CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017054
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DnaJ homolog subfamily C member 10 
Protein Synonyms/Alias
 ER-resident protein ERdj5; Macrothioredoxin; MTHr 
Gene Name
 DNAJC10 
Gene Synonyms/Alias
 ERDJ5; UNQ495/PRO1012 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
173PTWRDFAKEVDGLLRubiquitination[1]
196DRMLCRMKGVNSYPSubiquitination[1]
392KKLKTLLKNDHIQVGubiquitination[1]
438YEIHHGKKILYDILAubiquitination[2, 3]
725KGKVKAGKVDCQAYAubiquitination[1]
737AYAQTCQKAGIRAYPubiquitination[4]
778IAALISEKLETLRNQubiquitination[1, 5]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 This endoplasmic reticulum co-chaperone may play a role in protein folding and translocation across the endoplasmic reticulum membrane. 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 557 662 Thioredoxin 3.
 DOMAIN 671 778 Thioredoxin 4.
 MOTIF 790 793 Prevents secretion from ER (Potential).
 CARBOHYD 530 530 N-linked (GlcNAc...) (Potential).  
Keyword
 Alternative splicing; Chaperone; Complete proteome; Endoplasmic reticulum; Glycoprotein; Polymorphism; Reference proteome; Repeat; Secreted; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 793 AA 
Protein Sequence
MGVWLNKDDY IRDLKRIILC FLIVYMAILV GTDQDFYSLL GVSKTASSRE IRQAFKKLAL 60
KLHPDKNPNN PNAHGDFLKI NRAYEVLKDE DLRKKYDKYG EKGLEDNQGG QYESWNYYRY 120
DFGIYDDDPE IITLERREFD AAVNSGELWF VNFYSPGCSH CHDLAPTWRD FAKEVDGLLR 180
IGAVNCGDDR MLCRMKGVNS YPSLFIFRSG MAPVKYHGDR SKESLVSFAM QHVRSTVTEL 240
WTGNFVNSIQ TAFAAGIGWL ITFCSKGGDC LTSQTRLRLS GMLDGLVNVG WMDCATQDNL 300
CKSLDITTST TAYFPPGATL NNKEKNSILF LNSLDAKEIY LEVIHNLPDF ELLSANTLED 360
RLAHHRWLLF FHFGKNENSN DPELKKLKTL LKNDHIQVGR FDCSSAPDIC SNLYVFQPSL 420
AVFKGQGTKE YEIHHGKKIL YDILAFAKES VNSHVTTLGP QNFPANDKEP WLVDFFAPWC 480
PPCRALLPEL RRASNLLYGQ LKFGTLDCTV HEGLCNMYNI QAYPTTVVFN QSNIHEYEGH 540
HSAEQILEFI EDLMNPSVVS LTPTTFNELV TQRKHNEVWM VDFYSPWCHP CQVLMPEWKR 600
MARTLTGLIN VGSIDCQQYH SFCAQENVQR YPEIRFFPPK SNKAYHYHSY NGWNRDAYSL 660
RIWGLGFLPQ VSTDLTPQTF SEKVLQGKNH WVIDFYAPWC GPCQNFAPEF ELLARMIKGK 720
VKAGKVDCQA YAQTCQKAGI RAYPTVKFYF YERAKRNFQE EQINTRDAKA IAALISEKLE 780
TLRNQGKRNK DEL 793 
Gene Ontology
 GO:0034663; C:endoplasmic reticulum chaperone complex; IDA:UniProtKB.
 GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
 GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
 GO:0001671; F:ATPase activator activity; ISS:UniProtKB.
 GO:0051087; F:chaperone binding; IDA:UniProtKB.
 GO:0015036; F:disulfide oxidoreductase activity; ISS:UniProtKB.
 GO:0009055; F:electron carrier activity; IEA:InterPro.
 GO:0051787; F:misfolded protein binding; IDA:UniProtKB.
 GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro.
 GO:0030433; P:ER-associated protein catabolic process; IMP:UniProtKB.
 GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
 GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IDA:UniProtKB.
 GO:0001933; P:negative regulation of protein phosphorylation; IDA:UniProtKB. 
Interpro
 IPR001623; DnaJ_domain.
 IPR021170; DnaJ_homolog_subfam-C.
 IPR005746; Thioredoxin.
 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.
 PR00421; THIOREDOXIN.