HS71L_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HS71L_MOUSE
• UniProt AC: P16627
• Protein Name: Heat shock 70 kDa protein 1-like
• Gene Name: Hspa1l
• Organism: Mus musculus (Mouse).
• Sequence Length: 641
• 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. Positive regulator of PRKN translocation to damaged mitochondria..
• Protein Sequence: MAANKGMAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQSDMKLWPFQVINEAGKPKVMVSYKGEKKAFYPEEISSMVLTKMKETAEAFLGHNVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDKGSHGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEKSLRDAKMDKAKIHDIVLVGGSTRIPKVQKLLQDYFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSEKVQDLLLLDVAPLSLGLETAGGVMTVLIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTRDNNLLGRFDLTGIPPAPRGVPQIEVTFDIDANGILNVTAMDKSTGKANKITITNDKGRLSKEEIERMVQEAERYKAEDEGQREKIAAKNALESYAFNMKSAVGDEGLKDKISESDKKKILDKCNEVLSWLEANQLAEKDEFDHKRKELENMCNPIITKLYQSGCTGPTCTPGYTPGRAATGPTIEEVD

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	GIDLGTTYSCVGVFQ EEECCCCCEEEEEEE	10.42	15592455
39	Phosphorylation	ANDQGNRTTPSYVAF ECCCCCCCCCCEEEE	47.24	20415495
40	Phosphorylation	NDQGNRTTPSYVAFT CCCCCCCCCCEEEEE	13.65	25367039
42	Phosphorylation	QGNRTTPSYVAFTDT CCCCCCCCEEEEECH	30.10	24899341
43	Phosphorylation	GNRTTPSYVAFTDTE CCCCCCCEEEEECHH	9.30	22817900
47	Phosphorylation	TPSYVAFTDTERLIG CCCEEEEECHHHHHH	32.07	28066266
49	Phosphorylation	SYVAFTDTERLIGDA CEEEEECHHHHHHHH	21.68	25367039
58	Acetylation	RLIGDAAKNQVAMNP HHHHHHHHCCCCCCC	50.02	23954790
58	Succinylation	RLIGDAAKNQVAMNP HHHHHHHHCCCCCCC	50.02	23806337
68	Phosphorylation	VAMNPQNTVFDAKRL CCCCCCCCHHHHHHH	19.80	20139300
73	Acetylation	QNTVFDAKRLIGRKF CCCHHHHHHHHCCCC	49.97	19864867
109	Phosphorylation	KPKVMVSYKGEKKAF CCEEEEEECCCEEEE	16.17	30387612
147	Phosphorylation	NVTNAVITVPAYFND CCCCEEEEEECCCCH	17.53	-
155	Phosphorylation	VPAYFNDSQRQATKD EECCCCHHHCCHHHC	28.50	26370283
161	Ubiquitination	DSQRQATKDAGVIAG HHHCCHHHCCCCCCC	48.90	-
179	Phosphorylation	LRIINEPTAAAIAYG HHHCCCCCHHHHHHC	23.81	-
185	Phosphorylation	PTAAAIAYGLDKGSH CCHHHHHHCCCCCCC	16.47	23984901
224	Phosphorylation	GIFEVKATAGDTHLG CEEEEEEEECCCCCC	26.00	22817900
228	Phosphorylation	VKATAGDTHLGGEDF EEEEECCCCCCCCCC	20.34	22817900
248	Acetylation	SHFVEEFKRKHKKDI HHHHHHHHHHHHHCH	64.91	23954790
256	Phosphorylation	RKHKKDISQNKRAVR HHHHHCHHHHHHHHH	37.52	22802335
259	Ubiquitination	KKDISQNKRAVRRLR HHCHHHHHHHHHHHH	33.81	-
267	Phosphorylation	RAVRRLRTACERAKR HHHHHHHHHHHHHHH	40.01	22817900
321	Ubiquitination	GTLEPVEKSLRDAKM CCCHHHHHHHHHHCC	55.83	-
327	Ubiquitination	EKSLRDAKMDKAKIH HHHHHHHCCCHHHCC	52.50	-
364	Phosphorylation	NGRDLNKSINPDEAV CCCCCCCCCCHHHHH	26.90	26643407
420	Phosphorylation	TVLIKRNSTIPTKQT EEEEECCCCCCCCCE	31.57	28507225
502	Malonylation	KSTGKANKITITNDK CCCCCCCEEEEECCC	46.19	26320211
502	Ubiquitination	KSTGKANKITITNDK CCCCCCCEEEEECCC	46.19	-
509	Succinylation	KITITNDKGRLSKEE EEEEECCCCCCCHHH	48.26	23806337
509	Acetylation	KITITNDKGRLSKEE EEEEECCCCCCCHHH	48.26	23806337
509	Ubiquitination	KITITNDKGRLSKEE EEEEECCCCCCCHHH	48.26	-
514	Ubiquitination	NDKGRLSKEEIERMV CCCCCCCHHHHHHHH	65.05	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of HS71L_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HS71L_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of HS71L_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of HS71L_MOUSE !!

Drug and Disease Associations

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