HSP72_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HSP72_MOUSE
• UniProt AC: P17156
• Protein Name: Heat shock-related 70 kDa protein 2
• Gene Name: Hspa2
• Organism: Mus musculus (Mouse).
• Sequence Length: 633
• Subcellular Localization: Cytoplasm, cytoskeleton, spindle . Colocalizes with SHCBP1L at spindle during the meiosis process (PubMed:24557841).
• 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 (By similarity). Plays a role in spermatogenesis. [PubMed: 24557841 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
16	Phosphorylation	GIDLGTTYSCVGVFQ EEECCCCEEEEEEEE	10.42	15592455
38	Phosphorylation	ANDQGNRTTPSYVAF ECCCCCCCCCCEEEE	47.24	20415495
39	Phosphorylation	NDQGNRTTPSYVAFT CCCCCCCCCCEEEEE	13.65	25367039
41	Phosphorylation	QGNRTTPSYVAFTDT CCCCCCCCEEEEECH	30.10	24899341
42	Phosphorylation	GNRTTPSYVAFTDTE CCCCCCCEEEEECHH	9.30	22817900
46	Phosphorylation	TPSYVAFTDTERLIG CCCEEEEECHHHHHH	32.07	28066266
48	Phosphorylation	SYVAFTDTERLIGDA CEEEEECHHHHHHHH	21.68	25367039
57	Ubiquitination	RLIGDAAKNQVAMNP HHHHHHHHCCCCCCC	50.02	27667366
72	Acetylation	TNTIFDAKRLIGRKF CCCHHHHHHHHCCCC	49.97	7822229
78	Ubiquitination	AKRLIGRKFEDATVQ HHHHHCCCCCCCCCC	48.14	-
103	Ubiquitination	VSEGGKPKVQVEYKG EECCCCCEEEEEECC	49.11	27667366
114	Phosphorylation	EYKGEMKTFFPEEIS EECCEEEEECHHHHH	29.24	25777480
121	Phosphorylation	TFFPEEISSMVLTKM EECHHHHHHHHHHHH	18.70	25777480
122	Phosphorylation	FFPEEISSMVLTKMK ECHHHHHHHHHHHHH	20.69	25777480
126	Phosphorylation	EISSMVLTKMKEIAE HHHHHHHHHHHHHHH	20.06	25777480
127	Ubiquitination	ISSMVLTKMKEIAEA HHHHHHHHHHHHHHH	43.76	27667366
129	Acetylation	SMVLTKMKEIAEAYL HHHHHHHHHHHHHHH	47.74	23806337
129	Succinylation	SMVLTKMKEIAEAYL HHHHHHHHHHHHHHH	47.74	23806337
129	Ubiquitination	SMVLTKMKEIAEAYL HHHHHHHHHHHHHHH	47.74	27667366
160	Ubiquitination	DSQRQATKDAGTITG HHHCCCCCCCCCCCC	48.90	-
164	Phosphorylation	QATKDAGTITGLNVL CCCCCCCCCCCCCHH	19.65	27180971
166	Phosphorylation	TKDAGTITGLNVLRI CCCCCCCCCCCHHEE	35.14	27180971
178	Phosphorylation	LRIINEPTAAAIAYG HEECCCCHHHHHHHC	23.81	-
184	Phosphorylation	PTAAAIAYGLDKKGC CHHHHHHHCCCCCCC	16.47	23984901
188	Succinylation	AIAYGLDKKGCAGGE HHHHCCCCCCCCCCC	56.99	23806337
188	Malonylation	AIAYGLDKKGCAGGE HHHHCCCCCCCCCCC	56.99	26320211
188	Ubiquitination	AIAYGLDKKGCAGGE HHHHCCCCCCCCCCC	56.99	27667366
188	Acetylation	AIAYGLDKKGCAGGE HHHHCCCCCCCCCCC	56.99	22826441
189	Ubiquitination	IAYGLDKKGCAGGEK HHHCCCCCCCCCCCC	59.91	-
189	Acetylation	IAYGLDKKGCAGGEK HHHCCCCCCCCCCCC	59.91	155873
224	Phosphorylation	DGIFEVKSTAGDTHL CCEEEEEECCCCCCC	28.76	20139300
225	Phosphorylation	GIFEVKSTAGDTHLG CEEEEEECCCCCCCC	29.01	29233185
229	Phosphorylation	VKSTAGDTHLGGEDF EEECCCCCCCCCCCC	20.34	24899341
249	Acetylation	SHLAEEFKRKHKKDI HHHHHHHHHHHHHCC	64.91	7668493
268	Phosphorylation	RAVRRLRTACERAKR HHHHHHHHHHHHHHH	40.01	-
322	Ubiquitination	GTLEPVEKALRDAKL CCCHHHHHHHHHCCC	53.61	27667366
328	Ubiquitination	EKALRDAKLDKGQIQ HHHHHHCCCCCCCCC	62.60	-
348	Ubiquitination	GGSTRIPKIQKLLQD CCCCCHHHHHHHHHH	56.23	-
351	Acetylation	TRIPKIQKLLQDFFN CCHHHHHHHHHHHHC	55.42	22826441
351	Ubiquitination	TRIPKIQKLLQDFFN CCHHHHHHHHHHHHC	55.42	-
360	Ubiquitination	LQDFFNGKELNKSIN HHHHHCCCCCCCCCC	61.20	-
360	Acetylation	LQDFFNGKELNKSIN HHHHHCCCCCCCCCC	61.20	23806337
360	Succinylation	LQDFFNGKELNKSIN HHHHHCCCCCCCCCC	61.20	23954790
364	Acetylation	FNGKELNKSINPDEA HCCCCCCCCCCHHHH	66.39	22826441
365	Phosphorylation	NGKELNKSINPDEAV CCCCCCCCCCHHHHH	26.90	30352176
403	Phosphorylation	LLDVTPLSLGIETAG EEECCCCCCCEEECC	26.25	-
408	Phosphorylation	PLSLGIETAGGVMTP CCCCCEEECCCCCCC	28.78	-
414	Phosphorylation	ETAGGVMTPLIKRNT EECCCCCCCEEECCC	16.73	-
426	Ubiquitination	RNTTIPTKQTQTFTT CCCCCCCCCCEEEEE	46.09	27667366
454	Succinylation	EGERAMTKDNNLLGK ECCCCCCCCCCCCCC	45.43	23806337
454	Ubiquitination	EGERAMTKDNNLLGK ECCCCCCCCCCCCCC	45.43	27667366
454	Malonylation	EGERAMTKDNNLLGK ECCCCCCCCCCCCCC	45.43	26320211
454	Acetylation	EGERAMTKDNNLLGK ECCCCCCCCCCCCCC	45.43	23806337
461	Ubiquitination	KDNNLLGKFDLTGIP CCCCCCCCCCCCCCC	35.36	27667366
500	Ubiquitination	AADKSTGKENKITIT EECCCCCCCCCEEEE	59.19	27667366
503	Ubiquitination	KSTGKENKITITNDK CCCCCCCCEEEECCC	42.17	27667366
503	Malonylation	KSTGKENKITITNDK CCCCCCCCEEEECCC	42.17	26320211
510	Ubiquitination	KITITNDKGRLSKDD CEEEECCCCCCCHHH	48.26	27667366
529	Ubiquitination	VQEAERYKSEDEANR HHHHHHHHCCCHHHH	54.30	-
530	Phosphorylation	QEAERYKSEDEANRD HHHHHHHCCCHHHHH	41.15	29514104
542	Ubiquitination	NRDRVAAKNAVESYT HHHHHHHHHHHHHHE	35.38	-
560	Ubiquitination	KQTVEDEKLRGKISE EEHHCCHHHCCCCCH	56.67	27667366
564	"N6,N6,N6-trimethyllysine"	EDEKLRGKISEQDKN CCHHHCCCCCHHHHH	36.30	-
564	Methylation	EDEKLRGKISEQDKN CCHHHCCCCCHHHHH	36.30	-
595	Phosphorylation	QMAEKDEYEHKQKEL HHHCHHHHHHHHHHH	33.20	22802335
614	Phosphorylation	NPIISKLYQGGPGGG HHHHHHHHCCCCCCC	14.62	25293948
623	Phosphorylation	GGPGGGGSSGGPTIE CCCCCCCCCCCCCCC	29.14	25293948
624	Phosphorylation	GPGGGGSSGGPTIEE CCCCCCCCCCCCCCC	51.55	25293948
628	Phosphorylation	GGSSGGPTIEEVD-- CCCCCCCCCCCCC--	44.27	25293948

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

Oops, there are no upstream regulatory protein records of HSP72_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HSP72_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 HSP72_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NASP_MOUSE	Nasp	physical	19553603
CDK1_MOUSE	Cdk1	physical	9247342

Drug and Disease Associations

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