HSF_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HSF_DROME
• UniProt AC: P22813
• Protein Name: Heat shock factor protein
• Gene Name: Hsf
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 691
• Subcellular Localization: Nucleus.
• Protein Description: DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked..
• Protein Sequence: MSRSRSSAKAVQFKHESEEEEEDEEEQLPSRRMHSYGDAAAIGSGVPAFLAKLWRLVDDADTNRLICWTKDGQSFVIQNQAQFAKELLPLNYKHNNMASFIRQLNMYGFHKITSIDNGGLRFDRDEIEFSHPFFKRNSPFLLDQIKRKISNNKNGDDKGVLKPEAMSKILTDVKVMRGRQDNLDSRFSAMKQENEVLWREIASLRQKHAKQQQIVNKLIQFLITIVQPSRNMSGVKRHVQLMINNTPEIDRARTTSETESESGGGPVIHELREELLDEVMNPSPAGYTAASHYDQESVSPPAVERPRSNMSISSHNVDYSNQSVEDLLLQGNGTAGGNILVGGAASPMAQSVSQSPAQHDVYTVTEAPDSHVQEVPNSPPYYEEQNVLTTPMVREQEQQKRQQLKENNKLRRQAGDVILDAGDILVDSSSPKAQRTSIQHSTQPDVMVQPMIIKSEPENSSGLMDLMTPANDLYSVNFISEDMPTDIFEDALLPDGVEEAAKLDQQQKFGQSTVSSGKFASNFDVPTNSTLLDANQASTSKAAAKAQASEEEGMAVAKYSGAENGNNRDTNNSQLLRMASVDELHGHLESMQDELETLKDLLRGDGVAIDQNMLMGLFNDSDLMDNYGLSFPNDSISSEKKAPSGSELISYQPMYDLSDILDTDDGNNDQEASRRQMQTQSSVLNTPRHEL

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
17	Phosphorylation	AVQFKHESEEEEEDE HHHCCCCCCCCCCCH	50.45	19429919
174	Acetylation	SKILTDVKVMRGRQD HHHHHHHHHHCCCCC	32.88	21791702
254	Phosphorylation	PEIDRARTTSETESE CCCCCCCCCCCCCHH	33.42	19429919
255	Phosphorylation	EIDRARTTSETESES CCCCCCCCCCCCHHC	21.00	19429919
256	Phosphorylation	IDRARTTSETESESG CCCCCCCCCCCHHCC	41.74	19429919
258	Phosphorylation	RARTTSETESESGGG CCCCCCCCCHHCCCC	44.57	19429919
260	Phosphorylation	RTTSETESESGGGPV CCCCCCCHHCCCCCH	44.47	19429919
262	Phosphorylation	TSETESESGGGPVIH CCCCCHHCCCCCHHH	52.60	19429919
283	Phosphorylation	LDEVMNPSPAGYTAA HHHHHCCCCCCCCHH	23.52	22817900
297	Phosphorylation	ASHYDQESVSPPAVE HHCCCCCCCCCCCCC	23.43	22817900
299	Phosphorylation	HYDQESVSPPAVERP CCCCCCCCCCCCCCC	34.15	22817900
378	Phosphorylation	HVQEVPNSPPYYEEQ CCCCCCCCCCCCCCC	22.60	19129218
428	Phosphorylation	AGDILVDSSSPKAQR CCCEEECCCCCCHHH	25.82	23607784
429	Phosphorylation	GDILVDSSSPKAQRT CCEEECCCCCCHHHC	46.31	23607784
430	Phosphorylation	DILVDSSSPKAQRTS CEEECCCCCCHHHCC	34.08	28490779
518	Acetylation	QSTVSSGKFASNFDV CCCCCCCCCCCCCCC	39.44	21791702
580	Phosphorylation	SQLLRMASVDELHGH HHHHHHHHHHHHHHH	22.28	19429919

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
378	S	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
378	S	Phosphorylation	Kinase	MAPK_GROUP	-	PhosphoELM

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HSF_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 HSF_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MED17_DROME	MED17	physical	12021283
RS21_DROME	RpS21	physical	22036573
TIP60_DROME	Tip60	physical	24639513
MED21_DROME	MED21	physical	12556495
CDK8_DROME	Cdk8	physical	12556495
MED31_DROME	MED31	physical	12556495
MED17_DROME	MED17	physical	12556495
NKD_DROME	nkd	physical	18423435

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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 SER-256; THR-258; SER-260;SER-283; SER-299 AND SER-580, AND MASS SPECTROMETRY.
PubMed: 18327897