DNJC3_HUMAN - dbPTM
DNJC3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DNJC3_HUMAN
UniProt AC Q13217
Protein Name DnaJ homolog subfamily C member 3
Gene Name DNAJC3
Organism Homo sapiens (Human).
Sequence Length 504
Subcellular Localization Endoplasmic reticulum.
Protein Description Involved in the unfolded protein response (UPR) during endoplasmic reticulum (ER) stress. Acts as a negative regulator of the EIF2AK4/GCN2 kinase activity by preventing the phosphorylation of eIF-2-alpha at 'Ser-52' and hence attenuating general protein synthesis under ER stress, hypothermic and amino acid starving stress conditions (By similarity). Co-chaperone of HSPA8/HSC70, it stimulates its ATPase activity. May inhibit both the autophosphorylation of EIF2AK2/PKR and the ability of EIF2AK2 to catalyze phosphorylation of the EIF2A. May inhibit EIF2AK3/PERK activity..
Protein Sequence MVAPGSVTSRLGSVFPFLLVLVDLQYEGAECGVNADVEKHLELGKKLLAAGQLADALSQFHAAVDGDPDNYIAYYRRATVFLAMGKSKAALPDLTKVIQLKMDFTAARLQRGHLLLKQGKLDEAEDDFKKVLKSNPSENEEKEAQSQLIKSDEMQRLRSQALNAFGSGDYTAAIAFLDKILEVCVWDAELRELRAECFIKEGEPRKAISDLKAASKLKNDNTEAFYKISTLYYQLGDHELSLSEVRECLKLDQDHKRCFAHYKQVKKLNKLIESAEELIRDGRYTDATSKYESVMKTEPSIAEYTVRSKERICHCFSKDEKPVEAIRVCSEVLQMEPDNVNALKDRAEAYLIEEMYDEAIQDYETAQEHNENDQQIREGLEKAQRLLKQSQKRDYYKILGVKRNAKKQEIIKAYRKLALQWHPDNFQNEEEKKKAEKKFIDIAAAKEVLSDPEMRKKFDDGEDPLDAESQQGGGGNPFHRSWNSWQGFNPFSSGGPFRFKFHFN
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
6Phosphorylation--MVAPGSVTSRLGS
--CCCCCCHHHHHHH		22.5930619164
8PhosphorylationMVAPGSVTSRLGSVF
CCCCCCHHHHHHHHH		15.1530619164
9PhosphorylationVAPGSVTSRLGSVFP
CCCCCHHHHHHHHHH		24.2929262532
452-HydroxyisobutyrylationEKHLELGKKLLAAGQ
HHHHHHHHHHHHHHH		53.52-
46"N6,N6-dimethyllysine"KHLELGKKLLAAGQL
HHHHHHHHHHHHHHH		47.11-
46MethylationKHLELGKKLLAAGQL
HHHHHHHHHHHHHHH		47.11-
87PhosphorylationVFLAMGKSKAALPDL
HHHHCCCCHHHCCCH		23.0726074081
88UbiquitinationFLAMGKSKAALPDLT
HHHCCCCHHHCCCHH		40.96-
95PhosphorylationKAALPDLTKVIQLKM
HHHCCCHHHHHHHHC		30.5526074081
96UbiquitinationAALPDLTKVIQLKMD
HHCCCHHHHHHHHCC		44.64-
105PhosphorylationIQLKMDFTAARLQRG
HHHHCCHHHHHHHHH		18.3626074081
117UbiquitinationQRGHLLLKQGKLDEA
HHHHHHHHCCCCCCC		57.90-
133 (in isoform 1)Ubiquitination-51.6921906983
133UbiquitinationDDFKKVLKSNPSENE
HHHHHHHHHCCCHHH		51.6921906983
142UbiquitinationNPSENEEKEAQSQLI
CCCHHHHHHHHHHHH		52.77-
150UbiquitinationEAQSQLIKSDEMQRL
HHHHHHHCHHHHHHH		61.5221906983
150 (in isoform 1)Ubiquitination-61.5221906983
159PhosphorylationDEMQRLRSQALNAFG
HHHHHHHHHHHHHHC		25.13-
170PhosphorylationNAFGSGDYTAAIAFL
HHHCCCCHHHHHHHH		11.21-
200UbiquitinationLRAECFIKEGEPRKA
HHHHHEECCCCCCHH		39.14-
212UbiquitinationRKAISDLKAASKLKN
CHHHHHHHHHHHHCC		47.07-
218UbiquitinationLKAASKLKNDNTEAF
HHHHHHHCCCCHHHH		67.02-
232PhosphorylationFYKISTLYYQLGDHE
HHHHHHHHHHHCCCC		6.83-
256UbiquitinationLKLDQDHKRCFAHYK
HHCCCCHHHHHHHHH		60.18-
270UbiquitinationKQVKKLNKLIESAEE
HHHHHHHHHHHHHHH		62.37-
274PhosphorylationKLNKLIESAEELIRD
HHHHHHHHHHHHHHC		33.7126657352
284PhosphorylationELIRDGRYTDATSKY
HHHHCCCCCCCCHHH		17.9429083192
285PhosphorylationLIRDGRYTDATSKYE
HHHCCCCCCCCHHHH		20.1429083192
288PhosphorylationDGRYTDATSKYESVM
CCCCCCCCHHHHHHH		28.6729083192
289PhosphorylationGRYTDATSKYESVMK
CCCCCCCHHHHHHHC		34.6529083192
290AcetylationRYTDATSKYESVMKT
CCCCCCHHHHHHHCC		49.0025038526
290 (in isoform 1)Ubiquitination-49.0021906983
290UbiquitinationRYTDATSKYESVMKT
CCCCCCHHHHHHHCC		49.002190698
291PhosphorylationYTDATSKYESVMKTE
CCCCCHHHHHHHCCC		17.1329083192
296UbiquitinationSKYESVMKTEPSIAE
HHHHHHHCCCCCHHH		47.80-
304PhosphorylationTEPSIAEYTVRSKER
CCCCHHHHHHCCCCC		11.08-
305PhosphorylationEPSIAEYTVRSKERI
CCCHHHHHHCCCCCE		10.84-
318UbiquitinationRICHCFSKDEKPVEA
CEEECCCCCCCCHHH		50.05-
344UbiquitinationPDNVNALKDRAEAYL
CCCHHHHHHHHHHHH		42.64-
355SulfoxidationEAYLIEEMYDEAIQD
HHHHHHHHHHHHHHH		3.1130846556
382UbiquitinationQIREGLEKAQRLLKQ
HHHHHHHHHHHHHHH		55.66-
388UbiquitinationEKAQRLLKQSQKRDY
HHHHHHHHHHHHCCH		53.12-
407MethylationGVKRNAKKQEIIKAY
CCCCCHHHHHHHHHH		51.24-
412UbiquitinationAKKQEIIKAYRKLAL
HHHHHHHHHHHHHHH		45.05-
416UbiquitinationEIIKAYRKLALQWHP
HHHHHHHHHHHHHCC		25.99-
446UbiquitinationFIDIAAAKEVLSDPE
HHHHHHHHHHHCCHH		43.56-
450PhosphorylationAAAKEVLSDPEMRKK
HHHHHHHCCHHHHHH		57.19-
454SulfoxidationEVLSDPEMRKKFDDG
HHHCCHHHHHHCCCC		10.4121406390
457UbiquitinationSDPEMRKKFDDGEDP
CCHHHHHHCCCCCCC		43.60-
481PhosphorylationGGNPFHRSWNSWQGF
CCCCCCCCCCCCCCC		23.2626434776
484PhosphorylationPFHRSWNSWQGFNPF
CCCCCCCCCCCCCCC		17.9626434776
492PhosphorylationWQGFNPFSSGGPFRF
CCCCCCCCCCCCCEE		29.3628450419
493PhosphorylationQGFNPFSSGGPFRFK
CCCCCCCCCCCCEEE		48.4228450419
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
274SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DNJC3_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 DNJC3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
E2AK3_HUMANEIF2AK3physical
12446838
E2AK2_HUMANEIF2AK2physical
8576172
HSP7C_HUMANHSPA8physical
11116152
HSP74_HUMANHSPA4physical
11116152
P52K_HUMANPRKRIRphysical
9447982
E2AK2_HUMANEIF2AK2physical
9447982
HSP7E_HUMANHSPA14physical
26344197
HSP7C_HUMANHSPA8physical
26344197
HYOU1_HUMANHYOU1physical
26344197
GRP78_HUMANHSPA5physical
26085089
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616192Ataxia, combined cerebellar and peripheral, with hearing loss and diabetes mellitus (ACPHD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DNJC3_HUMAN

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Related Literatures of Post-Translational Modification

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