HSP7C_BOVIN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HSP7C_BOVIN
• UniProt AC: P19120
• Protein Name: Heat shock cognate 71 kDa protein
• Gene Name: HSPA8
• Organism: Bos taurus (Bovine).
• Sequence Length: 650
• 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: MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIINWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQSAGGMPGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD

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
2	Acetylation	------MSKGPAVGI ------CCCCCEEEE	46.44	-
108	Acetylation	PKVQVEYKGETKSFY CEEEEEECCCEECCC	36.44	-
153	Phosphorylation	VPAYFNDSQRQATKD EECCCCHHHCCHHCC	28.50	-
246	Acetylation	NHFIAEFKRKHKKDI HHHHHHHHHHHHCCC	52.63	-
319	Acetylation	GTLDPVEKALRDAKL CCCCHHHHHHHHCCC	53.61	-
319	Succinylation	GTLDPVEKALRDAKL CCCCHHHHHHHHCCC	53.61	-
319	Succinylation	GTLDPVEKALRDAKL CCCCHHHHHHHHCCC	53.61	-
328	Acetylation	LRDAKLDKSQIHDIV HHHCCCCHHHCCEEE	55.48	-
329	Phosphorylation	RDAKLDKSQIHDIVL HHCCCCHHHCCEEEE	33.75	-
362	Phosphorylation	NGKELNKSINPDEAV CCCCCCCCCCHHHHH	26.90	-
469	Methylation	TGIPPAPRGVPQIEV ECCCCCCCCCCEEEE	61.93	-
512	Succinylation	NDKGRLSKEDIERMV CCCCCCCHHHHHHHH	65.09	-
512	Succinylation	NDKGRLSKEDIERMV CCCCCCCHHHHHHHH	65.09	-
512	Acetylation	NDKGRLSKEDIERMV CCCCCCCHHHHHHHH	65.09	-
524	Acetylation	RMVQEAEKYKAEDEK HHHHHHHHHCHHCHH	60.13	-
541	Phosphorylation	DKVSSKNSLESYAFN HHCCCCHHHHHHHHE	36.93	-
561	Methylation	EDEKLQGKINDEDKQ CCHHHCCCCCHHHHH	25.94	-
561	"N6,N6,N6-trimethyllysine"	EDEKLQGKINDEDKQ CCHHHCCCCCHHHHH	25.94	-
589	Acetylation	DKNQTAEKEEFEHQQ CCCCHHHHHHHHHHH	61.14	-
597	Acetylation	EEFEHQQKELEKVCN HHHHHHHHHHHHHHH	58.66	-
601	Acetylation	HQQKELEKVCNPIIT HHHHHHHHHHHHHHH	65.79	-

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

Oops, there are no upstream regulatory protein records of HSP7C_BOVIN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HSP7C_BOVIN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of HSP7C_BOVIN !!

Protein-Protein Interaction

Oops, there are no PPI records of HSP7C_BOVIN !!

Drug and Disease Associations

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