dbPTM

DNJB1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DNJB1_HUMAN
UniProt AC	P25685
Protein Name	DnaJ homolog subfamily B member 1
Gene Name	DNAJB1
Organism	Homo sapiens (Human).
Sequence Length	340
Subcellular Localization	Cytoplasm . Nucleus . Nucleus, nucleolus . Translocates rapidly from the cytoplasm to the nucleus, and especially to the nucleoli, upon heat shock.
Protein Description	Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP. Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response. [PubMed: 9499401 Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro)]
Protein Sequence	MGKDYYQTLGLARGASDEEIKRAYRRQALRYHPDKNKEPGAEEKFKEIAEAYDVLSDPRKREIFDRYGEEGLKGSGPSGGSGGGANGTSFSYTFHGDPHAMFAEFFGGRNPFDTFFGQRNGEEGMDIDDPFSGFPMGMGGFTNVNFGRSRSAQEPARKKQDPPVTHDLRVSLEEIYSGCTKKMKISHKRLNPDGKSIRNEDKILTIEVKKGWKEGTKITFPKEGDQTSNNIPADIVFVLKDKPHNIFKRDGSDVIYPARISLREALCGCTVNVPTLDGRTIPVVFKDVIRPGMRRKVPGEGLPLPKTPEKRGDLIIEFEVIFPERIPQTSRTVLEQVLPI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	2-Hydroxyisobutyrylation	-----MGKDYYQTLG -----CCCHHHHHHH	41.06	-
3	Ubiquitination	-----MGKDYYQTLG -----CCCHHHHHHH	41.06	-
5	Phosphorylation	---MGKDYYQTLGLA ---CCCHHHHHHHHC	10.85	28152594
6	Phosphorylation	--MGKDYYQTLGLAR --CCCHHHHHHHHCC	12.73	28152594
8	Phosphorylation	MGKDYYQTLGLARGA CCCHHHHHHHHCCCC	13.48	28152594
13	Methylation	YQTLGLARGASDEEI HHHHHHCCCCCHHHH	46.37	115479707
16	Phosphorylation	LGLARGASDEEIKRA HHHCCCCCHHHHHHH	48.67	28985074
21	Ubiquitination	GASDEEIKRAYRRQA CCCHHHHHHHHHHHH	33.97	-
21	Succinylation	GASDEEIKRAYRRQA CCCHHHHHHHHHHHH	33.97	23954790
21	Acetylation	GASDEEIKRAYRRQA CCCHHHHHHHHHHHH	33.97	25953088
31	Phosphorylation	YRRQALRYHPDKNKE HHHHHHHHCCCCCCC	20.68	29496907
35	Ubiquitination	ALRYHPDKNKEPGAE HHHHCCCCCCCCCHH	74.50	-
37	Ubiquitination	RYHPDKNKEPGAEEK HHCCCCCCCCCHHHH	71.65	-
44	Ubiquitination	KEPGAEEKFKEIAEA CCCCHHHHHHHHHHH	53.92	19608861
44	2-Hydroxyisobutyrylation	KEPGAEEKFKEIAEA CCCCHHHHHHHHHHH	53.92	-
44	Acetylation	KEPGAEEKFKEIAEA CCCCHHHHHHHHHHH	53.92	19608861
46	Ubiquitination	PGAEEKFKEIAEAYD CCHHHHHHHHHHHHH	60.31	-
52	Phosphorylation	FKEIAEAYDVLSDPR HHHHHHHHHHHCCHH	9.70	-
58	Ubiquitination	AYDVLSDPRKREIFD HHHHHCCHHHHHHHH	40.07	-
60	Ubiquitination	DVLSDPRKREIFDRY HHHCCHHHHHHHHHH	60.82	-
66	Methylation	RKREIFDRYGEEGLK HHHHHHHHHCCCCCC	30.52	115479715
67	Phosphorylation	KREIFDRYGEEGLKG HHHHHHHHCCCCCCC	30.63	29496907
78	Phosphorylation	GLKGSGPSGGSGGGA CCCCCCCCCCCCCCC	60.35	25137130
81	Ubiquitination	GSGPSGGSGGGANGT CCCCCCCCCCCCCCC	37.48	-
88	Phosphorylation	SGGGANGTSFSYTFH CCCCCCCCEEEEEEC	26.80	-
89	Phosphorylation	GGGANGTSFSYTFHG CCCCCCCEEEEEECC	17.37	-
95	Ubiquitination	TSFSYTFHGDPHAMF CEEEEEECCCCCHHH	31.76	-
95	Acetylation	TSFSYTFHGDPHAMF CEEEEEECCCCCHHH	31.76	-
148	Ubiquitination	FTNVNFGRSRSAQEP CCCCCCCCCCCCCCC	25.43	-
149	Phosphorylation	TNVNFGRSRSAQEPA CCCCCCCCCCCCCCH	30.85	29978859
151	Phosphorylation	VNFGRSRSAQEPARK CCCCCCCCCCCCHHH	35.23	28102081
158	Ubiquitination	SAQEPARKKQDPPVT CCCCCHHHCCCCCCC	57.82	-
159	Ubiquitination	AQEPARKKQDPPVTH CCCCHHHCCCCCCCH	55.14	-
171	Phosphorylation	VTHDLRVSLEEIYSG CCHHHHHCHHHHHCC	24.51	21945579
176	Phosphorylation	RVSLEEIYSGCTKKM HHCHHHHHCCCCCCC	11.42	21945579
177	Phosphorylation	VSLEEIYSGCTKKMK HCHHHHHCCCCCCCC	32.81	21945579
180	Phosphorylation	EEIYSGCTKKMKISH HHHHCCCCCCCCCCC	36.91	21945579
181	2-Hydroxyisobutyrylation	EIYSGCTKKMKISHK HHHCCCCCCCCCCCC	55.75	-
181	Ubiquitination	EIYSGCTKKMKISHK HHHCCCCCCCCCCCC	55.75	-
181	Acetylation	EIYSGCTKKMKISHK HHHCCCCCCCCCCCC	55.75	25953088
186	Ubiquitination	CTKKMKISHKRLNPD CCCCCCCCCCCCCCC	19.89	-
186	Phosphorylation	CTKKMKISHKRLNPD CCCCCCCCCCCCCCC	19.89	-
195	Ubiquitination	KRLNPDGKSIRNEDK CCCCCCCCCCCCCCC	50.52	21906983
195	2-Hydroxyisobutyrylation	KRLNPDGKSIRNEDK CCCCCCCCCCCCCCC	50.52	-
195	Acetylation	KRLNPDGKSIRNEDK CCCCCCCCCCCCCCC	50.52	23749302
196	Phosphorylation	RLNPDGKSIRNEDKI CCCCCCCCCCCCCCE	32.10	19651622
202	Ubiquitination	KSIRNEDKILTIEVK CCCCCCCCEEEEEEE	33.18	-
205	Phosphorylation	RNEDKILTIEVKKGW CCCCCEEEEEEECCC	20.68	21406692
209	2-Hydroxyisobutyrylation	KILTIEVKKGWKEGT CEEEEEEECCCCCCC	32.55	-
217	Ubiquitination	KGWKEGTKITFPKEG CCCCCCCEEECCCCC	51.08	-
222	Ubiquitination	GTKITFPKEGDQTSN CCEEECCCCCCCCCC	70.86	-
227	Phosphorylation	FPKEGDQTSNNIPAD CCCCCCCCCCCCCCE	37.86	25693802
228	Phosphorylation	PKEGDQTSNNIPADI CCCCCCCCCCCCCEE	23.42	21712546
240	Ubiquitination	ADIVFVLKDKPHNIF CEEEEEECCCCCCCC	59.41	-
242	Acetylation	IVFVLKDKPHNIFKR EEEEECCCCCCCCCC	46.73	26051181
242	Ubiquitination	IVFVLKDKPHNIFKR EEEEECCCCCCCCCC	46.73	-
248	2-Hydroxyisobutyrylation	DKPHNIFKRDGSDVI CCCCCCCCCCCCCCE	45.87	-
248	Ubiquitination	DKPHNIFKRDGSDVI CCCCCCCCCCCCCCE	45.87	-
252	Phosphorylation	NIFKRDGSDVIYPAR CCCCCCCCCCEEECC	32.75	28152594
256	Phosphorylation	RDGSDVIYPARISLR CCCCCCEEECCCHHH	7.23	28152594
261	Phosphorylation	VIYPARISLREALCG CEEECCCHHHHHHCC	18.80	-
286	2-Hydroxyisobutyrylation	RTIPVVFKDVIRPGM CEECEEEEHHCCCCC	39.20	-
286	Ubiquitination	RTIPVVFKDVIRPGM CEECEEEEHHCCCCC	39.20	21890473
286	Ubiquitination	RTIPVVFKDVIRPGM CEECEEEEHHCCCCC	39.20	21890473
286	Acetylation	RTIPVVFKDVIRPGM CEECEEEEHHCCCCC	39.20	25953088
296	Ubiquitination	IRPGMRRKVPGEGLP CCCCCCCCCCCCCCC	42.28	-
306	Ubiquitination	GEGLPLPKTPEKRGD CCCCCCCCCCCCCCC	81.85	-
307	Phosphorylation	EGLPLPKTPEKRGDL CCCCCCCCCCCCCCE	34.44	25159151

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
149	S	Phosphorylation	Kinase	MAPKAPK5	Q8IW41	PSP
151	S	Phosphorylation	Kinase	MAPKAPK5	Q8IW41	PSP
171	S	Phosphorylation	Kinase	MAPKAPK5	Q8IW41	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DNJB1_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 DNJB1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HSP7C_HUMAN	HSPA8	physical	10075921
DNJC3_BOVIN	DNAJC3	physical	9920933
HSP7C_RAT	Hspa8	physical	9920933
PHLA1_HUMAN	PHLDA1	physical	17024176
A4_HUMAN	APP	physical	21832049
PUR8_HUMAN	ADSL	physical	22863883
DPYL2_HUMAN	DPYSL2	physical	22863883
PDE12_HUMAN	PDE12	physical	22863883
UBQL2_HUMAN	UBQLN2	physical	22863883
WDR4_HUMAN	WDR4	physical	22863883
XPO7_HUMAN	XPO7	physical	22863883
MDM2_HUMAN	MDM2	physical	24361594
P53_HUMAN	TP53	physical	24361594
DAG1_HUMAN	DAG1	physical	26344197
ERF1_HUMAN	ETF1	physical	26344197
HYOU1_HUMAN	HYOU1	physical	26344197
PPID_HUMAN	PPID	physical	26344197
STIP1_HUMAN	STIP1	physical	26344197
TTL12_HUMAN	TTLL12	physical	28514442
DNJB5_HUMAN	DNAJB5	physical	28514442
DCAF6_HUMAN	DCAF6	physical	28514442
BGAL_HUMAN	GLB1	physical	28514442
NUDC_HUMAN	NUDC	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 DNJB1_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-44, AND MASS SPECTROMETRY.	19608861 [Abstract]