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 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
35	N-linked_Glycosylation	IIANDQGNRTTPSYV EEECCCCCCCCCCEE	32.28	17893096
37	Phosphorylation	ANDQGNRTTPSYVAF ECCCCCCCCCCEEEE	47.24	23607784
38	Phosphorylation	NDQGNRTTPSYVAFT CCCCCCCCCCEEEEE	13.65	22668510
40	Phosphorylation	QGNRTTPSYVAFTDT CCCCCCCCEEEEECH	30.10	23607784
41	Phosphorylation	GNRTTPSYVAFTDTE CCCCCCCEEEEECHH	9.30	23607784
85	Phosphorylation	FDDAAVQSDMKHWPF CCHHHHHCCCCCCCE	32.83	21082442
88	Acetylation	AAVQSDMKHWPFEVV HHHHCCCCCCCEEEE	47.73	21791702
96	Phosphorylation	HWPFEVVSADGKPKI CCCEEEECCCCCEEE	26.31	21082442
108	Acetylation	PKIEVTYKDEKKTFF EEEEEEEECCCCCCC	50.47	21791702
111	Acetylation	EVTYKDEKKTFFPEE EEEEECCCCCCCCHH	68.21	21791702
153	Phosphorylation	VPAYFNDSQRQATKD EECCCCHHHCCHHCC	28.50	21082442
246	Acetylation	THFVQEFKRKHKKDL HHHHHHHHHHHHCCC	60.84	21791702
319	Acetylation	STMDPVEKALRDAKL HCCCHHHHHHHHCCC	53.61	21791702
329	Phosphorylation	RDAKLDKSVIHDIVL HHCCCCHHHHCEEEE	26.43	19429919
362	Phosphorylation	NGKELNKSINPDEAV CCHHHCCCCCHHHHH	26.90	19429919
511	Phosphorylation	TNDKGRLSKEDIERM ECCCCCCCHHHHHHH	32.41	22668510
524	Acetylation	RMVNEAEKYRNEDEK HHHHHHHHHCCCCHH	57.46	21791702
559	Acetylation	TLDEDNLKTKISDSD EECCCCCCCCCCCCC	54.77	21791702
589	Acetylation	DANQLADKEEYEHRQ CHHHCCCHHHHHHHH	47.00	21791702
597	Acetylation	EEYEHRQKELEGVCN HHHHHHHHHHHHCHH	65.31	21791702

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of HSP7D_DROME !!

Functions of PTM Sites

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.

Oops, there are no SNP-PTM records of HSP7D_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PSA2_DROME	Prosalpha2	physical	14605208
CALR_DROME	Crc	physical	14605208
GAP1_DROME	RasGAP1	genetic	9178011
OSGEP_DROME	CG4933	physical	22036573
RS27A_DROME	RpS27A	physical	24292889
DNJC5_DROME	Csp	genetic	11395008
HLES_DROME	H	genetic	10569241

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"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.
PubMed: 17893096