dbPTM

HSP83_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HSP83_DROME
UniProt AC	P02828
Protein Name	Heat shock protein 83
Gene Name	Hsp83
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	717
Subcellular Localization	Cytoplasm.
Protein Description	Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Together with Hop and piwi, mediates canalization, also known as developmental robustness, likely via epigenetic silencing of existing genetic variants and suppression of transposon-induced new genetic variation. Required for piRNA biogenesis by facilitating loading of piRNAs into PIWI proteins..
Protein Sequence	MPEEAETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELYIKLIPNKTAGTLTIIDTGIGMTKSDLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVADKVTVTSKNNDDEQYVWESSAGGSFTVRADNSEPLGRGTKIVLYIKEDQTDYLEESKIKEIVNKHSQFIGYPIKLLVEKEREKEVSDDEADDEKKEGDEKKEMETDEPKIEDVGEDEDADKKDKDAKKKKTIKEKYTEDEELNKTKPIWTRNPDDISQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRTPFDLFENQKKRNNIKLYVRRVFIMDNCEDLIPEYLNFMKGVVDSEDLPLNISREMLQQNKVLKVIRKNLVKKTMELIEELTEDKENYKKFYDQFSKNLKLGVHEDSNNRAKLADFLRFHTSASGDDFCSLADYVSRMKDNQKHVYFITGESKDQVSNSAFVERVKARGFEVVYMTEPIDEYVIQHLKEYKGKQLVSVTKEGLELPEDESEKKKREEDKAKFESLCKLMKSILDNKVEKVVVSNRLVDSPCCIVTSQFGWSANMERIMKAQALRDTATMGYMAGKKQLEINPDHPIVETLRQKADADKNDKAVKDLVILLFETSLLSSGFSLDSPQVHASRIYRMIKLGLGIDEDEPMTTDDAQSAGDAPSLVEDTEDASHMEEVD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
29	Acetylation	INTFYSNKEIFLREL HHHHCCCHHHHHHHH	46.37	21791702
62	Acetylation	PSKLDSGKELYIKLI HHHCCCCCEEEEEEC	48.80	21791702
67	Acetylation	SGKELYIKLIPNKTA CCCEEEEEECCCCCC	27.14	21791702
87	Phosphorylation	IDTGIGMTKSDLVNN EECCCCCCHHHHHHH	23.37	21082442
89	Phosphorylation	TGIGMTKSDLVNNLG CCCCCCHHHHHHHHH	27.32	21082442
190	Acetylation	TDYLEESKIKEIVNK CCHHHHHHHHHHHHH	62.16	21791702
197	Acetylation	KIKEIVNKHSQFIGY HHHHHHHHHHHHCCC	33.47	21791702
212	Acetylation	PIKLLVEKEREKEVS HHHHHHHHHHHHCCC	55.37	21791702
219	Phosphorylation	KEREKEVSDDEADDE HHHHHCCCCCCCCHH	40.20	21082442
238	Phosphorylation	DEKKEMETDEPKIED HHHHCCCCCCCCCCC	44.33	21082442
268	Acetylation	KKKTIKEKYTEDEEL HHHHHHHHCCCHHHH	53.09	21791702
277	Acetylation	TEDEELNKTKPIWTR CCHHHHHCCCCCCCC	71.23	21791702
278	Phosphorylation	EDEELNKTKPIWTRN CHHHHHCCCCCCCCC	40.76	22817900
294	Phosphorylation	DDISQEEYGEFYKSL CCCCHHHHHHHHHHH	22.62	18327897
332	Phosphorylation	LLFIPRRTPFDLFEN EEECCCCCCCCHHCC	29.59	19429919
384	Phosphorylation	EDLPLNISREMLQQN CCCCCCCCHHHHHCC	22.55	22817900
392	Acetylation	REMLQQNKVLKVIRK HHHHHCCCHHHHHHH	44.60	21791702
395	Acetylation	LQQNKVLKVIRKNLV HHCCCHHHHHHHHHH	38.31	21791702
405	Phosphorylation	RKNLVKKTMELIEEL HHHHHHHHHHHHHHH	15.34	21082442
428	Acetylation	KFYDQFSKNLKLGVH HHHHHHHHHCCEEEC	68.53	21791702
438	Phosphorylation	KLGVHEDSNNRAKLA CEEECCCCCCHHHHH	32.78	19429919
443	Acetylation	EDSNNRAKLADFLRF CCCCCHHHHHHHHHH	40.76	21791702
474	Acetylation	SRMKDNQKHVYFITG HHCCCCCCEEEEEEC	41.09	21791702
543	Acetylation	LPEDESEKKKREEDK CCCCHHHHHHHHHHH	73.25	21791702
558	Acetylation	AKFESLCKLMKSILD HHHHHHHHHHHHHHC	57.84	21791702
561	Acetylation	ESLCKLMKSILDNKV HHHHHHHHHHHCCCC	44.79	21791702
567	Acetylation	MKSILDNKVEKVVVS HHHHHCCCCEEEEEC	51.98	21791702
570	Acetylation	ILDNKVEKVVVSNRL HHCCCCEEEEECCCC	43.23	21791702
607	Phosphorylation	KAQALRDTATMGYMA HHHHHHHHHHHHHHC	20.00	22817900
612	Phosphorylation	RDTATMGYMAGKKQL HHHHHHHHHCCCCCE	3.49	22817900
691	Phosphorylation	DEDEPMTTDDAQSAG CCCCCCCCCHHHHCC	26.15	19429919
696	Phosphorylation	MTTDDAQSAGDAPSL CCCCHHHHCCCCCCH	35.62	19429919
702	Phosphorylation	QSAGDAPSLVEDTED HHCCCCCCHHCCCCC	46.93	19060867
707	Phosphorylation	APSLVEDTEDASHME CCCHHCCCCCHHHHC	23.43	22668510
711	Phosphorylation	VEDTEDASHMEEVD- HCCCCCHHHHCCCC-	35.37	22817900

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 HSP83_DROME !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HSP83_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 HSP83_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CAPZB_DROME	cpb	physical	14605208
ATPA_DROME	blw	physical	22036573
ATC1_DROME	Ca-P60A	physical	22036573
ATPB_DROME	ATPsyn-beta	physical	22036573
VDAC_DROME	porin	physical	22036573
CALR_DROME	Crc	physical	22036573
FAXC_DROME	fax	physical	22036573
NACA_DROME	Nacalpha	physical	22036573
NLP_DROME	Nlp	physical	22036573
ARF1_DROME	Arf79F	physical	22036573
PSMD4_DROME	Rpn10	physical	15946124
RS27A_DROME	RpS27A	physical	24292889
PIWI_DROME	piwi	physical	21186352
NELFE_DROME	Nelf-E	physical	22579285
NDUAA_DROME	ND42	physical	23509070

Drug and Disease Associations

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

Regulatory Network of HSP83_DROME

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells."; Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.; Mol. Biosyst. 3:275-286(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND MASSSPECTROMETRY.	17372656 [Abstract]
"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 TYR-294, AND MASSSPECTROMETRY.	18327897 [Abstract]