dbPTM

HS105_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HS105_RAT
UniProt AC	Q66HA8
Protein Name	Heat shock protein 105 kDa
Gene Name	Hsph1
Organism	Rattus norvegicus (Rat).
Sequence Length	858
Subcellular Localization	Cytoplasm .
Protein Description	Acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering substrate release. Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities..
Protein Sequence	MSVVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGPKNRTIGVAAKNQQITHANNTVSSFKRFHGRAFNDPFIQKEKENLSYDLVPMKNGGVGIKVMYMDEDHLFSVEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQIVGLNCLRLMNDMTAVALNYGIYKQDLPNADEKPRVVVFVDMGHSSFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLVEHFCAEFKTKYKLDAKSKIRALLRLHQECEKLKKLMSSNSTDLPLNIECFMNDKDVSAKMNRSQFEELCAELLQKIEVPLHLLMEQTHLKTEEVSAIEIVGGATRIPAVKERIARFFGKDVSTTLNADEAVARGCALQCAILSPAFKVREFSVTDAVPFPISLVWNHDSEETEGVHEVFSRNHAAPFSKVLTFLRRGPFELEAFYSDPQAVPYPEAKIGRFVVQNVSAQKDGEKSKVKVKVRVNTHGIFTISTASMVEKVPTEEEDGSSVEADMECPNQKPAESSDVDKNIQQDNSEAGTQPQVQTDGQQTSQSPPSPELTSEENKIPDADKANEKKVDQPPEAKKPKIKVVNVELPVEANLVWQLGRDLLNMYIETEGKMIMQDKLEKERNDAKNAVEECVYEFRDKLCGPYEKFICEQEHEKFLRLLTETEDWLYEEGEDQAKQAYIDKLEELMKMGTPVKVRFQEAEERPRVLEELGQRLQHYAKIAADFRGKDEKYNHIDESEMKKVEKSVNEVMEWMNNVMNAQAKRSLHQDPVVRTHEISAKVKELNNVCEPVVTQPKPKIESPKLERTPNGPNMDKKEDLEGKSNLGADAPHQNGECHPNEKGSVSMDLD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSVVGLDVG ------CCEEEEECC	26.05	-
34	S-nitrosocysteine	ANEFSDRCTPSVISF HHHCHHCCCCCCEEE	8.67	-
34	S-nitrosylation	ANEFSDRCTPSVISF HHHCHHCCCCCCEEE	8.67	22178444
40	Phosphorylation	RCTPSVISFGPKNRT CCCCCCEEECCCCCE	23.22	23984901
58	Phosphorylation	AAKNQQITHANNTVS EEECCEEECCCCCHH	15.59	23984901
63	Phosphorylation	QITHANNTVSSFKRF EEECCCCCHHHHHHH	22.90	23984901
65	Phosphorylation	THANNTVSSFKRFHG ECCCCCHHHHHHHCC	28.19	23984901
66	Phosphorylation	HANNTVSSFKRFHGR CCCCCHHHHHHHCCC	30.37	23984901
95	Ubiquitination	SYDLVPMKNGGVGIK CCCEEECCCCCEEEE	46.50	-
194	Acetylation	DLPNADEKPRVVVFV CCCCCCCCCEEEEEE	38.38	22902405
234	Acetylation	FDPFLGGKNFDEKLV CCHHCCCCCCCHHHH	53.28	174285
363	Phosphorylation	RFFGKDVSTTLNADE HHHCCCHHHCCCHHH	26.30	23984901
364	Phosphorylation	FFGKDVSTTLNADEA HHCCCHHHCCCHHHH	34.84	23984901
365	Phosphorylation	FGKDVSTTLNADEAV HCCCHHHCCCHHHHH	15.54	23984901
384	Phosphorylation	ALQCAILSPAFKVRE HHHHHHHCCCEEEEE	14.20	23984901
388	Ubiquitination	AILSPAFKVREFSVT HHHCCCEEEEEEECC	42.35	-
430	Acetylation	NHAAPFSKVLTFLRR CCCCCHHHHHHHHHH	41.46	22902405
471	Acetylation	VQNVSAQKDGEKSKV EEECCCCCCCCCCCE	68.37	-
486	Phosphorylation	KVKVRVNTHGIFTIS EEEEEECCCCEEEEE	20.72	22108457
503	Phosphorylation	SMVEKVPTEEEDGSS CEEEECCCCCCCCCC	60.04	28551015
509	Phosphorylation	PTEEEDGSSVEADME CCCCCCCCCCEECCC	43.46	28551015
510	Phosphorylation	TEEEDGSSVEADMEC CCCCCCCCCEECCCC	29.52	28551015
525	Phosphorylation	PNQKPAESSDVDKNI CCCCCCCCCCCCHHH	33.66	23984901
526	Phosphorylation	NQKPAESSDVDKNIQ CCCCCCCCCCCHHHH	32.91	23984901
537	Phosphorylation	KNIQQDNSEAGTQPQ HHHHCCCCCCCCCCC	36.79	28689409
541	Phosphorylation	QDNSEAGTQPQVQTD CCCCCCCCCCCEECC	44.09	28689409
547	Phosphorylation	GTQPQVQTDGQQTSQ CCCCCEECCCCCCCC	43.15	27097102
552	Phosphorylation	VQTDGQQTSQSPPSP EECCCCCCCCCCCCC	22.35	27097102
553	Phosphorylation	QTDGQQTSQSPPSPE ECCCCCCCCCCCCCC	25.07	27097102
555	Phosphorylation	DGQQTSQSPPSPELT CCCCCCCCCCCCCCC	38.25	27097102
558	Phosphorylation	QTSQSPPSPELTSEE CCCCCCCCCCCCCCC	34.10	27097102
562	Phosphorylation	SPPSPELTSEENKIP CCCCCCCCCCCCCCC	32.22	27097102
563	Phosphorylation	PPSPELTSEENKIPD CCCCCCCCCCCCCCC	56.38	27097102
627	Acetylation	GKMIMQDKLEKERND CCHHHHHHHHHHHHH	41.47	7714087
644	Phosphorylation	NAVEECVYEFRDKLC HHHHHHHHHHHHHHC	22.47	21940666
678	Phosphorylation	TETEDWLYEEGEDQA HHCCHHHHHCCHHHH	14.00	-
689	Phosphorylation	EDQAKQAYIDKLEEL HHHHHHHHHHHHHHH	13.73	-
774	Phosphorylation	MNAQAKRSLHQDPVV HHHHHHHHHCCCCCH	29.51	23984901
810	Phosphorylation	QPKPKIESPKLERTP CCCCCCCCCCCCCCC	30.70	23712012
816	Phosphorylation	ESPKLERTPNGPNMD CCCCCCCCCCCCCCC	16.25	30240740
852	Phosphorylation	CHPNEKGSVSMDLD- CCCCCCCCCCCCCC-	23.30	28551015
854	Phosphorylation	PNEKGSVSMDLD--- CCCCCCCCCCCC---	14.31	28432305

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
Oops, there are no upstream regulatory protein records of HS105_RAT !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
509	S	Phosphorylation		-
Phosphorylation on Ser-509 may be important for regulation of the HSPA8/HSC70 chaperone activity.

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 HS105_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of HS105_RAT !!

Drug and Disease Associations

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

Regulatory Network of HS105_RAT

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS."; Moser K., White F.M.; J. Proteome Res. 5:98-104(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-810, AND MASSSPECTROMETRY.	16396499 [Abstract]

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