Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Tyrosine-protein kinase ABL1  

UniProtKB / Swiss-Prot ID :  ABL1_HUMAN

Gene Name (Synonyms) : 
ABL1, ABL, JTK7  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm, cytoskeleton. Nucleus. Mitochondrion (By similarity). Note=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 res 

Protein Function :  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. 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 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. 

Protein Sequence MLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALY...
Predicted Secondary Structure CHHHHHHHHHHHHHHCCCCCCCHHHHHHHCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCEEEEEEE...
Protein Variant
LocationDescription
47R -> G (in a lung large cell carcinomasample; somatic mutation).
140L -> P (in dbSNP:rs1064152). VAR_051692
166R -> K (in a melanoma sample; somaticmutation).
247K -> R (in dbSNP:rs34549764). VAR_051693
706G -> V (in dbSNP:rs34634745). VAR_025043
810P -> L (in dbSNP:rs2229071). VAR_032678
852T -> P. VAR_025044
900P -> S (in dbSNP:rs35266696). VAR_025045
968S -> P (in dbSNP:rs1064165). VAR_051694
972S -> L (in dbSNP:rs2229067). VAR_025046
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
50PhosphoserineARWNSKENL
CCCCCCCCC
34.09HPRD
Link-
50PhosphoserineARWNSKENL
CCCCCCCCC
34.09Phosphositeplus
Link-
50PhosphoserineARWNSKENL
CCCCCCCCC
34.09SysPTM
Link-
50Phosphoserine.ARWNSKENL
CCCCCCCCC
34.09UniProtKB
Link-
70PhosphotyrosineFVALYDFVA
EEEEECCCC
9.52Phosphositeplus
Link-
70Phosphotyrosine; by autocatalysis.FVALYDFVA
EEEEECCCC
9.52UniProtKB
Link-
79PhosphothreonineSGDNTLSIT
CCCCCCEEE
26.99HPRD
Link-
93PhosphotyrosineRVLGYNHNG
EEEECCCCC
14.75Phosphositeplus
Link-
115PhosphotyrosineVPSNYITPV
CCCCCCCCC
15.54HPRD
Link-
115PhosphotyrosineVPSNYITPV
CCCCCCCCC
15.54Phosphositeplus
Link-
128PhosphotyrosineKHSWYHGPV
CCCCCCCCC
10.42Phosphositeplus
Link
139PhosphotyrosineNAAEYLLSS
HHHHHHHCC
14.28Phosphositeplus
Link
172PhosphotyrosineEGRVYHYRI
CCEEEEEEE
7.56Phosphositeplus
Link
185PhosphotyrosineDGKLYVSSE
CCCEEECCC
11.19HPRD
Link
185PhosphotyrosineDGKLYVSSE
CCCEEECCC
11.19PhosphoELM
Link
185PhosphotyrosineDGKLYVSSE
CCCEEECCC
11.19Phosphositeplus
Link
185PhosphotyrosineDGKLYVSSE
CCCEEECCC
11.19SysPTM
Link
185Phosphotyrosine.DGKLYVSSE
CCCEEECCC
11.19UniProtKB
Link
215PhosphotyrosineTTLHYPAPK
CCCCCCCCC
12.28Phosphositeplus
Link
226PhosphotyrosineKPTVYGVSP
CCCCCCCCC
17.81PhosphoELM
Link-
226PhosphotyrosineKPTVYGVSP
CCCCCCCCC
17.81Phosphositeplus
Link-
226Phosphotyrosine (ABL1)KPTVYGVSP
CCCCCCCCC
17.81HPRD
Link-
226Phosphotyrosine; by autocatalysis.KPTVYGVSP
CCCCCCCCC
17.81UniProtKB
Link-
229PhosphoserineVYGVSPNYD
CCCCCCCCC
11.76HPRD
Link-
232PhosphotyrosineVSPNYDKWE
CCCCCCCCC
23.45HPRD
Link-
232PhosphotyrosineVSPNYDKWE
CCCCCCCCC
23.45Phosphositeplus
Link-
253PhosphotyrosineGGGQYGEVY
ECCCCCEEE
20.66HPRD
Link-
253PhosphotyrosineGGGQYGEVY
ECCCCCEEE
20.66Phosphositeplus
Link-
253Phosphotyrosine.GGGQYGEVY
ECCCCCEEE
20.66UniProtKB
Link-
257PhosphotyrosineYGEVYEGVW
CCEEEEEEE
11.58HPRD
Link-
257PhosphotyrosineYGEVYEGVW
CCEEEEEEE
11.58Phosphositeplus
Link-
257Phosphotyrosine.YGEVYEGVW
CCEEEEEEE
11.58UniProtKB
Link-
264PhosphotyrosineVWKKYSLTV
EECCCCEEE
12.75HPRD
Link-
264PhosphotyrosineVWKKYSLTV
EECCCCEEE
12.75PhosphoELM
Link-
264PhosphotyrosineVWKKYSLTV
EECCCCEEE
12.75Phosphositeplus
Link-
264Phosphotyrosine.VWKKYSLTV
EECCCCEEE
12.75UniProtKB
Link-
312PhosphotyrosineEPPFYIITE
CCEEEEEEE
9.37Phosphositeplus
Link-
392PhosphothreonineMTGDTYTAH
ECCCCEEEE
24.90HPRD
Link-
392Phosphothreonine.MTGDTYTAH
ECCCCEEEE
24.90UniProtKB
Link-
393DePhosphotyrosineTGDTYTAHA
CCCCEEEEC
13.48HPRD
Link-
393PhosphotyrosineTGDTYTAHA
CCCCEEEEC
13.48Phosphositeplus
Link-
393PhosphotyrosineTGDTYTAHA
CCCCEEEEC
13.48SysPTM
Link-
393Phosphotyrosine (Abl;Abl)TGDTYTAHA
CCCCEEEEC
13.48PhosphoELM
Link-
393Phosphotyrosine (SRC)TGDTYTAHA
CCCCEEEEC
13.48HPRD
Link-
393Phosphotyrosine; by autocatalysis andSRC-type Tyr-kinases.TGDTYTAHA
CCCCEEEEC
13.48UniProtKB
Link-
394PhosphothreonineGDTYTAHAG
CCCEEEECC
17.66HPRD
Link-
394PhosphothreonineGDTYTAHAG
CCCEEEECC
17.66PhosphoELM
Link-
394PhosphothreonineGDTYTAHAG
CCCEEEECC
17.66Phosphositeplus
Link-
394PhosphothreonineGDTYTAHAG
CCCEEEECC
17.66SysPTM
Link-
394Phosphothreonine.GDTYTAHAG
CCCEEEECC
17.66UniProtKB
Link-
413PhosphotyrosineESLAYNKFS
HHHHCCCCC
24.95Phosphositeplus
Link-
446PhosphoserineGIDLSQVYE
CCCHHHHHH
17.53HPRD
Link-
446PhosphoserineGIDLSQVYE
CCCHHHHHH
17.53Phosphositeplus
Link-
446Phosphoserine (ATM)GIDLSQVYE
CCCHHHHHH
17.53HPRD
Link-
446Phosphoserine (ATM)GIDLSQVYE
CCCHHHHHH
17.53PhosphoELM
Link-
469PhosphotyrosinePEKVYELMR
CHHHHHHHH
17.89Phosphositeplus
Link-
469Phosphotyrosine (ABL1)PEKVYELMR
CHHHHHHHH
17.89HPRD
Link-
469Phosphotyrosine.PEKVYELMR
CHHHHHHHH
17.89UniProtKB
Link-
569PhosphoserineEPAVSPLLP
CCCCCCCCC
16.37PhosphoELM
Link-
569PhosphoserineEPAVSPLLP
CCCCCCCCC
16.37Phosphositeplus
Link-
569PhosphoserineEPAVSPLLP
CCCCCCCCC
16.37SysPTM
Link-
569Phosphoserine (CDK1)EPAVSPLLP
CCCCCCCCC
16.37HPRD
Link-
569Phosphoserine.EPAVSPLLP
CCCCCCCCC
16.37UniProtKB
Link-
610PhosphothreonineKKKKTAPTP
CCCCCCCCC
46.91Phosphositeplus
Link-
613PhosphothreonineKTAPTPPKR
CCCCCCCCC
50.16HPRD
Link-
613PhosphothreonineKTAPTPPKR
CCCCCCCCC
50.16Phosphositeplus
Link-
613PhosphothreonineKTAPTPPKR
CCCCCCCCC
50.16SysPTM
Link-
613Phosphothreonine.KTAPTPPKR
CCCCCCCCC
50.16UniProtKB
Link-
618PhosphoserinePPKRSSSFR
CCCCCCCCC
36.14HPRD
Link-
618PhosphoserinePPKRSSSFR
CCCCCCCCC
36.14Phosphositeplus
Link-
618Phosphoserine; by PAK2.PPKRSSSFR
CCCCCCCCC
36.14UniProtKB
Link-
619PhosphoserinePKRSSSFRE
CCCCCCCCC
37.21Phosphositeplus
Link-
619Phosphoserine; by PAK2.PKRSSSFRE
CCCCCCCCC
37.21UniProtKB
Link-
620PhosphoserineKRSSSFREM
CCCCCCCCC
29.57HPRD
Link-
620PhosphoserineKRSSSFREM
CCCCCCCCC
29.57Phosphositeplus
Link-
620PhosphoserineKRSSSFREM
CCCCCCCCC
29.57SysPTM
Link-
620Phosphoserine.KRSSSFREM
CCCCCCCCC
29.57UniProtKB
Link-
659PhosphoserineDPAKSPKPS
CCCCCCCCC
40.02HPRD
Link-
659PhosphoserineDPAKSPKPS
CCCCCCCCC
40.02Phosphositeplus
Link-
659PhosphoserineDPAKSPKPS
CCCCCCCCC
40.02SysPTM
Link-
659Phosphoserine.DPAKSPKPS
CCCCCCCCC
40.02UniProtKB
Link-
683PhosphoserineSGFRSPHLW
CCCCCCCCC
17.89HPRD
Link-
683PhosphoserineSGFRSPHLW
CCCCCCCCC
17.89Phosphositeplus
Link-
683PhosphoserineSGFRSPHLW
CCCCCCCCC
17.89SysPTM
Link-
683Phosphoserine.SGFRSPHLW
CCCCCCCCC
17.89UniProtKB
Link-
710PhosphoserineGGSSSKRFL
CCCCCCCCC
29.55HPRD
Link-
711N6-acetyllysineGSSSKRFLR
CCCCCCCCC
49.47Phosphositeplus
Link-
711N6-acetyllysine; by EP300.GSSSKRFLR
CCCCCCCCC
49.47UniProtKB
Link-
718PhosphoserineLRSCSASCV
CCCCCCCCC
25.18HPRD
Link-
718PhosphoserineLRSCSASCV
CCCCCCCCC
25.18Phosphositeplus
Link-
718PhosphoserineLRSCSASCV
CCCCCCCCC
25.18SysPTM
Link-
718Phosphoserine.LRSCSASCV
CCCCCCCCC
25.18UniProtKB
Link-
735PhosphothreonineWRSVTLPRD
CCCCCCCHH
32.09HPRD
Link-
735PhosphothreonineWRSVTLPRD
CCCCCCCHH
32.09Phosphositeplus
Link-
735Phosphothreonine (TTK)WRSVTLPRD
CCCCCCCHH
32.09PhosphoELM
Link-
735Phosphothreonine.WRSVTLPRD
CCCCCCCHH
32.09UniProtKB
Link-
781PhosphothreonineRGTVTPPPR
CCCCCCCCC
29.89HPRD
Link-
781PhosphothreonineRGTVTPPPR
CCCCCCCCC
29.89Phosphositeplus
Link-
781PhosphothreonineRGTVTPPPR
CCCCCCCCC
29.89SysPTM
Link-
781Phosphothreonine.RGTVTPPPR
CCCCCCCCC
29.89UniProtKB
Link-
804PhosphoserineDIMESSPGS
CCCCCCCCC
25.18HPRD
Link-
805PhosphoserineIMESSPGSS
CCCCCCCCC
21.70HPRD
Link-
805PhosphoserineIMESSPGSS
CCCCCCCCC
21.70Phosphositeplus
Link-
805PhosphoserineIMESSPGSS
CCCCCCCCC
21.70SysPTM
Link-
805Phosphoserine.IMESSPGSS
CCCCCCCCC
21.70UniProtKB
Link-
808PhosphoserineSSPGSSPPN
CCCCCCCCC
42.95HPRD
Link-
808PhosphoserineSSPGSSPPN
CCCCCCCCC
42.95Phosphositeplus
Link-
809PhosphoserineSPGSSPPNL
CCCCCCCCC
50.74HPRD
Link-
809PhosphoserineSPGSSPPNL
CCCCCCCCC
50.74Phosphositeplus
Link-
809PhosphoserineSPGSSPPNL
CCCCCCCCC
50.74SysPTM
Link-
809Phosphoserine.SPGSSPPNL
CCCCCCCCC
50.74UniProtKB
Link-
814PhosphothreoninePPNLTPKPL
CCCCCCCCC
35.59HPRD
Link-
814PhosphothreoninePPNLTPKPL
CCCCCCCCC
35.59Phosphositeplus
Link-
814PhosphothreoninePPNLTPKPL
CCCCCCCCC
35.59SysPTM
Link-
814Phosphothreonine.PPNLTPKPL
CCCCCCCCC
35.59UniProtKB
Link-
828PhosphoserineVAPASGLPH
CCCCCCCCC
39.54HPRD
Link-
844PhosphothreonineSALGTPAAA
CCCCCCCCC
15.59HPRD
Link-
844PhosphothreonineSALGTPAAA
CCCCCCCCC
15.59PhosphoELM
Link-
844PhosphothreonineSALGTPAAA
CCCCCCCCC
15.59Phosphositeplus
Link-
844PhosphothreonineSALGTPAAA
CCCCCCCCC
15.59SysPTM
Link-
844Phosphothreonine.SALGTPAAA
CCCCCCCCC
15.59UniProtKB
Link-
852PhosphothreonineAEPVTPTSK
CCCCCCCCC
31.40HPRD
Link-
852PhosphothreonineAEPVTPTSK
CCCCCCCCC
31.40PhosphoELM
Link-
852PhosphothreonineAEPVTPTSK
CCCCCCCCC
31.40Phosphositeplus
Link-
852PhosphothreonineAEPVTPTSK
CCCCCCCCC
31.40SysPTM
Link-
852Phosphothreonine.AEPVTPTSK
CCCCCCCCC
31.40UniProtKB
Link-
854PhosphothreoninePVTPTSKAG
CCCCCCCCC
33.23HPRD
Link-
854PhosphothreoninePVTPTSKAG
CCCCCCCCC
33.23PhosphoELM
Link-
855PhosphoserineVTPTSKAGS
CCCCCCCCC
23.01HPRD
Link-
855Phosphoserine.VTPTSKAGS
CCCCCCCCC
23.01UniProtKB
Link-
915PhosphoserineGGKPSQSPS
CCCCCCCCC
46.94HPRD
Link-
917PhosphoserineKPSQSPSQE
CCCCCCCCC
30.75HPRD
Link-
917PhosphoserineKPSQSPSQE
CCCCCCCCC
30.75PhosphoELM
Link-
917PhosphoserineKPSQSPSQE
CCCCCCCCC
30.75Phosphositeplus
Link-
917PhosphoserineKPSQSPSQE
CCCCCCCCC
30.75SysPTM
Link-
917Phosphoserine.KPSQSPSQE
CCCCCCCCC
30.75UniProtKB
Link-
919PhosphoserineSQSPSQEAA
CCCCCCCCC
45.99Phosphositeplus
Link-
919PhosphoserineSQSPSQEAA
CCCCCCCCC
45.99SysPTM
Link-
919Phosphoserine.SQSPSQEAA
CCCCCCCCC
45.99UniProtKB
Link-
919Phosphotyrosine (ABL1)SQSPSQEAA
CCCCCCCCC
45.99HPRD
Link-
936PhosphoserineTKATSLVDA
CCCCCCCCC
31.12HPRD
Link-
936PhosphoserineTKATSLVDA
CCCCCCCCC
31.12HPRD
Link-
936PhosphoserineTKATSLVDA
CCCCCCCCC
31.12Phosphositeplus
Link-
936PhosphoserineTKATSLVDA
CCCCCCCCC
31.12SysPTM
Link-
936Phosphoserine.TKATSLVDA
CCCCCCCCC
31.12UniProtKB
Link-
939Caspase cleavage aspartic acidTSLVDAVNS
CCCCCCCCC
50.52Phosphositeplus
Link-
949PhosphoserineAAKPSQPGE
CCCCCCCCC
48.58HPRD
Link-
949PhosphoserineAAKPSQPGE
CCCCCCCCC
48.58PhosphoELM
Link-
949PhosphoserineAAKPSQPGE
CCCCCCCCC
48.58Phosphositeplus
Link-
949PhosphoserineAAKPSQPGE
CCCCCCCCC
48.58SysPTM
Link-
949Phosphoserine.AAKPSQPGE
CCCCCCCCC
48.58UniProtKB
Link-
968PhosphoserinePKPQSAKPS
CCCCCCCCC
46.95HPRD
Link-
977PhosphoserineGTPISPAPV
CCCCCCCCC
19.06HPRD
Link-
977PhosphoserineGTPISPAPV
CCCCCCCCC
19.06Phosphositeplus
Link-
977PhosphoserineGTPISPAPV
CCCCCCCCC
19.06SysPTM
Link-
977Phosphoserine.GTPISPAPV
CCCCCCCCC
19.06UniProtKB
Link-
989PhosphoserineLPSASSALA
CCCCCCCCC
22.08HPRD
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
NMDE4_HUMANphysical interactionMINT-15264MINT10777567
NMDE4_HUMANphysical interactionMINT-15265MINT10777567
EGFR_HUMANphysical interactionMINT-74427MINT16273093
ERBB2_HUMANphysical interactionMINT-74428MINT16273093
RB_HUMANphysical interactionMINT-17913MINT7828850
SRC_HUMANphysical interactionMINT-4508163MINT17318191
MUC1_HUMANphysical interactionMINT-2880925MINT16888623
MUC1_HUMANphysical interactionMINT-2880944MINT16888623
MUC1_HUMANphysical interactionMINT-2881060MINT16888623
MUC1_HUMANphysical interactionMINT-2881084MINT16888623
MUC1_HUMANphysical interactionMINT-2881002MINT16888623
MUC1_HUMANcolocalizationMINT-2880967MINT16888623
MUC1_HUMANdirect interactionMINT-2881110MINT16888623
MUC1_HUMANphosphorylation reactionMINT-2881028MINT16888623
CTNB1_HUMANphosphorylation reactionMINT-4508216MINT17318191
KPCD_HUMANphysical interactionMINT-1955124MINT16631755
RIN1_HUMANphysical interactionMINT-59454MINT15886098
RIN1_HUMANphysical interactionMINT-59466MINT15886098
ERBB4_HUMANphysical interactionMINT-74431MINT16273093
ABI1_HUMANphysical interactionMINT-3390262MINT17101133
ABI1_HUMANphysical interactionMINT-3390323MINT17101133
WASF1_HUMANphysical interactionMINT-16418MINT10970852
WASF1_HUMANphysical interactionMINT-16419MINT10970852
ABI2_HUMANphysical interactionMINT-3390285MINT17101133
ATM_HUMANphysical interactionDIP:25EDIP9168117
1433F_HUMANphysical interactionEBI-593829
intact15696159
1433G_HUMANphysical interactionEBI-593829
intact15696159
1433S_HUMANphysical interaction
physical interaction
EBI-593829
EBI-593877
intact15696159
15696159
1433Z_HUMANphysical interaction
physical interaction
EBI-593829
EBI-593857
intact15696159
15696159
1433B_HUMANphysical interactionEBI-593829
intact15696159
1433E_HUMANphysical interactionEBI-593829
intact15696159
ATM_HUMANphysical interactionEBI-1005980
intact11375976
RIN1_HUMANphysical interaction
physical interaction
physical interaction
phosphorylation
EBI-1102773
EBI-1102761
EBI-1
intact15886098
15886098
15886098
9144171
ABI1_HUMANphysical interaction
physical interaction
physical interaction
EBI-389880
EBI-389836
EBI-375
intact11418237
11418237
9593709
A4_HUMANin vivoHPRD:01809HPRD11279131
ACTS_HUMANin vitro
in vivo
HPRD:01809HPRD11309382
CD19_HUMANin vitro
in vivo
HPRD:01809HPRD11120811
GRB2_HUMANin vitroHPRD:01809HPRD9516488
14725908
1433F_HUMANin vivoHPRD:01809HPRD15696159
CO3_HUMANin vitroHPRD:01809HPRD4062888
CDK5_HUMANin vitro
in vivo
HPRD:01809HPRD10896159
ST5_HUMANin vitroHPRD:01809HPRD9632734
HCK_HUMANin vitro
in vivo
HPRD:01809HPRD9407116
10849448
JAK2_HUMANin vitro
in vivo
HPRD:01809HPRD9111318
11593427
15143187
JAK1_HUMANin vivoHPRD:01809HPRD12130510
CRK_HUMANin vitro
in vivo
HPRD:01809HPRD12198159
11956190
9642287
8875975
9480911
8194526
11380621
MDM2_HUMANin vitro
in vivo
HPRD:01809HPRD12110584
BCR_HUMANin vitro
in vivo
HPRD:01809HPRD11780146
ROS_HUMANyeast 2-hybridHPRD:01809HPRD11266449
KU70_HUMANin vivoHPRD:01809HPRD9798959
JUN_HUMANin vitro
in vivo
HPRD:01809HPRD10637231
KPCD1_HUMANin vitroHPRD:01809HPRD12637538
CBL_HUMANin vitro
in vivo
HPRD:01809HPRD12475393
PTN6_HUMANin vitro
in vivo
HPRD:01809HPRD12468540
8114715
8692915
10488096
10574931
7512963
ZAP70_HUMANin vivoHPRD:01809HPRD7760813
ABL2_HUMANin vitro
in vivo
HPRD:01809HPRD12569093
RAD51_HUMANin vitro
in vivo
HPRD:01809HPRD9461559
10212258
RB_HUMANin vitro
in vivo
HPRD:01809HPRD8242749
7828850
ABL1_HUMANin vitro
in vivo
HPRD:01809HPRD8438166
12522270
BTK_HUMANin vitro
in vivo
HPRD:01809HPRD12445832
8630736
11598012
8629002
12573241
M4K1_HUMANin vitro
in vivo
HPRD:01809HPRD11278340
P73_HUMANin vitro
in vivo
HPRD:01809HPRD10391250
10391251
CASP9_HUMANin vitro
in vivo
HPRD:01809HPRD15657060
RAD9A_HUMANin vitro
in vivo
HPRD:01809HPRD11971963
PPIP1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:01809HPRD11163214
PLS1_HUMANin vitro
in vivo
HPRD:01809HPRD11390389
GPX1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:01809HPRD12893824
ABI1_HUMANin vitro
yeast 2-hybrid
HPRD:01809HPRD8943360
9010225
12672821
11418237
9593709
RAD52_HUMANin vitro
in vivo
HPRD:01809HPRD12379650
CAV1_HUMANin vivoHPRD:01809HPRD16151024
TAU_HUMANin vivoHPRD:01809HPRD16014719
WASL_HUMANin vitro
in vivo
HPRD:01809HPRD16199863
P85A_HUMANin vitroHPRD:01809HPRD1383690
PLCG1_HUMANin vitroHPRD:01809HPRD1383690
RASA1_HUMANin vitroHPRD:01809HPRD1383690
ROBO1_HUMANin vitroHPRD:01809HPRD10892742
TRAF6_HUMANin vitroHPRD:01809HPRD10635328
DDB1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:01809HPRD12107171
DDB2_HUMANin vivoHPRD:01809HPRD12107171
TERT_HUMANin vitro
in vivo
HPRD:01809HPRD10837221
CDN1B_HUMANin vitro
in vivo
HPRD:01809HPRD17254966
1433Z_HUMANin vivoHPRD:01809HPRD15696159
1433E_HUMANin vivoHPRD:01809HPRD15696159
1433B_HUMANin vivoHPRD:01809HPRD15696159
1433G_HUMANin vivoHPRD:01809HPRD15696159
1433S_HUMANin vivoHPRD:01809HPRD15696159
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Disease Reference
Kegg disease
H00001 Acute lymphoblastic leukemia (ALL) (precursor B lymphoblastic leukemia)
H00004 Chronic myeloid leukemia (CML)
OMIM disease
608232Leukemia, chronic myeloid (CML)
Drug Reference
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
DB00171Adenosine triphosphate
DB06616Bosutinib
DB01254Dasatinib
DB00619Imatinib
DB04868Nilotinib
DB08901Ponatinib
DB08896Regorafenib
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.
Phosphorylation
ReferencePubMed
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures