CCCCCCHHHHHHHHC	42.10	24719451
226	2-Hydroxyisobutyrylation	TEKHESQKDYVKGFG CCCCHHHHHHHHCCC	61.37	-
226	Succinylation	TEKHESQKDYVKGFG CCCCHHHHHHHHCCC	61.37	23954790
226	Ubiquitination	TEKHESQKDYVKGFG CCCCHHHHHHHHCCC	61.37	-
228	Phosphorylation	KHESQKDYVKGFGGK CCHHHHHHHHCCCCC	15.88	25394399
230	2-Hydroxyisobutyrylation	ESQKDYVKGFGGKFG HHHHHHHHCCCCCCC	42.15	-
230	Ubiquitination	ESQKDYVKGFGGKFG HHHHHHHHCCCCCCC	42.15	-
235	Acetylation	YVKGFGGKFGVQTDR HHHCCCCCCCCCCCC	39.05	19608861
235	Methylation	YVKGFGGKFGVQTDR HHHCCCCCCCCCCCC	39.05	19608861
235	Ubiquitination	YVKGFGGKFGVQTDR HHHCCCCCCCCCCCC	39.05	21890473
235	Ubiquitination	YVKGFGGKFGVQTDR HHHCCCCCCCCCCCC	39.05	21890473
235	Ubiquitination	YVKGFGGKFGVQTDR HHHCCCCCCCCCCCC	39.05	21890473
245	Ubiquitination	VQTDRQDKCALGWDH CCCCCCCCCCCCCCH	17.05	-
261	Phosphorylation	EKLQLHESQKDYKTG HHHHHCHHHCCHHCC	31.61	28355574
261 (in isoform 2)	Phosphorylation	-	31.61	23911959
261 (in isoform 3)	Phosphorylation	-	31.61	23911959
263	2-Hydroxyisobutyrylation	LQLHESQKDYKTGFG HHHCHHHCCHHCCCC	72.76	-
263	Acetylation	LQLHESQKDYKTGFG HHHCHHHCCHHCCCC	72.76	26051181
263	Succinylation	LQLHESQKDYKTGFG HHHCHHHCCHHCCCC	72.76	23954790
263	Ubiquitination	LQLHESQKDYKTGFG HHHCHHHCCHHCCCC	72.76	-
265	Phosphorylation	LHESQKDYKTGFGGK HCHHHCCHHCCCCCC	19.93	18180459
265 (in isoform 2)	Phosphorylation	-	19.93	25394399
265 (in isoform 3)	Phosphorylation	-	19.93	25394399
266	Malonylation	HESQKDYKTGFGGKF CHHHCCHHCCCCCCC	52.91	26320211
266	Ubiquitination	HESQKDYKTGFGGKF CHHHCCHHCCCCCCC	52.91	-
266 (in isoform 2)	Phosphorylation	-	52.91	25394399
266 (in isoform 3)	Phosphorylation	-	52.91	25394399
267	Phosphorylation	ESQKDYKTGFGGKFG HHHCCHHCCCCCCCC	31.36	21601212
272	Acetylation	YKTGFGGKFGVQSER HHCCCCCCCCCCCCC	39.05	19608861
272	Malonylation	YKTGFGGKFGVQSER HHCCCCCCCCCCCCC	39.05	26320211
272	Methylation	YKTGFGGKFGVQSER HHCCCCCCCCCCCCC	39.05	19608861
272	Ubiquitination	YKTGFGGKFGVQSER HHCCCCCCCCCCCCC	39.05	21890473
277	Phosphorylation	GGKFGVQSERQDSAA CCCCCCCCCCCCCCC	32.13	28857561
282	Phosphorylation	VQSERQDSAAVGFDY CCCCCCCCCCCCCCH	15.13	20068231
289	Phosphorylation	SAAVGFDYKEKLAKH CCCCCCCHHHHHHHC	20.84	25394399
290	2-Hydroxyisobutyrylation	AAVGFDYKEKLAKHE CCCCCCHHHHHHHCC	50.66	-
290	Acetylation	AAVGFDYKEKLAKHE CCCCCCHHHHHHHCC	50.66	26051181
290	Ubiquitination	AAVGFDYKEKLAKHE CCCCCCHHHHHHHCC	50.66	-
295	Sumoylation	DYKEKLAKHESQQDY CHHHHHHHCCCHHHH	59.34	-
295	Acetylation	DYKEKLAKHESQQDY CHHHHHHHCCCHHHH	59.34	-
295	Sumoylation	DYKEKLAKHESQQDY CHHHHHHHCCCHHHH	59.34	28112733
298	Phosphorylation	EKLAKHESQQDYSKG HHHHHCCCHHHHHHC	32.62	20363754
302	Phosphorylation	KHESQQDYSKGFGGK HCCCHHHHHHCCCCC	14.14	28152594
303	Phosphorylation	HESQQDYSKGFGGKY CCCHHHHHHCCCCCC	34.29	28152594
304	2-Hydroxyisobutyrylation	ESQQDYSKGFGGKYG CCHHHHHHCCCCCCC	52.62	-
304	Acetylation	ESQQDYSKGFGGKYG CCHHHHHHCCCCCCC	52.62	19608861
304	Ubiquitination	ESQQDYSKGFGGKYG CCHHHHHHCCCCCCC	52.62	19608861
309	Acetylation	YSKGFGGKYGVQKDR HHHCCCCCCCCCHHH	38.93	19608861
309	Methylation	YSKGFGGKYGVQKDR HHHCCCCCCCCCHHH	38.93	19608861
310	Phosphorylation	SKGFGGKYGVQKDRM HHCCCCCCCCCHHHC	26.29	28152594
314	Acetylation	GGKYGVQKDRMDKNA CCCCCCCHHHCCCCC	44.91	-
319	Acetylation	VQKDRMDKNASTFED CCHHHCCCCCCCHHC	45.10	166227
322	Phosphorylation	DRMDKNASTFEDVTQ HHCCCCCCCHHCHHH	42.92	21945579
323	Phosphorylation	RMDKNASTFEDVTQV HCCCCCCCHHCHHHH	28.74	21945579
328	Phosphorylation	ASTFEDVTQVSSAYQ CCCHHCHHHHHHHHH	35.26	21945579
331	Phosphorylation	FEDVTQVSSAYQKTV HHCHHHHHHHHHCCC	10.22	21945579
332	Phosphorylation	EDVTQVSSAYQKTVP HCHHHHHHHHHCCCC	31.94	21945579
334	Phosphorylation	VTQVSSAYQKTVPVE HHHHHHHHHCCCCHH	16.70	21945579
336	Ubiquitination	QVSSAYQKTVPVEAV HHHHHHHCCCCHHHH	38.52	21890473
337	O-linked_Glycosylation	VSSAYQKTVPVEAVT HHHHHHCCCCHHHHC	17.95	OGP
337	Phosphorylation	VSSAYQKTVPVEAVT HHHHHHCCCCHHHHC	17.95	29978859
344	O-linked_Glycosylation	TVPVEAVTSKTSNIR CCCHHHHCCCCCHHH	31.39	OGP
344	Phosphorylation	TVPVEAVTSKTSNIR CCCHHHHCCCCCHHH	31.39	20068231
345	O-linked_Glycosylation	VPVEAVTSKTSNIRA CCHHHHCCCCCHHHH	27.60	OGP
345	Phosphorylation	VPVEAVTSKTSNIRA CCHHHHCCCCCHHHH	27.60	20068231
346	Acetylation	PVEAVTSKTSNIRAN CHHHHCCCCCHHHHH	46.75	-
346	Malonylation	PVEAVTSKTSNIRAN CHHHHCCCCCHHHHH	46.75	26320211
346	Ubiquitination	PVEAVTSKTSNIRAN CHHHHCCCCCHHHHH	46.75	-
347	O-linked_Glycosylation	VEAVTSKTSNIRANF HHHHCCCCCHHHHHH	27.12	OGP
347	Phosphorylation	VEAVTSKTSNIRANF HHHHCCCCCHHHHHH	27.12	29978859
348	Phosphorylation	EAVTSKTSNIRANFE HHHCCCCCHHHHHHH	33.71	29978859
359	Malonylation	ANFENLAKEKEQEDR HHHHHHHHHHHHHHH	72.92	26320211
359	Succinylation	ANFENLAKEKEQEDR HHHHHHHHHHHHHHH	72.92	23954790
399	Phosphorylation	EEQARAKTQTPPVSP HHHHHHHHCCCCCCC	36.37	29255136
401	Phosphorylation	QARAKTQTPPVSPAP HHHHHHCCCCCCCCC	34.49	19664994
405	Phosphorylation	KTQTPPVSPAPQPTE HHCCCCCCCCCCCCC	22.55	19664994
411	Phosphorylation	VSPAPQPTEERLPSS CCCCCCCCCCCCCCC	45.27	20201521
414	Methylation	APQPTEERLPSSPVY CCCCCCCCCCCCCCC	45.74	-
417	Phosphorylation	PTEERLPSSPVYEDA CCCCCCCCCCCCCCH	52.44	29255136
418	Phosphorylation	TEERLPSSPVYEDAA CCCCCCCCCCCCCHH	19.22	19664994
421	Phosphorylation	RLPSSPVYEDAASFK CCCCCCCCCCHHHCE	16.10	29255136
426	Phosphorylation	PVYEDAASFKAELSY CCCCCHHHCEEEEEE	29.06	29255136
432	Phosphorylation	ASFKAELSYRGPVSG HHCEEEEEECCCCCC	12.32	21945579
433	Phosphorylation	SFKAELSYRGPVSGT HCEEEEEECCCCCCC	32.01	21945579
438	Phosphorylation	LSYRGPVSGTEPEPV EEECCCCCCCCCCCC	43.03	21945579
440	Phosphorylation	YRGPVSGTEPEPVYS ECCCCCCCCCCCCEE	40.64	21945579
446	Phosphorylation	GTEPEPVYSMEAADY CCCCCCCEECCCHHH	17.02	25159151
447	Phosphorylation	TEPEPVYSMEAADYR CCCCCCEECCCHHHH	15.47	21945579
448	Sulfoxidation	EPEPVYSMEAADYRE CCCCCEECCCHHHHH	1.91	28465586
453	Phosphorylation	YSMEAADYREASSQQ EECCCHHHHHHHHHH	12.96	21945579
464	Phosphorylation	SSQQGLAYATEAVYE HHHHCHHHHHHHHHH	21.06	20736484
470	Phosphorylation	AYATEAVYESAEAPG HHHHHHHHHHCCCCC	15.94	21696810
479	Phosphorylation	SAEAPGHYPAEDSTY HCCCCCCCCCCCCCC	15.28	20736484
484	Phosphorylation	GHYPAEDSTYDEYEN CCCCCCCCCCCHHCC	22.00	22468782
485	Phosphorylation	HYPAEDSTYDEYEND CCCCCCCCCCHHCCC	47.52	-
486	Phosphorylation	YPAEDSTYDEYENDL CCCCCCCCCHHCCCC	15.66	15561106
489	Phosphorylation	EDSTYDEYENDLGIT CCCCCCHHCCCCCEE	19.68	-
503	Phosphorylation	TAVALYDYQAAGDDE EEEEEEEHHHCCCCC	6.11	-
538	Phosphorylation	RGVCKGRYGLFPANY CCHHCCCCCEEECHH	27.18	20044836
545	Phosphorylation	YGLFPANYVELRQ-- CCEEECHHHEECC--	9.45	25106551
547 (in isoform 2)	Phosphorylation	-	28.07	25137130
548 (in isoform 2)	Phosphorylation	-	4.33	25137130
549	Methylation	PANYVELRQ------ ECHHHEECC------	27.02	-
551 (in isoform 2)	Phosphorylation	-		25137130

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
113	S	Phosphorylation	Kinase	ATM	Q13315	PSP
113	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
261	S	Phosphorylation	Kinase	PRKCI	P41743	GPS
298	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
298	S	Phosphorylation	Kinase	PRKD3	O94806	PSP
298	S	Phosphorylation	Kinase	PRKD2	Q9BZL6	PSP
298	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP
334	Y	Phosphorylation	Kinase	SRC	P12931	PSP
348	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP
401	T	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
405	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
405	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
405	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
405	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
405	S	Phosphorylation	Kinase	CDK2	P24941	PSP
405	S	Phosphorylation	Kinase	CDK1	P06493	PSP
418	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
418	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
418	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
421	Y	Phosphorylation	Kinase	FYN	P06241	PSP
421	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
421	Y	Phosphorylation	Kinase	PTK2B	Q14289	GPS
421	Y	Phosphorylation	Kinase	SYK	P43405	PSP
446	Y	Phosphorylation	Kinase	FYN	P06241	PSP
446	Y	Phosphorylation	Kinase	FGFR1	P11362	PhosphoELM
453	Y	Phosphorylation	Kinase	FYN	P06241	PSP
470	Y	Phosphorylation	Kinase	SRC	P12931	PSP
470	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
470	Y	Phosphorylation	Kinase	FYN	P06241	PSP
470	Y	Phosphorylation	Kinase	PTK2B	Q14289	GPS
470	Y	Phosphorylation	Kinase	FAK1	Q05397	Uniprot
486	Y	Phosphorylation	Kinase	FYN	P06241	PSP
486	Y	Phosphorylation	Kinase	PTK2B	Q14289	GPS
486	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
486	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
486	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
489	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:24658274
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF1	Q9HCE7	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	CBLL1	Q75N03	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF1	Q9HCE7	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SRC8_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 SRC8_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
WIPF1_HUMAN	WIPF1	physical	12620186
CTND1_HUMAN	CTNND1	physical	12835311
CHD3_HUMAN	CHD3	physical	16169070
WASL_HUMAN	WASL	physical	11830518
CRUM2_HUMAN	CRB2	physical	11439336
SHAN2_HUMAN	SHANK2	physical	9742101
MYLK_HUMAN	MYLK	physical	12408982
ARP2_HUMAN	ACTR2	physical	11018051
ARP3_HUMAN	ACTR3	physical	11018051
ARPC2_HUMAN	ARPC2	physical	11018051
ARPC4_HUMAN	ARPC4	physical	11018051
ARPC3_HUMAN	ARPC3	physical	11018051
EP300_HUMAN	EP300	physical	18850005
HDAC6_HUMAN	HDAC6	physical	17643370
FBW1A_HUMAN	BTRC	physical	22514278
CD2AP_HUMAN	CD2AP	physical	12672817
ASAP1_HUMAN	ASAP1	physical	12672817
SPD2A_HUMAN	SH3PXD2A	physical	12672817
WASL_HUMAN	WASL	physical	12672817
ASAP1_HUMAN	ASAP1	physical	17893324
FAK1_HUMAN	PTK2	physical	17893324
HDAC6_HUMAN	HDAC6	physical	21847094
KCNA2_HUMAN	KCNA2	physical	17959782
ASAP1_HUMAN	ASAP1	physical	15719014
PAXI_HUMAN	PXN	physical	15719014
ACK1_HUMAN	TNK2	physical	22952966
THY1_HUMAN	THY1	physical	22939629
UPAR_HUMAN	PLAUR	physical	22939629
UBL4A_HUMAN	UBL4A	physical	22939629
SUCB2_HUMAN	SUCLG2	physical	22939629
ASAP1_HUMAN	ASAP1	physical	16636290
DYN2_HUMAN	DNM2	physical	16636290
ARP3_HUMAN	ACTR3	physical	11231575
ARP2_HUMAN	ACTR2	physical	12732638
ARP3_HUMAN	ACTR3	physical	12732638
ACTG_HUMAN	ACTG1	physical	11231575
ERF3A_HUMAN	GSPT1	physical	22863883
ERF3B_HUMAN	GSPT2	physical	22863883
SYSC_HUMAN	SARS	physical	22863883
SNX1_HUMAN	SNX1	physical	22863883
SNX2_HUMAN	SNX2	physical	22863883
UGDH_HUMAN	UGDH	physical	22863883
SRC8_HUMAN	CTTN	physical	24867096
SPR2A_HUMAN	SPRR2A	physical	18155796
CSN7A_HUMAN	COPS7A	physical	26344197
HEXI1_HUMAN	HEXIM1	physical	26344197
MYO1E_HUMAN	MYO1E	physical	26344197
USO1_HUMAN	USO1	physical	26344197
CASL_HUMAN	NEDD9	physical	24574519
KCNA3_HUMAN	KCNA3	physical	25739456
KEAP1_HUMAN	KEAP1	physical	26602019

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 SRC8_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-87; LYS-198; LYS-218;LYS-235; LYS-272; LYS-304 AND LYS-309, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-405; SER-418; TYR-421AND TYR-446, AND MASS SPECTROMETRY.	19690332 [Abstract]
"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 THR-399; THR-401; SER-405;SER-417; SER-418 AND TYR-421, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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 THR-399; THR-401; SER-405;THR-411; SER-417 AND SER-418, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401 AND SER-405, ANDMASS SPECTROMETRY.	18220336 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-399; THR-401; SER-405;SER-418 AND TYR-421, AND MASS SPECTROMETRY.	18088087 [Abstract]
"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 THR-401; SER-405 ANDSER-418, AND MASS SPECTROMETRY.	18187866 [Abstract]
"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-113; SER-117; THR-399;THR-401; SER-405; SER-417 AND TYR-421, AND MASS SPECTROMETRY.	17287340 [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 THR-401; SER-405 ANDSER-418, AND MASS SPECTROMETRY.	17081983 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-418, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401; SER-405 ANDSER-418, AND MASS SPECTROMETRY.	15302935 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-154; TYR-421 ANDTYR-446, AND MASS SPECTROMETRY.	19534553 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-421 AND TYR-446, ANDMASS SPECTROMETRY.	17389395 [Abstract]
"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-141, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling."; Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.; EMBO J. 25:5058-5070(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-446, AND MASSSPECTROMETRY.	17053785 [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 [LARGE SCALE ANALYSIS] AT TYR-215; TYR-446 ANDTYR-453, AND MASS SPECTROMETRY.	15592455 [Abstract]
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-446, AND MASSSPECTROMETRY.	15951569 [Abstract]
"Phosphoproteome analysis of HeLa cells using stable isotope labelingwith amino acids in cell culture (SILAC)."; Amanchy R., Kalume D.E., Iwahori A., Zhong J., Pandey A.; J. Proteome Res. 4:1661-1671(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-334; TYR-446 ANDTYR-453, AND MASS SPECTROMETRY.	16212419 [Abstract]
"Profiling of tyrosine phosphorylation pathways in human cells usingmass spectrometry."; Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T.,Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.; Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-421, AND MASSSPECTROMETRY.	12522270 [Abstract]