DNJA2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DNJA2_MOUSE
• UniProt AC: Q9QYJ0
• Protein Name: DnaJ homolog subfamily A member 2
• Gene Name: Dnaja2
• Organism: Mus musculus (Mouse).
• Sequence Length: 412
• Subcellular Localization: Membrane ; Lipid-anchor .
• Protein Description: Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro)..
• Protein Sequence: MANVADTKLYDILGVPPGASENELKKAYRKLAKEYHPDKNPNAGDKFKEISFAYEVLSNPEKRELYDRYGEQGLREGSGGGGGMDDIFSHIFGGGLFGFMGNQSRSRNGRRRGEDMMHPLKVSLEDLYNGKTTKLQLSKNVLCSACSGQGGKSGAVQKCSACRGRGVRIMIRQLAPGMVQQMQSVCSDCNGEGEVINEKDRCKKCEGKKVIKEVKILEVHVDKGMKHGQRITFTGEADQAPGVEPGDIVLLLQEKEHEVFQRDGNDLHMTYKIGLVEALCGFQFTFKHLDARQIVVKYPPGKVIEPGCVRVVRGEGMPQYRNPFEKGDLYIKFDVQFPENNWINPDKLSELEDLLPSRPEVPNVIGETEEVELQEFDSTRGSGGGQRREAYNDSSDEESSSHHGPGVQCAHQ

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
33	Ubiquitination	KAYRKLAKEYHPDKN HHHHHHHHHHCCCCC	70.06	27667366
39	Acetylation	AKEYHPDKNPNAGDK HHHHCCCCCCCCCHH	77.93	23806337
39	Ubiquitination	AKEYHPDKNPNAGDK HHHHCCCCCCCCCHH	77.93	27667366
39	Malonylation	AKEYHPDKNPNAGDK HHHHCCCCCCCCCHH	77.93	26320211
46	Ubiquitination	KNPNAGDKFKEISFA CCCCCCHHHHHCHHH	58.37	27667366
78	Phosphorylation	EQGLREGSGGGGGMD HHCCCCCCCCCCCHH	29.52	27180971
104	Phosphorylation	FGFMGNQSRSRNGRR HHHCCCCCCCCCCCC	35.90	29899451
123	Phosphorylation	MMHPLKVSLEDLYNG CCCCEECCHHHHHCC	25.18	27180971
128	Phosphorylation	KVSLEDLYNGKTTKL ECCHHHHHCCCCCEE	33.90	20469934
131	Ubiquitination	LEDLYNGKTTKLQLS HHHHHCCCCCEEEEC	49.75	-
134	Ubiquitination	LYNGKTTKLQLSKNV HHCCCCCEEEECCCE	39.19	27667366
134	Malonylation	LYNGKTTKLQLSKNV HHCCCCCEEEECCCE	39.19	26320211
144	Phosphorylation	LSKNVLCSACSGQGG ECCCEEEHHHCCCCC	28.31	29472430
147	Phosphorylation	NVLCSACSGQGGKSG CEEEHHHCCCCCCCC	33.59	25521595
152	Acetylation	ACSGQGGKSGAVQKC HHCCCCCCCCHHEEC	53.17	23806337
152	Ubiquitination	ACSGQGGKSGAVQKC HHCCCCCCCCHHEEC	53.17	-
152	Malonylation	ACSGQGGKSGAVQKC HHCCCCCCCCHHEEC	53.17	26320211
153	Phosphorylation	CSGQGGKSGAVQKCS HCCCCCCCCHHEECH	34.95	-
158	Ubiquitination	GKSGAVQKCSACRGR CCCCHHEECHHCCCC	24.45	-
184	Phosphorylation	GMVQQMQSVCSDCNG HHHHHHHHHHHHCCC	21.54	28285833
187	Phosphorylation	QQMQSVCSDCNGEGE HHHHHHHHHCCCCCC	42.94	25521595
255	Ubiquitination	IVLLLQEKEHEVFQR EEEEEECCCCHHHCC	51.95	-
280	S-palmitoylation	IGLVEALCGFQFTFK HHHHHHHHCCEEEEC	7.08	26165157
297	Ubiquitination	DARQIVVKYPPGKVI CCEEEEEECCCCCEE	40.94	27667366
302	Ubiquitination	VVKYPPGKVIEPGCV EEECCCCCEECCCCE	45.90	-
308	S-nitrosocysteine	GKVIEPGCVRVVRGE CCEECCCCEEEECCC	2.30	-
308	Glutathionylation	GKVIEPGCVRVVRGE CCEECCCCEEEECCC	2.30	24333276
308	S-nitrosylation	GKVIEPGCVRVVRGE CCEECCCCEEEECCC	2.30	21278135
326	Ubiquitination	QYRNPFEKGDLYIKF CCCCCCCCCCEEEEE	59.09	27667366
391	Phosphorylation	GGQRREAYNDSSDEE CCCCCCCCCCCCCCC	18.10	25159016
394	Phosphorylation	RREAYNDSSDEESSS CCCCCCCCCCCCHHC	35.73	23684622
395	Phosphorylation	REAYNDSSDEESSSH CCCCCCCCCCCHHCC	52.48	23684622
399	Phosphorylation	NDSSDEESSSHHGPG CCCCCCCHHCCCCCC	34.78	25159016
400	Phosphorylation	DSSDEESSSHHGPGV CCCCCCHHCCCCCCC	36.65	25159016
401	Phosphorylation	SSDEESSSHHGPGVQ CCCCCHHCCCCCCCC	28.87	25159016
409	Methylation	HHGPGVQCAHQ---- CCCCCCCCCCC----	3.20	-
409	Farnesylation	HHGPGVQCAHQ---- CCCCCCCCCCC----	3.20	-

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

Oops, there are no upstream regulatory protein records of DNJA2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DNJA2_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 DNJA2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of DNJA2_MOUSE !!

Drug and Disease Associations

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