DJB12_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DJB12_MOUSE
• UniProt AC: Q9QYI4
• Protein Name: DnaJ homolog subfamily B member 12 {ECO:0000312|MGI:MGI:1931881}
• Gene Name: Dnajb12 {ECO:0000312|MGI:MGI:1931881}
• Organism: Mus musculus (Mouse).
• Sequence Length: 376
• Subcellular Localization: Endoplasmic reticulum membrane ; Single-pass membrane protein . Nucleus membrane ; Single-pass membrane protein . Localizes to the endoplasmic reticulum membrane. When overexpressed, forms membranous structures in the nucleus.
• Protein Description: Acts as a co-chaperone with HSPA8/Hsc70; required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum-associated degradation (ERAD) pathway. Acts by determining HSPA8/Hsc70's ATPase and polypeptide-binding activities. Can also act independently of HSPA8/Hsc70: together with DNAJB14, acts as a chaperone that promotes maturation of potassium channels KCND2 and KCNH2 by stabilizing nascent channel subunits and assembling them into tetramers. While stabilization of nascent channel proteins is dependent on HSPA8/Hsc70, the process of oligomerization of channel subunits is independent of HSPA8/Hsc70. When overexpressed, forms membranous structures together with DNAJB14 and HSPA8/Hsc70 within the nucleus; the role of these structures, named DJANGOs, is still unclear..
• Protein Sequence: MESNKDEAERCISIALKAIQSNQPERALRFLEKAQRLYPTPRVSALIESLNQKPQSTGDHPQPTDTTHTTTKKAGGTETPSANGEAGGGESAKGYTSEQVAAVKRVKQCKDYYEILGVSRSASDEDLKKAYRKLALKFHPDKNHAPGATEAFKAIGTAYAVLSNPEKRKQYDQFGDDKSQAARHGHSHGDFHRGFEADISPEDLFNMFFGGGFPSSNVHVYSNGRMRYTYQQRQDRRDNQGDGGLGVFVQLMPILILILVSALSQLMVSSPPYSLSPRPSVGHIHKRVTDHLNVAYYVADTFSEEYTGSSLKTVERNVEDDYIANLRNNCWKEKQQKEGLLYRARYFGDTDMYHRAQKMGTPSCNRLSEVQASLHG

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
1	Acetylation	-------MESNKDEA -------CCCCHHHH	13.22	-
33	Ubiquitination	RALRFLEKAQRLYPT HHHHHHHHHHHHCCC	52.55	27667366
33	Malonylation	RALRFLEKAQRLYPT HHHHHHHHHHHHCCC	52.55	26320211
79	Phosphorylation	KKAGGTETPSANGEA EECCCCCCCCCCCCC	23.52	29899451
97	Phosphorylation	ESAKGYTSEQVAAVK CCCCCCCHHHHHHHH	19.97	27841257
104	Ubiquitination	SEQVAAVKRVKQCKD HHHHHHHHHHHHCCC	46.90	-
104	Malonylation	SEQVAAVKRVKQCKD HHHHHHHHHHHHCCC	46.90	26320211
123	Phosphorylation	LGVSRSASDEDLKKA HCCCCCCCHHHHHHH	42.66	27841257
142	Ubiquitination	ALKFHPDKNHAPGAT HHHHCCCCCCCCCHH	55.90	-
167	Ubiquitination	AVLSNPEKRKQYDQF HHHCCHHHHHHHHHH	67.18	27667366
169	Ubiquitination	LSNPEKRKQYDQFGD HCCHHHHHHHHHHCC	65.36	-
178	Ubiquitination	YDQFGDDKSQAARHG HHHHCCCHHHHHHHC	49.56	27667366
179	Phosphorylation	DQFGDDKSQAARHGH HHHCCCHHHHHHHCC	31.85	28066266
337	Ubiquitination	CWKEKQQKEGLLYRA CHHHHHHHCCHHHHH	51.78	27667366

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

Oops, there are no upstream regulatory protein records of DJB12_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DJB12_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 DJB12_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of DJB12_MOUSE !!

Drug and Disease Associations

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