dbPTM

DNJC8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DNJC8_HUMAN
UniProt AC	O75937
Protein Name	DnaJ homolog subfamily C member 8
Gene Name	DNAJC8
Organism	Homo sapiens (Human).
Sequence Length	253
Subcellular Localization	Nucleus .
Protein Description	Suppresses polyglutamine (polyQ) aggregation of ATXN3 in neuronal cells. [PubMed: 27133716]
Protein Sequence	MAASGESGTSGGGGSTEEAFMTFYSEVKQIEKRDSVLTSKNQIERLTRPGSSYFNLNPFEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADRAQKAFEAVDKAYKLLLDQEQKKRALDVIQAGKEYVEHTVKERKKQLKKEGKPTIVEEDDPELFKQAVYKQTMKLFAELEIKRKEREAKEMHERKRQREEEIEAQEKAKREREWQKNFEESRDGRVDSWRNFQANTKGKKEKKNRTFLRPPKVKMEQRE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAASGESGT ------CCCCCCCCC	15.44	19413330
4	Phosphorylation	----MAASGESGTSG ----CCCCCCCCCCC	33.29	23401153
7	Phosphorylation	-MAASGESGTSGGGG -CCCCCCCCCCCCCC	51.39	24043423
9	Phosphorylation	AASGESGTSGGGGST CCCCCCCCCCCCCCH	33.21	28348404
10	Phosphorylation	ASGESGTSGGGGSTE CCCCCCCCCCCCCHH	38.68	28348404
15	Phosphorylation	GTSGGGGSTEEAFMT CCCCCCCCHHHHHHH	35.60	25849741
16	Phosphorylation	TSGGGGSTEEAFMTF CCCCCCCHHHHHHHH	40.91	28348404
22	Phosphorylation	STEEAFMTFYSEVKQ CHHHHHHHHHHHHHH	16.99	24043423
24	Phosphorylation	EEAFMTFYSEVKQIE HHHHHHHHHHHHHHH	8.51	24043423
25	Phosphorylation	EAFMTFYSEVKQIEK HHHHHHHHHHHHHHH	31.55	24043423
35	Phosphorylation	KQIEKRDSVLTSKNQ HHHHHHHCCCCCHHH	24.06	30266825
38	Phosphorylation	EKRDSVLTSKNQIER HHHHCCCCCHHHHHH	35.18	23403867
39	Phosphorylation	KRDSVLTSKNQIERL HHHCCCCCHHHHHHH	26.00	23403867
40	2-Hydroxyisobutyrylation	RDSVLTSKNQIERLT HHCCCCCHHHHHHHC	47.86	-
40	Ubiquitination	RDSVLTSKNQIERLT HHCCCCCHHHHHHHC	47.86	32015554
47	Phosphorylation	KNQIERLTRPGSSYF HHHHHHHCCCCCCCC	40.83	28450419
51	Phosphorylation	ERLTRPGSSYFNLNP HHHCCCCCCCCCCCH	25.25	28450419
52	Phosphorylation	RLTRPGSSYFNLNPF HHCCCCCCCCCCCHH	39.39	28450419
53	Phosphorylation	LTRPGSSYFNLNPFE HCCCCCCCCCCCHHC	9.74	28122231
74	Ubiquitination	EVTDEEIKKRFRQLS CCCHHHHHHHHHHHH	40.97	29967540
75	Acetylation	VTDEEIKKRFRQLSI CCHHHHHHHHHHHHH	63.53	7265649
81	Phosphorylation	KKRFRQLSILVHPDK HHHHHHHHHHCCCCC	12.92	29514088
88	Acetylation	SILVHPDKNQDDADR HHHCCCCCCCCHHHH	62.04	25953088
105	Acetylation	KAFEAVDKAYKLLLD HHHHHHHHHHHHHCC	47.20	25953088
105	Ubiquitination	KAFEAVDKAYKLLLD HHHHHHHHHHHHHCC	47.20	22817900
107	Phosphorylation	FEAVDKAYKLLLDQE HHHHHHHHHHHCCHH	14.12	28674151
108	Acetylation	EAVDKAYKLLLDQEQ HHHHHHHHHHCCHHH	37.20	25953088
108	Ubiquitination	EAVDKAYKLLLDQEQ HHHHHHHHHHCCHHH	37.20	22817900
116	2-Hydroxyisobutyrylation	LLLDQEQKKRALDVI HHCCHHHHHHHHHHH	43.40	-
116	Ubiquitination	LLLDQEQKKRALDVI HHCCHHHHHHHHHHH	43.40	29967540
117	Ubiquitination	LLDQEQKKRALDVIQ HCCHHHHHHHHHHHH	42.47	24816145
118	Methylation	LDQEQKKRALDVIQA CCHHHHHHHHHHHHH	47.63	-
118	Dimethylation	LDQEQKKRALDVIQA CCHHHHHHHHHHHHH	47.63	-
127	2-Hydroxyisobutyrylation	LDVIQAGKEYVEHTV HHHHHHHHHHHHHHH	49.22	-
127	Ubiquitination	LDVIQAGKEYVEHTV HHHHHHHHHHHHHHH	49.22	33845483
129	Phosphorylation	VIQAGKEYVEHTVKE HHHHHHHHHHHHHHH	18.02	28152594
133	Phosphorylation	GKEYVEHTVKERKKQ HHHHHHHHHHHHHHH	21.55	28152594
135	Ubiquitination	EYVEHTVKERKKQLK HHHHHHHHHHHHHHH	53.62	24816145
135	Acetylation	EYVEHTVKERKKQLK HHHHHHHHHHHHHHH	53.62	23749302
143	Ubiquitination	ERKKQLKKEGKPTIV HHHHHHHHCCCCCCC	79.06	29967540
143	Acetylation	ERKKQLKKEGKPTIV HHHHHHHHCCCCCCC	79.06	26822725
146	Acetylation	KQLKKEGKPTIVEED HHHHHCCCCCCCCCC	39.83	19608861
146	Ubiquitination	KQLKKEGKPTIVEED HHHHHCCCCCCCCCC	39.83	19608861
159	Acetylation	EDDPELFKQAVYKQT CCCHHHHHHHHHHHH	50.39	26051181
159	Ubiquitination	EDDPELFKQAVYKQT CCCHHHHHHHHHHHH	50.39	29967540
176	2-Hydroxyisobutyrylation	LFAELEIKRKEREAK HHHHHHHHHHHHHHH	48.30	-
176	Ubiquitination	LFAELEIKRKEREAK HHHHHHHHHHHHHHH	48.30	33845483
201	Ubiquitination	EEIEAQEKAKREREW HHHHHHHHHHHHHHH	47.32	24816145
210	Ubiquitination	KREREWQKNFEESRD HHHHHHHHHHHHHCC	65.75	29967540
215	Phosphorylation	WQKNFEESRDGRVDS HHHHHHHHCCCCCCC	28.59	23403867
222	Phosphorylation	SRDGRVDSWRNFQAN HCCCCCCCHHHHHCC	25.69	23401153
224	Methylation	DGRVDSWRNFQANTK CCCCCCHHHHHCCCC	37.73	-
230	Phosphorylation	WRNFQANTKGKKEKK HHHHHCCCCCCCCCC	44.16	-
231	Ubiquitination	RNFQANTKGKKEKKN HHHHCCCCCCCCCCC	69.42	27667366
237	Ubiquitination	TKGKKEKKNRTFLRP CCCCCCCCCCCCCCC	53.40	24816145
239	Methylation	GKKEKKNRTFLRPPK CCCCCCCCCCCCCCC	35.42	-
240	Phosphorylation	KKEKKNRTFLRPPKV CCCCCCCCCCCCCCC	36.09	28555341
243	Methylation	KKNRTFLRPPKVKME CCCCCCCCCCCCCHH	41.08	-
248	Sumoylation	FLRPPKVKMEQRE-- CCCCCCCCHHHCC--	42.73	-
248	Sumoylation	FLRPPKVKMEQRE-- CCCCCCCCHHHCC--	42.73	-
248	Ubiquitination	FLRPPKVKMEQRE-- CCCCCCCCHHHCC--	42.73	24816145

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 DNJC8_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DNJC8_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 DNJC8_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
RAP1A_HUMAN	RAP1A	physical	22939629
PIN4_HUMAN	PIN4	physical	22939629
TPX2_HUMAN	TPX2	physical	22939629
HMGA1_HUMAN	HMGA1	physical	18850631
HS74L_HUMAN	HSPA4L	physical	26344197
HYOU1_HUMAN	HYOU1	physical	26344197
NEDD8_HUMAN	NEDD8	physical	26344197
TRAP1_HUMAN	TRAP1	physical	27173435
SND1_HUMAN	SND1	physical	27173435
ANXA5_HUMAN	ANXA5	physical	27173435
UBE2N_HUMAN	UBE2N	physical	27173435

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 DNJC8_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-146, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND MASSSPECTROMETRY.	17287340 [Abstract]