dbPTM

HS71L_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HS71L_HUMAN
UniProt AC	P34931
Protein Name	Heat shock 70 kDa protein 1-like
Gene Name	HSPA1L
Organism	Homo sapiens (Human).
Sequence Length	641
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 Positive regulator of PRKN translocation to damaged mitochondria]
Protein Sequence	MATAKGIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQADMKLWPFQVINEGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDKGGQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSEKVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIEVTFDIDANGILNVTATDKSTGKVNKITITNDKGRLSKEEIERMVLDAEKYKAEDEVQREKIAAKNALESYAFNMKSVVSDEGLKGKISESDKNKILDKCNELLSWLEVNQLAEKDEFDHKRKELEQMCNPIITKLYQGGCTGPACGTGYVPGRPATGPTIEEVD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
15	Phosphorylation	AIGIDLGTTYSCVGV EEEEECCCCEEEEEE	29.83	-
17	Phosphorylation	GIDLGTTYSCVGVFQ EEECCCCEEEEEEEE	10.42	-
18	Phosphorylation	IDLGTTYSCVGVFQH EECCCCEEEEEEEEC	10.55	29759185
27	Ubiquitination	VGVFQHGKVEIIAND EEEEECCEEEEEECC	34.27	-
39	Phosphorylation	ANDQGNRTTPSYVAF ECCCCCCCCCCEEEE	47.24	21945579
40	Phosphorylation	NDQGNRTTPSYVAFT CCCCCCCCCCEEEEE	13.65	21945579
42	Phosphorylation	QGNRTTPSYVAFTDT CCCCCCCCEEEEECH	30.10	21945579
42	O-linked_Glycosylation	QGNRTTPSYVAFTDT CCCCCCCCEEEEECH	30.10	28657654
43	Phosphorylation	GNRTTPSYVAFTDTE CCCCCCCEEEEECHH	9.30	21945579
47	Phosphorylation	TPSYVAFTDTERLIG CCCEEEEECHHHHHH	32.07	21945579
49	Phosphorylation	SYVAFTDTERLIGDA CEEEEECHHHHHHHH	21.68	21945579
51	Methylation	VAFTDTERLIGDAAK EEEECHHHHHHHHHH	33.43	-
58	Ubiquitination	RLIGDAAKNQVAMNP HHHHHHHHCCCCCCC	50.02	-
68	Phosphorylation	VAMNPQNTVFDAKRL CCCCCCCCHHHHHHH	19.80	20068231
73	Methylation	QNTVFDAKRLIGRKF CCCHHHHHHHHCCCC	49.97	19864871
73	Ubiquitination	QNTVFDAKRLIGRKF CCCHHHHHHHHCCCC	49.97	-
117	Phosphorylation	KGENKAFYPEEISSM CCCCCCCCHHHHHHH	18.00	20068231
122	Phosphorylation	AFYPEEISSMVLTKL CCCHHHHHHHHHHHH	18.70	20068231
123	Phosphorylation	FYPEEISSMVLTKLK CCHHHHHHHHHHHHH	20.69	20068231
127	Phosphorylation	EISSMVLTKLKETAE HHHHHHHHHHHHHHH	23.95	20068231
132	Phosphorylation	VLTKLKETAEAFLGH HHHHHHHHHHHHHCC	28.36	20068231
142	Phosphorylation	AFLGHPVTNAVITVP HHHCCCCCCEEEEEE	23.16	20068231
147	Phosphorylation	PVTNAVITVPAYFND CCCCEEEEEECCCCH	17.53	28152594
151	Phosphorylation	AVITVPAYFNDSQRQ EEEEEECCCCHHHCC	9.24	28152594
155	Phosphorylation	VPAYFNDSQRQATKD EECCCCHHHCCHHHC	28.50	17525332
160	Phosphorylation	NDSQRQATKDAGVIA CHHHCCHHHCCCCCC	22.56	-
161	Ubiquitination	DSQRQATKDAGVIAG HHHCCHHHCCCCCCC	48.90	21906983
179	Phosphorylation	LRIINEPTAAAIAYG HHHCCCCCHHHHHHC	23.81	28152594
185	Phosphorylation	PTAAAIAYGLDKGGQ CCHHHHHHCCCCCCC	16.47	28152594
189	Methylation	AIAYGLDKGGQGERH HHHHCCCCCCCCCCE	70.73	-
222	Ubiquitination	DDGIFEVKATAGDTH CCCEEEEEEEECCCC	32.59	-
224	Phosphorylation	GIFEVKATAGDTHLG CEEEEEEEECCCCCC	26.00	29396449
241	Phosphorylation	DFDNRLVSHFVEEFK CCHHHHHHHHHHHHH	18.79	-
248	Acetylation	SHFVEEFKRKHKKDI HHHHHHHHHHHHHCH	64.91	25038526
252	Ubiquitination	EEFKRKHKKDISQNK HHHHHHHHHCHHHHH	56.00	-
253	Ubiquitination	EFKRKHKKDISQNKR HHHHHHHHCHHHHHH	61.07	-
256	Phosphorylation	RKHKKDISQNKRAVR HHHHHCHHHHHHHHH	37.52	20068231
259	Ubiquitination	KKDISQNKRAVRRLR HHCHHHHHHHHHHHH	33.81	21890473
267	Phosphorylation	RAVRRLRTACERAKR HHHHHHHHHHHHHHH	40.01	27273156
275	Phosphorylation	ACERAKRTLSSSTQA HHHHHHHHHCCCHHH	30.22	-
298	Phosphorylation	EGIDFYTSITRARFE CCCCHHHHHHHHHHH	15.58	20860994
300	Phosphorylation	IDFYTSITRARFEEL CCHHHHHHHHHHHHH	20.31	20860994
321	Acetylation	GTLEPVEKALRDAKM CCCHHHHHHHHHCCC	53.61	19608861
330	Ubiquitination	LRDAKMDKAKIHDIV HHHCCCCHHCCCEEE	48.34	-
332	Acetylation	DAKMDKAKIHDIVLV HCCCCHHCCCEEEEE	46.44	25038526
332	Ubiquitination	DAKMDKAKIHDIVLV HCCCCHHCCCEEEEE	46.44	-
363	Ubiquitination	FNGRDLNKSINPDEA HCCCCCCCCCCHHHH	61.07	21906983
364	Phosphorylation	NGRDLNKSINPDEAV CCCCCCCCCCHHHHH	26.90	30278072
373	Phosphorylation	NPDEAVAYGAAVQAA CHHHHHHHHHHHHHH	10.74	18669648
387	Phosphorylation	AILMGDKSEKVQDLL HHHCCCCCHHHHHHH	47.60	-
402	Phosphorylation	LLDVAPLSLGLETAG HHCHHCCCCCCCCCH	21.23	-
413	Phosphorylation	ETAGGVMTALIKRNS CCCHHHHHHHHHCCC	18.86	-
417	Ubiquitination	GVMTALIKRNSTIPT HHHHHHHHCCCCCCC	46.51	-
418	Methylation	VMTALIKRNSTIPTK HHHHHHHCCCCCCCC	35.02	-
420	Phosphorylation	TALIKRNSTIPTKQT HHHHHCCCCCCCCCE	31.57	30266825
421	Phosphorylation	ALIKRNSTIPTKQTQ HHHHCCCCCCCCCEE	34.23	30266825
424	Phosphorylation	KRNSTIPTKQTQIFT HCCCCCCCCCEEEEE	31.75	28102081
425	Ubiquitination	RNSTIPTKQTQIFTT CCCCCCCCCEEEEEE	46.09	21906983
431	Phosphorylation	TKQTQIFTTYSDNQP CCCEEEEEEECCCCC	26.84	28152594
432	Phosphorylation	KQTQIFTTYSDNQPG CCEEEEEEECCCCCE	15.41	28152594
433	Phosphorylation	QTQIFTTYSDNQPGV CEEEEEEECCCCCEE	15.80	28152594
434	Phosphorylation	TQIFTTYSDNQPGVL EEEEEEECCCCCEEE	28.17	28152594
445	Phosphorylation	PGVLIQVYEGERAMT CEEEEEEEECCCCCC	11.22	20068231
453	Ubiquitination	EGERAMTKDNNLLGR ECCCCCCCCCCCCCC	45.43	21906983
464	Phosphorylation	LLGRFDLTGIPPAPR CCCCCCCCCCCCCCC	34.60	21406692
471	Methylation	TGIPPAPRGVPQIEV CCCCCCCCCCCEEEE	61.93	-
479	Phosphorylation	GVPQIEVTFDIDANG CCCEEEEEEEECCCC	11.64	22817900
502	Ubiquitination	KSTGKVNKITITNDK CCCCCEEEEEEECCC	44.19	-
504	Phosphorylation	TGKVNKITITNDKGR CCCEEEEEEECCCCC	24.29	22817900
509	Acetylation	KITITNDKGRLSKEE EEEEECCCCCCCHHH	48.26	72617493
509	Sumoylation	KITITNDKGRLSKEE EEEEECCCCCCCHHH	48.26	-
509	Ubiquitination	KITITNDKGRLSKEE EEEEECCCCCCCHHH	48.26	21906983
509	Sumoylation	KITITNDKGRLSKEE EEEEECCCCCCCHHH	48.26	-
513	Phosphorylation	TNDKGRLSKEEIERM ECCCCCCCHHHHHHH	36.34	20873877
514	Ubiquitination	NDKGRLSKEEIERMV CCCCCCCHHHHHHHH	65.05	21906983
514	Acetylation	NDKGRLSKEEIERMV CCCCCCCHHHHHHHH	65.05	72589429
527	Phosphorylation	MVLDAEKYKAEDEVQ HHHCHHHHCCHHHHH	13.61	30257219
528	Ubiquitination	VLDAEKYKAEDEVQR HHCHHHHCCHHHHHH	57.26	21906983
528	Acetylation	VLDAEKYKAEDEVQR HHCHHHHCCHHHHHH	57.26	25038526
541	Ubiquitination	QREKIAAKNALESYA HHHHHHHHHHHHHHC	33.46	-
546	Phosphorylation	AAKNALESYAFNMKS HHHHHHHHHCCCCHH	23.70	28152594
547	Phosphorylation	AKNALESYAFNMKSV HHHHHHHHCCCCHHC	13.06	28152594
556	Phosphorylation	FNMKSVVSDEGLKGK CCCHHCCCCCCCCCC	27.99	30622161
599	Acetylation	DEFDHKRKELEQMCN CCHHHHHHHHHHHHH	72.03	25038526

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
241	S	Phosphorylation	Kinase	MAPKAPK2	P49137	PSP
241	S	Phosphorylation	Kinase	MAPKAPK2	P49138	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HS71L_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 HS71L_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HSP76_HUMAN	HSPA6	physical	22939629
QCR1_HUMAN	UQCRC1	physical	22939629
RM01_HUMAN	MRPL1	physical	22939629
NDUB7_HUMAN	NDUFB7	physical	22939629
HACD3_HUMAN	PTPLAD1	physical	22939629
MUC18_HUMAN	MCAM	physical	22939629
K2013_HUMAN	KIAA2013	physical	22939629
MPCP_HUMAN	SLC25A3	physical	22939629
RL3_HUMAN	RPL3	physical	22939629
TOM22_HUMAN	TOMM22	physical	22939629
THIOM_HUMAN	TXN2	physical	22939629
NU214_HUMAN	NUP214	physical	22939629
NB5R3_HUMAN	CYB5R3	physical	22939629
RT36_HUMAN	MRPS36	physical	22939629
TIM14_HUMAN	DNAJC19	physical	22939629
NDUB9_HUMAN	NDUFB9	physical	22939629
ODP2_HUMAN	DLAT	physical	22939629
STML2_HUMAN	STOML2	physical	22939629
NDUS2_HUMAN	NDUFS2	physical	22939629
RB11A_HUMAN	RAB11A	physical	22939629
RRBP1_HUMAN	RRBP1	physical	22939629
PIGS_HUMAN	PIGS	physical	22939629
NDUV1_HUMAN	NDUFV1	physical	22939629
RBP2_HUMAN	RANBP2	physical	22939629
IPO7_HUMAN	IPO7	physical	22863883
XPO1_HUMAN	XPO1	physical	22863883
M3K1_HUMAN	MAP3K1	physical	25241761
TF65_HUMAN	RELA	physical	25241761
P53_HUMAN	TP53	physical	25241761
TAB1_HUMAN	TAB1	physical	25241761
MARE2_HUMAN	MAPRE2	physical	27173435
HSF1_HUMAN	HSF1	physical	27173435
CC28B_HUMAN	CCDC28B	physical	27173435
HIF1A_HUMAN	HIF1A	physical	28759037
AMFR_HUMAN	AMFR	physical	28759037

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 HS71L_HUMAN

Related Literatures of Post-Translational Modification