HSP7D_DROME - dbPTM
HSP7D_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HSP7D_DROME
UniProt AC P11147
Protein Name Heat shock 70 kDa protein cognate 4
Gene Name Hsc70-4
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 651
Subcellular Localization Cytoplasm, perinuclear region. Nucleus. Localized to a meshwork of cytoplasmic fibers around the nucleus. Translocates to the nucleus after thermal stress.
Protein Description
Protein Sequence MSKAPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTQTIFDAKRLIGRKFDDAAVQSDMKHWPFEVVSADGKPKIEVTYKDEKKTFFPEEISSMVLTKMKETAEAYLGKTVTNAVITVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKAVGERNVLIFDLGGGTFDVSILSIDDGIFEVKSTAGDTHLGGEDFDNRLVTHFVQEFKRKHKKDLTTNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGTDFYTSITRARFEELNADLFRSTMDPVEKALRDAKLDKSVIHDIVLVGGSTRIPKVQRLLQDLFNGKELNKSINPDEAVAYGAAVQAAILHGDKSQEVQDLLLLDVTPLSLGIETAGGVMSVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELSGIPPAPRGVPQIEVTFDIDANGILNVTALERSTNKENKITITNDKGRLSKEDIERMVNEAEKYRNEDEKQKETIAAKNGLESYCFNMKATLDEDNLKTKISDSDRTTILDKCNETIKWLDANQLADKEEYEHRQKELEGVCNPIITKLYQGAGFPPGGMPGGPGGMPGAAGAAGAAGAGGAGPTIEEVD
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
35N-linked_GlycosylationIIANDQGNRTTPSYV
EEECCCCCCCCCCEE
32.2817893096
37PhosphorylationANDQGNRTTPSYVAF
ECCCCCCCCCCEEEE
47.2423607784
38PhosphorylationNDQGNRTTPSYVAFT
CCCCCCCCCCEEEEE
13.6522668510
40PhosphorylationQGNRTTPSYVAFTDT
CCCCCCCCEEEEECH
30.1023607784
41PhosphorylationGNRTTPSYVAFTDTE
CCCCCCCEEEEECHH
9.3023607784
85PhosphorylationFDDAAVQSDMKHWPF
CCHHHHHCCCCCCCE
32.8321082442
88AcetylationAAVQSDMKHWPFEVV
HHHHCCCCCCCEEEE
47.7321791702
96PhosphorylationHWPFEVVSADGKPKI
CCCEEEECCCCCEEE
26.3121082442
108AcetylationPKIEVTYKDEKKTFF
EEEEEEEECCCCCCC
50.4721791702
111AcetylationEVTYKDEKKTFFPEE
EEEEECCCCCCCCHH
68.2121791702
153PhosphorylationVPAYFNDSQRQATKD
EECCCCHHHCCHHCC
28.5021082442
246AcetylationTHFVQEFKRKHKKDL
HHHHHHHHHHHHCCC
60.8421791702
319AcetylationSTMDPVEKALRDAKL
HCCCHHHHHHHHCCC
53.6121791702
329PhosphorylationRDAKLDKSVIHDIVL
HHCCCCHHHHCEEEE
26.4319429919
362PhosphorylationNGKELNKSINPDEAV
CCHHHCCCCCHHHHH
26.9019429919
511PhosphorylationTNDKGRLSKEDIERM
ECCCCCCCHHHHHHH
32.4122668510
524AcetylationRMVNEAEKYRNEDEK
HHHHHHHHHCCCCHH
57.4621791702
559AcetylationTLDEDNLKTKISDSD
EECCCCCCCCCCCCC
54.7721791702
589AcetylationDANQLADKEEYEHRQ
CHHHCCCHHHHHHHH
47.0021791702
597AcetylationEEYEHRQKELEGVCN
HHHHHHHHHHHHCHH
65.3121791702

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 HSP7D_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HSP7D_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 HSP7D_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PSA2_DROMEProsalpha2physical
14605208
CALR_DROMECrcphysical
14605208
GAP1_DROMERasGAP1genetic
9178011
OSGEP_DROMECG4933physical
22036573
RS27A_DROMERpS27Aphysical
24292889
DNJC5_DROMECspgenetic
11395008
HLES_DROMEHgenetic
10569241

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HSP7D_DROME

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Identification of N-glycosylated proteins from the central nervoussystem of Drosophila melanogaster.";
Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,Panin V.;
Glycobiology 17:1388-1403(2007).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-35, AND MASS SPECTROMETRY.

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