dbPTM

HSP76_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HSP76_HUMAN
UniProt AC	P17066
Protein Name	Heat shock 70 kDa protein 6
Gene Name	HSPA6
Organism	Homo sapiens (Human).
Sequence Length	643
Subcellular Localization
Protein Description	Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. [PubMed: 26865365]
Protein Sequence	MQAPRELAVGIDLGTTYSCVGVFQQGRVEILANDQGNRTTPSYVAFTDTERLVGDAAKSQAALNPHNTVFDAKRLIGRKFADTTVQSDMKHWPFRVVSEGGKPKVRVCYRGEDKTFYPEEISSMVLSKMKETAEAYLGQPVKHAVITVPAYFNDSQRQATKDAGAIAGLNVLRIINEPTAAAIAYGLDRRGAGERNVLIFDLGGGTFDVSVLSIDAGVFEVKATAGDTHLGGEDFDNRLVNHFMEEFRRKHGKDLSGNKRALRRLRTACERAKRTLSSSTQATLEIDSLFEGVDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDVVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAVLMGDKCEKVQDLLLLDVAPLSLGLETAGGVMTTLIQRNATIPTKQTQTFTTYSDNQPGVFIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILSVTATDRSTGKANKITITNDKGRLSKEEVERMVHEAEQYKAEDEAQRDRVAAKNSLEAHVFHVKGSLQEESLRDKIPEEDRRKMQDKCREVLAWLEHNQLAEKEEYEHQKRELEQICRPIFSRLYGGPGVPGGSSCGTQARQGDPSTGPIIEEVD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
15	Phosphorylation	AVGIDLGTTYSCVGV EECEECCCCEEEEEE	29.83	-
17	Phosphorylation	GIDLGTTYSCVGVFQ CEECCCCEEEEEEEE	10.42	-
39	Phosphorylation	ANDQGNRTTPSYVAF ECCCCCCCCCCEEEE	47.24	21945579
40	Phosphorylation	NDQGNRTTPSYVAFT CCCCCCCCCCEEEEE	13.65	21945579
42	Phosphorylation	QGNRTTPSYVAFTDT CCCCCCCCEEEEECH	30.10	21945579
43	Phosphorylation	GNRTTPSYVAFTDTE CCCCCCCEEEEECHH	9.30	21945579
47	Phosphorylation	TPSYVAFTDTERLVG CCCEEEEECHHHHHH	32.07	21945579
49	Phosphorylation	SYVAFTDTERLVGDA CEEEEECHHHHHHHH	21.68	21945579
51	Methylation	VAFTDTERLVGDAAK EEEECHHHHHHHHHH	36.44	-
58	Ubiquitination	RLVGDAAKSQAALNP HHHHHHHHHCHHHCC	44.83	-
59	Phosphorylation	LVGDAAKSQAALNPH HHHHHHHHCHHHCCC	21.96	24719451
73	Ubiquitination	HNTVFDAKRLIGRKF CCCHHHHHHHHCCCC	49.97	-
79	Ubiquitination	AKRLIGRKFADTTVQ HHHHHCCCCCCCCCC	39.42	-
90	Ubiquitination	TTVQSDMKHWPFRVV CCCCCCCCCCCEEEE	47.73	-
102	Ubiquitination	RVVSEGGKPKVRVCY EEEEECCCCCEEEEE	53.15	-
102	Acetylation	RVVSEGGKPKVRVCY EEEEECCCCCEEEEE	53.15	-
104	Ubiquitination	VSEGGKPKVRVCYRG EEECCCCCEEEEECC	46.27	-
114	Ubiquitination	VCYRGEDKTFYPEEI EEECCCCCCCCHHHH	35.91	-
115	Phosphorylation	CYRGEDKTFYPEEIS EECCCCCCCCHHHHH	40.50	20860994
117	Phosphorylation	RGEDKTFYPEEISSM CCCCCCCCHHHHHHH	18.24	29438985
123	Phosphorylation	FYPEEISSMVLSKMK CCHHHHHHHHHHHHH	20.69	-
127	Phosphorylation	EISSMVLSKMKETAE HHHHHHHHHHHHHHH	21.20	29438985
128	Ubiquitination	ISSMVLSKMKETAEA HHHHHHHHHHHHHHH	50.24	-
130	Ubiquitination	SMVLSKMKETAEAYL HHHHHHHHHHHHHHC	56.50	-
136	Nitrated tyrosine	MKETAEAYLGQPVKH HHHHHHHHCCCCCEE	11.67	-
142	Ubiquitination	AYLGQPVKHAVITVP HHCCCCCEEEEEEEE	32.31	-
142	Methylation	AYLGQPVKHAVITVP HHCCCCCEEEEEEEE	32.31	23644510
151	Phosphorylation	AVITVPAYFNDSQRQ EEEEEECCCCHHHCH	9.24	-
155	Phosphorylation	VPAYFNDSQRQATKD EECCCCHHHCHHHCC	28.50	17525332
161	Ubiquitination	DSQRQATKDAGAIAG HHHCHHHCCCCHHCC	48.90	-
179	Phosphorylation	LRIINEPTAAAIAYG HHHCCCHHHHHHHHC	23.81	28152594
185	Phosphorylation	PTAAAIAYGLDRRGA HHHHHHHHCCCCCCC	16.47	28152594
224	Phosphorylation	GVFEVKATAGDTHLG CEEEEEECCCCCCCC	26.00	29396449
259	Ubiquitination	GKDLSGNKRALRRLR CCCCCCCHHHHHHHH	42.44	-
267	Phosphorylation	RALRRLRTACERAKR HHHHHHHHHHHHHHH	40.01	27273156
275	Phosphorylation	ACERAKRTLSSSTQA HHHHHHHHHCCCCCE	30.22	-
278	Phosphorylation	RAKRTLSSSTQATLE HHHHHHCCCCCEEHH	40.28	-
298	Phosphorylation	EGVDFYTSITRARFE CCCCCCHHHHHHHHH	15.58	20860994
300	Phosphorylation	VDFYTSITRARFEEL CCCCHHHHHHHHHHH	20.31	20860994
309	Phosphorylation	ARFEELCSDLFRSTL HHHHHHHHHHHHHCC	50.39	21712546
314	Phosphorylation	LCSDLFRSTLEPVEK HHHHHHHHCCHHHHH	29.97	-
315	Phosphorylation	CSDLFRSTLEPVEKA HHHHHHHCCHHHHHH	30.77	21712546
321	Ubiquitination	STLEPVEKALRDAKL HCCHHHHHHHHHCCC	53.61	21890473
321	Acetylation	STLEPVEKALRDAKL HCCHHHHHHHHHCCC	53.61	22640907
327	Ubiquitination	EKALRDAKLDKAQIH HHHHHHCCCCHHHCC	62.60	21890473
330	Ubiquitination	LRDAKLDKAQIHDVV HHHCCCCHHHCCEEE	53.26	-
330	Methylation	LRDAKLDKAQIHDVV HHHCCCCHHHCCEEE	53.26	-
330	Acetylation	LRDAKLDKAQIHDVV HHHCCCCHHHCCEEE	53.26	-
347	Ubiquitination	GGSTRIPKVQKLLQD CCCCCCHHHHHHHHH	55.73	-
350	Ubiquitination	TRIPKVQKLLQDFFN CCCHHHHHHHHHHHC	54.90	21890473
350	Acetylation	TRIPKVQKLLQDFFN CCCHHHHHHHHHHHC	54.90	25953088
359	Ubiquitination	LQDFFNGKELNKSIN HHHHHCCCCCCCCCC	61.20	21890473
359	Acetylation	LQDFFNGKELNKSIN HHHHHCCCCCCCCCC	61.20	24513421
359	Sumoylation	LQDFFNGKELNKSIN HHHHHCCCCCCCCCC	61.20	-
363	Ubiquitination	FNGKELNKSINPDEA HCCCCCCCCCCHHHH	66.39	-
363	Sumoylation	FNGKELNKSINPDEA HCCCCCCCCCCHHHH	66.39	-
364	Phosphorylation	NGKELNKSINPDEAV CCCCCCCCCCHHHHH	26.90	25159151
373	Phosphorylation	NPDEAVAYGAAVQAA CHHHHHHHHHHHHHH	10.74	18669648
386	Ubiquitination	AAVLMGDKCEKVQDL HHHHCCCCCCHHHHE	38.27	-
402	Phosphorylation	LLDVAPLSLGLETAG EEECCCCCCCCCCCC	21.23	-
407	Phosphorylation	PLSLGLETAGGVMTT CCCCCCCCCCHHHHH	35.33	-
414	Phosphorylation	TAGGVMTTLIQRNAT CCCHHHHHHHHCCCC	12.08	21601212
424	Phosphorylation	QRNATIPTKQTQTFT HCCCCCCCCCEEEEE	31.75	21601212
429	Phosphorylation	IPTKQTQTFTTYSDN CCCCCEEEEEEECCC	26.74	-
433	Phosphorylation	QTQTFTTYSDNQPGV CEEEEEEECCCCCEE	15.80	-
453	Ubiquitination	EGERAMTKDNNLLGR ECCCCCCCCCCEECC	45.43	21890473
460	Methylation	KDNNLLGRFELSGIP CCCCEECCEEECCCC	23.10	-
471	Methylation	SGIPPAPRGVPQIEV CCCCCCCCCCCEEEE	61.93	18600857
479	Phosphorylation	GVPQIEVTFDIDANG CCCEEEEEEEECCCC	11.64	15302935
495	Methylation	LSVTATDRSTGKANK EEEEEEECCCCCCCE	31.59	115384363
497	Phosphorylation	VTATDRSTGKANKIT EEEEECCCCCCCEEE	43.53	-
499	Ubiquitination	ATDRSTGKANKITIT EEECCCCCCCEEEEE	49.20	-
502	Ubiquitination	RSTGKANKITITNDK CCCCCCCEEEEECCC	46.19	21890473
502	Acetylation	RSTGKANKITITNDK CCCCCCCEEEEECCC	46.19	22640903
504	Phosphorylation	TGKANKITITNDKGR CCCCCEEEEECCCCC	24.29	25159151
509	Sumoylation	KITITNDKGRLSKEE EEEEECCCCCCCHHH	48.26	-
509	Ubiquitination	KITITNDKGRLSKEE EEEEECCCCCCCHHH	48.26	21890473
509	Sumoylation	KITITNDKGRLSKEE EEEEECCCCCCCHHH	48.26	-
509	Acetylation	KITITNDKGRLSKEE EEEEECCCCCCCHHH	48.26	83037561
513	Phosphorylation	TNDKGRLSKEEVERM ECCCCCCCHHHHHHH	36.34	26091039
514	Ubiquitination	NDKGRLSKEEVERMV CCCCCCCHHHHHHHH	63.59	-
528	Ubiquitination	VHEAEQYKAEDEAQR HHHHHHHHHHCHHHH	45.02	-
541	Ubiquitination	QRDRVAAKNSLEAHV HHHHHHHHHHHHEEE	37.01	-
552	Ubiquitination	EAHVFHVKGSLQEES HEEEEEECCCCCHHH	33.92	-
563	"N6,N6,N6-trimethyllysine"	QEESLRDKIPEEDRR CHHHHHHHCCHHHHH	54.44	-
563	Ubiquitination	QEESLRDKIPEEDRR CHHHHHHHCCHHHHH	54.44	-
563	Methylation	QEESLRDKIPEEDRR CHHHHHHHCCHHHHH	54.44	23921388
591	Ubiquitination	EHNQLAEKEEYEHQK HHHHHHCHHHHHHHH	50.68	-
598	Ubiquitination	KEEYEHQKRELEQIC HHHHHHHHHHHHHHH	50.15	-
626	Phosphorylation	PGGSSCGTQARQGDP CCCCCCCCCCCCCCC	24.31	-

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 HSP76_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HSP76_HUMAN !!

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 HSP76_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SCFD1_HUMAN	SCFD1	physical	22939629
HSP7C_HUMAN	HSPA8	physical	22863883
DNJA1_HUMAN	DNAJA1	physical	21231916
DNJA2_HUMAN	DNAJA2	physical	21231916
DNJA4_HUMAN	DNAJA4	physical	21231916
DNJB1_HUMAN	DNAJB1	physical	21231916
DNJB4_HUMAN	DNAJB4	physical	21231916
DNJB5_HUMAN	DNAJB5	physical	21231916
DNJB6_HUMAN	DNAJB6	physical	21231916
DNJB7_HUMAN	DNAJB7	physical	21231916
DNJB8_HUMAN	DNAJB8	physical	21231916

Drug and Disease Associations

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

Regulatory Network of HSP76_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-321 AND LYS-502, AND MASSSPECTROMETRY.	19608861 [Abstract]