KLC_DROME - dbPTM
KLC_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KLC_DROME
UniProt AC P46824
Protein Name Kinesin light chain
Gene Name Klc
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 508
Subcellular Localization Cytoplasm, cytoskeleton .
Protein Description Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity..
Protein Sequence MTQMSQDEIITNTKTVLQGLEALRVEHVSIMNGIAEVQKDNEKSDMLRKNIENIELGLSEAQVMMALTSHLQNIEAEKHKLKTQVRRLHQENAWLRDELANTQQKFQASEQLVAQLEEEKKHLEFMASVKKYDENQEQDDACDKSRTDPVVELFPDEENEDRHNMSPTPPSQFANQTSGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLERTSGHDHPDVATMLNILALVYRDQNKYKEAANLLNDALSIRGKTLGENHPAVAATLNNLAVLYGKRGKYKDAEPLCKRALEIREKVLGKDHPDVAKQLNNLALLCQNQGKYDEVEKYYQRALDIYESKLGPDDPNVAKTKNNLAGCYLKQGRYTEAEILYKQVLTRAHEREFGAIDSKNKPIWQVAEEREEHKFDNRENTPYGEYGGWHKAAKVDSPTVTTTLKNLGALYRRQGMFEAAETLEDCAMRSKKEAYDLAKQTKLSQLLTSNEKRRSKAIKEDLDFSEEKNAKP
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
128PhosphorylationKHLEFMASVKKYDEN
HHHHHHHHHHCCCCC		23.7619429919
145PhosphorylationQDDACDKSRTDPVVE
CCCCCCCCCCCCCCH		27.4519429919
147PhosphorylationDACDKSRTDPVVELF
CCCCCCCCCCCCHHC		52.3119429919
166PhosphorylationNEDRHNMSPTPPSQF
CCCCCCCCCCCHHHH		30.8219429919
168PhosphorylationDRHNMSPTPPSQFAN
CCCCCCCCCHHHHCC		40.2919429919
171PhosphorylationNMSPTPPSQFANQTS
CCCCCCHHHHCCCCC		38.8519429919
366AcetylationNLAGCYLKQGRYTEA
CCCCHHHHCCCCCHH		25.0021791702
433PhosphorylationHKAAKVDSPTVTTTL
CCCCCCCCCCHHHHH		26.0019429919
435PhosphorylationAAKVDSPTVTTTLKN
CCCCCCCCHHHHHHH		34.1422668510
477PhosphorylationAYDLAKQTKLSQLLT
HHHHHHHHHHHHHHH		32.9918327897
480PhosphorylationLAKQTKLSQLLTSNE
HHHHHHHHHHHHCCH		21.9719429919
484PhosphorylationTKLSQLLTSNEKRRS
HHHHHHHHCCHHHHH		37.7929892262
485PhosphorylationKLSQLLTSNEKRRSK
HHHHHHHCCHHHHHH		42.8522817900
491PhosphorylationTSNEKRRSKAIKEDL
HCCHHHHHHHHHHHC		30.3922817900
501PhosphorylationIKEDLDFSEEKNAKP
HHHHCCCCHHHCCCC		44.5022817900
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 KLC_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KLC_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 KLC_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KLC_DROMEKlcphysical
14605208
KINH_DROMEKhcphysical
14605208
AKIRN_DROMEakirinphysical
14605208
ATTC_DROMEAttCphysical
15575970
SLX1_DROMEslx1physical
15575970
CSN3_DROMECSN3physical
15575970
RG68F_DROMERhoGAP68Fphysical
15575970
DS_DROMEdsphysical
15575970
ARNT_DROMEtgophysical
15575970
MSIR6_DROMERbp6physical
15575970
GUS_DROMEgusphysical
15575970
PGPLA_DROMEPGRP-LAphysical
15575970
YPL1_DROMECG15309physical
15575970
TUD_DROMEtudphysical
15575970
ATTB_DROMEAttBphysical
15575970
PSA1_DROMEProsalpha6physical
22036573
PSA2_DROMEProsalpha2physical
22036573
PSA5_DROMEProsalpha5physical
22036573
PSB4_DROMEProsbeta7physical
22036573
PSB3_DROMEProsbeta3physical
22036573
PNCB_DROMECG3714physical
22036573
A4_DROMEApplgenetic
11709151
MAEL_DROMEmaelgenetic
24531791
KINH_DROMEKhcphysical
20630947
KINH_DROMEKhcphysical
27802167
JIP1_DROMEAplip1physical
11912189
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KLC_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 THR-168; THR-477; SER-480AND SER-485, AND MASS SPECTROMETRY.

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