dbPTM

DJC17_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DJC17_HUMAN
UniProt AC	Q9NVM6
Protein Name	DnaJ homolog subfamily C member 17
Gene Name	DNAJC17
Organism	Homo sapiens (Human).
Sequence Length	304
Subcellular Localization	Cytoplasm . Nucleus . Predominantly nuclear.
Protein Description	May negatively affect PAX8-induced thyroglobulin/TG transcription..
Protein Sequence	MAVTKELLQMDLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAELFHQLSQALEVLTDAAARAAYDKVRKAKKQAAERTQKLDEKRKKVKLDLEARERQAQAQESEEEEESRSTRTLEQEIERLREEGSRQLEEQQRLIREQIRQERDQRLRGKAENTEGQGTPKLKLKWKCKKEDESKGGYSKDVLLRLLQKYGEVLNLVLSSKKPGTAVVEFATVKAAELAVQNEVGLVDNPLKISWLEGQPQDAVGRSHSGLSKGSVLSERDYESLVMMRMRQAAERQQLIARMQQEDQEGPPT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MAVTKELLQMD ----CCCCHHHHHHH	14.84	25262027
5	Methylation	---MAVTKELLQMDL ---CCCCHHHHHHHH	39.50	23644510
13	Phosphorylation	ELLQMDLYALLGIEE HHHHHHHHHHHCCHH	7.31	23403867
25	Methylation	IEEKAADKEVKKAYR CHHHHCCHHHHHHHH	60.73	23644510
42	Ubiquitination	ALSCHPDKNPDNPRA HHHCCCCCCCCCHHH	74.88	24816145
46	Ubiquitination	HPDKNPDNPRAAELF CCCCCCCCHHHHHHH	29.25	24816145
97	Acetylation	DEKRKKVKLDLEARE HHHHHHHHHHHHHHH	45.20	25953088
112	Phosphorylation	RQAQAQESEEEEESR HHHHHHHCHHHHHHH	37.92	29255136
118	Phosphorylation	ESEEEEESRSTRTLE HCHHHHHHHHHHHHH	34.51	24732914
120	Phosphorylation	EEEEESRSTRTLEQE HHHHHHHHHHHHHHH	31.36	27486199
121	Phosphorylation	EEEESRSTRTLEQEI HHHHHHHHHHHHHHH	26.94	27486199
123	Phosphorylation	EESRSTRTLEQEIER HHHHHHHHHHHHHHH	34.43	21815630
165	Phosphorylation	LRGKAENTEGQGTPK HCCCCCCCCCCCCCC	32.76	23403867
170	Phosphorylation	ENTEGQGTPKLKLKW CCCCCCCCCCEEEEE	14.90	23403867
210	Phosphorylation	EVLNLVLSSKKPGTA HHHHHHHCCCCCCEE	32.41	25247763
211	Phosphorylation	VLNLVLSSKKPGTAV HHHHHHCCCCCCEEE	40.30	25247763
225	Ubiquitination	VVEFATVKAAELAVQ EEEEEHHHHHHHHHH	37.21	21890473
229	Ubiquitination	ATVKAAELAVQNEVG EHHHHHHHHHHCCCC	4.92	21890473
264	Ubiquitination	RSHSGLSKGSVLSER CCCCCCCCCCCCCHH	61.31	29967540
264	Methylation	RSHSGLSKGSVLSER CCCCCCCCCCCCCHH	61.31	24129315
269	Phosphorylation	LSKGSVLSERDYESL CCCCCCCCHHHHHHH	28.56	28555341
273	Phosphorylation	SVLSERDYESLVMMR CCCCHHHHHHHHHHH	17.40	28796482
275	Phosphorylation	LSERDYESLVMMRMR CCHHHHHHHHHHHHH	21.75	28674419
304	Phosphorylation	EDQEGPPT------- HHCCCCCC-------	55.14	28674419

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
Oops, there are no upstream regulatory protein records of DJC17_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DJC17_HUMAN !!

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 DJC17_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CA123_HUMAN	C1orf123	physical	26344197
HSP7E_HUMAN	HSPA14	physical	26344197
GRP75_HUMAN	HSPA9	physical	26344197
HS105_HUMAN	HSPH1	physical	26344197
HYOU1_HUMAN	HYOU1	physical	26344197

Drug and Disease Associations

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

Regulatory Network of DJC17_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASSSPECTROMETRY.	19690332 [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-112, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASSSPECTROMETRY.	19367720 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASSSPECTROMETRY.	17081983 [Abstract]