dbPTM

SRC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SRC_HUMAN
UniProt AC	P12931
Protein Name	Proto-oncogene tyrosine-protein kinase Src
Gene Name	SRC
Organism	Homo sapiens (Human).
Sequence Length	536
Subcellular Localization	Cell membrane . Mitochondrion inner membrane . Nucleus . Cytoplasm, cytoskeleton . Cytoplasm, perinuclear region . Localizes to focal adhesion sites following integrin engagement. Localization to focal adhesion sites requires myristoylation and the S
Protein Description	Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN) (Probable). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN). [PubMed: 21411625 In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43 (GJA1 SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1 (Probable Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors (By similarity Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1]
Protein Sequence	MGSNKSKPKDASQRRRSLEPAENVHGAGGGAFPASQTPSKPASADGHRGPSAAFAPAAAEPKLFGGFNSSDTVTSPQRAGPLAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGLCHRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGETGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	N-myristoyl glycine	------MGSNKSKPK ------CCCCCCCCC	39.67	-
2	Myristoylation	------MGSNKSKPK ------CCCCCCCCC	39.67	7525268
6	Phosphorylation	--MGSNKSKPKDASQ --CCCCCCCCCCHHH	59.44	20860994
12	Phosphorylation	KSKPKDASQRRRSLE CCCCCCHHHHHHCCC	34.06	2996780
17 (in isoform 2)	Phosphorylation	-	34.96	21406692
17	Phosphorylation	DASQRRRSLEPAENV CHHHHHHCCCCCCCC	34.96	19664994
35	Phosphorylation	GGGAFPASQTPSKPA CCCCCCCCCCCCCCC	34.52	7929427
37	Phosphorylation	GAFPASQTPSKPASA CCCCCCCCCCCCCCC	27.34	23927012
39	Phosphorylation	FPASQTPSKPASADG CCCCCCCCCCCCCCC	55.44	23927012
43	Phosphorylation	QTPSKPASADGHRGP CCCCCCCCCCCCCCC	35.11	23927012
51	Phosphorylation	ADGHRGPSAAFAPAA CCCCCCCCCCCCCCC	34.74	20071362
62	Acetylation	APAAAEPKLFGGFNS CCCCCCCCCCCCCCC	48.21	156773
69	Phosphorylation	KLFGGFNSSDTVTSP CCCCCCCCCCCCCCC	27.59	7929427
70	Phosphorylation	LFGGFNSSDTVTSPQ CCCCCCCCCCCCCCC	38.10	28176443
72	Phosphorylation	GGFNSSDTVTSPQRA CCCCCCCCCCCCCCC	27.86	28176443
74	Phosphorylation	FNSSDTVTSPQRAGP CCCCCCCCCCCCCCC	36.46	7929427
75	Phosphorylation	NSSDTVTSPQRAGPL CCCCCCCCCCCCCCC	18.07	29255136
93	Phosphorylation	VTTFVALYDYESRTE CEEEEEEEECCCCCC	13.52	-
97	Phosphorylation	VALYDYESRTETDLS EEEEECCCCCCEECC	37.97	1713455
101	Phosphorylation	DYESRTETDLSFKKG ECCCCCCEECCCCCC	41.44	30108239
104	Phosphorylation	SRTETDLSFKKGERL CCCCEECCCCCCCCE	37.52	30108239
106	Ubiquitination	TETDLSFKKGERLQI CCEECCCCCCCCEEE	57.39	33845483
180	Phosphorylation	GTFLVRESETTKGAY CCEEEECCCCCCCEE	29.67	28060719
182	Phosphorylation	FLVRESETTKGAYCL EEEECCCCCCCEEEE	42.99	28060719
183	Phosphorylation	LVRESETTKGAYCLS EEECCCCCCCEEEEE	24.35	28060719
184	Ubiquitination	VRESETTKGAYCLSV EECCCCCCCEEEEEH	49.30	33845483
187	Phosphorylation	SETTKGAYCLSVSDF CCCCCCEEEEEHHHC	11.55	28152594
190	Phosphorylation	TKGAYCLSVSDFDNA CCCEEEEEHHHCCCC	18.93	28060719
203	Acetylation	NAKGLNVKHYKIRKL CCCCCCCCEEEEEEC	39.89	25953088
212	Phosphorylation	YKIRKLDSGGFYITS EEEEECCCCCEEEEE	51.78	28060719
216	Phosphorylation	KLDSGGFYITSRTQF ECCCCCEEEEEHHHC	13.43	14760089
218	Phosphorylation	DSGGFYITSRTQFNS CCCCEEEEEHHHCCC	10.77	28060719
219	Phosphorylation	SGGFYITSRTQFNSL CCCEEEEEHHHCCCH	24.62	28060719
246	Phosphorylation	GLCHRLTTVCPTSKP CHHHEEEEECCCCCC	25.38	-
250	Phosphorylation	RLTTVCPTSKPQTQG EEEEECCCCCCCCCC	44.23	-
252	Ubiquitination	TTVCPTSKPQTQGLA EEECCCCCCCCCCCC	43.56	33845483
255	Phosphorylation	CPTSKPQTQGLAKDA CCCCCCCCCCCCCCH	32.88	20860994
269	Phosphorylation	AWEIPRESLRLEVKL HHHCCHHHHHEEEEE	21.77	30266825
298	Ubiquitination	GTTRVAIKTLKPGTM CCEEEEEEEECCCCC	37.76	PubMed
304	Phosphorylation	IKTLKPGTMSPEAFL EEEECCCCCCHHHHH	24.01	20068231
306	Phosphorylation	TLKPGTMSPEAFLQE EECCCCCCHHHHHHH	21.30	20068231
338	Phosphorylation	VVSEEPIYIVTEYMS EECCCCEEEEEEECC	10.47	7578094
348	Phosphorylation	TEYMSKGSLLDFLKG EEECCCCCHHHHHHC	29.51	27251275
375	Phosphorylation	DMAAQIASGMAYVER HHHHHHHHCCHHHHH	30.63	22210691
379	Phosphorylation	QIASGMAYVERMNYV HHHHCCHHHHHHHHH	8.24	22210691
385	Phosphorylation	AYVERMNYVHRDLRA HHHHHHHHHCHHHHH	6.57	20071362
404	Ubiquitination	VGENLVCKVADFGLA ECCCEEEEEHHHHHH	32.74	33845483
419	Phosphorylation	RLIEDNEYTARQGAK HHHCCCCCCCCCCCC	16.38	19664994
420	Phosphorylation	LIEDNEYTARQGAKF HHCCCCCCCCCCCCC	14.80	29255136
426	Ubiquitination	YTARQGAKFPIKWTA CCCCCCCCCCCEECC	59.50	22817900
426	Acetylation	YTARQGAKFPIKWTA CCCCCCCCCCCEECC	59.50	-
430	Ubiquitination	QGAKFPIKWTAPEAA CCCCCCCEECCCCHH	38.44	21890473
430	Acetylation	QGAKFPIKWTAPEAA CCCCCCCEECCCCHH	38.44	-
430 (in isoform 1)	Ubiquitination	-	38.44	21890473
432	Ubiquitination	AKFPIKWTAPEAALY CCCCCEECCCCHHHH	27.60	22817900
436 (in isoform 2)	Ubiquitination	-	11.16	21890473
436	Ubiquitination	IKWTAPEAALYGRFT CEECCCCHHHHCCEE	11.16	21890473
439	Phosphorylation	TAPEAALYGRFTIKS CCCCHHHHCCEEEEH	11.09	27273156
443	Phosphorylation	AALYGRFTIKSDVWS HHHHCCEEEEHHHHH	26.57	24505115
511	Phosphorylation	KEPEERPTFEYLQAF CCCCCCCHHHHHHHH	35.01	7929427
522	Phosphorylation	LQAFLEDYFTSTEPQ HHHHHHHHHCCCCCC	10.20	7929427
524	Phosphorylation	AFLEDYFTSTEPQYQ HHHHHHHCCCCCCCC	28.63	26074081
525	Phosphorylation	FLEDYFTSTEPQYQP HHHHHHCCCCCCCCC	22.37	26356563
526	Phosphorylation	LEDYFTSTEPQYQPG HHHHHCCCCCCCCCC	48.94	26356563
530	Phosphorylation	FTSTEPQYQPGENL- HCCCCCCCCCCCCC-	27.65	17449913
536 (in isoform 2)	Phosphorylation	-	6.90	27642862

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
12	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
12	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
17	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
17	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
17	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
39	S	Phosphorylation	Kinase	PIK3CG	P48736	PSP
51	S	Phosphorylation	Kinase	CHK1	O14757	PSP
70	S	Phosphorylation	Kinase	PIK3CG	P48736	PSP
75	S	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
75	S	Phosphorylation	Kinase	CDK5	Q00535	Uniprot
75	S	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
216	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
216	Y	Phosphorylation	Kinase	SRC	P12931	GPS
338	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
338	Y	Phosphorylation	Kinase	SRC	P12931	PSP
419	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
419	Y	Phosphorylation	Kinase	AXL	P30530	PSP
419	Y	Phosphorylation	Kinase	SRC	P05480	PSP
419	Y	Phosphorylation	Kinase	SRC	P12931	PSP
419	Y	Phosphorylation	Kinase	PDGFRB	P09619	PSP
419	Y	Phosphorylation	Kinase	PDGFRA	P16234	PSP
419	Y	Phosphorylation	Kinase	PRKACA	P17612	GPS
419	Y	Phosphorylation	Kinase	FAK2	Q14289	Uniprot
419	Y	Phosphorylation	Kinase	CSK	P41240	PSP
419	Y	Phosphorylation	Kinase	CHEK1	O14757	GPS
530	Y	Phosphorylation	Kinase	SRC	Q9WUD9	PSP
530	Y	Phosphorylation	Kinase	SRC	P12931	PSP
530	Y	Phosphorylation	Kinase	CSK	P41240	Uniprot
530	Y	Phosphorylation	Kinase	CHEK1	O14757	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	STUB1	Q9UNE7	PMID:21911421
-	K	Ubiquitination	E3 ubiquitin ligase	CBLC	Q9ULV8	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	CBLB	Q13191	PMID:12907674
-	K	Ubiquitination	E3 ubiquitin ligase	CBL	P22681	PMID:10514377
-	K	Ubiquitination	E3 ubiquitin ligase	LNX1	Q8TBB1	PMID:17936276
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4	P46934	PMID:12907674

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
2	G	Myristoylation	7525268
Myristoylated at Gly-2, and this is essential for targeting to membranes.
75	S	Phosphorylation	21442427
CDK5-mediated phosphorylation at Ser-75 targets SRC to ubiquitin-dependent degradation and thus leads to cytoskeletal reorganization.
75	S	ubiquitylation	21442427
CDK5-mediated phosphorylation at Ser-75 targets SRC to ubiquitin-dependent degradation and thus leads to cytoskeletal reorganization.

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 SRC_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EPHB2_HUMAN	EPHB2	physical	9632142
NU2M_HUMAN	ND2	physical	15069201
P85A_HUMAN	PIK3R1	physical	10487518
ESR2_HUMAN	ESR2	physical	11032808
BCAR1_HUMAN	BCAR1	physical	10487518
ESR1_HUMAN	ESR1	physical	11032808
ANDR_HUMAN	AR	physical	11032808
ANDR_HUMAN	AR	physical	15466214
PELP1_HUMAN	PELP1	physical	15466214
TRPC6_HUMAN	TRPC6	physical	14761972
NMDE1_HUMAN	GRIN2A	physical	12932824
PLS1_HUMAN	PLSCR1	physical	12871937
PLD2_HUMAN	PLD2	physical	12697812
PLD1_HUMAN	PLD1	physical	12697812
CNRG_HUMAN	PDE6G	physical	12624098
ARBK1_HUMAN	ADRBK1	physical	12624098
GRB2_HUMAN	GRB2	physical	12624098
ESR1_HUMAN	ESR1	physical	11564893
KHDR1_HUMAN	KHDRBS1	physical	16169070
WASP_HUMAN	WAS	physical	8805332
KIFA3_HUMAN	KIFAP3	physical	8900189
KHDR1_HUMAN	KHDRBS1	physical	11960376
ADRB3_HUMAN	ADRB3	physical	11013230
GRB10_HUMAN	GRB10	physical	10871840
JIP3_HUMAN	MAPK8IP3	physical	12226752
PTN21_HUMAN	PTPN21	physical	7519780
FAK1_HUMAN	PTK2	physical	11980671
MTAP2_HUMAN	MAP2	physical	10781592
LRP1_HUMAN	LRP1	physical	11854294
RET_HUMAN	RET	physical	10070972
FYN_HUMAN	FYN	physical	9169421
LYN_HUMAN	LYN	physical	9169421
EGFR_HUMAN	EGFR	physical	10358079
STAT1_HUMAN	STAT1	physical	10358079
FAK2_HUMAN	PTK2B	physical	10777553
EFNB1_HUMAN	EFNB1	physical	8878483
KSYK_HUMAN	SYK	physical	7513017
ASAP1_HUMAN	ASAP1	physical	9819391
GAB3_HUMAN	GAB3	physical	11739737
ERBB2_HUMAN	ERBB2	physical	11940572
KS6B1_HUMAN	RPS6KB1	physical	16640565
KS6B2_HUMAN	RPS6KB2	physical	16640565
DAG1_HUMAN	DAG1	physical	11724572
RAF1_HUMAN	RAF1	physical	7517401
KHDR1_HUMAN	KHDRBS1	physical	8766817
SKAP1_HUMAN	SKAP1	physical	9195899
EVL_HUMAN	EVL	physical	10945997
PECA1_HUMAN	PECAM1	physical	10858437
FAK1_HUMAN	PTK2	physical	10085298
PAXI_HUMAN	PXN	physical	10085298
BCAR1_HUMAN	BCAR1	physical	10085298
MUC1_HUMAN	MUC1	physical	11152665
EPHB2_HUMAN	EPHB2	physical	10644995
MET_HUMAN	MET	physical	9837958
RL10_HUMAN	RPL10	physical	12138090
WASP_HUMAN	WAS	physical	8824280
RHG01_HUMAN	ARHGAP1	physical	8253717
FAK2_HUMAN	PTK2B	physical	10521452
RACK1_HUMAN	GNB2L1	physical	9584165
KPCZ_HUMAN	PRKCZ	physical	10527887
PTPRA_HUMAN	PTPRA	physical	11923305
STAT3_HUMAN	STAT3	physical	8657134
MUC1_HUMAN	MUC1	physical	11483589
EPS8_HUMAN	EPS8	physical	10395945
GAB2_HUMAN	GAB2	physical	10391903
FAK2_HUMAN	PTK2B	physical	8849729
MICA1_HUMAN	MICAL1	physical	11827972
RASA1_HUMAN	RASA1	physical	11389730
MCP_HUMAN	CD46	physical	10657632
EPHA3_HUMAN	EPHA3	physical	9632142
EPHA4_HUMAN	EPHA4	physical	9632142
FLNA_HUMAN	FLNA	physical	20936779
EGFR_HUMAN	EGFR	physical	17158602
PGFRB_HUMAN	PDGFRB	physical	17158602
HDAC3_HUMAN	HDAC3	physical	16532030
ESR1_HUMAN	ESR1	physical	15784253
NEF_HV1H2	nef	physical	9778343
PRDM2_HUMAN	PRDM2	physical	15282304
RXRA_HUMAN	RXRA	physical	15116119
THB_HUMAN	THRB	physical	14985366
ESR1_HUMAN	ESR1	physical	14766010
HDAC3_HUMAN	HDAC3	physical	17699109
COF1_HUMAN	CFL1	physical	19802004
CADH1_HUMAN	CDH1	physical	21685945
HAKAI_HUMAN	CBLL1	physical	21685945
ACK1_HUMAN	TNK2	physical	19144635
HAKAI_HUMAN	CBLL1	physical	18057010
CADH1_HUMAN	CDH1	physical	18057010
DPYL1_HUMAN	CRMP1	physical	21900206
EGLN1_HUMAN	EGLN1	physical	21335603
SRC_HUMAN	SRC	physical	21335603
BCAR1_HUMAN	BCAR1	physical	15020686
SRC_HUMAN	SRC	physical	15020686
ERBB2_HUMAN	ERBB2	physical	17875712
CCNA1_HUMAN	CCNA1	physical	15601848
KHDR1_HUMAN	KHDRBS1	physical	22745667
SH3K1_HUMAN	SH3KBP1	physical	15707590
PDC6I_HUMAN	PDCD6IP	physical	15557335
CBL_HUMAN	CBL	physical	12941616
CBL_HUMAN	CBL	physical	17141222
CBL_HUMAN	CBL	physical	10829062
CBL_HUMAN	CBL	physical	19861161
P85A_HUMAN	PIK3R1	physical	19861161
SRBS1_HUMAN	SORBS1	physical	19891780
STAT3_HUMAN	STAT3	physical	21573184
EGFR_HUMAN	EGFR	physical	21573184
BCAR1_HUMAN	BCAR1	physical	17038317
ACK1_HUMAN	TNK2	physical	17038317
KHDR1_HUMAN	KHDRBS1	physical	15190072
CBL_HUMAN	CBL	physical	17094785
KIT_HUMAN	KIT	physical	12444928
FYN_HUMAN	FYN	physical	19711372
LNX1_HUMAN	LNX1	physical	17936276
SH3K1_HUMAN	SH3KBP1	physical	22833562
VGFR2_HUMAN	KDR	physical	19050761
IQGA1_HUMAN	IQGAP1	physical	19050761
CBLC_HUMAN	CBLC	physical	22888118
CBP_HUMAN	CREBBP	physical	22364282
CBL_HUMAN	CBL	physical	7782294
IKKB_HUMAN	IKBKB	physical	12645577
KCNB1_HUMAN	KCNB1	physical	12615930
KCND3_HUMAN	KCND3	physical	18620005
CBL_HUMAN	CBL	physical	15135048
KCNA5_HUMAN	KCNA5	physical	8953041
EGFR_HUMAN	EGFR	physical	20333651
EFS_HUMAN	EFS	physical	8647432
ACK1_HUMAN	TNK2	physical	21309750
ACK1_HUMAN	TNK2	physical	14506255
SKAP2_HUMAN	SKAP2	physical	12893833
VGFR2_HUMAN	KDR	physical	18194650
SRC_HUMAN	SRC	physical	12606547
CLH1_HUMAN	CLTC	physical	17785434
TM1L1_HUMAN	TOM1L1	physical	17785434
PGFRB_HUMAN	PDGFRB	physical	17785434
NEMO_HUMAN	IKBKG	physical	15749833
IKKA_HUMAN	CHUK	physical	15749833
IKKB_HUMAN	IKBKB	physical	15749833
SYUA_HUMAN	SNCA	physical	11078745
ENOA_HUMAN	ENO1	physical	11078745
SRC_HUMAN	SRC	physical	11078745
WASL_HUMAN	WASL	physical	15791211
ESR1_HUMAN	ESR1	physical	17284441
EGFR_HUMAN	EGFR	physical	17284441
ENOA_HUMAN	ENO1	physical	17525734
SRCN1_HUMAN	SRCIN1	physical	17525734
UBP8_HUMAN	USP8	physical	23333852
EGFR_HUMAN	EGFR	physical	23175185
CDN1B_HUMAN	CDKN1B	physical	17254967
PDE4D_HUMAN	PDE4D	physical	10571082
CBL_HUMAN	CBL	physical	16636290
DDX4_HUMAN	DDX4	physical	17868192
K1C10_HUMAN	KRT10	physical	17868192
ERBB3_HUMAN	ERBB3	physical	16273093
ARRB1_HUMAN	ARRB1	physical	19202075
EDNRA_HUMAN	EDNRA	physical	19202075
JAK2_HUMAN	JAK2	physical	21075308
ERBB2_HUMAN	ERBB2	physical	21075308
EPOR_HUMAN	EPOR	physical	21075308
CSK21_HUMAN	CSNK2A1	physical	21075308
PTN1_CHICK	PTPN1	physical	9600099
PTN1_HUMAN	PTPN1	physical	9600099
STAT1_HUMAN	STAT1	physical	14978237
KHDR1_HUMAN	KHDRBS1	physical	18606683
P85A_HUMAN	PIK3R1	physical	19903481
ANXA7_HUMAN	ANXA7	physical	11278415
ENOA_HUMAN	ENO1	physical	16609991
KHDR1_HUMAN	KHDRBS1	physical	1374686
TNR1A_HUMAN	TNFRSF1A	physical	9237663
RGS16_HUMAN	RGS16	physical	12588871
EGFR_HUMAN	EGFR	physical	21268077
PE2R4_HUMAN	PTGER4	physical	16432186
ARRB1_HUMAN	ARRB1	physical	16432186
TLR4_HUMAN	TLR4	physical	20379791
CBLC_HUMAN	CBLC	physical	14661060
NEMO_HUMAN	IKBKG	physical	23131831
ESR1_HUMAN	ESR1	physical	24051437
SPR2A_HUMAN	SPRR2A	physical	18155796
CAH3_HUMAN	CA3	physical	16099843
ARRB2_HUMAN	ARRB2	physical	19122674
NEDD4_HUMAN	NEDD4	physical	25292214
TAU_HUMAN	MAPT	physical	16115884
ESR1_HUMAN	ESR1	physical	16957778
PSB9_HUMAN	PSMB9	physical	16957778
RPB1_HUMAN	POLR2A	physical	16957778
RPB2_HUMAN	POLR2B	physical	16957778
RPB3_HUMAN	POLR2C	physical	16957778
RPB4_HUMAN	POLR2D	physical	16957778
RPAB1_HUMAN	POLR2E	physical	16957778
RPAB2_HUMAN	POLR2F	physical	16957778
RPB7_HUMAN	POLR2G	physical	16957778
RPAB3_HUMAN	POLR2H	physical	16957778
RPB9_HUMAN	POLR2I	physical	16957778
RPAB5_HUMAN	POLR2L	physical	16957778
RPB11_HUMAN	POLR2J	physical	16957778
RPAB4_HUMAN	POLR2K	physical	16957778
CORO7_HUMAN	CORO7	physical	18581049
KHDR1_HUMAN	KHDRBS1	physical	9038356
FBX5_HUMAN	FBXO5	physical	20717963
BCAR1_HUMAN	BCAR1	physical	17129785
P53_HUMAN	TP53	physical	25071020
MDM2_HUMAN	MDM2	physical	25624478
KHDR1_HUMAN	KHDRBS1	physical	10635328
RGRF1_HUMAN	RASGRF1	physical	11389730
P55G_HUMAN	PIK3R3	physical	25814554
FAK1_HUMAN	PTK2	physical	25814554
PE2R2_HUMAN	PTGER2	physical	23242524
PE2R4_HUMAN	PTGER4	physical	23242524
ARRB1_HUMAN	ARRB1	physical	23242524
ARRB2_HUMAN	ARRB2	physical	23242524
TLN1_HUMAN	TLN1	physical	23242524
FAK1_HUMAN	PTK2	physical	23242524
MK01_HUMAN	MAPK1	physical	23242524
MK03_HUMAN	MAPK3	physical	23242524
AKT1_HUMAN	AKT1	physical	23242524
TOPK_HUMAN	PBK	physical	27016416
HNRPK_HUMAN	HNRNPK	physical	16854432
ENOA_HUMAN	ENO1	physical	15456896
SRC_HUMAN	SRC	physical	15456896
IKKB_HUMAN	IKBKB	physical	15456896
ERRFI_HUMAN	ERRFI1	physical	26280531
PGFRB_HUMAN	PDGFRB	physical	18315570
MPIP1_HUMAN	CDC25A	physical	27485204
EP300_HUMAN	EP300	physical	26695438
S100B_HUMAN	S100B	physical	19147496
SRC_HUMAN	SRC	physical	14670955
PROM1_HUMAN	PROM1	physical	23569237
GRM1_HUMAN	GRM1	physical	15173175
GRASP_HUMAN	GRASP	physical	15173175
KSYK_HUMAN	SYK	physical	15173175
BCAR1_HUMAN	BCAR1	physical	16849545
PTN11_HUMAN	PTPN11	physical	8959326
EMD_HUMAN	EMD	physical	19789182
LAP2A_HUMAN	TMPO	physical	19789182
LAP2B_HUMAN	TMPO	physical	19789182
SRC_HUMAN	SRC	physical	19789182
PTN6_HUMAN	PTPN6	physical	14699166
PTPRA_HUMAN	PTPRA	physical	23532252
ITB3_HUMAN	ITGB3	physical	10896934
LATS1_HUMAN	LATS1	physical	28754671
FAK1_HUMAN	PTK2	physical	11119718

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
D03252	Bosutinib (USAN)
D03658	Dasatinib (INN)
D06414	Dasatinib hydrate (JAN); Dasatinib (USAN); Sprycel (TN)
D09664	Saracatinib (USAN/INN)
D09665	Saracatinib difumarate (USAN)
D09728	Bosutinib hydrate (JAN); Bosutinib monohydrate; Bosulif (TN)
D10423	Ilorasertib (USAN)
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SRC_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Cdk5 targets active Src for ubiquitin-dependent degradation byphosphorylating Src(S75)."; Pan Q., Qiao F., Gao C., Norman B., Optican L., Zelenka P.S.; Cell. Mol. Life Sci. 68:3425-3436(2011). Cited for: PHOSPHORYLATION AT SER-75.	21442427 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-35; SER-69;THR-74; SER-75; THR-511; TYR-522 AND TYR-530, AND MASS SPECTROMETRY.	19369195 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND MASSSPECTROMETRY.	18691976 [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 SER-17; THR-74 AND TYR-419,AND MASS SPECTROMETRY.	18088087 [Abstract]
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry."; Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.; Mol. Cell. Proteomics 6:537-547(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-69; SER-75 ANDTYR-419, AND MASS SPECTROMETRY.	17192257 [Abstract]
"New role for the protein tyrosine phosphatase DEP-1 in Akt activationand endothelial cell survival."; Chabot C., Spring K., Gratton J.P., Elchebly M., Royal I.; Mol. Cell. Biol. 29:241-253(2009). Cited for: PHOSPHORYLATION AT TYR-419, AND DEPHOSPHORYLATION BY PTPRJ AT TYR-419.	18936167 [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-530, AND MASSSPECTROMETRY.	19534553 [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-439, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Association of the amino-terminal half of c-Src with focal adhesionsalters their properties and is regulated by phosphorylation oftyrosine 527."; Kaplan K.B., Bibbins K.B., Swedlow J.R., Arnaud M., Morgan D.O.,Varmus H.E.; EMBO J. 13:4745-4756(1994). Cited for: SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT TYR-530.	7525268 [Abstract]
"Characterization of sites for tyrosine phosphorylation in thetransforming protein of Rous sarcoma virus (pp60v-src) and its normalcellular homologue (pp60c-src)."; Smart J.E., Oppermann H., Czernilofsky A.P., Purchio A.F.,Erikson R.L., Bishop J.M.; Proc. Natl. Acad. Sci. U.S.A. 78:6013-6017(1981). Cited for: PHOSPHORYLATION AT TYR-419.	6273838 [Abstract]

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