dbPTM

HS105_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HS105_MOUSE
UniProt AC	Q61699
Protein Name	Heat shock protein 105 kDa
Gene Name	Hsph1
Organism	Mus musculus (Mouse).
Sequence Length	858
Subcellular Localization	Cytoplasm . Nucleus . Strictly cytoplasmic in neurons.
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 client/substrate protein release (By similarity). 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. [PubMed: 14644449]
Protein Sequence	MSVVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSSFKRFHGRAFNDPFIQKEKENLSYDLVPMKNGGVGIKVMYMDEEHFFSVEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQIVGLNCLRLMNDMTAVALNYGIYKQDLPNAEEKPRVVVFVDMGHSSFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLVEHFCAEFKTKYKLDAKSKIRALLRLHQECEKLKKLMSSNSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIEVPLHSLMAQTQLKAEDVSAIEIVGGATRIPAVKERIAKFFGKDVSTTLNADEAVARGCALQCAILSPAFKVREFSVTDAVPFPISLVWNHDSEETEGVHEVFSRNHAAPFSKVLTFLRRGPFELEAFYSDPQGVPYPEAKIGRFVVQNVSAQKDGEKSRVKVKVRVNTHGIFTISTASMVEKVPTEEEDGSSLEADMECPNQRPTESSDVDKNIQQDNSEAGTQPQVQTDGQQTSQSPPSPELTSEESKTPDADKANEKKVDQPPEAKKPKIKVVNVELPVEANLVWQLGRDLLNMYIETEGKMIMQDKLEKERNDAKNAVEECVYEFRDKLCGPYEKFICEQEHEKFLRLLTETEDWLYEEGEDQAKQAYIDKLEELMKMGTPVKVRFQEAEERPKVLEELGQRLQHYAKIAADFRGKDEKYNHIDESEMKKVEKSVNEVMEWMNNVMNAQAKRSLDQDPVVRTHEIRAKVKELNNVCEPVVTQPKPKIESPKLERTPNGPNIDKKEDLEGKNNLGAEAPHQNGECHPNEKGSVNMDLD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSVVGLDVG ------CCEEEEECC	26.05	25293948
2	Acetylation	------MSVVGLDVG ------CCEEEEECC	26.05	-
10	Phosphorylation	VVGLDVGSQSCYIAV EEEEECCCCEEEEEH	20.83	25293948
12	Phosphorylation	GLDVGSQSCYIAVAR EEECCCCEEEEEHHH	15.58	25293948
14	Phosphorylation	DVGSQSCYIAVARAG ECCCCEEEEEHHHCC	9.36	25293948
34	Glutathionylation	ANEFSDRCTPSVISF HHHCCCCCCCCEEEE	8.67	24333276
43	Phosphorylation	PSVISFGSKNRTIGV CCEEEECCCCCEEEE	25.42	18779572
63	Phosphorylation	QITHANNTVSSFKRF EEECCCCCHHHHHHH	22.90	28285833
65	Phosphorylation	THANNTVSSFKRFHG ECCCCCHHHHHHHCC	28.19	23684622
66	Phosphorylation	HANNTVSSFKRFHGR CCCCCHHHHHHHCCC	30.37	23684622
68	Acetylation	NNTVSSFKRFHGRAF CCCHHHHHHHCCCCC	56.98	129941
95	Ubiquitination	SYDLVPMKNGGVGIK CCCEEECCCCCEEEE	46.50	22790023
114	Ubiquitination	DEEHFFSVEQITAML CHHHCCCHHHHHHHH	5.47	27667366
140	S-palmitoylation	LKKPVTDCVISVPSF CCCCCCCEEEECCCC	1.82	28680068
167	Glutathionylation	AQIVGLNCLRLMNDM HHHHCHHHHHHHCHH	2.55	24333276
206	Phosphorylation	VFVDMGHSSFQVSAC EEEECCCCCEEEEEE	27.41	25159016
207	Phosphorylation	FVDMGHSSFQVSACA EEECCCCCEEEEEEE	17.64	25159016
211	Phosphorylation	GHSSFQVSACAFNKG CCCCEEEEEEEECCC	13.57	25159016
221	Acetylation	AFNKGKLKVLGTAFD EECCCCEEEEEEECC	38.61	22826441
234	Ubiquitination	FDPFLGGKNFDEKLV CCHHCCCCCCCHHHH	53.28	22790023
263	Ubiquitination	AKSKIRALLRLHQEC HHHHHHHHHHHHHHH	1.73	27667366
278	Phosphorylation	EKLKKLMSSNSTDLP HHHHHHHHCCCCCCC	36.48	26643407
279	Phosphorylation	KLKKLMSSNSTDLPL HHHHHHHCCCCCCCC	22.34	26643407
281	Phosphorylation	KKLMSSNSTDLPLNI HHHHHCCCCCCCCEE	25.83	26643407
282	Phosphorylation	KLMSSNSTDLPLNIE HHHHCCCCCCCCEEE	45.89	26643407
310	S-palmitoylation	RSQFEELCAELLQKI HHHHHHHHHHHHHHC	2.90	28680068
356	Ubiquitination	AVKERIAKFFGKDVS HHHHHHHHHHCCCHH	38.56	27667366
375	Ubiquitination	ADEAVARGCALQCAI HHHHHHHHHHHHHHH	7.42	27667366
376	Glutathionylation	DEAVARGCALQCAIL HHHHHHHHHHHHHHH	2.59	24333276
378	Ubiquitination	AVARGCALQCAILSP HHHHHHHHHHHHHCC	5.10	27667366
380	Glutathionylation	ARGCALQCAILSPAF HHHHHHHHHHHCCCE	2.37	24333276
384	Phosphorylation	ALQCAILSPAFKVRE HHHHHHHCCCEEEEE	14.20	26745281
388	Ubiquitination	AILSPAFKVREFSVT HHHCCCEEEEEEECC	42.35	-
429	Phosphorylation	RNHAAPFSKVLTFLR CCCCCCHHHHHHHHH	22.31	22324799
458	Ubiquitination	GVPYPEAKIGRFVVQ CCCCCHHHHCCEEEE	43.99	22790023
468	Phosphorylation	RFVVQNVSAQKDGEK CEEEEECCCCCCCCC	32.31	27841257
471	Ubiquitination	VQNVSAQKDGEKSRV EEECCCCCCCCCCCE	68.37	22790023
471	Acetylation	VQNVSAQKDGEKSRV EEECCCCCCCCCCCE	68.37	23806337
486	Phosphorylation	KVKVRVNTHGIFTIS EEEEEECCCCEEEEE	20.72	28833060
490	Ubiquitination	RVNTHGIFTISTASM EECCCCEEEEEECHH	6.17	27667366
503	Phosphorylation	SMVEKVPTEEEDGSS HHEEECCCCCCCCCC	60.04	25521595
509	Phosphorylation	PTEEEDGSSLEADME CCCCCCCCCCCCCCC	44.03	25521595
510	Phosphorylation	TEEEDGSSLEADMEC CCCCCCCCCCCCCCC	35.44	25521595
523	Phosphorylation	ECPNQRPTESSDVDK CCCCCCCCCCHHCHH	51.17	23984901
525	Phosphorylation	PNQRPTESSDVDKNI CCCCCCCCHHCHHHH	34.02	23984901
526	Phosphorylation	NQRPTESSDVDKNIQ CCCCCCCHHCHHHHH	35.11	23984901
537	Phosphorylation	KNIQQDNSEAGTQPQ HHHHCCCCCCCCCCC	36.79	25619855
541	Phosphorylation	QDNSEAGTQPQVQTD CCCCCCCCCCCEECC	44.09	25619855
547	Phosphorylation	GTQPQVQTDGQQTSQ CCCCCEECCCCCCCC	43.15	25619855
552	Phosphorylation	VQTDGQQTSQSPPSP EECCCCCCCCCCCCC	22.35	25619855
553	Phosphorylation	QTDGQQTSQSPPSPE ECCCCCCCCCCCCCC	25.07	25619855
555	Phosphorylation	DGQQTSQSPPSPELT CCCCCCCCCCCCCCC	38.25	27087446
558	Phosphorylation	QTSQSPPSPELTSEE CCCCCCCCCCCCCCC	34.10	25521595
562	Phosphorylation	SPPSPELTSEESKTP CCCCCCCCCCCCCCC	32.22	22942356
563	Phosphorylation	PPSPELTSEESKTPD CCCCCCCCCCCCCCC	52.57	25521595
566	Phosphorylation	PELTSEESKTPDADK CCCCCCCCCCCCHHH	37.47	25619855
568	Phosphorylation	LTSEESKTPDADKAN CCCCCCCCCCHHHHH	35.36	23375375
611	Ubiquitination	VWQLGRDLLNMYIET HHHHHHHHHHHHHHH	3.42	27667366
627	Acetylation	GKMIMQDKLEKERND CCHHHHHHHHHHHHH	41.47	7714081
642	S-nitrosocysteine	AKNAVEECVYEFRDK HHHHHHHHHHHHHHH	2.21	-
642	S-nitrosylation	AKNAVEECVYEFRDK HHHHHHHHHHHHHHH	2.21	20925432
644	Phosphorylation	NAVEECVYEFRDKLC HHHHHHHHHHHHHHC	22.47	25263469
656	Acetylation	KLCGPYEKFICEQEH HHCCCHHHHCCHHHH	33.90	22826441
659	Glutathionylation	GPYEKFICEQEHEKF CCHHHHCCHHHHHHH	5.06	24333276
660	Ubiquitination	PYEKFICEQEHEKFL CHHHHCCHHHHHHHH	54.94	27667366
665	Acetylation	ICEQEHEKFLRLLTE CCHHHHHHHHHHHHH	52.16	22826441
665	Ubiquitination	ICEQEHEKFLRLLTE CCHHHHHHHHHHHHH	52.16	22790023
701	Phosphorylation	EELMKMGTPVKVRFQ HHHHHCCCCEEEEHH	22.78	24759943
704	Ubiquitination	MKMGTPVKVRFQEAE HHCCCCEEEEHHHHH	28.97	27667366
723	Ubiquitination	VLEELGQRLQHYAKI HHHHHHHHHHHHHHH	34.22	27667366
750	Ubiquitination	HIDESEMKKVEKSVN CCCHHHHHHHHHHHH	50.01	22790023
774	Phosphorylation	MNAQAKRSLDQDPVV HHHHHHHCCCCCCCC	35.27	24759943
791	Ubiquitination	HEIRAKVKELNNVCE HHHHHHHHHHCCCCC	56.64	22790023
810	Phosphorylation	QPKPKIESPKLERTP CCCCCCCCCCCCCCC	30.70	27087446
812	Ubiquitination	KPKIESPKLERTPNG CCCCCCCCCCCCCCC	72.72	22790023
816	Phosphorylation	ESPKLERTPNGPNID CCCCCCCCCCCCCCC	16.25	25263469
824	Ubiquitination	PNGPNIDKKEDLEGK CCCCCCCHHHHCCCC	55.02	-
852	Phosphorylation	CHPNEKGSVNMDLD- CCCCCCCCCCCCCC-	22.76	25521595

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
509	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
509	S	Phosphorylation	Kinase	CSK21	Q60737	PhosphoELM
509	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
509	S	Phosphorylation		12558502
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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TBA1A_MOUSE	Tuba1a	physical	12749852
B2CL1_HUMAN	BCL2L1	physical	26496610
IF2G_HUMAN	EIF2S3	physical	26496610
DNJB1_HUMAN	DNAJB1	physical	26496610
PLD1_HUMAN	PLD1	physical	26496610
RUXG_HUMAN	SNRPG	physical	26496610
USP9Y_HUMAN	USP9Y	physical	26496610
BAZ1B_HUMAN	BAZ1B	physical	26496610
BUB3_HUMAN	BUB3	physical	26496610
DNJB4_HUMAN	DNAJB4	physical	26496610
XPOT_HUMAN	XPOT	physical	26496610
TUSC2_HUMAN	TUSC2	physical	26496610
T11L1_HUMAN	TCP11L1	physical	26496610
ZNFX1_HUMAN	ZNFX1	physical	26496610
ANO3_HUMAN	ANO3	physical	26496610
USMG5_HUMAN	USMG5	physical	26496610

Drug and Disease Associations

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

Regulatory Network of HS105_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-810, AND MASSSPECTROMETRY.	19131326 [Abstract]
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-810, AND MASSSPECTROMETRY.	19144319 [Abstract]
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-810, AND MASSSPECTROMETRY.	17114649 [Abstract]
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-558, AND MASSSPECTROMETRY.	15345747 [Abstract]
"Protein kinase CK2 phosphorylates Hsp105 alpha at Ser509 andmodulates its function."; Ishihara K., Yamagishi N., Hatayama T.; Biochem. J. 371:917-925(2003). Cited for: PHOSPHORYLATION AT SER-509.	12558502 [Abstract]

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