DJC10_HUMAN - dbPTM
DJC10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DJC10_HUMAN
UniProt AC Q8IXB1
Protein Name DnaJ homolog subfamily C member 10
Gene Name DNAJC10
Organism Homo sapiens (Human).
Sequence Length 793
Subcellular Localization Endoplasmic reticulum lumen .
Protein Description Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. Required for efficient folding of proteins in the endoplasmic reticulum by catalyzing the removal of non-native disulfide bonds formed during the folding of proteins, such as LDLR. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. Interaction with HSPA5 is required its activity, not for the disulfide reductase activity, but to facilitate the release of DNAJC10 from its substrate. Promotes apoptotic signaling pathway in response to endoplasmic reticulum stress..
Protein Sequence MGVWLNKDDYIRDLKRIILCFLIVYMAILVGTDQDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLEDNQGGQYESWNYYRYDFGIYDDDPEIITLERREFDAAVNSGELWFVNFYSPGCSHCHDLAPTWRDFAKEVDGLLRIGAVNCGDDRMLCRMKGVNSYPSLFIFRSGMAPVKYHGDRSKESLVSFAMQHVRSTVTELWTGNFVNSIQTAFAAGIGWLITFCSKGGDCLTSQTRLRLSGMLDGLVNVGWMDCATQDNLCKSLDITTSTTAYFPPGATLNNKEKNSILFLNSLDAKEIYLEVIHNLPDFELLSANTLEDRLAHHRWLLFFHFGKNENSNDPELKKLKTLLKNDHIQVGRFDCSSAPDICSNLYVFQPSLAVFKGQGTKEYEIHHGKKILYDILAFAKESVNSHVTTLGPQNFPANDKEPWLVDFFAPWCPPCRALLPELRRASNLLYGQLKFGTLDCTVHEGLCNMYNIQAYPTTVVFNQSNIHEYEGHHSAEQILEFIEDLMNPSVVSLTPTTFNELVTQRKHNEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGLINVGSIDCQQYHSFCAQENVQRYPEIRFFPPKSNKAYHYHSYNGWNRDAYSLRIWGLGFLPQVSTDLTPQTFSEKVLQGKNHWVIDFYAPWCGPCQNFAPEFELLARMIKGKVKAGKVDCQAYAQTCQKAGIRAYPTVKFYFYERAKRNFQEEQINTRDAKAIAALISEKLETLRNQGKRNKDEL
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
66UbiquitinationALKLHPDKNPNNPNA
HHHHCCCCCCCCCCC		77.9329967540
112PhosphorylationEDNQGGQYESWNYYR
CCCCCCCEEECEEEE		18.40-
133PhosphorylationDDDPEIITLERREFD
CCCCCEEEEECHHHC		28.3821406692
173UbiquitinationPTWRDFAKEVDGLLR
HHHHHHHHHCCCEEE		59.2624816145
196UbiquitinationDRMLCRMKGVNSYPS
CCEEHHCCCCCCCCE		40.11-
303PhosphorylationTQDNLCKSLDITTST
CCCCCHHHCCCCCCC		30.2220068231
309PhosphorylationKSLDITTSTTAYFPP
HHCCCCCCCCEECCC		18.3420068231
310PhosphorylationSLDITTSTTAYFPPG
HCCCCCCCCEECCCC		17.2220068231
311PhosphorylationLDITTSTTAYFPPGA
CCCCCCCCEECCCCC		21.0820068231
313PhosphorylationITTSTTAYFPPGATL
CCCCCCEECCCCCCC		17.9620068231
319PhosphorylationAYFPPGATLNNKEKN
EECCCCCCCCCCCCC		35.6120068231
327PhosphorylationLNNKEKNSILFLNSL
CCCCCCCEEEEECCC		31.5621406692
333PhosphorylationNSILFLNSLDAKEIY
CEEEEECCCCHHHHH		29.7621406692
391UbiquitinationLKKLKTLLKNDHIQV
HHHHHHHHHCCCCCC		6.1922817900
392 (in isoform 2)Ubiquitination-64.5421890473
392UbiquitinationKKLKTLLKNDHIQVG
HHHHHHHHCCCCCCC		64.5421890473
4292-HydroxyisobutyrylationVFKGQGTKEYEIHHG
EECCCCCCEEEEECC		66.19-
4372-HydroxyisobutyrylationEYEIHHGKKILYDIL
EEEEECCCHHHHHHH		32.08-
437UbiquitinationEYEIHHGKKILYDIL
EEEEECCCHHHHHHH		32.0822817900
438UbiquitinationYEIHHGKKILYDILA
EEEECCCHHHHHHHH		42.4021890473
438 (in isoform 1)Ubiquitination-42.4021890473
438UbiquitinationYEIHHGKKILYDILA
EEEECCCHHHHHHHH		42.4021890473
530N-linked_GlycosylationYPTTVVFNQSNIHEY
CCEEEEEECCCCCEE		32.53UniProtKB CARBOHYD
640AcetylationEIRFFPPKSNKAYHY
CEEEECCCCCCCEEE		67.897712375
659PhosphorylationGWNRDAYSLRIWGLG
CCCCCCHHEEEECCC		16.9424719451
672PhosphorylationLGFLPQVSTDLTPQT
CCCCCCCCCCCCCCC		15.7924719451
673PhosphorylationGFLPQVSTDLTPQTF
CCCCCCCCCCCCCCC		35.8524719451
681PhosphorylationDLTPQTFSEKVLQGK
CCCCCCCCHHHHCCC		39.6424719451
691UbiquitinationVLQGKNHWVIDFYAP
HHCCCCCEEEEEECC		9.7322817900
691 (in isoform 2)Ubiquitination-9.7321890473
723UbiquitinationMIKGKVKAGKVDCQA
HHCCCCCCCCCCHHH		26.4829967540
725UbiquitinationKGKVKAGKVDCQAYA
CCCCCCCCCCHHHHH		39.50-
732UbiquitinationKVDCQAYAQTCQKAG
CCCHHHHHHHHHHCC		10.9629967540
737UbiquitinationAYAQTCQKAGIRAYP
HHHHHHHHCCCCCCC		51.2122817900
737 (in isoform 1)Ubiquitination-51.2121890473
769UbiquitinationQINTRDAKAIAALIS
HCCHHHHHHHHHHHH		44.6129967540
776PhosphorylationKAIAALISEKLETLR
HHHHHHHHHHHHHHH		29.5424719451
778UbiquitinationIAALISEKLETLRNQ
HHHHHHHHHHHHHHC		44.8529967540
783MethylationSEKLETLRNQGKRNK
HHHHHHHHHCCCCCC		40.62-
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 DJC10_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DJC10_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 DJC10_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FXRD2_HUMANFOXRED2physical
19706418
EDEM1_HUMANEDEM1physical
21632540
TXNL1_HUMANTXNL1physical
26344197
PI4KB_HUMANPI4KBphysical
28514442
MTMR4_HUMANMTMR4physical
28514442
FBLN5_HUMANFBLN5physical
28514442
TPC13_HUMANTRAPPC13physical
28514442
MYOME_HUMANPDE4DIPphysical
28514442
GRN_HUMANGRNphysical
28514442
LTBP4_HUMANLTBP4physical
28514442
AKAP9_HUMANAKAP9physical
28514442
SSFA2_HUMANSSFA2physical
28514442
WAPL_HUMANWAPALphysical
28514442
NOTC3_HUMANNOTCH3physical
28514442
LRP1B_HUMANLRP1Bphysical
28514442
PRGC2_HUMANPPARGC1Bphysical
28514442
LAMB2_HUMANLAMB2physical
28514442
MTMR3_HUMANMTMR3physical
28514442
N42L2_HUMANN4BP2L2physical
28514442
LTBP3_HUMANLTBP3physical
28514442
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 DJC10_HUMAN

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Related Literatures of Post-Translational Modification

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