ABL_DROME - dbPTM
ABL_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABL_DROME
UniProt AC P00522
Protein Name Tyrosine-protein kinase Abl
Gene Name Abl
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1620
Subcellular Localization Cytoplasm.
Protein Description Arm and Abl proteins function cooperatively at adherens junctions in both the CNS and epidermis; critical for embryonic epithelial morphogenesis regulating cell shape changes and cell migration. Plays a critical role in transducing embryonic midline repulsive cues; may regulate cytoskeletal dynamics underlying a growth cone's response to midline cues. The ability of pCC/MP2 axons to correctly interpret midline repulsive cues and stay on the ipsilateral side is dependent on the strength of both Slit/robo and Abl-dependent signaling pathways..
Protein Sequence MGAQQGKDRGAHSGGGGSGAPVSCIGLSSSPVASVSPHCISSSSGVSSAPLGGGSTLRGSRIKSSSSGVASGSGSGGGGGGSGSGLSQRSGGHKDARCNPTVGLNIFTEHNEALLQSRPLPHIPAGSTAASLLADAAELQQHQQDSGGLGLQGSSLGGGHSSTTSVFESAHRWTSKENLLAPGPEEDDPQLFVALYDFQAGGENQLSLKKGEQVRILSYNKSGEWCEAHSDSGNVGWVPSNYVTPLNSLEKHSWYHGPISRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRISEDPDGKVFVTQEAKFNTLAELVHHHSVPHEGHGLITPLLYPAPKQNKPTVFPLSPEPDEWEICRTDIMMKHKLGGGQYGEVYEAVWKRYGNTVAVKTLKEDTMALKDFLEEAAIMKEMKHPNLVQLIGVCTREPPFYIITEFMSHGNLLDFLRSAGRETLDAVALLYMATQIASGMSYLESRNYIHRDLAARNCLVGDNKLVKVADFGLARLMRDDTYTAHAGAKFPIKWTAPEGLAYNKFSTKSDVWAFGVLLWEIATYGMSPYPAIDLTDVYHKLDKGYRMERPPGCPPEVYDLMRQCWQWDATDRPTFKSIHHALEHMFQESSITEAVEKQLNANATSASSSAPSTSGVATGGGATTTTAASGCASSSSATASLSLTPQMVKKGLPGGQALTPNAHHNDPHQQQASTPMSETGSTSTKLSTFSSQGKGNVQMRRTTNKQGKQAPAPPKRTSLLSSSRDSTYREEDPANARCNFIDDLSTNGLARDINSLTQRYDSETDPAADPDTDATGDSLEQSLSQVIAAPVTNKMQHSLHSGGGGGGIGPRSSQQHSSFKRPTGTPVMGNRGLETRQSKRSQLHSQAPGPGPPSTQPHHGNNGVVTSAHPITVGALDVMNVKQVVNRYGTLPKGARIGAYLDSLEDSSEAAPALPATAPSLPPANGHATPPAARLNPKASPIPPQQMIRSNSSGGVTMQNNAAASLNKLQRHRTTTEGTMMTFSSFRAGGSSSSPKRSASGVASGVQPALANLEFPPPPLDLPPPPEEFEGGPPPPPPAPESAVQAIQQHLHAQLPNNGNISNGNGTNNNDSSHNDVSNIAPSVEEASSRFGVSLRKREPSTDSCSSLGSPPEDLKEKLITEIKAAGKDTAPASHLANGSGIAVVDPVSLLVTELAESMNLPKPPPQQQQKLTNGNSTGSGFKAQLKKVEPKKMSAPMPKAEPANTIIDFKAHLRRVDKEKEPATPAPAPATVAVANNANCNTTGTLNRKEDGSKKFSQAMQKTEIKIDVTNSNVEADAGAAGEGDLGKRRSTGSINSLKKLWEQQPPAPDYATSTILQQQPSVVNGGGTPNAQLSPKYGMKSGAINTVGTLPAKLGNKQPPAAPPPPPPNCTTSNSSTTSISTSSRDCTSRQQASSTIKTSHSTQLFTDDEEQSHTEGLGSGGQGSADMTQSLYEQKPQIQQKPAVPHKPTKLTIYATPIAKLTEPASSASSTQISRESILELVGLLEGSLKHPVNAIAGSQWLQLSDKLNILHNSCVIFAENGAMPPHSKFQFRELVTRVEAQSQHLRSAGSKNVQDNERLVAEVGQSLRQISNALNR
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
521PhosphorylationARLMRDDTYTAHAGA
HHHHCCCCEECCCCC		27.3619429919
522PhosphorylationRLMRDDTYTAHAGAK
HHHCCCCEECCCCCC		14.6619429919
523PhosphorylationLMRDDTYTAHAGAKF
HHCCCCEECCCCCCC		17.6619429919
758PhosphorylationPAPPKRTSLLSSSRD
CCCCCCCCCCCCCCC		31.2019429919
795PhosphorylationGLARDINSLTQRYDS
CHHHHHHHHHHHCCC		32.8819429919
928PhosphorylationVKQVVNRYGTLPKGA
HHHHHHHHCCCCCCC		14.8425749252
930PhosphorylationQVVNRYGTLPKGARI
HHHHHHCCCCCCCCH		30.8422817900
990PhosphorylationPPQQMIRSNSSGGVT
CHHHHHCCCCCCCCC		30.0921082442
992PhosphorylationQQMIRSNSSGGVTMQ
HHHHCCCCCCCCCCC		31.4421082442
993PhosphorylationQMIRSNSSGGVTMQN
HHHCCCCCCCCCCCC		43.7629892262
1025PhosphorylationGTMMTFSSFRAGGSS
CCEEEEECEECCCCC		17.9821082442
1283PhosphorylationANNANCNTTGTLNRK
ECCCCCCCCCCCCCC		28.8921082442
1284PhosphorylationNNANCNTTGTLNRKE
CCCCCCCCCCCCCCC		17.7421082442
1286PhosphorylationANCNTTGTLNRKEDG
CCCCCCCCCCCCCCC		20.8321082442
1332PhosphorylationGDLGKRRSTGSINSL
CCCCCCCCCCCHHHH		40.9519429919
1333PhosphorylationDLGKRRSTGSINSLK
CCCCCCCCCCHHHHH		32.8919429919
1335PhosphorylationGKRRSTGSINSLKKL
CCCCCCCCHHHHHHH		20.7719429919
1338PhosphorylationRSTGSINSLKKLWEQ
CCCCCHHHHHHHHHC		39.6419429919
1497PhosphorylationKPTKLTIYATPIAKL
CCCEEEEEECCCCHH		10.1319429919
1499PhosphorylationTKLTIYATPIAKLTE
CEEEEEECCCCHHCC		9.7719429919
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

Oops, there are no upstream regulatory protein records of ABL_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ABL_DROME !!
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 ABL_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NOTCH_DROMENgenetic
9581760
NOTCH_DROMENgenetic
12781136
EYA_DROMEeyagenetic
19217428
LAR_DROMELargenetic
12441051
DIA_DROMEdiagenetic
14676307
SLIT_DROMEsligenetic
10892742
SLIT_DROMEsligenetic
12973825
RHO1_DROMERho1genetic
17568577
ENA_DROMEenagenetic
2188361
ENA_DROMEenagenetic
10798396
ENA_DROMEenagenetic
11756472
ENA_DROMEenagenetic
12441051
ENA_DROMEenagenetic
14676307
PTP61_DROMEPtp61Fgenetic
19398577
PTP61_DROMEPtp61Fgenetic
24752400
FAXC_DROMEfaxgenetic
8647396
FAXC_DROMEfaxgenetic
10798396
NRT_DROMENrtgenetic
2502313
NRT_DROMENrtgenetic
10798396
NRT_DROMENrtgenetic
12783792
HEM_DROMEHemgenetic
21726548
AMAL_DROMEAmagenetic
12783792
PROS_DROMEprosgenetic
2502313
CLASP_DROMEchbgenetic
15207236
DSH_DROMEdshphysical
20837657
EYA_DROMEeyaphysical
19217428
CDK1_DROMEcdc2physical
15591787
LAR_DROMELarphysical
10069336
ENA_DROMEenaphysical
9418863
ENA_DROMEenaphysical
9693373
ENA_DROMEenaphysical
10069336
ENA_DROMEenaphysical
7535279
PTP69_DROMEPtp69Dphysical
10069336
DAB_DROMEDabphysical
28087633
ABL_DROMEAblphysical
15591787
ABL_DROMEAblphysical
7535279
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ABL_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells.";
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
Mol. Biosyst. 3:275-286(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1497, AND MASSSPECTROMETRY.

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