HSF4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HSF4_HUMAN
• UniProt AC: Q9ULV5
• Protein Name: Heat shock factor protein 4
• Gene Name: HSF4
• Organism: Homo sapiens (Human).
• Sequence Length: 492
• Subcellular Localization: Nucleus.
• Protein Description: DNA-binding protein that specifically binds heat shock promoter elements (HSE). Isoform HSF4A represses transcription while the isoform HSF4B activates transcription..
• Protein Sequence: MQEAPAALPTEPGPSPVPAFLGKLWALVGDPGTDHLIRWSPSGTSFLVSDQSRFAKEVLPQYFKHSNMASFVRQLNMYGFRKVVSIEQGGLLRPERDHVEFQHPSFVRGREQLLERVRRKVPALRGDDGRWRPEDLGRLLGEVQALRGVQESTEARLRELRQQNEILWREVVTLRQSHGQQHRVIGKLIQCLFGPLQAGPSNAGGKRKLSLMLDEGSSCPTPAKFNTCPLPGALLQDPYFIQSPLPETNLGLSPHRARGPIISDIPEDSPSPEGTRLSPSSDGRREKGLALLKEEPASPGGDGEAGLALAPNECDFCVTAPPPLPVAVVQAILEGKGSFSPEGPRNAQQPEPGDPREIPDRGPLGLESGDRSPESLLPPMLLQPPQESVEPAGPLDVLGPSLQGREWTLMDLDMELSLMQPLVPERGEPELAVKGLNSPSPGKDPTLGAPLLLDVQAALGGPALGLPGALTIYSTPESRTASYLGPEASPSP

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
40	Phosphorylation	TDHLIRWSPSGTSFL CCCEEEECCCCCCEE	10.19	29052541
42	Phosphorylation	HLIRWSPSGTSFLVS CEEEECCCCCCEEEC	49.54	29052541
44	Phosphorylation	IRWSPSGTSFLVSDQ EEECCCCCCEEECCH	22.20	29052541
45	Phosphorylation	RWSPSGTSFLVSDQS EECCCCCCEEECCHH	21.80	29052541
49	Phosphorylation	SGTSFLVSDQSRFAK CCCCEEECCHHHHHH	31.89	22210691
52	Phosphorylation	SFLVSDQSRFAKEVL CEEECCHHHHHHHHH	34.06	22210691
206	Ubiquitination	GPSNAGGKRKLSLML CCCCCCCCEEEEEEE	45.50	-
210	Phosphorylation	AGGKRKLSLMLDEGS CCCCEEEEEEECCCC	18.12	28857561
217	Phosphorylation	SLMLDEGSSCPTPAK EEEECCCCCCCCCCC	27.07	28111955
218	Phosphorylation	LMLDEGSSCPTPAKF EEECCCCCCCCCCCC	34.67	28111955
221	Phosphorylation	DEGSSCPTPAKFNTC CCCCCCCCCCCCCCC	39.96	28111955
239 (in isoform 2)	Phosphorylation	-	22.92	24719451
273 (in isoform 2)	Phosphorylation	-	77.01	-
280	O-linked_Glycosylation	EGTRLSPSSDGRREK CCCCCCCCCCCCHHH	37.37	30379171
287	Sumoylation	SSDGRREKGLALLKE CCCCCHHHHEEEEEC	58.37	-
287	Sumoylation	SSDGRREKGLALLKE CCCCCHHHHEEEEEC	58.37	-
293	Sumoylation	EKGLALLKEEPASPG HHHEEEEECCCCCCC	61.96	16371476
293	Sumoylation	EKGLALLKEEPASPG HHHEEEEECCCCCCC	61.96	-
298	Phosphorylation	LLKEEPASPGGDGEA EEECCCCCCCCCCHH	34.49	16371476
308 (in isoform 2)	Phosphorylation	-	10.76	22210691
310 (in isoform 2)	Phosphorylation	-	10.16	22210691
340	Phosphorylation	LEGKGSFSPEGPRNA HCCCCCCCCCCCCCC	24.60	28857561
471	Phosphorylation	LGLPGALTIYSTPES CCCCCCEEEEECCCC	19.82	-
489	Phosphorylation	SYLGPEASPSP---- HHCCCCCCCCC----	25.01	27732954
491	Phosphorylation	LGPEASPSP------ CCCCCCCCC------	40.52	28857561

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
298	S	Phosphorylation	Kinase	ERK2	P28482	PSP
298	S	Phosphorylation	Kinase	ERK1	P27361	PSP
471	T	Phosphorylation	Kinase	MAP2K6	P52564	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
293	K	Phosphorylation	Phosphorylation on Ser-298 promotes sumoylation on Lys-293.	16371476
293	K	Sumoylation	Phosphorylation on Ser-298 promotes sumoylation on Lys-293.	16371476
298	S	Phosphorylation	Phosphorylation on Ser-298 promotes sumoylation on Lys-293.	16371476
298	S	Phosphorylation	Sumoylation represses the transcriptional activity and is promoted by phosphorylation on Ser-298.	16371476
298	S	Sumoylation	Phosphorylation on Ser-298 promotes sumoylation on Lys-293.	16371476
298	S	Sumoylation	Sumoylation represses the transcriptional activity and is promoted by phosphorylation on Ser-298.	16371476

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of HSF4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMCA4_HUMAN	SMARCA4	physical	16552721
DUS26_HUMAN	DUSP26	physical	16581800
MK01_HUMAN	MAPK1	physical	16581800
FKBP5_HUMAN	FKBP5	physical	25036637
HSF1_HUMAN	HSF1	physical	25036637
HSF2_HUMAN	HSF2	physical	25036637
RABE1_HUMAN	RABEP1	physical	25036637
SESD1_HUMAN	SESTD1	physical	25036637
TARB1_HUMAN	TARBP1	physical	25036637
TIM13_HUMAN	TIMM13	physical	25036637
SGT1_HUMAN	SUGT1	physical	25036637
MYO15_HUMAN	MYO15A	physical	25036637

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 116800: Cataract 5, multiple types (CTRCT5)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"PDSM, a motif for phosphorylation-dependent SUMO modification.";
Hietakangas V., Anckar J., Blomster H.A., Fujimoto M., Palvimo J.J.,Nakai A., Sistonen L.;
Proc. Natl. Acad. Sci. U.S.A. 103:45-50(2006).
Cited for: SUMOYLATION AT LYS-293, PHOSPHORYLATION AT SER-298, FUNCTION, ANDMUTAGENESIS OF LYS-293 AND SER-298.
PubMed: 16371476

Sumoylation

"PDSM, a motif for phosphorylation-dependent SUMO modification.";
Hietakangas V., Anckar J., Blomster H.A., Fujimoto M., Palvimo J.J.,Nakai A., Sistonen L.;
Proc. Natl. Acad. Sci. U.S.A. 103:45-50(2006).
Cited for: SUMOYLATION AT LYS-293, PHOSPHORYLATION AT SER-298, FUNCTION, ANDMUTAGENESIS OF LYS-293 AND SER-298.
PubMed: 16371476