DNJB9_HUMAN - dbPTM
DNJB9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DNJB9_HUMAN
UniProt AC Q9UBS3
Protein Name DnaJ homolog subfamily B member 9 {ECO:0000305}
Gene Name DNAJB9
Organism Homo sapiens (Human).
Sequence Length 223
Subcellular Localization Endoplasmic reticulum lumen .
Protein Description Co-chaperone for Hsp70 protein HSPA5/BiP that acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (By similarity). J domain-containing co-chaperones stimulate the ATPase activity of Hsp70 proteins and are required for efficient substrate recognition by Hsp70 proteins. [PubMed: 18400946 In the unstressed endoplasmic reticulum, interacts with the luminal region of ERN1/IRE1 and selectively recruits HSPA5/BiP: HSPA5/BiP disrupts the dimerization of the active ERN1/IRE1 luminal region, thereby inactivating ERN1/IRE1 (By similarity Also involved in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins. Required for survival of B-cell progenitors and normal antibody production (By similarity]
Protein Sequence MATPQSIFIFAICILMITELILASKSYYDILGVPKSASERQIKKAFHKLAMKYHPDKNKSPDAEAKFREIAEAYETLSDANRRKEYDTLGHSAFTSGKGQRGSGSSFEQSFNFNFDDLFKDFGFFGQNQNTGSKKRFENHFQTRQDGGSSRQRHHFQEFSFGGGLFDDMFEDMEKMFSFSGFDSTNQHTVQTENRFHGSSKHCRTVTQRRGNMVTTYTDCSGQ
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
3Phosphorylation-----MATPQSIFIF
-----CCCHHHHHHH
22.1424043423
6Phosphorylation--MATPQSIFIFAIC
--CCCHHHHHHHHHH
22.2224043423
18PhosphorylationAICILMITELILASK
HHHHHHHHHHHHHCC
15.6924043423
24PhosphorylationITELILASKSYYDIL
HHHHHHHCCCHHHHH
20.7724043423
35"N6,N6-dimethyllysine"YDILGVPKSASERQI
HHHHCCCCCCCHHHH
57.14-
35MethylationYDILGVPKSASERQI
HHHHCCCCCCCHHHH
57.14-
66UbiquitinationKSPDAEAKFREIAEA
CCCCHHHHHHHHHHH
36.14-
84UbiquitinationLSDANRRKEYDTLGH
HHHHHHHHHCCCCCC
58.34-
98UbiquitinationHSAFTSGKGQRGSGS
CCCCCCCCCCCCCCC
52.1921906983
103PhosphorylationSGKGQRGSGSSFEQS
CCCCCCCCCCCCHHH
37.3820166139
105PhosphorylationKGQRGSGSSFEQSFN
CCCCCCCCCCHHHCC
33.2925072903
106PhosphorylationGQRGSGSSFEQSFNF
CCCCCCCCCHHHCCC
36.0126657352
110PhosphorylationSGSSFEQSFNFNFDD
CCCCCHHHCCCCHHH
18.2429691806
133PhosphorylationGQNQNTGSKKRFENH
CCCCCCCCCHHHHHC
32.7223917254
134UbiquitinationQNQNTGSKKRFENHF
CCCCCCCCHHHHHCC
49.6821906983
136MethylationQNTGSKKRFENHFQT
CCCCCCHHHHHCCEE
48.09-
143O-linked_GlycosylationRFENHFQTRQDGGSS
HHHHCCEECCCCCCC
29.38OGP
178PhosphorylationEDMEKMFSFSGFDST
HHHHHHHHCCCCCCC
18.2729691806
180PhosphorylationMEKMFSFSGFDSTNQ
HHHHHHCCCCCCCCC
37.0329691806
184PhosphorylationFSFSGFDSTNQHTVQ
HHCCCCCCCCCCEEE
27.3120166139
185PhosphorylationSFSGFDSTNQHTVQT
HCCCCCCCCCCEEEC
40.5224275569
189PhosphorylationFDSTNQHTVQTENRF
CCCCCCCEEECCCCC
12.4429691806
192PhosphorylationTNQHTVQTENRFHGS
CCCCEEECCCCCCCC
30.7829691806
215PhosphorylationQRRGNMVTTYTDCSG
ECCCCEEEEEECCCC
11.8724043423
216PhosphorylationRRGNMVTTYTDCSGQ
CCCCEEEEEECCCCC
17.0224043423
217PhosphorylationRGNMVTTYTDCSGQ-
CCCEEEEEECCCCC-
7.3924043423
218PhosphorylationGNMVTTYTDCSGQ--
CCEEEEEECCCCC--
28.5624043423
221PhosphorylationVTTYTDCSGQ-----
EEEEECCCCC-----
42.9324043423

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 DNJB9_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DNJB9_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 DNJB9_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RIFK_HUMANRFKphysical
16169070
MOT3_HUMANSLC16A8physical
16169070
DYL1_HUMANDYNLL1physical
16169070
FSCN1_HUMANFSCN1physical
16169070
MYL6_HUMANMYL6physical
16169070
TCEA2_HUMANTCEA2physical
16169070
PLK1_HUMANPLK1physical
16169070
ECM29_HUMANKIAA0368physical
20682791
GRP78_HUMANHSPA5physical
18400946
FA71C_HUMANFAM71Cphysical
21988832

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 DNJB9_HUMAN

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Related Literatures of Post-Translational Modification

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