HSP72_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HSP72_RAT
• UniProt AC: P14659
• Protein Name: Heat shock-related 70 kDa protein 2
• Gene Name: Hspa2
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 633
• Subcellular Localization: Cytoplasm, cytoskeleton, spindle . Colocalizes with SHCBP1L at spindle during the meiosis process.
• 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. 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. Plays a role in spermatogenesis. In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells..
• Protein Sequence: MSARGPAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDATVQSDMKHWPFRVVSEGGKPKVQVEYKGEMKTFFPEEISSMVLTKMKEIAEAYLGGKVQSAVITVPAYFNDSQRQATKDAGTITGLNVLRIINEPTAAAIAYGLDKKGCAGGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSHLAEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLEPVEKALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILIGDKSENVQDLLLLDVTPLSLGIETAGGVMTPLIKRNTTIPTKQTQTFTTYSDNQSSVLVQVYEGERAMTKDNNLLGKFDLTGIPPAPRGVPQIEVTFDIDANGILNVTAADKSTGKENKITITNDKGRLSKDDIDRMVQEAERYKSEDEANRDRVAAKNAVESYTYNIKQTVEDEKLRGKISEQDKNKILDKCQEVINWLDRNQMAEKDEYEHKQKELERVCNPIISKLYQGGPGGGGSSGGPTIEEVD

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
42	Phosphorylation	GNRTTPSYVAFTDTE CCCCCCCEEEEECHH	9.30	-
57	Acetylation	RLIGDAAKNQVAMNP HHHHHHHHCCCCCCC	50.02	22902405
72	Acetylation	TNTIFDAKRLIGRKF CCCHHHHHHHHCCCC	49.97	22902405
78	Acetylation	AKRLIGRKFEDATVQ HHHHHCCCCCCCCCC	48.14	22902405
89	Acetylation	ATVQSDMKHWPFRVV CCCCCCCCCCCEEEE	47.73	22902405
109	Acetylation	PKVQVEYKGEMKTFF CEEEEEECCEEEEEC	34.58	22902405
129	Acetylation	SMVLTKMKEIAEAYL HHHHHHHHHHHHHHH	47.74	72589461
160	Acetylation	DSQRQATKDAGTITG HHHCCCCCCCCCCCC	48.90	22902405
188	Acetylation	AIAYGLDKKGCAGGE HHHHCCCCCCCCCCC	56.99	26302492
189	Acetylation	IAYGLDKKGCAGGEK HHHCCCCCCCCCCCC	59.91	26302492
229	Phosphorylation	VKSTAGDTHLGGEDF EEECCCCCCCCCCCC	20.34	22673903
249	Acetylation	SHLAEEFKRKHKKDI HHHHHHHHHHHHHCC	64.91	22902405
322	Acetylation	GTLEPVEKALRDAKL CCCHHHHHHHHHCCC	53.61	37418447
328	Acetylation	EKALRDAKLDKGQIQ HHHHHHCCCCCCCCC	62.60	72587747
348	Ubiquitination	GGSTRIPKIQKLLQD CCCCCHHHHHHHHHH	56.23	-
348	Acetylation	GGSTRIPKIQKLLQD CCCCCHHHHHHHHHH	56.23	22902405
351	Acetylation	TRIPKIQKLLQDFFN CCHHHHHHHHHHHHC	55.42	25786129
351	Ubiquitination	TRIPKIQKLLQDFFN CCHHHHHHHHHHHHC	55.42	-
360	Acetylation	LQDFFNGKELNKSIN HHHHHCCCCCCCCCC	61.20	72584809
364	Acetylation	FNGKELNKSINPDEA HCCCCCCCCCCHHHH	66.39	22902405
365	Phosphorylation	NGKELNKSINPDEAV CCCCCCCCCCHHHHH	26.90	-
374	Phosphorylation	NPDEAVAYGAAVQAA CHHHHHHHHHHHHHH	10.74	-
403	Phosphorylation	LLDVTPLSLGIETAG EEECCCCCCCEEECC	26.25	16641100
408	Phosphorylation	PLSLGIETAGGVMTP CCCCCEEECCCCCCC	28.78	16641100
414	Phosphorylation	ETAGGVMTPLIKRNT EECCCCCCCEEECCC	16.73	16641100
454	Acetylation	EGERAMTKDNNLLGK ECCCCCCCCCCCCCC	45.43	22902405
503	Acetylation	KSTGKENKITITNDK CCCCCCCCEEEECCC	42.17	22902405
510	Ubiquitination	KITITNDKGRLSKDD CEEEECCCCCCCHHH	48.26	-
510	Acetylation	KITITNDKGRLSKDD CEEEECCCCCCCHHH	48.26	72617497
514	Phosphorylation	TNDKGRLSKDDIDRM ECCCCCCCHHHHHHH	32.45	30181290
515	Acetylation	NDKGRLSKDDIDRMV CCCCCCCHHHHHHHH	65.10	22902405
553	Acetylation	ESYTYNIKQTVEDEK HHHEEECEEHHCCHH	35.96	22902405
560	Acetylation	KQTVEDEKLRGKISE EEHHCCHHHCCCCCH	56.67	22902405
564	Methylation	EDEKLRGKISEQDKN CCHHHCCCCCHHHHH	36.30	-
564	"N6,N6,N6-trimethyllysine"	EDEKLRGKISEQDKN CCHHHCCCCCHHHHH	36.30	-
572	Acetylation	ISEQDKNKILDKCQE CCHHHHHHHHHHHHH	50.84	22902405
600	Acetylation	DEYEHKQKELERVCN HHHHHHHHHHHHHHH	69.90	22902405
623	Phosphorylation	GGPGGGGSSGGPTIE CCCCCCCCCCCCCCC	29.14	30240740
624	Phosphorylation	GPGGGGSSGGPTIEE CCCCCCCCCCCCCCC	51.55	16641100

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

Oops, there are no upstream regulatory protein records of HSP72_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HSP72_RAT !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of HSP72_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of HSP72_RAT !!

Drug and Disease Associations

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