ABL2_HUMAN - dbPTM
ABL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABL2_HUMAN
UniProt AC P42684
Protein Name Tyrosine-protein kinase ABL2
Gene Name ABL2
Organism Homo sapiens (Human).
Sequence Length 1182
Subcellular Localization Cytoplasm, cytoskeleton.
Protein Description Non-receptor tyrosine-protein kinase that plays an ABL1-overlapping role in key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion and receptor endocytosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like MYH10 (involved in movement); CTTN (involved in signaling); or TUBA1 and TUBB (microtubule subunits). Binds directly F-actin and regulates actin cytoskeletal structure through its F-actin-bundling activity. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as CRK, CRKL, DOK1 or ARHGAP35. Adhesion-dependent phosphorylation of ARHGAP35 promotes its association with RASA1, resulting in recruitment of ARHGAP35 to the cell periphery where it inhibits RHO. Phosphorylates multiple receptor tyrosine kinases like PDGFRB and other substrates which are involved in endocytosis regulation such as RIN1. In brain, may regulate neurotransmission by phosphorylating proteins at the synapse. ABL2 acts also as a regulator of multiple pathological signaling cascades during infection. Pathogens can highjack ABL2 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 MGQQVGRVGEAPGLQQPQPRGIRGSSAARPSGRRRDPAGRTTETGFNIFTQHDHFASCVEDGFEGDKTGGSSPEALHRPYGCDVEPQALNEAIRWSSKENLLGATESDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNQNGEWSEVRSKNGQGWVPSNYITPVNSLEKHSWYHGPVSRSAAEYLLSSLINGSFLVRESESSPGQLSISLRYEGRVYHYRINTTADGKVYVTAESRFSTLAELVHHHSTVADGLVTTLHYPAPKCNKPTVYGVSPIHDKWEMERTDITMKHKLGGGQYGEVYVGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTLEPPFYIVTEYMPYGNLLDYLRECNREEVTAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHVVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNTFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYDLLEKGYRMEQPEGCPPKVYELMRACWKWSPADRPSFAETHQAFETMFHDSSISEEVAEELGRAASSSSVVPYLPRLPILPSKTRTLKKQVENKENIEGAQDATENSASSLAPGFIRGAQASSGSPALPRKQRDKSPSSLLEDAKETCFTRDRKGGFFSSFMKKRNAPTPPKRSSSFREMENQPHKKYELTGNFSSVASLQHADGFSFTPAQQEANLVPPKCYGGSFAQRNLCNDDGGGGGGSGTAGGGWSGITGFFTPRLIKKTLGLRAGKPTASDDTSKPFPRSNSTSSMSSGLPEQDRMAMTLPRNCQRSKLQLERTVSTSSQPEENVDRANDMLPKKSEESAAPSRERPKAKLLPRGATALPLRTPSGDLAITEKDPPGVGVAGVAAAPKGKEKNGGARLGMAGVPEDGEQPGWPSPAKAAPVLPTTHNHKVPVLISPTLKHTPADVQLIGTDSQGNKFKLLSEHQVTSSGDKDRPRRVKPKCAPPPPPVMRLLQHPSICSDPTEEPTALTAGQSTSETQEGGKKAALGAVPISGKAGRPVMPPPQVPLPTSSISPAKMANGTAGTKVALRKTKQAAEKISADKISKEALLECADLLSSALTEPVPNSQLVDTGHQLLDYCSGYVDCIPQTRNKFAFREAVSKLELSLQELQVSSAAAGVPGTNPVLNNLLSCVQEISDVVQR
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Myristoylation------MGQQVGRVG
------CCCCCCCCC
37.62-
5 (in isoform 10)Phosphorylation-3.9824043423
5 (in isoform 2)Phosphorylation-3.9824043423
5 (in isoform 3)Phosphorylation-3.9824043423
5 (in isoform 4)Phosphorylation-3.9824043423
12 (in isoform 10)Phosphorylation-39.4624043423
12 (in isoform 2)Phosphorylation-39.4624043423
12 (in isoform 3)Phosphorylation-39.4624043423
12 (in isoform 4)Phosphorylation-39.4624043423
13 (in isoform 10)Phosphorylation-43.0724043423
13 (in isoform 2)Phosphorylation-43.0724043423
13 (in isoform 3)Phosphorylation-43.0724043423
13 (in isoform 4)Phosphorylation-43.0724043423
23MethylationQPQPRGIRGSSAARP
CCCCCCCCCCCCCCC
41.59-
25PhosphorylationQPRGIRGSSAARPSG
CCCCCCCCCCCCCCC
13.6220068231
26PhosphorylationPRGIRGSSAARPSGR
CCCCCCCCCCCCCCC
28.8620068231
31PhosphorylationGSSAARPSGRRRDPA
CCCCCCCCCCCCCCC
39.1020068231
57PhosphorylationTQHDHFASCVEDGFE
CCCCHHHHHHHCCCC
20.1132142685
59 (in isoform 6)Phosphorylation-7.5227307780
59 (in isoform 7)Phosphorylation-7.5227307780
59 (in isoform 8)Phosphorylation-7.5227307780
60 (in isoform 2)Phosphorylation-57.66-
68PhosphorylationDGFEGDKTGGSSPEA
CCCCCCCCCCCCHHH
52.0625159151
71PhosphorylationEGDKTGGSSPEALHR
CCCCCCCCCHHHHCC
44.0325159151
72PhosphorylationGDKTGGSSPEALHRP
CCCCCCCCHHHHCCC
29.9925159151
80PhosphorylationPEALHRPYGCDVEPQ
HHHHCCCCCCCCCHH
30.2818691976
80 (in isoform 2)Phosphorylation-30.28-
96PhosphorylationLNEAIRWSSKENLLG
HHHHHHHHCCCCCCC
22.9918691976
97PhosphorylationNEAIRWSSKENLLGA
HHHHHHHCCCCCCCC
36.7128464451
107PhosphorylationNLLGATESDPNLFVA
CCCCCCCCCCCEEEE
54.7528464451
116PhosphorylationPNLFVALYDFVASGD
CCEEEEEHHHHHCCC
9.5217192257
121PhosphorylationALYDFVASGDNTLSI
EEHHHHHCCCCEEEE
41.1820071362
125PhosphorylationFVASGDNTLSITKGE
HHHCCCCEEEEECCC
26.9920068231
127PhosphorylationASGDNTLSITKGEKL
HCCCCEEEEECCCEE
26.6124719451
139PhosphorylationEKLRVLGYNQNGEWS
CEEEEEEECCCCCCE
14.9319275932
159PhosphorylationNGQGWVPSNYITPVN
CCCCEECCCCCCCCH
32.4221945579
161PhosphorylationQGWVPSNYITPVNSL
CCEECCCCCCCCHHH
15.5421945579
163PhosphorylationWVPSNYITPVNSLEK
EECCCCCCCCHHHCC
15.7221945579
164 (in isoform 2)Phosphorylation-17.46-
167PhosphorylationNYITPVNSLEKHSWY
CCCCCCHHHCCCCCC
37.8318691976
167 (in isoform 2)Phosphorylation-37.83-
172PhosphorylationVNSLEKHSWYHGPVS
CHHHCCCCCCCCCCC
40.1621945579
172 (in isoform 2)Phosphorylation-40.16-
174PhosphorylationSLEKHSWYHGPVSRS
HHCCCCCCCCCCCHH
10.4221945579
179PhosphorylationSWYHGPVSRSAAEYL
CCCCCCCCHHHHHHH
24.5321945579
185PhosphorylationVSRSAAEYLLSSLIN
CCHHHHHHHHHHHHC
14.28-
194PhosphorylationLSSLINGSFLVRESE
HHHHHCCCEEEEECC
15.77-
195 (in isoform 2)Phosphorylation-8.51-
200PhosphorylationGSFLVRESESSPGQL
CCEEEEECCCCCCEE
32.0122496350
202PhosphorylationFLVRESESSPGQLSI
EEEEECCCCCCEEEE
51.6229255136
203PhosphorylationLVRESESSPGQLSIS
EEEECCCCCCEEEEE
29.0629255136
208PhosphorylationESSPGQLSISLRYEG
CCCCCEEEEEEEECC
11.4025159151
210PhosphorylationSPGQLSISLRYEGRV
CCCEEEEEEEECCEE
11.9229496963
213PhosphorylationQLSISLRYEGRVYHY
EEEEEEEECCEEEEE
28.2023917254
218PhosphorylationLRYEGRVYHYRINTT
EEECCEEEEEEEEEC
7.5621447384
224PhosphorylationVYHYRINTTADGKVY
EEEEEEEECCCCEEE
22.4628152594
225PhosphorylationYHYRINTTADGKVYV
EEEEEEECCCCEEEE
20.4728152594
231PhosphorylationTTADGKVYVTAESRF
ECCCCEEEEEEECHH
8.7925159151
233PhosphorylationADGKVYVTAESRFST
CCCEEEEEEECHHHH
13.6628152594
236PhosphorylationKVYVTAESRFSTLAE
EEEEEEECHHHHHHH
35.8428152594
236 (in isoform 2)Phosphorylation-35.84-
239PhosphorylationVTAESRFSTLAELVH
EEEECHHHHHHHHHH
22.7718691976
239 (in isoform 2)Phosphorylation-22.77-
261PhosphorylationGLVTTLHYPAPKCNK
CCEEEEECCCCCCCC
12.2815735735
270PhosphorylationAPKCNKPTVYGVSPI
CCCCCCCCEEEECCC
28.1529978859
272PhosphorylationKCNKPTVYGVSPIHD
CCCCCCEEEECCCCC
17.8116464493
275PhosphorylationKPTVYGVSPIHDKWE
CCCEEEECCCCCCCE
17.4925159151
277 (in isoform 2)Phosphorylation-5.23-
286PhosphorylationDKWEMERTDITMKHK
CCCEECCCEEEEEEE
20.6024719451
289PhosphorylationEMERTDITMKHKLGG
EECCCEEEEEEECCC
23.99-
299PhosphorylationHKLGGGQYGEVYVGV
EECCCCCCCEEEEEE
20.6619060867
303PhosphorylationGGQYGEVYVGVWKKY
CCCCCEEEEEEEECE
6.2816464493
310PhosphorylationYVGVWKKYSLTVAVK
EEEEEECEEEEEEEE
12.7512522270
311PhosphorylationVGVWKKYSLTVAVKT
EEEEECEEEEEEEEC
26.8328152594
313PhosphorylationVWKKYSLTVAVKTLK
EEECEEEEEEEECCC
10.6520068231
320AcetylationTVAVKTLKEDTMEVE
EEEEECCCCCCHHHH
59.7919815467
331UbiquitinationMEVEEFLKEAAVMKE
HHHHHHHHHHHHHHH
51.10-
352PhosphorylationVQLLGVCTLEPPFYI
HHHHCEEECCCCEEE
31.5822210691
358PhosphorylationCTLEPPFYIVTEYMP
EECCCCEEEEEECCC
10.5624043423
361PhosphorylationEPPFYIVTEYMPYGN
CCCEEEEEECCCCCH
16.3122210691
363PhosphorylationPFYIVTEYMPYGNLL
CEEEEEECCCCCHHH
8.2724043423
366PhosphorylationIVTEYMPYGNLLDYL
EEEECCCCCHHHHHH
11.3424043423
372PhosphorylationPYGNLLDYLRECNRE
CCCHHHHHHHHCCHH
13.9724043423
388PhosphorylationVTAVVLLYMATQISS
HHHHHHHHHHHHHHH
4.7930377224
391PhosphorylationVVLLYMATQISSAME
HHHHHHHHHHHHHHH
15.2022210691
394PhosphorylationLYMATQISSAMEYLE
HHHHHHHHHHHHHHH
11.3922210691
395PhosphorylationYMATQISSAMEYLEK
HHHHHHHHHHHHHHH
33.0122210691
399PhosphorylationQISSAMEYLEKKNFI
HHHHHHHHHHHCCCC
13.6922210691
402 (in isoform 2)Phosphorylation-50.88-
404 (in isoform 2)Phosphorylation-52.77-
410UbiquitinationKNFIHRDLAARNCLV
CCCCCHHHHHCCCCC
3.9622817900
414UbiquitinationHRDLAARNCLVGENH
CHHHHHCCCCCCCCC
20.8122817900
425UbiquitinationGENHVVKVADFGLSR
CCCCEEEEHHHCCCH
4.1122817900
429UbiquitinationVVKVADFGLSRLMTG
EEEEHHHCCCHHCCC
24.2422817900
431UbiquitinationKVADFGLSRLMTGDT
EEHHHCCCHHCCCCE
24.6122817900
435PhosphorylationFGLSRLMTGDTYTAH
HCCCHHCCCCEEECC
36.1821945579
435UbiquitinationFGLSRLMTGDTYTAH
HCCCHHCCCCEEECC
36.1822817900
438PhosphorylationSRLMTGDTYTAHAGA
CHHCCCCEEECCCCC
24.9021945579
439PhosphorylationRLMTGDTYTAHAGAK
HHCCCCEEECCCCCC
13.4822322096
440PhosphorylationLMTGDTYTAHAGAKF
HCCCCEEECCCCCCC
17.6621945579
446UbiquitinationYTAHAGAKFPIKWTA
EECCCCCCCCCEECC
51.2422817900
450UbiquitinationAGAKFPIKWTAPESL
CCCCCCCEECCCCHH
38.4422817900
452PhosphorylationAKFPIKWTAPESLAY
CCCCCEECCCCHHHC
27.60-
459PhosphorylationTAPESLAYNTFSIKS
CCCCHHHCCCCCCCC
21.74-
492PhosphorylationPYPGIDLSQVYDLLE
CCCCCCHHHHHHHHH
17.53-
515PhosphorylationEGCPPKVYELMRACW
CCCCHHHHHHHHHHH
14.9612522270
542UbiquitinationTHQAFETMFHDSSIS
HHHHHHHHHCCCCCC
1.9029967540
557UbiquitinationEEVAEELGRAASSSS
HHHHHHHHHHHHCCC
22.0629967540
561PhosphorylationEELGRAASSSSVVPY
HHHHHHHHCCCCCCC
29.7528442448
562PhosphorylationELGRAASSSSVVPYL
HHHHHHHCCCCCCCC
23.1621945579
563PhosphorylationLGRAASSSSVVPYLP
HHHHHHCCCCCCCCC
25.3421945579
563UbiquitinationLGRAASSSSVVPYLP
HHHHHHCCCCCCCCC
25.3429967540
563 (in isoform 2)Phosphorylation-25.34-
564PhosphorylationGRAASSSSVVPYLPR
HHHHHCCCCCCCCCC
29.1428442448
566 (in isoform 2)Phosphorylation-2.52-
568PhosphorylationSSSSVVPYLPRLPIL
HCCCCCCCCCCCCCC
20.0921945579
577PhosphorylationPRLPILPSKTRTLKK
CCCCCCCCCCHHHHH
43.1221945579
578AcetylationRLPILPSKTRTLKKQ
CCCCCCCCCHHHHHH
39.8325953088
578UbiquitinationRLPILPSKTRTLKKQ
CCCCCCCCCHHHHHH
39.8329967540
581PhosphorylationILPSKTRTLKKQVEN
CCCCCCHHHHHHHHC
48.4318691976
581 (in isoform 2)Phosphorylation-48.43-
582 (in isoform 2)Phosphorylation-6.17-
584 (in isoform 2)Phosphorylation-63.79-
595PhosphorylationNKENIEGAQDATENS
CCCCCCCCCCCCCCC
7.4132142685
595 (in isoform 2)Phosphorylation-7.41-
597 (in isoform 2)Phosphorylation-55.73-
598 (in isoform 2)Phosphorylation-12.53-
599PhosphorylationIEGAQDATENSASSL
CCCCCCCCCCCHHHC
43.9518691976
602PhosphorylationAQDATENSASSLAPG
CCCCCCCCHHHCCCC
24.2425159151
604PhosphorylationDATENSASSLAPGFI
CCCCCCHHHCCCCHH
26.2125850435
605PhosphorylationATENSASSLAPGFIR
CCCCCHHHCCCCHHH
28.4125850435
610PhosphorylationASSLAPGFIRGAQAS
HHHCCCCHHHCHHCC
3.1532142685
616PhosphorylationGFIRGAQASSGSPAL
CHHHCHHCCCCCCCC
12.7232142685
617PhosphorylationFIRGAQASSGSPALP
HHHCHHCCCCCCCCC
24.1330266825
618PhosphorylationIRGAQASSGSPALPR
HHCHHCCCCCCCCCH
46.4330266825
619 (in isoform 2)Phosphorylation-34.84-
620PhosphorylationGAQASSGSPALPRKQ
CHHCCCCCCCCCHHH
14.6719664994
631PhosphorylationPRKQRDKSPSSLLED
CHHHCCCCHHHHHHH
34.0129255136
633PhosphorylationKQRDKSPSSLLEDAK
HHCCCCHHHHHHHHH
40.4829255136
634PhosphorylationQRDKSPSSLLEDAKE
HCCCCHHHHHHHHHH
40.1230266825
634 (in isoform 4)Phosphorylation-40.1224719451
635 (in isoform 2)Phosphorylation-7.72-
642PhosphorylationLLEDAKETCFTRDRK
HHHHHHHHHCCCCCC
16.5324732914
645PhosphorylationDAKETCFTRDRKGGF
HHHHHHCCCCCCCCC
33.5324732914
647 (in isoform 4)Phosphorylation-54.2928796482
649 (in isoform 7)Phosphorylation-68.6124719451
654PhosphorylationDRKGGFFSSFMKKRN
CCCCCCHHHHHHHCC
22.0225159151
655PhosphorylationRKGGFFSSFMKKRNA
CCCCCHHHHHHHCCC
24.9728355574
655 (in isoform 10)Phosphorylation-24.9724719451
659AcetylationFFSSFMKKRNAPTPP
CHHHHHHHCCCCCCC
38.817678533
662 (in isoform 7)Phosphorylation-17.2428796482
664PhosphorylationMKKRNAPTPPKRSSS
HHHCCCCCCCCCCHH
50.2221815630
667"N6,N6-dimethyllysine"RNAPTPPKRSSSFRE
CCCCCCCCCCHHHHH
67.14-
667MethylationRNAPTPPKRSSSFRE
CCCCCCCCCCHHHHH
67.14-
668 (in isoform 10)Phosphorylation-47.7728796482
669PhosphorylationAPTPPKRSSSFREME
CCCCCCCCHHHHHHC
36.1423403867
670PhosphorylationPTPPKRSSSFREMEN
CCCCCCCHHHHHHCC
37.2123403867
670UbiquitinationPTPPKRSSSFREMEN
CCCCCCCHHHHHHCC
37.2129967540
670 (in isoform 5)Phosphorylation-37.2124719451
671PhosphorylationTPPKRSSSFREMENQ
CCCCCCHHHHHHCCC
29.5725159151
681PhosphorylationEMENQPHKKYELTGN
HHCCCCCCEEECCCC
64.8333259812
682 (in isoform 2)Phosphorylation-40.71-
683PhosphorylationENQPHKKYELTGNFS
CCCCCCEEECCCCCC
22.4522817900
683 (in isoform 5)Phosphorylation-22.4528796482
685UbiquitinationQPHKKYELTGNFSSV
CCCCEEECCCCCCCC
7.2529967540
691UbiquitinationELTGNFSSVASLQHA
ECCCCCCCCEEEEEC
19.9829967540
696PhosphorylationFSSVASLQHADGFSF
CCCCEEEEECCCCCC
27.5133259812
702PhosphorylationLQHADGFSFTPAQQE
EEECCCCCCCHHHHH
33.4733259812
706UbiquitinationDGFSFTPAQQEANLV
CCCCCCHHHHHCCCC
22.1929967540
717PhosphorylationANLVPPKCYGGSFAQ
CCCCCCCCCCCCHHH
4.7533259812
718PhosphorylationNLVPPKCYGGSFAQR
CCCCCCCCCCCHHHC
30.5527273156
738PhosphorylationDGGGGGGSGTAGGGW
CCCCCCCCCCCCCCC
35.9230576142
745 (in isoform 2)Phosphorylation-9.17-
747 (in isoform 2)Phosphorylation-18.24-
748 (in isoform 2)Phosphorylation-2.58-
749PhosphorylationGGGWSGITGFFTPRL
CCCCCCCCCCCCHHH
31.3130576142
752 (in isoform 2)Phosphorylation-11.00-
753PhosphorylationSGITGFFTPRLIKKT
CCCCCCCCHHHHHHH
12.7718691976
753 (in isoform 2)Phosphorylation-12.77-
762PhosphorylationRLIKKTLGLRAGKPT
HHHHHHHCCCCCCCC
20.5332645325
768PhosphorylationLGLRAGKPTASDDTS
HCCCCCCCCCCCCCC
32.0732645325
771PhosphorylationRAGKPTASDDTSKPF
CCCCCCCCCCCCCCC
38.2028555341
776AcetylationTASDDTSKPFPRSNS
CCCCCCCCCCCCCCC
53.41-
779 (in isoform 2)Phosphorylation-47.52-
781PhosphorylationTSKPFPRSNSTSSMS
CCCCCCCCCCCCCCC
35.0617525332
781 (in isoform 2)Phosphorylation-35.06-
782 (in isoform 2)Phosphorylation-51.06-
783PhosphorylationKPFPRSNSTSSMSSG
CCCCCCCCCCCCCCC
30.8023401153
784PhosphorylationPFPRSNSTSSMSSGL
CCCCCCCCCCCCCCC
29.1329255136
784 (in isoform 2)Phosphorylation-29.13-
785PhosphorylationFPRSNSTSSMSSGLP
CCCCCCCCCCCCCCC
24.7029255136
786PhosphorylationPRSNSTSSMSSGLPE
CCCCCCCCCCCCCCH
23.8329255136
788PhosphorylationSNSTSSMSSGLPEQD
CCCCCCCCCCCCHHH
24.1728450419
788UbiquitinationSNSTSSMSSGLPEQD
CCCCCCCCCCCCHHH
24.1729967540
789PhosphorylationNSTSSMSSGLPEQDR
CCCCCCCCCCCHHHH
35.3928450419
794UbiquitinationMSSGLPEQDRMAMTL
CCCCCCHHHHHHHHC
41.4929967540
797PhosphorylationGLPEQDRMAMTLPRN
CCCHHHHHHHHCCCC
3.9332142685
799PhosphorylationPEQDRMAMTLPRNCQ
CHHHHHHHHCCCCHH
2.6433259812
800PhosphorylationEQDRMAMTLPRNCQR
HHHHHHHHCCCCHHC
24.8728555341
805PhosphorylationAMTLPRNCQRSKLQL
HHHCCCCHHCCHHEE
3.6233259812
808PhosphorylationLPRNCQRSKLQLERT
CCCCHHCCHHEEEEE
16.3130622161
809UbiquitinationPRNCQRSKLQLERTV
CCCHHCCHHEEEEEE
42.3029967540
812PhosphorylationCQRSKLQLERTVSTS
HHCCHHEEEEEECCC
7.5332142685
815PhosphorylationSKLQLERTVSTSSQP
CHHEEEEEECCCCCC
14.9421955146
817PhosphorylationLQLERTVSTSSQPEE
HEEEEEECCCCCCHH
23.2025159151
818PhosphorylationQLERTVSTSSQPEEN
EEEEEECCCCCCHHH
28.2325159151
818UbiquitinationQLERTVSTSSQPEEN
EEEEEECCCCCCHHH
28.2329967540
819PhosphorylationLERTVSTSSQPEENV
EEEEECCCCCCHHHH
21.3325159151
820PhosphorylationERTVSTSSQPEENVD
EEEECCCCCCHHHHH
50.2525159151
828 (in isoform 2)Phosphorylation-30.89-
833PhosphorylationVDRANDMLPKKSEES
HHHHHHCCCCCCHHC
6.6632142685
833UbiquitinationVDRANDMLPKKSEES
HHHHHHCCCCCCHHC
6.6629967540
839UbiquitinationMLPKKSEESAAPSRE
CCCCCCHHCCCCCCC
53.4129967540
854UbiquitinationRPKAKLLPRGATALP
CCCCCCCCCCCCCCC
42.9929967540
858PhosphorylationKLLPRGATALPLRTP
CCCCCCCCCCCCCCC
31.3929514088
864PhosphorylationATALPLRTPSGDLAI
CCCCCCCCCCCCEEE
29.5017192257
866PhosphorylationALPLRTPSGDLAITE
CCCCCCCCCCEEEEE
44.3121815630
872PhosphorylationPSGDLAITEKDPPGV
CCCCEEEEECCCCCC
31.2320068231
879 (in isoform 2)Phosphorylation-7.41-
900 (in isoform 2)Phosphorylation-9.80-
902 (in isoform 2)Phosphorylation-17.65-
915PhosphorylationGEQPGWPSPAKAAPV
CCCCCCCCCCCCCCC
30.8625159151
921PhosphorylationPSPAKAAPVLPTTHN
CCCCCCCCCCCCCCC
32.7932142685
925PhosphorylationKAAPVLPTTHNHKVP
CCCCCCCCCCCCCCC
36.2023312004
926PhosphorylationAAPVLPTTHNHKVPV
CCCCCCCCCCCCCCE
20.8123312004
930PhosphorylationLPTTHNHKVPVLISP
CCCCCCCCCCEEECC
54.2632142685
932 (in isoform 2)Phosphorylation-21.72-
936PhosphorylationHKVPVLISPTLKHTP
CCCCEEECCCCCCCC
13.9919664994
936UbiquitinationHKVPVLISPTLKHTP
CCCCEEECCCCCCCC
13.9929967540
938PhosphorylationVPVLISPTLKHTPAD
CCEEECCCCCCCCCC
41.4730266825
942UbiquitinationISPTLKHTPADVQLI
ECCCCCCCCCCEEEE
20.7029967540
951PhosphorylationADVQLIGTDSQGNKF
CCEEEEEECCCCCEE
26.0332142685
953PhosphorylationVQLIGTDSQGNKFKL
EEEEEECCCCCEEEE
39.5625627689
957MethylationGTDSQGNKFKLLSEH
EECCCCCEEEEEEEC
51.18-
957UbiquitinationGTDSQGNKFKLLSEH
EECCCCCEEEEEEEC
51.1829967540
959MethylationDSQGNKFKLLSEHQV
CCCCCEEEEEEECCC
50.56-
962PhosphorylationGNKFKLLSEHQVTSS
CCEEEEEEECCCCCC
43.3927174698
967PhosphorylationLLSEHQVTSSGDKDR
EEEECCCCCCCCCCC
15.5927174698
968PhosphorylationLSEHQVTSSGDKDRP
EEECCCCCCCCCCCC
33.2018691976
969PhosphorylationSEHQVTSSGDKDRPR
EECCCCCCCCCCCCC
41.4625159151
981AcetylationRPRRVKPKCAPPPPP
CCCCCCCCCCCCCCC
36.9930586989
997PhosphorylationMRLLQHPSICSDPTE
HHHHCCCCCCCCCCC
33.8225159151
1000PhosphorylationLQHPSICSDPTEEPT
HCCCCCCCCCCCCCC
44.9825159151
1003PhosphorylationPSICSDPTEEPTALT
CCCCCCCCCCCCCCC
58.9523312004
1014 (in isoform 2)Phosphorylation-32.74-
1018 (in isoform 2)Phosphorylation-31.52-
1023AcetylationSETQEGGKKAALGAV
CCCCCCCCEEEEECC
50.5326051181
1033PhosphorylationALGAVPISGKAGRPV
EEECCCCCCCCCCCC
28.3332142685
1039PhosphorylationISGKAGRPVMPPPQV
CCCCCCCCCCCCCCC
26.3332142685
1050PhosphorylationPPQVPLPTSSISPAK
CCCCCCCCCCCCHHH
42.6725159151
1051PhosphorylationPQVPLPTSSISPAKM
CCCCCCCCCCCHHHC
24.5930576142
1052PhosphorylationQVPLPTSSISPAKMA
CCCCCCCCCCHHHCC
29.5730576142
1054PhosphorylationPLPTSSISPAKMANG
CCCCCCCCHHHCCCC
22.2825159151
1057MethylationTSSISPAKMANGTAG
CCCCCHHHCCCCCCC
41.76-
1066MethylationANGTAGTKVALRKTK
CCCCCCCHHHHHHHH
25.29-
1072PhosphorylationTKVALRKTKQAAEKI
CHHHHHHHHHHHHHC
23.1929396449
1107PhosphorylationLTEPVPNSQLVDTGH
HCCCCCCHHHCCCHH
20.87-
1112PhosphorylationPNSQLVDTGHQLLDY
CCHHHCCCHHHHHHH
29.14-

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
116YPhosphorylationKinaseLYNP07948
GPS
116YPhosphorylationKinaseHCKP08631
GPS
116YPhosphorylationKinaseFYNP06241
GPS
139YPhosphorylationKinasePDGFRBP09619
PSP
161YPhosphorylationKinasePDGFRBP09619
PSP
161YPhosphorylationKinaseLYNP07948
GPS
161YPhosphorylationKinaseHCKP08631
GPS
161YPhosphorylationKinaseFYNP06241
GPS
174YPhosphorylationKinaseHCKP08631
GPS
174YPhosphorylationKinaseLYNP07948
GPS
174YPhosphorylationKinaseFYNP06241
GPS
185YPhosphorylationKinaseFYNP06241
GPS
185YPhosphorylationKinaseHCKP08631
GPS
185YPhosphorylationKinaseLYNP07948
GPS
218YPhosphorylationKinaseFYNP06241
GPS
218YPhosphorylationKinaseHCKP08631
GPS
218YPhosphorylationKinaseLYNP07948
GPS
231YPhosphorylationKinaseFYNP06241
GPS
231YPhosphorylationKinaseHCKP08631
GPS
231YPhosphorylationKinaseLYNP07948
GPS
261YPhosphorylationKinaseLYNP07948
GPS
261YPhosphorylationKinaseABL2P42684
GPS
261YPhosphorylationKinaseHCKP08631
GPS
261YPhosphorylationKinaseFYNP06241
GPS
261YPhosphorylationKinaseABLP00519
PSP
272YPhosphorylationKinasePDGFRBP09619
PSP
439YPhosphorylationKinaseABL2P42684
GPS
439YPhosphorylationKinaseSRC-TYPE TYR-KINASES-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ABL2_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 ABL2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ABL1_HUMANABL1physical
12569093
CATA_HUMANCATphysical
12777400
SRBS2_HUMANSORBS2physical
9211900
PSA7_HUMANPSMA7physical
16678104
ERBB4_HUMANERBB4physical
16273093
FBX38_HUMANFBXO38physical
21988832
HCK_HUMANHCKphysical
21988832
TPD53_HUMANTPD52L1physical
21988832
NMES1_HUMANC15orf48physical
21988832
MS18B_HUMANOIP5physical
21988832
GPX1_HUMANGPX1physical
12893824
CIP4_HUMANTRIP10physical
18330356
ABL2_HUMANABL2physical
15735735
CRK_HUMANCRKphysical
8194526
GRB2_HUMANGRB2physical
8194526
RIN1_HUMANRIN1physical
15886098
ABL2_HUMANABL2physical
15886098
CRK_CHICKCRKphysical
15886098
CRK_HUMANCRKphysical
15886098
RASH_HUMANHRASphysical
15886098
MDM2_HUMANMDM2physical
25624478
P55G_HUMANPIK3R3physical
25814554

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 ABL2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-817; SER-820 ANDSER-936, 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 SER-96; SER-620; SER-631;TYR-683; TYR-718; SER-781; THR-784; THR-815; SER-817; SER-819; SER-820AND SER-936, 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-620; SER-631; SER-783;SER-817; THR-818; SER-819; SER-820; SER-936 AND THR-938, AND MASSSPECTROMETRY.
"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-620; SER-631; SER-633;SER-655; SER-817; SER-820; SER-915 AND SER-936, AND MASS SPECTROMETRY.
"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 TYR-116; SER-203; TYR-231;SER-275; SER-602; SER-620; SER-631; SER-671; TYR-718; SER-820;THR-864; SER-915 AND SER-936, AND MASS SPECTROMETRY.
"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 SER-71, AND MASSSPECTROMETRY.
"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 SER-203, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817 AND SER-820, ANDMASS SPECTROMETRY.
"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-631; SER-783; SER-817AND SER-936, AND MASS SPECTROMETRY.
"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-203 AND SER-631, ANDMASS SPECTROMETRY.
"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-310; TYR-439; THR-440AND TYR-515, AND MASS SPECTROMETRY.
"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-439, AND MASSSPECTROMETRY.
"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.
"Ubiquitination and degradation of the Arg tyrosine kinase isregulated by oxidative stress.";
Cao C., Li Y., Leng Y., Li P., Ma Q., Kufe D.;
Oncogene 24:2433-2440(2005).
Cited for: FUNCTION, PHOSPHORYLATION AT TYR-261, AND UBIQUITINATION.
"Two distinct phosphorylation pathways have additive effects on Ablfamily kinase activation.";
Tanis K.Q., Veach D., Duewel H.S., Bornmann W.G., Koleske A.J.;
Mol. Cell. Biol. 23:3884-3896(2003).
Cited for: AUTOPHOSPHORYLATION AT TYR-272; TYR-439; TYR-568 AND TYR-683, ANDENZYME REGULATION.

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