dbPTM

HSP7C_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HSP7C_MOUSE
UniProt AC	P63017
Protein Name	Heat shock cognate 71 kDa protein
Gene Name	Hspa8
Organism	Mus musculus (Mouse).
Sequence Length	646
Subcellular Localization	Cytoplasm. Melanosome. Nucleus, nucleolus. Cell membrane. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock (By similarity)..
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 co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity of HSP70 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. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1..
Protein Sequence	MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIISWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSKGPAVGI ------CCCCCEEEE	46.44	-
2	Phosphorylation	------MSKGPAVGI ------CCCCCEEEE	46.44	26745281
3	Acetylation	-----MSKGPAVGID -----CCCCCEEEEE	68.56	23201123
3	Malonylation	-----MSKGPAVGID -----CCCCCEEEEE	68.56	26320211
3	Ubiquitination	-----MSKGPAVGID -----CCCCCEEEEE	68.56	-
13	Phosphorylation	AVGIDLGTTYSCVGV EEEEECCCCEEEEEE	29.83	25293948
14	Phosphorylation	VGIDLGTTYSCVGVF EEEECCCCEEEEEEE	16.19	25293948
15	Phosphorylation	GIDLGTTYSCVGVFQ EEECCCCEEEEEEEE	10.42	28464351
16	Phosphorylation	IDLGTTYSCVGVFQH EECCCCEEEEEEEEC	10.55	25293948
17	Glutathionylation	DLGTTYSCVGVFQHG ECCCCEEEEEEEECC	1.86	24333276
17	S-nitrosylation	DLGTTYSCVGVFQHG ECCCCEEEEEEEECC	1.86	24895380
17	S-palmitoylation	DLGTTYSCVGVFQHG ECCCCEEEEEEEECC	1.86	26165157
37	Phosphorylation	ANDQGNRTTPSYVAF ECCCCCCCCCCEEEE	47.24	20415495
38	Phosphorylation	NDQGNRTTPSYVAFT CCCCCCCCCCEEEEE	13.65	25367039
40	Phosphorylation	QGNRTTPSYVAFTDT CCCCCCCCEEEEECH	30.10	24899341
41	Phosphorylation	GNRTTPSYVAFTDTE CCCCCCCEEEEECHH	9.30	22817900
45	Phosphorylation	TPSYVAFTDTERLIG CCCEEEEECHHHHHH	32.07	28066266
47	Phosphorylation	SYVAFTDTERLIGDA CEEEEECHHHHHHHH	21.68	25367039
56	Acetylation	RLIGDAAKNQVAMNP HHHHHHHHCCCCCCC	50.02	51082507
56	Malonylation	RLIGDAAKNQVAMNP HHHHHHHHCCCCCCC	50.02	26320211
56	Ubiquitination	RLIGDAAKNQVAMNP HHHHHHHHCCCCCCC	50.02	27667366
64	Phosphorylation	NQVAMNPTNTVFDAK CCCCCCCCCCHHHHH	38.22	26643407
66	Phosphorylation	VAMNPTNTVFDAKRL CCCCCCCCHHHHHHH	25.65	26643407
71	Acetylation	TNTVFDAKRLIGRRF CCCHHHHHHHHCCCC	49.97	22826441
71	Succinylation	TNTVFDAKRLIGRRF CCCHHHHHHHHCCCC	49.97	23954790
71	Ubiquitination	TNTVFDAKRLIGRRF CCCHHHHHHHHCCCC	49.97	27667366
85	Phosphorylation	FDDAVVQSDMKHWPF CCCHHHCCCCCCCCE	28.23	25521595
88	Acetylation	AVVQSDMKHWPFMVV HHHCCCCCCCCEEEE	47.73	22826441
88	Ubiquitination	AVVQSDMKHWPFMVV HHHCCCCCCCCEEEE	47.73	22790023
107	Phosphorylation	RPKVQVEYKGETKSF CCEEEEEECCCEECC	25.99	25367039
108	Acetylation	PKVQVEYKGETKSFY CEEEEEECCCEECCC	36.44	23806337
108	Malonylation	PKVQVEYKGETKSFY CEEEEEECCCEECCC	36.44	26320211
108	Ubiquitination	PKVQVEYKGETKSFY CEEEEEECCCEECCC	36.44	27667366
111	Phosphorylation	QVEYKGETKSFYPEE EEEECCCEECCCHHH	40.43	-
112	Acetylation	VEYKGETKSFYPEEV EEECCCEECCCHHHH	33.98	22826441
112	Ubiquitination	VEYKGETKSFYPEEV EEECCCEECCCHHHH	33.98	22790023
113	Phosphorylation	EYKGETKSFYPEEVS EECCCEECCCHHHHH	37.12	25195567
120	Phosphorylation	SFYPEEVSSMVLTKM CCCHHHHHHHHHHHH	18.92	26643407
121	Phosphorylation	FYPEEVSSMVLTKMK CCHHHHHHHHHHHHH	20.34	26643407
126	Acetylation	VSSMVLTKMKEIAEA HHHHHHHHHHHHHHH	43.76	22826441
126	Ubiquitination	VSSMVLTKMKEIAEA HHHHHHHHHHHHHHH	43.76	22790023
128	Acetylation	SMVLTKMKEIAEAYL HHHHHHHHHHHHHHC	47.74	-
128	Succinylation	SMVLTKMKEIAEAYL HHHHHHHHHHHHHHC	47.74	-
128	Ubiquitination	SMVLTKMKEIAEAYL HHHHHHHHHHHHHHC	47.74	22790023
137	Succinylation	IAEAYLGKTVTNAVV HHHHHCCCCCCCEEE	36.91	23954790
137	Ubiquitination	IAEAYLGKTVTNAVV HHHHHCCCCCCCEEE	36.91	-
138	Phosphorylation	AEAYLGKTVTNAVVT HHHHCCCCCCCEEEE	30.66	23984901
140	Phosphorylation	AYLGKTVTNAVVTVP HHCCCCCCCEEEEEE	23.77	23984901
145	Phosphorylation	TVTNAVVTVPAYFND CCCCEEEEEECCCCH	17.74	23984901
153	Phosphorylation	VPAYFNDSQRQATKD EECCCCHHHCCHHCC	28.50	-
159	Acetylation	DSQRQATKDAGTIAG HHHCCHHCCCCCCCC	48.90	23806337
159	Malonylation	DSQRQATKDAGTIAG HHHCCHHCCCCCCCC	48.90	26320211
159	Succinylation	DSQRQATKDAGTIAG HHHCCHHCCCCCCCC	48.90	-
159	Ubiquitination	DSQRQATKDAGTIAG HHHCCHHCCCCCCCC	48.90	27667366
163	Phosphorylation	QATKDAGTIAGLNVL CHHCCCCCCCCCHHH	14.90	23984901
177	Phosphorylation	LRIINEPTAAAIAYG HHHCCCHHHHHHHHC	23.81	-
183	Phosphorylation	PTAAAIAYGLDKKVG HHHHHHHHCCCCCCC	16.47	23984901
187	Acetylation	AIAYGLDKKVGAERN HHHHCCCCCCCCCCC	55.17	12016757
187	Malonylation	AIAYGLDKKVGAERN HHHHCCCCCCCCCCC	55.17	26320211
187	Ubiquitination	AIAYGLDKKVGAERN HHHHCCCCCCCCCCC	55.17	22790023
188	Acetylation	IAYGLDKKVGAERNV HHHCCCCCCCCCCCE	45.64	155877
188	Ubiquitination	IAYGLDKKVGAERNV HHHCCCCCCCCCCCE	45.64	22790023
221	O-linked_Glycosylation	DGIFEVKSTAGDTHL CCEEEEEECCCCCCC	28.76	22645316
221	Phosphorylation	DGIFEVKSTAGDTHL CCEEEEEECCCCCCC	28.76	20139300
222	Phosphorylation	GIFEVKSTAGDTHLG CEEEEEECCCCCCCC	29.01	29233185
226	Phosphorylation	VKSTAGDTHLGGEDF EEECCCCCCCCCCCC	20.34	24899341
246	Acetylation	NHFIAEFKRKHKKDI HHHHHHHHHHHHCCC	52.63	23806337
246	Malonylation	NHFIAEFKRKHKKDI HHHHHHHHHHHHCCC	52.63	26320211
246	Succinylation	NHFIAEFKRKHKKDI HHHHHHHHHHHHCCC	52.63	-
246	Ubiquitination	NHFIAEFKRKHKKDI HHHHHHHHHHHHCCC	52.63	-
254	Phosphorylation	RKHKKDISENKRAVR HHHHCCCHHHHHHHH	45.29	25266776
257	Acetylation	KKDISENKRAVRRLR HCCCHHHHHHHHHHH	37.37	2388013
257	Succinylation	KKDISENKRAVRRLR HCCCHHHHHHHHHHH	37.37	23954790
257	Ubiquitination	KKDISENKRAVRRLR HCCCHHHHHHHHHHH	37.37	27667366
265	Phosphorylation	RAVRRLRTACERAKR HHHHHHHHHHHHHHH	40.01	-
313	Phosphorylation	NADLFRGTLDPVEKA CHHHHCCCCCHHHHH	24.59	24899341
319	Acetylation	GTLDPVEKALRDAKL CCCCHHHHHHHHCCC	53.61	23806337
319	Malonylation	GTLDPVEKALRDAKL CCCCHHHHHHHHCCC	53.61	26320211
319	Succinylation	GTLDPVEKALRDAKL CCCCHHHHHHHHCCC	53.61	-
319	Succinylation	GTLDPVEKALRDAKL CCCCHHHHHHHHCCC	53.61	23806337
319	Ubiquitination	GTLDPVEKALRDAKL CCCCHHHHHHHHCCC	53.61	27667366
325	Ubiquitination	EKALRDAKLDKSQIH HHHHHHCCCCHHHCC	62.60	22790023
328	Acetylation	LRDAKLDKSQIHDIV HHHCCCCHHHCCEEE	55.48	23806337
328	Malonylation	LRDAKLDKSQIHDIV HHHCCCCHHHCCEEE	55.48	26320211
328	Succinylation	LRDAKLDKSQIHDIV HHHCCCCHHHCCEEE	55.48	-
328	Ubiquitination	LRDAKLDKSQIHDIV HHHCCCCHHHCCEEE	55.48	27667366
329	Phosphorylation	RDAKLDKSQIHDIVL HHCCCCHHHCCEEEE	33.75	27742792
341	Phosphorylation	IVLVGGSTRIPKIQK EEEECCCCCCHHHHH	35.57	24759943
345	Ubiquitination	GGSTRIPKIQKLLQD CCCCCCHHHHHHHHH	56.23	22790023
348	Acetylation	TRIPKIQKLLQDFFN CCCHHHHHHHHHHHC	55.42	22640795
348	Malonylation	TRIPKIQKLLQDFFN CCCHHHHHHHHHHHC	55.42	26073543
348	Ubiquitination	TRIPKIQKLLQDFFN CCCHHHHHHHHHHHC	55.42	-
357	Ubiquitination	LQDFFNGKELNKSIN HHHHHCCCCCCCCCC	61.20	22790023
361	Acetylation	FNGKELNKSINPDEA HCCCCCCCCCCHHHH	66.39	66694809
361	Ubiquitination	FNGKELNKSINPDEA HCCCCCCCCCCHHHH	66.39	22790023
362	Phosphorylation	NGKELNKSINPDEAV CCCCCCCCCCHHHHH	26.90	30352176
371	Phosphorylation	NPDEAVAYGAAVQAA CHHHHHHHHHHHHHH	10.74	29899451
423	Ubiquitination	RNTTIPTKQTQTFTT CCCCCCCCEEEEEEE	46.09	22790023
451	Acetylation	EGERAMTKDNNLLGK ECCCCCCCCCCCCCE	45.43	66696409
451	Malonylation	EGERAMTKDNNLLGK ECCCCCCCCCCCCCE	45.43	26320211
451	Ubiquitination	EGERAMTKDNNLLGK ECCCCCCCCCCCCCE	45.43	22790023
458	Ubiquitination	KDNNLLGKFELTGIP CCCCCCCEEEEECCC	35.32	22790023
462	Phosphorylation	LLGKFELTGIPPAPR CCCEEEEECCCCCCC	26.35	29109428
469	Methylation	TGIPPAPRGVPQIEV ECCCCCCCCCCEEEE	61.93	24129315
497	Ubiquitination	AVDKSTGKENKITIT EEECCCCCCCCEEEE	59.19	22790023
500	Malonylation	KSTGKENKITITNDK CCCCCCCCEEEECCC	42.17	26320211
500	Ubiquitination	KSTGKENKITITNDK CCCCCCCCEEEECCC	42.17	22790023
507	Ubiquitination	KITITNDKGRLSKED CEEEECCCCCCCHHH	48.26	22790023
511	Phosphorylation	TNDKGRLSKEDIERM ECCCCCCCHHHHHHH	32.41	29514104
512	Acetylation	NDKGRLSKEDIERMV CCCCCCCHHHHHHHH	65.09	23806337
512	Malonylation	NDKGRLSKEDIERMV CCCCCCCHHHHHHHH	65.09	26320211
512	Succinylation	NDKGRLSKEDIERMV CCCCCCCHHHHHHHH	65.09	-
512	Succinylation	NDKGRLSKEDIERMV CCCCCCCHHHHHHHH	65.09	23806337
512	Ubiquitination	NDKGRLSKEDIERMV CCCCCCCHHHHHHHH	65.09	27667366
524	Acetylation	RMVQEAEKYKAEDEK HHHHHHHHHCHHCHH	60.13	23806337
524	Malonylation	RMVQEAEKYKAEDEK HHHHHHHHHCHHCHH	60.13	26320211
524	Ubiquitination	RMVQEAEKYKAEDEK HHHHHHHHHCHHCHH	60.13	27667366
525	Phosphorylation	MVQEAEKYKAEDEKQ HHHHHHHHCHHCHHH	13.61	18563927
526	Acetylation	VQEAEKYKAEDEKQR HHHHHHHCHHCHHHH	57.26	23201123
526	Ubiquitination	VQEAEKYKAEDEKQR HHHHHHHCHHCHHHH	57.26	22790023
531	Ubiquitination	KYKAEDEKQRDKVSS HHCHHCHHHHHHCCC	64.06	22790023
537	Phosphorylation	EKQRDKVSSKNSLES HHHHHHCCCCHHHHH	41.14	23984901
538	Phosphorylation	KQRDKVSSKNSLESY HHHHHCCCCHHHHHH	38.55	26745281
539	Acetylation	QRDKVSSKNSLESYA HHHHCCCCHHHHHHH	42.95	23806337
539	Succinylation	QRDKVSSKNSLESYA HHHHCCCCHHHHHHH	42.95	23806337
539	Ubiquitination	QRDKVSSKNSLESYA HHHHCCCCHHHHHHH	42.95	27667366
541	Phosphorylation	DKVSSKNSLESYAFN HHCCCCHHHHHHHHE	36.93	25521595
544	Phosphorylation	SSKNSLESYAFNMKA CCCHHHHHHHHEEEC	27.36	26745281
545	Phosphorylation	SKNSLESYAFNMKAT CCHHHHHHHHEEECE	13.06	28066266
550	Ubiquitination	ESYAFNMKATVEDEK HHHHHEEECEECCHH	41.85	22790023
557	Ubiquitination	KATVEDEKLQGKIND ECEECCHHHCCCCCH	59.43	27667366
561	"N6,N6,N6-trimethyllysine"	EDEKLQGKINDEDKQ CCHHHCCCCCHHHHH	25.94	-
561	Methylation	EDEKLQGKINDEDKQ CCHHHCCCCCHHHHH	25.94	23921388
561	Ubiquitination	EDEKLQGKINDEDKQ CCHHHCCCCCHHHHH	25.94	27667366
569	Ubiquitination	INDEDKQKILDKCNE CCHHHHHHHHHHHHH	51.48	27667366
573	Acetylation	DKQKILDKCNEIISW HHHHHHHHHHHHHHH	35.20	22826441
573	Ubiquitination	DKQKILDKCNEIISW HHHHHHHHHHHHHHH	35.20	22790023
574	Glutathionylation	KQKILDKCNEIISWL HHHHHHHHHHHHHHH	5.73	24333276
574	S-palmitoylation	KQKILDKCNEIISWL HHHHHHHHHHHHHHH	5.73	28526873
579	Phosphorylation	DKCNEIISWLDKNQT HHHHHHHHHHHHCCC	27.52	18779572
583	Ubiquitination	EIISWLDKNQTAEKE HHHHHHHHCCCHHHH	49.11	22790023
589	Acetylation	DKNQTAEKEEFEHQQ HHCCCHHHHHHHHHH	61.14	23201123
589	Ubiquitination	DKNQTAEKEEFEHQQ HHCCCHHHHHHHHHH	61.14	22790023
597	Acetylation	EEFEHQQKELEKVCN HHHHHHHHHHHHHHH	58.66	22826441
597	Malonylation	EEFEHQQKELEKVCN HHHHHHHHHHHHHHH	58.66	26320211
597	Ubiquitination	EEFEHQQKELEKVCN HHHHHHHHHHHHHHH	58.66	27667366
601	Acetylation	HQQKELEKVCNPIIT HHHHHHHHHHHHHHH	65.79	23806337
601	Malonylation	HQQKELEKVCNPIIT HHHHHHHHHHHHHHH	65.79	26320211
601	Ubiquitination	HQQKELEKVCNPIIT HHHHHHHHHHHHHHH	65.79	-
603	S-nitrosocysteine	QKELEKVCNPIITKL HHHHHHHHHHHHHHH	8.10	-
603	Glutathionylation	QKELEKVCNPIITKL HHHHHHHHHHHHHHH	8.10	24333276
603	S-nitrosylation	QKELEKVCNPIITKL HHHHHHHHHHHHHHH	8.10	24926564
603	S-palmitoylation	QKELEKVCNPIITKL HHHHHHHHHHHHHHH	8.10	28526873
608	Phosphorylation	KVCNPIITKLYQSAG HHHHHHHHHHHHHCC	18.73	22006019
609	Ubiquitination	VCNPIITKLYQSAGG HHHHHHHHHHHHCCC	34.49	22790023
611	Phosphorylation	NPIITKLYQSAGGMP HHHHHHHHHHCCCCC	11.28	25777480
613	Phosphorylation	IITKLYQSAGGMPGG HHHHHHHHCCCCCCC	18.48	25777480
633	Phosphorylation	PGGGAPPSGGASSGP CCCCCCCCCCCCCCC	49.12	22006019
637	Phosphorylation	APPSGGASSGPTIEE CCCCCCCCCCCCCCC	38.82	25777480
638	Phosphorylation	PPSGGASSGPTIEEV CCCCCCCCCCCCCCC	48.54	24453211
641	Phosphorylation	GGASSGPTIEEVD-- CCCCCCCCCCCCC--	44.54	25777480

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
-	K	Ubiquitination	E3 ubiquitin ligase	Stub1	Q9WUD1	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
561	K	Methylation		23921388
Trimethylation at Lys-561 reduces fibrillar SNCA binding.

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 HSP7C_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SNP25_MOUSE	Snap25	physical	21151134
HSP7C_MOUSE	Hspa8	physical	21151134
DNJC5_MOUSE	Dnajc5	physical	21151134
SGTA_MOUSE	Sgta	physical	21151134
CDK4_MOUSE	Cdk4	physical	12588994
M3K14_MOUSE	Map3k14	physical	25792747

Drug and Disease Associations

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

Regulatory Network of HSP7C_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15 AND TYR-41, AND MASSSPECTROMETRY.	18034455 [Abstract]

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