CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004633
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein disulfide-isomerase 
Protein Synonyms/Alias
 PDI; Thioredoxin-related glycoprotein 1 
Gene Name
 PDI1 
Gene Synonyms/Alias
 MFP1; TRG1; YCL043C; YCL313; YCL43C 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
112FPSLKIFKNSDVNNSubiquitination[1]
347DKIVLESKAIESLVKacetylation[2]
354KAIESLVKDFLKGDAacetylation[2]
358SLVKDFLKGDASPIVacetylation[2]
394DEIVNDPKKDVLVLYacetylation[2]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919
Functional Description
 Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer. 
Sequence Annotation
 DOMAIN 29 141 Thioredoxin 1.
 DOMAIN 356 485 Thioredoxin 2.
 MOTIF 519 522 Prevents secretion from ER.
 ACT_SITE 61 61 Nucleophile (By similarity).
 ACT_SITE 64 64 Nucleophile (By similarity).
 ACT_SITE 406 406 Nucleophile (By similarity).
 ACT_SITE 409 409 Nucleophile (By similarity).
 CARBOHYD 82 82 N-linked (GlcNAc...) (Potential).
 CARBOHYD 117 117 N-linked (GlcNAc...) (Potential).
 CARBOHYD 155 155 N-linked (GlcNAc...) (Potential).
 CARBOHYD 174 174 N-linked (GlcNAc...) (Potential).
 CARBOHYD 425 425 N-linked (GlcNAc...) (Potential).
 DISULFID 61 64 Redox-active.
 DISULFID 406 409 Redox-active.  
Keyword
 3D-structure; Complete proteome; Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Isomerase; Redox-active center; Reference proteome; Repeat; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 522 AA 
Protein Sequence
MKFSAGAVLS WSSLLLASSV FAQQEAVAPE DSAVVKLATD SFNEYIQSHD LVLAEFFAPW 60
CGHCKNMAPE YVKAAETLVE KNITLAQIDC TENQDLCMEH NIPGFPSLKI FKNSDVNNSI 120
DYEGPRTAEA IVQFMIKQSQ PAVAVVADLP AYLANETFVT PVIVQSGKID ADFNATFYSM 180
ANKHFNDYDF VSAENADDDF KLSIYLPSAM DEPVVYNGKK ADIADADVFE KWLQVEALPY 240
FGEIDGSVFA QYVESGLPLG YLFYNDEEEL EEYKPLFTEL AKKNRGLMNF VSIDARKFGR 300
HAGNLNMKEQ FPLFAIHDMT EDLKYGLPQL SEEAFDELSD KIVLESKAIE SLVKDFLKGD 360
ASPIVKSQEI FENQDSSVFQ LVGKNHDEIV NDPKKDVLVL YYAPWCGHCK RLAPTYQELA 420
DTYANATSDV LIAKLDHTEN DVRGVVIEGY PTIVLYPGGK KSESVVYQGS RSLDSLFDFI 480
KENGHFDVDG KALYEEAQEK AAEEADADAE LADEEDAIHD EL 522 
Gene Ontology
 GO:0005788; C:endoplasmic reticulum lumen; IDA:SGD.
 GO:0009055; F:electron carrier activity; IEA:InterPro.
 GO:0003756; F:protein disulfide isomerase activity; IDA:SGD.
 GO:0015035; F:protein disulfide oxidoreductase activity; IDA:SGD.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro.
 GO:0006662; P:glycerol ether metabolic process; IEA:InterPro. 
Interpro
 IPR005792; Prot_disulphide_isomerase.
 IPR005746; Thioredoxin.
 IPR012336; Thioredoxin-like_fold.
 IPR017937; Thioredoxin_CS.
 IPR013766; Thioredoxin_domain. 
Pfam
 PF00085; Thioredoxin 
SMART
  
PROSITE
 PS00014; ER_TARGET
 PS00194; THIOREDOXIN_1
 PS51352; THIOREDOXIN_2 
PRINTS
 PR00421; THIOREDOXIN.