CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024711
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein disulfide-isomerase A2 
Protein Synonyms/Alias
 PDIp 
Gene Name
 Pdia2 
Gene Synonyms/Alias
 Pdip 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
113PAEPELTKEFEVVGYubiquitination[1]
229DTVVLFKKFDEGRADacetylation[2]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] 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
 Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins (By similarity). 
Sequence Annotation
 DOMAIN 29 155 Thioredoxin 1.
 DOMAIN 355 499 Thioredoxin 2.
 MOTIF 524 527 Prevents secretion from ER (Potential).
 ACT_SITE 74 74 Nucleophile (By similarity).
 ACT_SITE 77 77 Nucleophile (By similarity).
 ACT_SITE 421 421 Nucleophile (By similarity).
 ACT_SITE 424 424 Nucleophile (By similarity).
 CARBOHYD 130 130 N-linked (GlcNAc...) (Potential).
 CARBOHYD 287 287 N-linked (GlcNAc...) (Potential).
 CARBOHYD 518 518 N-linked (GlcNAc...) (Potential).
 DISULFID 74 77 Redox-active (By similarity).
 DISULFID 421 424 Redox-active (By similarity).  
Keyword
 Alternative splicing; Chaperone; Complete proteome; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Isomerase; Lipid-binding; Redox-active center; Reference proteome; Repeat; Signal; Steroid-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 527 AA 
Protein Sequence
MDKQLLPVLL LLLGVSGSWG QGEEPGGPSE VLPEEPTGEE VPKEDGILVL NHRTLSLALQ 60
EHSALMVEFY APWCGHCKEL APEYSKAAAL LAAESAVVTL AKVDGPAEPE LTKEFEVVGY 120
PTLKFFQNGN RTNPEEYAGP KTAEGIAEWL RRRVGPSATH LEDEEGVQAL MAKWDMVVIG 180
FFQDLQGKDM ATFLALAKDA LDMTFGFTDQ PQLFEKFGLT KDTVVLFKKF DEGRADFPVD 240
KETGLDLGDL SRFLVIHSMH LVTEFNSQTS PKIFAAKILN HLLLFVNQTL AQHRELLTDF 300
REAAPPFRGQ VLFVMVDVAA DNSHVLNYFG LKAEEAPTLR LINVETTKKY APTGVIAITA 360
ASVAAFCQAV LHGEIKHYLL SQEIPPDWDQ GPVKTLVSKN FEQVAFDETK NVFVKFYAPW 420
CSHCKEMAPA WEALAEKYKD REDIVIAELD ATANELEAFS VLGYPTLKFF PAGPDRKVID 480
YKSTRDLETF SKFLDSGGHL PKEEPKEPAA SAPEAQANST LGPKEEL 527 
Gene Ontology
 GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
 GO:0009055; F:electron carrier activity; IEA:InterPro.
 GO:0003756; F:protein disulfide isomerase activity; TAS:MGI.
 GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
 GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
 GO:0006915; P:apoptotic process; IEA:Compara.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro.
 GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
 GO:0001666; P:response to hypoxia; IEA:Compara. 
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.