KARG_DROME - dbPTM
KARG_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KARG_DROME
UniProt AC P48610
Protein Name Arginine kinase
Gene Name Argk
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 356
Subcellular Localization
Protein Description
Protein Sequence MVDAAVLAKLEEGYAKLAASDSKSLLKKYLTKEVFDNLKNKVTPTFKSTLLDVIQSGLENHDSGVGIYAPDAEAYTVFADLFDPIIEDYHGGFKKTDKHPASNFGDVSTFGNVDPTNEYVISTRVRCGRSMQGYPFNPCLTEAQYKEMESKVSSTLSGLEGELKGKFYPLTGMEKAVQQQLIDDHFLFKEGDRFLQAANACRFWPSGRGIYHNDAKTFLVWCNEEDHLRIISMQQGGDLGQIYKRLVTAVNEIEKRVPFSHDDRLGFLTFCPTNLGTTIRASVHIKVPKLASNKAKLEEVAAKYNLQVRGTRGEHTEAEGGVYDISNKRRMGLTEFEAVKEMYDGITELIKLEKSL
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
150PhosphorylationAQYKEMESKVSSTLS
HHHHHHHHHHHHHHH
36.7327794539
153PhosphorylationKEMESKVSSTLSGLE
HHHHHHHHHHHHHHH
22.7227794539
154PhosphorylationEMESKVSSTLSGLEG
HHHHHHHHHHHHHHC
36.0327794539
157PhosphorylationSKVSSTLSGLEGELK
HHHHHHHHHHHCHHC
41.2327794539

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 KARG_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KARG_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 KARG_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYSP1_DROMEPrmphysical
22036573
MYSP2_DROMEPrmphysical
22036573
MYSA_DROMEMhcphysical
22036573
TPM2_DROMETm2physical
22036573
GPDA_DROMEGpdhphysical
22036573
TNNT_DROMEupphysical
22036573
MLC1_DROMEMlc1physical
22036573
ACTN_DROMEActnphysical
22036573
MLR_DROMEMlc2physical
22036573
APLP_DROMERfabgphysical
22036573
TNNI_DROMEwupAphysical
22036573
LSP2_DROMELsp2physical
22036573
VIT3_DROMEYp3physical
22036573
TNNC1_DROMETpnC41Cphysical
22036573
PGK_DROMEPgkphysical
22036573
PYG_DROMEGlyPphysical
22036573
OB56D_DROMEObp56dphysical
22036573
VIT2_DROMEYp2physical
22036573
CYC2_DROMECyt-c-pphysical
22036573
ENO_DROMEEnophysical
22036573
NPLP2_DROMENplp2physical
22036573
VIT1_DROMEYp1physical
22036573
ATP5J_DROMEATPsyn-Cf6physical
22036573
DHE3_DROMEGdhphysical
22036573
G3P2_DROMEGapdh2physical
22036573
IDH3A_DROMEl(1)G0156physical
22036573
RS27A_DROMERpS27Aphysical
24292889
CISY_DROMEkdnphysical
22036573

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KARG_DROME

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Related Literatures of Post-Translational Modification

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