dbPTM

ABL1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ABL1_HUMAN
UniProt AC	P00519
Protein Name	Tyrosine-protein kinase ABL1
Gene Name	ABL1
Organism	Homo sapiens (Human).
Sequence Length	1130
Subcellular Localization	Cytoplasm, cytoskeleton. Nucleus. Mitochondrion. Shuttles between the nucleus and cytoplasm depending on environmental signals. Sequestered into the cytoplasm through interaction with 14-3-3 proteins. Localizes to mitochondria in response to oxidativ
Protein Description	Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9. Phosphorylates multiple receptor tyrosine kinases and more particularly promotes endocytosis of EGFR, facilitates the formation of neuromuscular synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of activated B-cell receptor complexes. Other substrates which are involved in endocytosis regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive receptor down-regulation and actin remodeling. Phosphorylation of CBL leads to increased EGFR stability. Involved in late-stage autophagy by regulating positively the trafficking and function of lysosomal components. ABL1 targets to mitochondria in response to oxidative stress and thereby mediates mitochondrial dysfunction and cell death. In response to oxidative stress, phosphorylates serine/threonine kinase PRKD2 at 'Tyr-717'. [PubMed: 28428613 ABL1 is also translocated in the nucleus where it has DNA-binding activity and is involved in DNA-damage response and apoptosis. Many substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates TP73, a primary regulator for this type of damage-induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-153' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks. ABL1 acts also as a regulator of multiple pathological signaling cascades during infection. Several known tyrosine-phosphorylated microbial proteins have been identified as ABL1 substrates. This is the case of A36R of Vaccinia virus, Tir (translocated intimin receptor) of pathogenic E.coli and possibly Citrobacter, CagA (cytotoxin-associated gene A) of H.pylori, or AnkA (ankyrin repeat-containing protein A) of A.phagocytophilum. Pathogens can highjack ABL1 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. Regulates T-cell differentiation in a TBX21-dependent manner. Phosphorylates TBX21 on tyrosine residues leading to an enhancement of its transcriptional activator activity (By similarity]
Protein Sequence	MLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKQGVRGAVSTLLQAPELPTKTRTSRRAAEHRDTTDVPEMPHSKGQGESDPLDHEPAVSPLLPRKERGPPEGGLNEDERLLPKDKKTNLFSALIKKKKKTAPTPPKRSSSFREMDGQPERRGAGEEEGRDISNGALAFTPLDTADPAKSPKPSNGAGVPNGALRESGGSGFRSPHLWKKSSTLTSSRLATGEEEGGGSSSKRFLRSCSASCVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRAGENRSDQVTRGTVTPPPRLVKKNEEAADEVFKDIMESSPGSSPPNLTPKPLRRQVTVAPASGLPHKEEAGKGSALGTPAAAEPVTPTSKAGSGAPGGTSKGPAEESRVRRHKHSSESPGRDKGKLSRLKPAPPPPPAASAGKAGGKPSQSPSQEAAGEAVLGAKTKATSLVDAVNSDAAKPSQPGEGLKKPVLPATPKPQSAKPSGTPISPAPVPSTLPSASSALAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGVVLDSTEALCLAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENNLRELQICPATAGSGPAATQDFSKLLSSVKEISDIVQR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2 (in isoform 2)	Myristoylation	-	10.12	-
16 (in isoform 2)	Phosphorylation	-	34.23	23927012
24	Phosphorylation	LSSSSSCYLEEALQR CCCCCHHHHHHHHHC	21.06	27642862
43	Phosphorylation	DFEPQGLSEAARWNS CCCCCCHHHHHHHCC	31.82	26074081
50	Phosphorylation	SEAARWNSKENLLAG HHHHHHCCCCCCCCC	34.09	17192257
59	Phosphorylation	ENLLAGPSENDPNLF CCCCCCCCCCCCCCE	48.38	26074081
70	Phosphorylation	PNLFVALYDFVASGD CCCEEEEEEHHHCCC	9.52	18691976
75	Phosphorylation	ALYDFVASGDNTLSI EEEEHHHCCCCEEEE	41.18	20068231
79	Phosphorylation	FVASGDNTLSITKGE HHHCCCCEEEECCCC	26.99	20068231
81	Phosphorylation	ASGDNTLSITKGEKL HCCCCEEEECCCCEE	26.61	24719451
83	Phosphorylation	GDNTLSITKGEKLRV CCCEEEECCCCEEEE	29.62	20068231
93	Phosphorylation	EKLRVLGYNHNGEWC CEEEEEEECCCCCEE	14.75	47733
113	Phosphorylation	NGQGWVPSNYITPVN CCCCCCCCCCCCCCH	32.42	21945579
115	Phosphorylation	QGWVPSNYITPVNSL CCCCCCCCCCCCHHH	15.54	21945579
117	Phosphorylation	WVPSNYITPVNSLEK CCCCCCCCCCHHHCC	15.72	21945579
126	Phosphorylation	VNSLEKHSWYHGPVS CHHHCCCCCCCCCCC	40.16	21945579
128	Phosphorylation	SLEKHSWYHGPVSRN HHCCCCCCCCCCCCH	10.42	21945579
133	Phosphorylation	SWYHGPVSRNAAEYL CCCCCCCCCHHHHHH	23.97	21945579
134 (in isoform 2)	Phosphorylation	-	36.72	16497976
139	Phosphorylation	VSRNAAEYLLSSGIN CCCHHHHHHHHCCCC	14.28	23917254
142	Phosphorylation	NAAEYLLSSGINGSF HHHHHHHHCCCCCCE	24.75	-
154	Phosphorylation	GSFLVRESESSPGQR CCEEEEECCCCCCCE	32.01	22817900
157	Phosphorylation	LVRESESSPGQRSIS EEEECCCCCCCEEEE	29.06	28787133
162	Phosphorylation	ESSPGQRSISLRYEG CCCCCCEEEEEEECC	14.51	29496963
164	Phosphorylation	SPGQRSISLRYEGRV CCCCEEEEEEECCEE	14.19	29496963
167	Phosphorylation	QRSISLRYEGRVYHY CEEEEEEECCEEEEE	28.20	23917254
172	Phosphorylation	LRYEGRVYHYRINTA EEECCEEEEEEEEEC	7.56	24732914
174	Phosphorylation	YEGRVYHYRINTASD ECCEEEEEEEEECCC	8.76	24732914
178	Phosphorylation	VYHYRINTASDGKLY EEEEEEEECCCCCEE	25.76	28152594
180	Phosphorylation	HYRINTASDGKLYVS EEEEEECCCCCEEEC	44.87	24732914
185	Phosphorylation	TASDGKLYVSSESRF ECCCCCEEECCHHHH	11.19	21082442
187	Phosphorylation	SDGKLYVSSESRFNT CCCCEEECCHHHHHH	18.16	28152594
188	Phosphorylation	DGKLYVSSESRFNTL CCCEEECCHHHHHHH	29.55	28442448
190	Phosphorylation	KLYVSSESRFNTLAE CEEECCHHHHHHHHH	44.08	28442448
204 (in isoform 2)	Phosphorylation	-	18.50	16497976
215	Phosphorylation	GLITTLHYPAPKRNK CCEEECCCCCCCCCC	12.28	16912036
224	Phosphorylation	APKRNKPTVYGVSPN CCCCCCCCEEEECCC	28.15	29978859
226	Phosphorylation	KRNKPTVYGVSPNYD CCCCCCEEEECCCCC	17.81	22322096
229	Phosphorylation	KPTVYGVSPNYDKWE CCCEEEECCCCCCCC	11.76	30849837
232	Phosphorylation	VYGVSPNYDKWEMER EEEECCCCCCCCEEE	23.45	22322096
243	Phosphorylation	EMERTDITMKHKLGG CEEECCCEEEECCCC	23.99	-
245 (in isoform 2)	Phosphorylation	-	29.01	16497976
251 (in isoform 2)	Phosphorylation	-	18.75	12644574
253	Phosphorylation	HKLGGGQYGEVYEGV ECCCCCCCCEEECCH	20.66	21082442
257	Phosphorylation	GGQYGEVYEGVWKKY CCCCCEEECCHHHHE	11.58	21082442
264	Phosphorylation	YEGVWKKYSLTVAVK ECCHHHHEEEEEEEE	12.75	21082442
265	Phosphorylation	EGVWKKYSLTVAVKT CCHHHHEEEEEEEEC	26.83	28152594
267	Phosphorylation	VWKKYSLTVAVKTLK HHHHEEEEEEEECCC	10.65	20068231
272 (in isoform 2)	Phosphorylation	-	36.14	16497976
274	Acetylation	TVAVKTLKEDTMEVE EEEEECCCCCCHHHH	59.79	19815429
276 (in isoform 2)	Phosphorylation	-	50.17	16497976
283 (in isoform 2)	Phosphorylation	-	8.16	12644574
285	Ubiquitination	MEVEEFLKEAAVMKE HHHHHHHHHHHHHHH	51.10	-
306	Phosphorylation	VQLLGVCTREPPFYI HHHHCEECCCCCEEE	35.34	46157193
312	Phosphorylation	CTREPPFYIITEFMT ECCCCCEEEEEEHHH	9.37	18775312
320	Phosphorylation	IITEFMTYGNLLDYL EEEEHHHHHHHHHHH	7.70	9845501
389	Phosphorylation	FGLSRLMTGDTYTAH HCCCHHCCCCCEECC	36.18	21945579
392	Phosphorylation	SRLMTGDTYTAHAGA CHHCCCCCEECCCCC	24.90	21945579
393	Dephosphorylation	RLMTGDTYTAHAGAK HHCCCCCEECCCCCC	13.48	11163214
393	Phosphorylation	RLMTGDTYTAHAGAK HHCCCCCEECCCCCC	13.48	22322096
394	Phosphorylation	LMTGDTYTAHAGAKF HCCCCCEECCCCCCC	17.66	21945579
400	Ubiquitination	YTAHAGAKFPIKWTA EECCCCCCCCCEECC	51.24	-
406	Phosphorylation	AKFPIKWTAPESLAY CCCCCEECCCHHHHC	27.60	-
412 (in isoform 2)	Phosphorylation	-	18.35	15592455
413	Phosphorylation	TAPESLAYNKFSIKS CCCHHHHCCCCCCCC	24.95	16464493
417	Phosphorylation	SLAYNKFSIKSDVWA HHHCCCCCCCCHHHH	30.62	-
446	Phosphorylation	PYPGIDLSQVYELLE CCCCCCHHHHHHHHH	17.53	8668151
456	Phosphorylation	YELLEKDYRMERPEG HHHHHHHHCCCCCCC	23.95	7347443
469	Phosphorylation	EGCPEKVYELMRACW CCCCHHHHHHHHHHH	17.89	12522270
488 (in isoform 2)	Phosphorylation	-	38.71	16464493
512	Ubiquitination	EVEKELGKQGVRGAV HHHHHHHHCCHHHHH	57.41	-
532	Phosphorylation	APELPTKTRTSRRAA CCCCCCCCCHHHHHH	41.48	-
535	Phosphorylation	LPTKTRTSRRAAEHR CCCCCCHHHHHHHCC	19.24	20810815
545	Phosphorylation	AAEHRDTTDVPEMPH HHHCCCCCCCCCCCC	39.01	28555341
559	Phosphorylation	HSKGQGESDPLDHEP CCCCCCCCCCCCCCC	51.88	23927012
569	Phosphorylation	LDHEPAVSPLLPRKE CCCCCCCCCCCCCHH	16.37	29255136
597	Phosphorylation	LLPKDKKTNLFSALI CCCCCCCCCHHHHHH	42.78	69214187
601	Phosphorylation	DKKTNLFSALIKKKK CCCCCHHHHHHHHHC	25.90	46157163
610	Phosphorylation	LIKKKKKTAPTPPKR HHHHHCCCCCCCCCC	46.91	37816903
613	Phosphorylation	KKKKTAPTPPKRSSS HHCCCCCCCCCCCCC	50.16	17192257
618	Phosphorylation	APTPPKRSSSFREMD CCCCCCCCCCHHHCC	36.14	23401153
619	Phosphorylation	PTPPKRSSSFREMDG CCCCCCCCCHHHCCC	37.21	23401153
620	Phosphorylation	TPPKRSSSFREMDGQ CCCCCCCCHHHCCCC	29.57	25159151
642	Phosphorylation	EEEGRDISNGALAFT CCCCCCCCCCCEEEE	33.24	24667141
649	Phosphorylation	SNGALAFTPLDTADP CCCCEEEEECCCCCC	19.82	80535829
653	Phosphorylation	LAFTPLDTADPAKSP EEEEECCCCCCCCCC	40.41	25850435
659	Phosphorylation	DTADPAKSPKPSNGA CCCCCCCCCCCCCCC	40.02	30631047
663	Phosphorylation	PAKSPKPSNGAGVPN CCCCCCCCCCCCCCC	54.76	22199227
676	Phosphorylation	PNGALRESGGSGFRS CCCCCCCCCCCCCCC	41.86	25159151
679	Phosphorylation	ALRESGGSGFRSPHL CCCCCCCCCCCCCCC	37.98	23401153
683	Phosphorylation	SGGSGFRSPHLWKKS CCCCCCCCCCCCCCC	17.89	23401153
689	Methylation	RSPHLWKKSSTLTSS CCCCCCCCCCCCCCC	37.75	-
690	Phosphorylation	SPHLWKKSSTLTSSR CCCCCCCCCCCCCCC	25.48	30576142
691	Phosphorylation	PHLWKKSSTLTSSRL CCCCCCCCCCCCCCC	35.99	26074081
692	Phosphorylation	HLWKKSSTLTSSRLA CCCCCCCCCCCCCCC	40.94	26074081
694	Phosphorylation	WKKSSTLTSSRLATG CCCCCCCCCCCCCCC	25.41	23312004
695	Phosphorylation	KKSSTLTSSRLATGE CCCCCCCCCCCCCCC	19.30	23186163
696	Phosphorylation	KSSTLTSSRLATGEE CCCCCCCCCCCCCCC	26.52	23312004
700	Phosphorylation	LTSSRLATGEEEGGG CCCCCCCCCCCCCCC	50.12	12300595
708	Phosphorylation	GEEEGGGSSSKRFLR CCCCCCCCCHHHHHH	34.41	21815630
709	Phosphorylation	EEEGGGSSSKRFLRS CCCCCCCCHHHHHHH	43.06	12300613
710	Phosphorylation	EEGGGSSSKRFLRSC CCCCCCCHHHHHHHC	29.55	30576142
711	Acetylation	EGGGSSSKRFLRSCS CCCCCCHHHHHHHCC	49.47	16648821
716	Phosphorylation	SSKRFLRSCSASCVP CHHHHHHHCCCCCCC	17.99	23927012
718	Phosphorylation	KRFLRSCSASCVPHG HHHHHHCCCCCCCCC	25.18	23401153
720	Phosphorylation	FLRSCSASCVPHGAK HHHHCCCCCCCCCCC	10.19	23927012
729	Phosphorylation	VPHGAKDTEWRSVTL CCCCCCCCCCEEEEC	36.42	23312004
730	Acetylation	PHGAKDTEWRSVTLP CCCCCCCCCEEEECC	51.53	16648821
730 (in isoform 2)	Acetylation	-	51.53	-
733	Phosphorylation	AKDTEWRSVTLPRDL CCCCCCEEEECCHHH	22.11	23403867
735	Phosphorylation	DTEWRSVTLPRDLQS CCCCEEEECCHHHHH	32.09	19643477
743	Phosphorylation	LPRDLQSTGRQFDSS CCHHHHHHCCCCCCC	24.35	24719451
751	Phosphorylation	GRQFDSSTFGGHKSE CCCCCCCCCCCCCCC	30.19	23917254
754 (in isoform 2)	Phosphorylation	-	22.36	15696159
759	Acetylation	FGGHKSEKPALPRKR CCCCCCCCCCCCCCC	42.56	7822139
779	Phosphorylation	SDQVTRGTVTPPPRL CCCCCCCCCCCCCCH	20.23	23403867
781	Phosphorylation	QVTRGTVTPPPRLVK CCCCCCCCCCCCHHC	29.89	17192257
804	Phosphorylation	VFKDIMESSPGSSPP HHHHHHHHCCCCCCC	25.18	25159151
805	Phosphorylation	FKDIMESSPGSSPPN HHHHHHHCCCCCCCC	21.70	25159151
808	Phosphorylation	IMESSPGSSPPNLTP HHHHCCCCCCCCCCC	42.95	29255136
809	Phosphorylation	MESSPGSSPPNLTPK HHHCCCCCCCCCCCC	50.74	29255136
814	Phosphorylation	GSSPPNLTPKPLRRQ CCCCCCCCCCCCCCC	35.59	29255136
823	Phosphorylation	KPLRRQVTVAPASGL CCCCCCEEEEECCCC	11.56	26074081
828	Phosphorylation	QVTVAPASGLPHKEE CEEEEECCCCCCHHH	39.54	18691976
840	Phosphorylation	KEEAGKGSALGTPAA HHHCCCCCCCCCCCC	24.65	29396449
844	Phosphorylation	GKGSALGTPAAAEPV CCCCCCCCCCCCCCC	15.59	25159151
852	Phosphorylation	PAAAEPVTPTSKAGS CCCCCCCCCCCCCCC	31.40	30266825
854	Phosphorylation	AAEPVTPTSKAGSGA CCCCCCCCCCCCCCC	33.23	29255136
855	O-linked_Glycosylation	AEPVTPTSKAGSGAP CCCCCCCCCCCCCCC	23.01	30059200
855	Phosphorylation	AEPVTPTSKAGSGAP CCCCCCCCCCCCCCC	23.01	30266825
859	Phosphorylation	TPTSKAGSGAPGGTS CCCCCCCCCCCCCCC	36.32	82313401
884	Phosphorylation	RHKHSSESPGRDKGK HCCCCCCCCCCCCCC	34.30	23099
915	Phosphorylation	GKAGGKPSQSPSQEA CCCCCCCCCCCCHHH	46.94	22167270
917	Phosphorylation	AGGKPSQSPSQEAAG CCCCCCCCCCHHHHH	30.75	22167270
919	Phosphorylation	GKPSQSPSQEAAGEA CCCCCCCCHHHHHHH	45.99	22167270
935	Phosphorylation	LGAKTKATSLVDAVN HCCCHHHHHHHHHHC	24.93	-
936	Phosphorylation	GAKTKATSLVDAVNS CCCHHHHHHHHHHCC	31.12	17192257
943	Phosphorylation	SLVDAVNSDAAKPSQ HHHHHHCCCCCCCCC	23.25	-
949	Phosphorylation	NSDAAKPSQPGEGLK CCCCCCCCCCCCCCC	48.58	21406692
963	Phosphorylation	KKPVLPATPKPQSAK CCCCCCCCCCCCCCC	29.88	25159151
968	Phosphorylation	PATPKPQSAKPSGTP CCCCCCCCCCCCCCC	46.95	17081983
977	Phosphorylation	KPSGTPISPAPVPST CCCCCCCCCCCCCCC	19.06	17192257
989	Phosphorylation	PSTLPSASSALAGDQ CCCCCCCCHHHCCCC	22.08	18691976
1011	Phosphorylation	PLISTRVSLRKTRQP HHEECHHCCCCCCCC	21.11	25627689
1044	Phosphorylation	EALCLAISRNSEQMA HHHHHHHHCCCHHHH	21.58	24719451
1064	Phosphorylation	LEAGKNLYTFCVSYV HHHHCHHHHHHHHHH	13.73	45559739
1070	Phosphorylation	LYTFCVSYVDSIQQM HHHHHHHHHHHHHHH	6.46	69101443
1103	Phosphorylation	ELQICPATAGSGPAA HCEECHHCCCCCCCH	19.38	25262027
1106	Phosphorylation	ICPATAGSGPAATQD ECHHCCCCCCCHHHH	38.86	62175385
1111	Phosphorylation	AGSGPAATQDFSKLL CCCCCCHHHHHHHHH	30.67	23917254
1115	Phosphorylation	PAATQDFSKLLSSVK CCHHHHHHHHHHHHH	30.59	25262027
1119	Phosphorylation	QDFSKLLSSVKEISD HHHHHHHHHHHHHHH	43.45	24719451
1125	Phosphorylation	LSSVKEISDIVQR-- HHHHHHHHHHHHC--	23.52	24719451

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
70	Y	Phosphorylation	Kinase	FYN	P06241	PSP
70	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
70	Y	Phosphorylation	Kinase	HCK	P08631	PSP
70	Y	Phosphorylation	Kinase	LYN	P07948	PSP
89	Y	Phosphorylation	Kinase	HCK	P08631	GPS
115	Y	Phosphorylation	Kinase	LYN	P07948	PSP
115	Y	Phosphorylation	Kinase	FYN	P06241	PSP
115	Y	Phosphorylation	Kinase	HCK	P08631	PSP
128	Y	Phosphorylation	Kinase	FYN	P06241	PSP
128	Y	Phosphorylation	Kinase	HCK	P08631	PSP
128	Y	Phosphorylation	Kinase	LYN	P07948	PSP
139	Y	Phosphorylation	Kinase	LYN	P07948	PSP
139	Y	Phosphorylation	Kinase	HCK	P08631	PSP
139	Y	Phosphorylation	Kinase	FYN	P06241	PSP
172	Y	Phosphorylation	Kinase	HCK	P08631	PSP
172	Y	Phosphorylation	Kinase	LYN	P07948	PSP
172	Y	Phosphorylation	Kinase	FYN	P06241	PSP
185	Y	Phosphorylation	Kinase	LYN	P07948	PSP
185	Y	Phosphorylation	Kinase	HCK	P08631	PSP
185	Y	Phosphorylation	Kinase	FYN	P06241	PSP
197	T	Phosphorylation	Kinase	LATS2	Q9NRM7	PSP
215	Y	Phosphorylation	Kinase	FYN	P06241	PSP
215	Y	Phosphorylation	Kinase	HCK	P08631	PSP
215	Y	Phosphorylation	Kinase	LYN	P07948	PSP
226	Y	Phosphorylation	Kinase	HCK	P08631	PSP
226	Y	Phosphorylation	Kinase	FYN	P06241	PSP
226	Y	Phosphorylation	Kinase	LYN	P07948	PSP
226	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
232	Y	Phosphorylation	Kinase	BCR-ABL1	A9UF07	PSP
245	Y	Phosphorylation	Kinase	PDGFRB	P09619	GPS
245	Y	Phosphorylation	Kinase	HCK	P08631	GPS
253	Y	Phosphorylation	Kinase	BCR-ABL1	A9UF07	PSP
257	Y	Phosphorylation	Kinase	BCR-ABL1	A9UF07	PSP
393	Y	Phosphorylation	Kinase	HCK	P08631	PSP
393	Y	Phosphorylation	Kinase	SRC-TYPE TYR-KINASES	-	Uniprot
393	Y	Phosphorylation	Kinase	SRC-FAMILY	-	GPS
393	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS
393	Y	Phosphorylation	Kinase	ABL1	P00519	PhosphoELM
393	Y	Phosphorylation	Kinase	FYN	P06241	PSP
393	Y	Phosphorylation	Kinase	LYN	P07948	PSP
412	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
412	Y	Phosphorylation	Kinase	PDGFRB	P09619	GPS
412	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS
446	S	Phosphorylation	Kinase	ATM	Q13315	PhosphoELM
446	S	Phosphorylation	Kinase	ATM	Q62388	PSP
488	Y	Phosphorylation	Kinase	SRC	P12931	PSP
618	S	Phosphorylation	Kinase	PAK2	Q13177	Uniprot
619	S	Phosphorylation	Kinase	PAK2	Q13177	Uniprot
735	T	Phosphorylation	Kinase	MAP3K8	P41279	GPS
735	T	Phosphorylation	Kinase	CLK1	P49759	PSP
735	T	Phosphorylation	Kinase	STK3	Q13188	GPS
735	T	Phosphorylation	Kinase	STK4	Q13043	GPS
735	T	Phosphorylation	Kinase	TTK	P33981	PSP
735	T	Phosphorylation	Kinase	CLK4	Q9HAZ1	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	FBXL5	Q9UKA1	PMID:24658274
-	K	Ubiquitination	E3 ubiquitin ligase	CBL	P22681	PMID:12475393

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
446	S	Phosphorylation	-
DNA damage-induced activation of ABL1 requires the function of ATM and Ser-446 phosphorylation (By similarity).
569	S	Phosphorylation	17081983
Phosphorylation at Ser-569 has been attributed to a CDC2-associated kinase and is coupled to cell division (By similarity).
618	S	Phosphorylation	18161990
Phosphorylation at Ser-618 and Ser-619 by PAK2 increases binding to CRK and reduces binding to ABI1.
619	S	Phosphorylation	18161990
Phosphorylation at Ser-618 and Ser-619 by PAK2 increases binding to CRK and reduces binding to ABI1.
711	K	Acetylation	16648821
Acetylated at Lys-711 by EP300 which promotes the cytoplasmic translocation.
735	T	Phosphorylation	15696159
Phosphorylation on Thr-735 is required for binding 14-3-3 proteins for cytoplasmic translocation.

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 ABL1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PTN6_HUMAN	PTPN6	physical	8692915
RB_HUMAN	RB1	physical	9071815
BRCA1_HUMAN	BRCA1	physical	12024016
BCR_HUMAN	BCR	physical	1712671
ABL1_HUMAN	ABL1	physical	12654250
P85A_HUMAN	PIK3R1	physical	8294442
RAD51_HUMAN	RAD51	physical	10212258
ABI2_HUMAN	ABI2	physical	12569093
CREB1_MOUSE	Creb1	physical	7565761
ABL2_HUMAN	ABL2	physical	12569093
ATM_HUMAN	ATM	physical	10212258
CREB1_HUMAN	CREB1	physical	7565761
CRKL_HUMAN	CRKL	physical	8978305
CRKL_HUMAN	CRKL	physical	7926767
JAK1_HUMAN	JAK1	physical	9774693
GPX1_HUMAN	GPX1	physical	12893824
CATA_HUMAN	CAT	physical	12777400
ABI1_HUMAN	ABI1	physical	9010225
P53_HUMAN	TP53	physical	10629029
SHIP2_HUMAN	INPPL1	physical	10194451
SHC1_HUMAN	SHC1	physical	8112292
BCR_HUMAN	BCR	physical	8112292
PRKDC_HUMAN	PRKDC	physical	9312071
P73_HUMAN	TP73	physical	10391251
P73_HUMAN	TP73	physical	10391250
RFX1_HUMAN	RFX1	physical	9583676
RAD9A_HUMAN	RAD9A	physical	11971963
ATM_HUMAN	ATM	physical	11375976
TERF1_HUMAN	TERF1	physical	11375976
HCK_HUMAN	HCK	physical	9407116
GRB2_HUMAN	GRB2	physical	9407116
DOK1_HUMAN	DOK1	physical	9008161
VAV_HUMAN	VAV1	physical	11790798
MDM2_HUMAN	MDM2	physical	12110584
MTOR_HUMAN	MTOR	physical	10753870
ZDH16_HUMAN	ZDHHC16	physical	12021275
SPTA1_HUMAN	SPTA1	physical	9593709
SPTN1_HUMAN	SPTAN1	physical	9593709
EVL_HUMAN	EVL	physical	10945997
CASL_HUMAN	NEDD9	physical	8668148
SRBS2_HUMAN	SORBS2	physical	9211900
TUB_HUMAN	TUB	physical	10455176
GRB10_HUMAN	GRB10	physical	9006901
RYBP_HUMAN	RYBP	physical	8943360
PHAG1_HUMAN	PAG1	physical	9334312
ATM_HUMAN	ATM	physical	9168117
CBL_HUMAN	CBL	physical	11494134
NTRK1_HUMAN	NTRK1	physical	10708759
PLCG1_HUMAN	PLCG1	physical	10708759
BCAR1_HUMAN	BCAR1	physical	7780740
MICA1_HUMAN	MICAL1	physical	11827972
SHD_HUMAN	SHD	physical	9315092
SHE_HUMAN	SHE	physical	9315092
NCK1_HUMAN	NCK1	physical	7926767
GRB2_HUMAN	GRB2	physical	7926767
EPHB2_HUMAN	EPHB2	physical	11494128
EPHA3_HUMAN	EPHA3	physical	11494128
SRC_HUMAN	SRC	physical	11494128
NCOA3_HUMAN	NCOA3	physical	18765637
TOPB1_HUMAN	TOPBP1	physical	15961388
HS90A_HUMAN	HSP90AA1	physical	15937340
HSP74_HUMAN	HSPA4	physical	15937340
IKBA_HUMAN	NFKBIA	physical	12167702
PRKN_HUMAN	PARK2	physical	20823226
STK4_HUMAN	STK4	physical	21715626
ATR_HUMAN	ATR	physical	20798688
BAG1_HUMAN	BAG1	physical	20675402
PRKN_HUMAN	PARK2	physical	21209200
PCNA_HUMAN	PCNA	physical	22238610
PSA7_HUMAN	PSMA7	physical	16678104
PSA4_HUMAN	PSMA4	physical	16678104
WRIP1_HUMAN	WRNIP1	physical	17888034
NCK1_HUMAN	NCK1	physical	10372803
CBL_HUMAN	CBL	physical	16955467
CRKL_HUMAN	CRKL	physical	16955467
GRB2_HUMAN	GRB2	physical	16955467
GRB2_HUMAN	GRB2	physical	19823681
DOK1_HUMAN	DOK1	physical	19823681
CBL_HUMAN	CBL	physical	10829062
SRBS1_HUMAN	SORBS1	physical	19891780
GRB2_HUMAN	GRB2	physical	14725908
CBL_HUMAN	CBL	physical	9174058
HUWE1_HUMAN	HUWE1	physical	7968380
MDM4_HUMAN	MDM4	physical	19075013
CBL_HUMAN	CBL	physical	8626543
CBL_HUMAN	CBL	physical	9195915
CBL_HUMAN	CBL	physical	15556646
DDB1_MOUSE	Ddb1	physical	12107171
P85B_HUMAN	PIK3R2	physical	19380743
SHIP2_HUMAN	INPPL1	physical	19380743
SHC1_HUMAN	SHC1	physical	19380743
GRB2_HUMAN	GRB2	physical	19380743
P85A_HUMAN	PIK3R1	physical	19380743
AP2M1_HUMAN	AP2M1	physical	19380743
CBL_HUMAN	CBL	physical	19380743
UBS3B_HUMAN	UBASH3B	physical	19380743
EPS15_HUMAN	EPS15	physical	19380743
CRK_HUMAN	CRK	physical	19380743
AP2B1_HUMAN	AP2B1	physical	19380743
BMP2K_HUMAN	BMP2K	physical	19380743
REPS1_HUMAN	REPS1	physical	19380743
STON2_HUMAN	STON2	physical	19380743
CBLB_HUMAN	CBLB	physical	19380743
AP2A1_HUMAN	AP2A1	physical	19380743
TAU_HUMAN	MAPT	physical	18070606
CRK_HUMAN	CRK	physical	18835194
CRKL_HUMAN	CRKL	physical	18835194
PFD4_HUMAN	PFDN4	physical	22939629
PDE4D_HUMAN	PDE4D	physical	10571082
PRDX1_HUMAN	PRDX1	physical	17352427
BRCA1_HUMAN	BRCA1	physical	17352427
EGFR_HUMAN	EGFR	physical	16273093
ERBB2_HUMAN	ERBB2	physical	16273093
ERBB3_HUMAN	ERBB3	physical	16273093
ERBB4_HUMAN	ERBB4	physical	16273093
WASF1_HUMAN	WASF1	physical	10970852
MUC1_HUMAN	MUC1	physical	16888623
DOK2_HUMAN	DOK2	physical	9478921
CDN1B_HUMAN	CDKN1B	physical	17254966
DOK1_HUMAN	DOK1	physical	9822717
HS90A_HUMAN	HSP90AA1	physical	16723087
TEBP_HUMAN	PTGES3	physical	16723087
HSP74_HUMAN	HSPA4	physical	16723087
CH60_HUMAN	HSPD1	physical	16723087
CTNB1_HUMAN	CTNNB1	physical	23950177
DOK1_HUMAN	DOK1	physical	10688886
UBP7_HUMAN	USP7	physical	24317448
LATS2_HUMAN	LATS2	physical	23852372
SPR2A_HUMAN	SPRR2A	physical	18155796
CASP9_HUMAN	CASP9	physical	15657060
1433G_HUMAN	YWHAG	physical	15696159
1433B_HUMAN	YWHAB	physical	15696159
1433E_HUMAN	YWHAE	physical	15696159
1433Z_HUMAN	YWHAZ	physical	15696159
1433F_HUMAN	YWHAH	physical	15696159
1433T_HUMAN	YWHAQ	physical	15696159
CRK_HUMAN	CRK	physical	15696159
YAP1_HUMAN	YAP1	physical	18280240
ABI1_HUMAN	ABI1	physical	18328268
ABL2_HUMAN	ABL2	physical	15735735
JUN_HUMAN	JUN	physical	18619508
CRK_HUMAN	CRK	physical	18619508
FOS_HUMAN	FOS	physical	18619508
RB_HUMAN	RB1	physical	7828850
CCND2_HUMAN	CCND2	physical	7828850
CRK_HUMAN	CRK	physical	8194526
GRB2_HUMAN	GRB2	physical	8194526
TAU_HUMAN	MAPT	physical	16014719
CDON_HUMAN	CDON	physical	19470755
CDON_RAT	Cdon	physical	19470755
MBP_HUMAN	MBP	physical	19470755
JIP4_HUMAN	SPAG9	physical	19470755
MSH5_HUMAN	MSH5	physical	16397227
ABL1_HUMAN	ABL1	physical	16397227
MSH5_HUMAN	MSH5	physical	19442657
MSH5_MOUSE	Msh5	physical	19442657
RAD51_HUMAN	RAD51	physical	19427856
MAVS_HUMAN	MAVS	physical	19914245
RPGF1_HUMAN	RAPGEF1	physical	16443220
KPCZ_HUMAN	PRKCZ	physical	16631755
B2CL1_HUMAN	BCL2L1	physical	16631755
CKAP4_HUMAN	CKAP4	physical	25852190
DDX5_HUMAN	DDX5	physical	25852190
DRG1_HUMAN	DRG1	physical	25852190
EF1G_HUMAN	EEF1G	physical	25852190
EIF2A_HUMAN	EIF2A	physical	25852190
EWS_HUMAN	EWSR1	physical	25852190
FUS_HUMAN	FUS	physical	25852190
HNRPM_HUMAN	HNRNPM	physical	25852190
CH10_HUMAN	HSPE1	physical	25852190
ILF3_HUMAN	ILF3	physical	25852190
LRC59_HUMAN	LRRC59	physical	25852190
RL37_HUMAN	RPL37	physical	25852190
RLA1_HUMAN	RPLP1	physical	25852190
RS21_HUMAN	RPS21	physical	25852190
TCP4_HUMAN	SUB1	physical	25852190
XRCC6_HUMAN	XRCC6	physical	25852190
1433B_HUMAN	YWHAB	physical	25852190
1433E_HUMAN	YWHAE	physical	25852190
1433G_HUMAN	YWHAG	physical	25852190
1433F_HUMAN	YWHAH	physical	25852190
1433T_HUMAN	YWHAQ	physical	25852190
1433Z_HUMAN	YWHAZ	physical	25852190
ABI2_HUMAN	ABI2	physical	17101133
SHB_HUMAN	SHB	physical	17112510
MDM2_HUMAN	MDM2	physical	25624478
SYLC_HUMAN	LARS	physical	26344197
NAA25_HUMAN	NAA25	physical	26344197
SYNC_HUMAN	NARS	physical	26344197
PAK4_HUMAN	PAK4	physical	26344197
PPM1B_HUMAN	PPM1B	physical	26344197
CRK_HUMAN	CRK	physical	9747873
HIPK2_HUMAN	HIPK2	physical	25944899
CDN1A_HUMAN	CDKN1A	physical	23007395
KS6B1_HUMAN	RPS6KB1	genetic	28319113
CHIP_HUMAN	STUB1	physical	28128329
EMD_HUMAN	EMD	physical	19789182
LAP2A_HUMAN	TMPO	physical	19789182
LAP2B_HUMAN	TMPO	physical	19789182
ABI2_HUMAN	ABI2	physical	27229929
APC15_HUMAN	ANAPC15	physical	27229929
DVL2_HUMAN	DVL2	physical	27229929
PKHA4_HUMAN	PLEKHA4	physical	27229929
RAD51_HUMAN	RAD51	physical	21653319
CRK_HUMAN	CRK	physical	12097319

Drug and Disease Associations

Kegg Disease
H00001	Acute lymphoblastic leukemia (ALL) (precursor B lymphoblastic leukemia)
H00004	Chronic myeloid leukemia (CML)
OMIM Disease
608232	Leukemia, chronic myeloid (CML)
Kegg Drug
D01441	Imatinib mesilate (JAN); Imatinib mesylate (USAN); Gleevec (TN); Glivec (TN)
D03252	Bosutinib (USAN)
D03658	Dasatinib (INN)
D06413	Nilotinib hydrochloride hydrate (JAN); Tasigna (TN)
D06414	Dasatinib hydrate (JAN); Dasatinib (USAN); Sprycel (TN)
D08066	Imatinib (INN); Glamox (TN)
D08279	Tozasertib (USAN)
D08344	Tozasertib lactate (USAN); MK-0457
D08953	Nilotinib (USAN/INN)
D09664	Saracatinib (USAN/INN)
D09665	Saracatinib difumarate (USAN)
D09728	Bosutinib hydrate (JAN); Bosutinib monohydrate; Bosulif (TN)
D09950	Ponatinib (USAN/INN)
D09951	Ponatinib hydrochloride (USAN); Iclusig (TN)
D10202	Bafetinib (USAN)
D10334	Rebastinib (USAN)
D10399	Rebastinib Tosylate (USAN)
DrugBank
DB00171	Adenosine triphosphate
DB06616	Bosutinib
DB01254	Dasatinib
DB00619	Imatinib
DB04868	Nilotinib
DB08901	Ponatinib
DB08896	Regorafenib

Regulatory Network of ABL1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"c-Abl acetylation by histone acetyltransferases regulates itsnuclear-cytoplasmic localization."; di Bari M.G., Ciuffini L., Mingardi M., Testi R., Soddu S., Barila D.; EMBO Rep. 7:727-733(2006). Cited for: ACETYLATION AT LYS-711, AND SUBCELLULAR LOCATION.	16648821 [Abstract]
Phosphorylation
Reference	PubMed
"Organization of the SH3-SH2 unit in active and inactive forms of thec-Abl tyrosine kinase."; Nagar B., Hantschel O., Seeliger M., Davies J.M., Weis W.I.,Superti-Furga G., Kuriyan J.; Mol. Cell 21:787-798(2006). Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 38-512, MASS SPECTROMETRY,MYRISTOYLATION OF N-TERMINUS (ISOFORM IB), PHOSPHORYLATION AT SER-50,AUTOINHIBITION MECHANISM, AND ENZYME REGULATION.	16543148 [Abstract]
"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-50 AND SER-569, AND MASSSPECTROMETRY.	19690332 [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 THR-392; TYR-393 ANDSER-569, AND MASS SPECTROMETRY.	19369195 [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 SER-805; SER-809; THR-852AND SER-855, 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 SER-569; THR-844; THR-852AND SER-917, AND MASS SPECTROMETRY.	18669648 [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-50; TYR-185; TYR-393;SER-569; THR-613; SER-620; SER-659; SER-683; SER-718; THR-781;SER-805; SER-809; THR-814; THR-844; THR-852; SER-917; SER-919; SER-936AND SER-977, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Phosphorylation of c-Abl by protein kinase Pak2 regulatesdifferential binding of ABI2 and CRK."; Jung J.H., Pendergast A.M., Zipfel P.A., Traugh J.A.; Biochemistry 47:1094-1104(2008). Cited for: PHOSPHORYLATION AT SER-618 AND SER-619, AND INTERACTION WITH ABI2 ANDCRK.	18161990 [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-569, AND MASSSPECTROMETRY.	17192257 [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 SER-569; SER-683; SER-805;SER-809 AND SER-949, AND MASS SPECTROMETRY.	17081983 [Abstract]
"JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting ofc-Abl in the apoptotic response to DNA damage."; Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y.; Nat. Cell Biol. 7:278-285(2005). Cited for: INTERACTION WITH YWHAB; YWHAE; YWHAG; YWHAH; SFN AND YWHAZ,PHOSPHORYLATION AT THR-735, MASS SPECTROMETRY, SUBCELLULAR LOCATION,AND MUTAGENESIS OF THR-735.	15696159 [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-185; TYR-226; TYR-253;TYR-257; TYR-264; TYR-393; THR-394 AND TYR-469, AND MASS SPECTROMETRY.	12522270 [Abstract]
"Tyrosine phosphorylation in the SH3 domain disrupts negativeregulatory interactions within the c-Abl kinase core."; Chen S., O'Reilly L.P., Smithgall T.E., Engen J.R.; J. Mol. Biol. 383:414-423(2008). Cited for: PHOSPHORYLATION AT TYR-70, AND INTERACTION WITH ABI1.	18775435 [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-185, AND MASSSPECTROMETRY.	18083107 [Abstract]

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