dbPTM

DNJC5_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DNJC5_RAT
UniProt AC	P60905
Protein Name	DnaJ homolog subfamily C member 5 {ECO:0000305}
Gene Name	Dnajc5 {ECO:0000312\|RGD:620516}
Organism	Rattus norvegicus (Rat).
Sequence Length	198
Subcellular Localization	Membrane Lipid-anchor . Melanosome . Cell membrane .
Protein Description	Acts as a general chaperone in regulated exocytosis (By similarity). Acts as a co-chaperone for the SNARE protein SNAP-25 (By similarity). Involved in the calcium-mediated control of a late stage of exocytosis (By similarity). May have an important role in presynaptic function. May be involved in calcium-dependent neurotransmitter release at nerve endings (By similarity)..
Protein Sequence	MADQRQRSLSTSGESLYHVLGLDKNATSDDIKKSYRKLALKYHPDKNPDNPEAADKFKEINNAHAILTDATKRNIYDKYGSLGLYVAEQFGEENVNTYFVLSSWWAKALFVVCGLLTCCYCCCCLCCCFNCCCGKCKPKAPEGEETEFYVSPEDLEAQLQSDEREATDTPIVIQPASATETTQLTADSHPSYHTDGFN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MADQRQRSLSTSGES CCHHHHHHCCCCCCH	20.52	23712012
10	Phosphorylation	DQRQRSLSTSGESLY HHHHHHCCCCCCHHH	23.05	23712012
11	Phosphorylation	QRQRSLSTSGESLYH HHHHHCCCCCCHHHH	46.15	27097102
12	Phosphorylation	RQRSLSTSGESLYHV HHHHCCCCCCHHHHH	36.87	28689409
15	Phosphorylation	SLSTSGESLYHVLGL HCCCCCCHHHHHHCC	37.44	27097102
17	Phosphorylation	STSGESLYHVLGLDK CCCCCHHHHHHCCCC	10.12	27097102
34	Phosphorylation	TSDDIKKSYRKLALK CHHHHHHHHHHHHHH	25.76	30240740
41	Ubiquitination	SYRKLALKYHPDKNP HHHHHHHHHCCCCCC	35.59	-
56	Acetylation	DNPEAADKFKEINNA CCHHHHHHHHHHHHH	54.32	22902405
56	Ubiquitination	DNPEAADKFKEINNA CCHHHHHHHHHHHHH	54.32	-
58	Ubiquitination	PEAADKFKEINNAHA HHHHHHHHHHHHHHH	64.52	-
72	Ubiquitination	AILTDATKRNIYDKY HHCCHHHHCCHHHHH	45.21	-
149	Phosphorylation	EGEETEFYVSPEDLE CCCCCEEEECHHHHH	8.19	28551015
151	Phosphorylation	EETEFYVSPEDLEAQ CCCEEEECHHHHHHH	15.93	28551015
167	Phosphorylation	QSDEREATDTPIVIQ HCCCCCCCCCCEEEE	35.34	28432305
169	Phosphorylation	DEREATDTPIVIQPA CCCCCCCCCEEEECC	15.57	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
10	S	Phosphorylation	Kinase	AKT1	P31749	PSP
10	S	Phosphorylation	Kinase	PRKACA	P27791	GPS
10	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
10	S	Phosphorylation	11604405
Ser-10 phosphorylation induces an order-to-disorder transition triggering the interaction with Lys-58 (By similarity).
58	K	Phosphorylation	11931641
Ser-10 phosphorylation induces an order-to-disorder transition triggering the interaction with Lys-58 (By similarity).

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 DNJC5_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of DNJC5_RAT !!

Drug and Disease Associations

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

Regulatory Network of DNJC5_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-10, AND MASSSPECTROMETRY.	16396499 [Abstract]