dbPTM

DNJC5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DNJC5_HUMAN
UniProt AC	Q9H3Z4
Protein Name	DnaJ homolog subfamily C member 5 {ECO:0000305}
Gene Name	DNAJC5 {ECO:0000312\|HGNC:HGNC:16235}
Organism	Homo sapiens (Human).
Sequence Length	198
Subcellular Localization	Membrane Lipid-anchor . Melanosome . Cell membrane . Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
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	MADQRQRSLSTSGESLYHVLGLDKNATSDDIKKSYRKLALKYHPDKNPDNPEAADKFKEINNAHAILTDATKRNIYDKYGSLGLYVAEQFGEENVNTYFVLSSWWAKALFVFCGLLTCCYCCCCLCCCFNCCCGKCKPKAPEGEETEFYVSPEDLEAQLQSDEREATDTPIVIQPASATETTQLTADSHPSYHTDGFN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MADQRQRSLSTSGES CCHHHHHHCCCCCCH	20.52	29255136
10	Phosphorylation	DQRQRSLSTSGESLY HHHHHHCCCCCCHHH	23.05	29255136
11	Phosphorylation	QRQRSLSTSGESLYH HHHHHCCCCCCHHHH	46.15	29255136
12	Phosphorylation	RQRSLSTSGESLYHV HHHHCCCCCCHHHHH	36.87	22167270
15	Phosphorylation	SLSTSGESLYHVLGL HCCCCCCHHHHHHCC	37.44	22167270
17	Phosphorylation	STSGESLYHVLGLDK CCCCCHHHHHHCCCC	10.12	22167270
24	Ubiquitination	YHVLGLDKNATSDDI HHHHCCCCCCCHHHH	54.23	-
27	Phosphorylation	LGLDKNATSDDIKKS HCCCCCCCHHHHHHH	41.92	23401153
28	Phosphorylation	GLDKNATSDDIKKSY CCCCCCCHHHHHHHH	30.76	27080861
34	Phosphorylation	TSDDIKKSYRKLALK CHHHHHHHHHHHHHH	25.76	23312004
35	Phosphorylation	SDDIKKSYRKLALKY HHHHHHHHHHHHHHH	22.20	23312004
41	Acetylation	SYRKLALKYHPDKNP HHHHHHHHHCCCCCC	35.59	7774243
41	Ubiquitination	SYRKLALKYHPDKNP HHHHHHHHHCCCCCC	35.59	21890473
41 (in isoform 1)	Ubiquitination	-	35.59	21890473
41 (in isoform 2)	Ubiquitination	-	35.59	21890473
42	Phosphorylation	YRKLALKYHPDKNPD HHHHHHHHCCCCCCC	21.31	28152594
46 (in isoform 1)	Ubiquitination	-	74.88	21890473
46 (in isoform 2)	Ubiquitination	-	74.88	21890473
46	Ubiquitination	ALKYHPDKNPDNPEA HHHHCCCCCCCCHHH	74.88	21906983
56 (in isoform 1)	Ubiquitination	-	54.32	21890473
56 (in isoform 2)	Ubiquitination	-	54.32	21890473
56	Ubiquitination	DNPEAADKFKEINNA CCHHHHHHHHHHHHH	54.32	21890473
56	Acetylation	DNPEAADKFKEINNA CCHHHHHHHHHHHHH	54.32	19608861
58 (in isoform 1)	Ubiquitination	-	64.52	21890473
58	Ubiquitination	PEAADKFKEINNAHA HHHHHHHHHHHHHHH	64.52	21890473
58 (in isoform 2)	Ubiquitination	-	64.52	21890473
72 (in isoform 1)	Ubiquitination	-	45.21	21890473
72	Ubiquitination	AILTDATKRNIYDKY HHCCHHHHCCHHHHH	45.21	2190698
72	2-Hydroxyisobutyrylation	AILTDATKRNIYDKY HHCCHHHHCCHHHHH	45.21	-
72 (in isoform 2)	Ubiquitination	-	45.21	21890473
113	S-palmitoylation	AKALFVFCGLLTCCY HHHHHHHHHHHHHHH	2.93	28127059
118	S-palmitoylation	VFCGLLTCCYCCCCL HHHHHHHHHHHHHHH	1.25	28127059
119	S-palmitoylation	FCGLLTCCYCCCCLC HHHHHHHHHHHHHHH	2.16	28127059
121	S-palmitoylation	GLLTCCYCCCCLCCC HHHHHHHHHHHHHHH	0.62	28127059
122	S-palmitoylation	LLTCCYCCCCLCCCF HHHHHHHHHHHHHHH	0.49	28127059
123	S-palmitoylation	LTCCYCCCCLCCCFN HHHHHHHHHHHHHHH	1.45	28127059
124	S-palmitoylation	TCCYCCCCLCCCFNC HHHHHHHHHHHHHHH	1.71	28127059
126	S-palmitoylation	CYCCCCLCCCFNCCC HHHHHHHHHHHHHHC	0.88	28127059
127	S-palmitoylation	YCCCCLCCCFNCCCG HHHHHHHHHHHHHCC	1.59	28127059
128	S-palmitoylation	CCCCLCCCFNCCCGK HHHHHHHHHHHHCCC	2.40	28127059
131	S-palmitoylation	CLCCCFNCCCGKCKP HHHHHHHHHCCCCCC	0.73	28127059
132	S-palmitoylation	LCCCFNCCCGKCKPK HHHHHHHHCCCCCCC	3.44	28127059
133	S-palmitoylation	CCCFNCCCGKCKPKA HHHHHHHCCCCCCCC	6.77	28127059
136	S-palmitoylation	FNCCCGKCKPKAPEG HHHHCCCCCCCCCCC	5.75	28127059
146	Phosphorylation	KAPEGEETEFYVSPE CCCCCCCCEEEECHH	27.39	29978859
149 (in isoform 2)	Phosphorylation	-	8.19	24173317
149	Phosphorylation	EGEETEFYVSPEDLE CCCCCEEEECHHHHH	8.19	28796482
151	Phosphorylation	EETEFYVSPEDLEAQ CCCEEEECHHHHHHH	15.93	28442448
161 (in isoform 2)	Phosphorylation	-	50.46	25849741
161	Phosphorylation	DLEAQLQSDEREATD HHHHHHHCCCCCCCC	50.46	25849741
167	Phosphorylation	QSDEREATDTPIVIQ HCCCCCCCCCCEEEE	35.34	25002506
169	Phosphorylation	DEREATDTPIVIQPA CCCCCCCCCEEEECC	15.57	25002506
177	Phosphorylation	PIVIQPASATETTQL CEEEECCCCCCCEEC	42.27	26471730
179	Phosphorylation	VIQPASATETTQLTA EEECCCCCCCEECCC	31.22	24076635
181	Phosphorylation	QPASATETTQLTADS ECCCCCCCEECCCCC	18.58	26471730
182	Phosphorylation	PASATETTQLTADSH CCCCCCCEECCCCCC	18.49	29978859
185	Phosphorylation	ATETTQLTADSHPSY CCCCEECCCCCCCCC	20.71	29978859
188	Phosphorylation	TTQLTADSHPSYHTD CEECCCCCCCCCCCC	34.53	29978859
191	Phosphorylation	LTADSHPSYHTDGFN CCCCCCCCCCCCCCC	24.91	29978859
192	Phosphorylation	TADSHPSYHTDGFN- CCCCCCCCCCCCCC-	17.12	25884760
194	Phosphorylation	DSHPSYHTDGFN--- CCCCCCCCCCCC---	29.59	24719451

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	PRKACA	P17612	GPS
10	S	Phosphorylation	Kinase	PRKCG	P05129	GPS
34	S	Phosphorylation	Kinase	PRKCG	P05129	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.
58	K	Phosphorylation	27452402
Ser-10 phosphorylation induces an order-to-disorder transition triggering the interaction with Lys-58.

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CFTR_HUMAN	CFTR	physical	12039948
CHIP_HUMAN	STUB1	physical	19098309
HSP74_HUMAN	HSPA4	physical	19098309
VINC_HUMAN	VCL	physical	22939629
ECE1_HUMAN	ECE1	physical	22939629

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
162350	Ceroid lipofuscinosis, neuronal, 4B (CLN4B)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of DNJC5_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-41 AND LYS-56, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND MASSSPECTROMETRY.	19369195 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-15, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND MASSSPECTROMETRY.	16083285 [Abstract]
"Identification and characterization of phosphorylated proteins in thehuman pituitary."; Giorgianni F., Beranova-Giorgianni S., Desiderio D.M.; Proteomics 4:587-598(2004). Cited for: PHOSPHORYLATION AT SER-10.	14997482 [Abstract]

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