CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020974
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DnaJ homolog subfamily C member 10 
Protein Synonyms/Alias
 ER-resident protein ERdj5; Endoplasmic reticulum DnaJ-PDI fusion protein 1; J domain-containing protein disulfide isomerase-like protein; J domain-containing PDI-like protein; JPDI 
Gene Name
 Dnajc10 
Gene Synonyms/Alias
 Erdj5; Jpdi 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
778IAALIYGKLETLQSQacetylation[1]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441] 
Functional Description
 This endoplasmic reticulum co-chaperone may play a role in protein folding and translocation across the endoplasmic reticulum membrane. May be involved in disulfide formation. May act as a co-chaperone for Hspa5. 
Sequence Annotation
 DOMAIN 35 100 J.
 DOMAIN 130 232 Thioredoxin 1.
 DOMAIN 454 553 Thioredoxin 2.
 DOMAIN 557 665 Thioredoxin 3.
 DOMAIN 671 776 Thioredoxin 4.
 MOTIF 790 793 Prevents secretion from ER (Potential).
 CARBOHYD 530 530 N-linked (GlcNAc...) (Potential).  
Keyword
 3D-structure; Chaperone; Complete proteome; Endoplasmic reticulum; Glycoprotein; Reference proteome; Repeat; Secreted; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 793 AA 
Protein Sequence
MGVWLNKDDF IRDLKRISLC LLILYVVVVV GTDQNFYSLL GVSKTASSRE IRQAFKKLAL 60
KLHPDKNPNN PNAHGDFLKI NRAYEVLKDE DLRKKYDKYG EKGLEDNQGG QYESWSYYRY 120
DFGIYDDDPE IITLERREFD AAVNSGELWF VNFYSPGCSH CHDLAPTWRE FAKEVDGLLR 180
IGAVNCGDDR MLCRMKGVNS YPSLFIFRSG MAAVKYNGDR SKESLVAFAM QHVRSTVTEL 240
STGNFVNAIE TAFAAGVGWL ITFCSKGEDC LTSQTRLRLS GMLDGLVNVG WVDCDAQDSL 300
CKSLDTTAST TAYFPPGATL NDREKSSVLF LNSLDAKEIY MEIIHNLPDF ELLSANQLED 360
RLAHHRWLVF FHFGKNENAN DPELKKLKTL LKNEHIQVGR FDCSSAPGIC SDLYVFQPCL 420
AVFKGQGTKE YEIHHGKKIL YDILAFAKES VNSHVTTLGP QNFPASDKEP WLVDFFAPWC 480
PPCRALLPEL RKASTLLYGQ LKVGTLDCTI HEGLCNMYNI QAYPTTVVFN QSSIHEYEGH 540
HSAEQILEFI EDLRNPSVVS LTPSTFNELV KQRKHDEVWM VDFYSPWCHP CQVLMPEWKR 600
MARTLTGLIN VGSVDCQQYH SFCTQENVQR YPEIRFYPQK SSKAYQYHSY NGWNRDAYSL 660
RSWGLGFLPQ ASIDLTPQTF NEKVLQGKTH WVVDFYAPWC GPCQNFAPEF ELLARMIKGK 720
VRAGKVDCQA YPQTCQKAGI KAYPSVKLYQ YERAKKSIWE EQINSRDAKT IAALIYGKLE 780
TLQSQVKRNK DEL 793 
Gene Ontology
 GO:0034663; C:endoplasmic reticulum chaperone complex; ISS:UniProtKB.
 GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
 GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
 GO:0001671; F:ATPase activator activity; IMP:UniProtKB.
 GO:0051087; F:chaperone binding; IDA:UniProtKB.
 GO:0015036; F:disulfide oxidoreductase activity; IDA:UniProtKB.
 GO:0051787; F:misfolded protein binding; ISS:UniProtKB.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro.
 GO:0030433; P:ER-associated protein catabolic process; IDA:UniProtKB.
 GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB.
 GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB. 
Interpro
 IPR001623; DnaJ_domain.
 IPR021170; DnaJ_homolog_subfam-C.
 IPR012336; Thioredoxin-like_fold.
 IPR017937; Thioredoxin_CS.
 IPR013766; Thioredoxin_domain. 
Pfam
 PF00226; DnaJ
 PF00085; Thioredoxin 
SMART
 SM00271; DnaJ 
PROSITE
 PS00636; DNAJ_1
 PS50076; DNAJ_2
 PS00014; ER_TARGET
 PS00194; THIOREDOXIN_1
 PS51352; THIOREDOXIN_2 
PRINTS
 PR00625; JDOMAIN.