KRAF1_DROME - dbPTM
KRAF1_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KRAF1_DROME
UniProt AC P11346
Protein Name Raf homolog serine/threonine-protein kinase Raf {ECO:0000303|PubMed:3135183}
Gene Name Raf {ECO:0000303|PubMed:3135183, ECO:0000312|FlyBase:FBgn0003079}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 739
Subcellular Localization
Protein Description Serine/threonine kinase required in the early embryo for the formation of terminal structure. [PubMed: 3135183]
Protein Sequence MSSESSTEGDSDLYDPLAEELHNVQLVKHVTRENIDALNAKFANLQEPPAMYLIEYQELTSKLHELEAKEQELMERLNSQDQQEDSSLVERFKEQPHYQNQTQILQQQRQLARVHHGNDLTDSLGSQPGSQCGTLTRQPKILLRAHLPNQQRTSVEVISGVRLCDALMKALKLRQLTPDMCEVSTTHSGRHIIPWHTDIGTLHVEEIFVRLLDKFPIRTHIKHQIIRKTFFSLVFCEGCRRLLFTGFYCSQCNFRFHQRCANRVPMLCQPFPMDSYYQLLLAENPDNGVGFPGRGTAVRFNMSSRSRSRRCSSSGSSSSSKPPSSSSGNHRQGRPPRISQDDRSNSAPNVCINNIRSVTSEVQRSLIMQARPPLPHPCTDHSNSTQASPTSTLKHNRPRARSADESNKNLLLRDAKSSEENWNILAEEILIGPRIGSGSFGTVYRAHWHGPVAVKTLNVKTPSPAQLQAFKNEVAMLKKTRHCNILLFMGCVSKPSLAIVTQWCEGSSLYKHVHVSETKFKLNTLIDIGRQVAQGMDYLHAKNIIHRDLKSNNIFLHEDLSVKIGDFGLATAKTRWSGEKQANQPTGSILWMAPEVIRMQELNPYSFQSDVYAFGIVMYELLAECLPYGHISNKDQILFMVGRGLLRPDMSQVRSDAPQALKRLAEDCIKYTPKDRPLFRPLLNMLENMLRTLPKIHRSASEPNLTQSQLQNDEFLYLPSPKTPVNFNNFQFFGSAGNI
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
134PhosphorylationQPGSQCGTLTRQPKI
CCCCCCCCCCCCCEE		40.2221082442
303PhosphorylationTAVRFNMSSRSRSRR
CEEEEECCCCCCCCC		2.9425749252
344PhosphorylationRISQDDRSNSAPNVC
CCCCCCCCCCCCCCC		20.8921082442
346PhosphorylationSQDDRSNSAPNVCIN
CCCCCCCCCCCCCCC		24.5725749252
388PhosphorylationHSNSTQASPTSTLKH
CCCCCCCCCCHHHCC		42.9821082442
402PhosphorylationHNRPRARSADESNKN
CCCCCCCCCCHHHCC		22.0319429919
461PhosphorylationVKTLNVKTPSPAQLQ
EEEECCCCCCHHHHH		48.5025749252
463PhosphorylationTLNVKTPSPAQLQAF
EECCCCCCHHHHHHH		70.2825749252
701PhosphorylationPKIHRSASEPNLTQS
HHHHHCCCCCCCCHH		25.6027794539
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 KRAF1_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KRAF1_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 KRAF1_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DSOR1_DROMEDsor1genetic
7958887
DSOR1_DROMEDsor1genetic
8013459
DSOR1_DROMEDsor1genetic
8381718
DSOR1_DROMEDsor1genetic
9136016
HEP_DROMEhepgenetic
16150723
DOD_DROMEdodgenetic
11389437
STAR_DROMESgenetic
10068471
STAR_DROMESgenetic
11063697
POK_DROMEaopgenetic
8722784
POK_DROMEaopgenetic
11063697
AFF4_DROMElilligenetic
11171403
EYA_DROMEeyagenetic
10655223
WNTG_DROMEwggenetic
10860999
SOS_DROMESosgenetic
11063697
SRC42_DROMESrc42Agenetic
8013459
SRC42_DROMESrc42Agenetic
9927462
SRC42_DROMESrc42Agenetic
10075855
SRC42_DROMESrc42Agenetic
10906455
SRC42_DROMESrc42Agenetic
11063697
JRA_DROMEJragenetic
8670899
MAM_DROMEmamgenetic
8722784
SPS1_DROMESelDgenetic
11784000
PHYL_DROMEphylgenetic
7859287
PHYL_DROMEphylgenetic
8770593
EGFR_DROMEEgfrgenetic
11063697
RAC1_DROMERac1genetic
11076763
RAS3_DROMERgenetic
24899161
HSP83_DROMEHsp83genetic
21576228
SPY_DROMEstygenetic
10457022
BRM_DROMEbrmgenetic
20416294
TAF4_DROMETaf4genetic
10655223
TAF6_DROMETaf6genetic
8722784
RAS1_DROMERas85Dgenetic
11063697
1433E_DROME14-3-3epsilongenetic
11063697
HH_DROMEhhgenetic
8722784
PNT1_DROMEpntgenetic
8033205
PNT2_DROMEpntgenetic
8033205
PNT1_DROMEpntgenetic
11063697
PNT2_DROMEpntgenetic
11063697
SPEN_DROMEspengenetic
8770593
SPEN_DROMEspengenetic
11063697
LAP4_DROMEscribgenetic
16150723
PP2A_DROMEmtsgenetic
8595878
PP2A_DROMEmtsgenetic
8722784
ERKA_DROMErlgenetic
8722784
ERKA_DROMErlgenetic
11063697
ERKA_DROMErlgenetic
24899161
ERKA_DROMErlgenetic
8124723
ERKA_DROMErlgenetic
10511556
PPP6_DROMEPpVphysical
22028469
RL17_DROMERpL17physical
22028469
DSOR1_DROMEDsor1physical
22028469
ADT_DROMEsesBphysical
22028469
CH60_DROMEHsp60physical
22028469
COPB_DROMEbetaCOPphysical
22028469
ERKA_DROMErlphysical
22028469
RL27A_DROMERpL27Aphysical
22028469
IF4A_DROMEeIF-4aphysical
22028469
GBLP_DROMERack1physical
22028469
TCP4_DROMESsb-c31aphysical
22028469
RS27A_DROMERpS27Aphysical
22028469
NFS1_DROMECG12264physical
22028469
RS26_DROMERpS26physical
22028469
EF2_DROMEEF2physical
22028469
ACT2_DROMEAct42Aphysical
22028469
1433Z_DROME14-3-3zetaphysical
22028469
CATL_DROMECp1physical
22028469
RS18_DROMERpS18physical
22028469
TBB3_DROMEbetaTub60Dphysical
22028469
CDC37_DROMECdc37physical
22028469
HSP83_DROMEHsp83physical
22028469
RL28_DROMERpL28physical
22028469
RAS2_DROMERas64Bphysical
22500634
ACADM_DROMECG12262physical
22028469
U195A_DROMECG7949physical
22028469
RAS1_DROMERas85Dphysical
22500634
RL3_DROMERpL3physical
22028469
DDB1_DROMEpicphysical
22028469
1433E_DROME14-3-3epsilonphysical
22028469
DYLT_DROMEDlc90Fphysical
22028469
KPYK_DROMEPyKphysical
22028469
TCPA_DROMET-cp1physical
22028469
GGYF1_DROMECG11148physical
22028469
RS15A_DROMERpS15Aaphysical
22028469
HSP71_DROMEHsp70Abphysical
22028469
HSP70_DROMEHsp70Abphysical
22028469
RB87F_DROMEHrb87Fphysical
22028469
CSN8_DROMECSN8physical
22028469
ATC1_DROMECa-P60Aphysical
22028469
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KRAF1_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, AND MASSSPECTROMETRY.

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