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USC-OGP 2-DE database

Two-dimensional polyacrylamide gel electrophoresis database


USC-OGP 2-DE database 
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Searching in 'USC-OGP 2-DE database' for entry matching: PDIA3_HUMAN




USC-OGP 2-DE database:  PDIA3_HUMAN


PDIA3_HUMAN


General information about the entry
View entry in simple text format
Entry namePDIA3_HUMAN
Primary accession numberP30101
integrated into USC-OGP 2-DE database on January 17, 2017 (release 1)
2D Annotations were last modified onJanuary 17, 2017 (version 1)
General Annotations were last modified on April 5, 2017 (version 2)
Name and origin of the protein
DescriptionRecName: Full=Protein disulfide-isomerase A3; EC=5.3.4.1; AltName: Full=58 kDa glucose-regulated protein; AltName: Full=58 kDa microsomal protein; Short=p58; AltName: Full=Disulfide isomerase ER-60; AltName: Full=Endoplasmic reticulum resident protein 57; Short=ER protein 57; Short=ERp57; AltName: Full=Endoplasmic reticulum resident protein 60; Short=ER protein 60; Short=ERp60; Flags: Precursor;.
Gene nameName=PDIA3
Synonyms=ERP57, ERP60, GRP58
Annotated speciesHomo sapiens (Human) [TaxID: 9606]
TaxonomyEukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
References
[1]   2D GEL CHARACTERIZATION
Author 1., Author 2.
Submitted (Mar-2011) to Current
2D PAGE maps for identified proteins
How to interpret a protein

PLATELET_4-7 {PLATELET 4-7}
Homo sapiens (Human)
PLATELET_4-7
  map experimental info
 
PLATELET_4-7

MAP LOCATIONS:
pI=5.34; Mw=54833
pI=5.40; Mw=54664
pI=5.46; Mw=54664
pI=5.55; Mw=54328
pI=5.48; Mw=40808



PLATELET_5-6 {PLATELET 5-6}
Homo sapiens (Human)
PLATELET_5-6
  map experimental info
 
PLATELET_5-6

MAP LOCATIONS:
pI=5.41; Mw=55942
pI=5.48; Mw=55779
pI=5.57; Mw=55616
pI=5.49; Mw=41434



UVEAL_MELANOMA_3-10 {UVEAL MELANOMA 3-10}
Homo sapiens (Human)
UVEAL_MELANOMA_3-10
  map experimental info
 
UVEAL_MELANOMA_3-10

MAP LOCATIONS:
pI=5.63; Mw=55013
pI=5.74; Mw=54155
pI=6.30; Mw=54155
pI=5.77; Mw=31502

Cross-references
UniProtKB/Swiss-ProtP30101; PDIA3_HUMAN.



2D PAGE maps for identified proteins
  • How to interpret a protein map
  • You may obtain an estimated location of the protein on various 2D PAGE maps, provided the whole amino acid sequence is known. The estimation is obtained according to the computed protein's pI and Mw.
  • Warning 1: the displayed region reflects an area around the theoretical pI and molecular weight of the protein and is only provided for the user's information. It should be used with caution, as the experimental and theoretical positions of a protein may differ significantly.
  • Warning 2: the 2D PAGE map is built on demand. This may take some few seconds to be computed.



External data extracted from UniProtKB/Swiss-Prot
Extracted from UniProtKB/Swiss-Prot, release: 0.0
Entry namePDIA3_HUMAN
Primary accession numberP30101
Secondary accession number(s) Q13453 Q14255 Q8IYF8 Q9UMU7
Sequence was last modified on November 1, 1997 (version 4)
Annotations were last modified on March 15, 2017 (version 203)
Name and origin of the protein
DescriptionRecName: Full=Protein disulfide-isomerase A3; EC=5.3.4.1; AltName: Full=58 kDa glucose-regulated protein; AltName: Full=58 kDa microsomal protein; Short=p58; AltName: Full=Disulfide isomerase ER-60; AltName: Full=Endoplasmic reticulum resident protein 57; Short=ER protein 57; Short=ERp57; AltName: Full=Endoplasmic reticulum resident protein 60; Short=ER protein 60; Short=ERp60; Flags: Precursor;
Gene nameName=PDIA3
Synonyms=ERP57, ERP60, GRP58
Encoded onName=PDIA3; Synonyms=ERP57, ERP60, GRP58
Keywords3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; Isomerase; Methylation; Phosphoprotein; Polymorphism; Redox-active center; Reference proteome; Repeat; Signal.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLD16234; BAA03759.1; -; mRNA
EMBLU42068; AAC50331.1; -; mRNA
EMBLZ49835; CAA89996.1; -; mRNA
EMBLU75885; AAC51518.1; -; Genomic_DNA
EMBLU75875; AAC51518.1; JOINED; Genomic_DNA
EMBLU75876; AAC51518.1; JOINED; Genomic_DNA
EMBLU75877; AAC51518.1; JOINED; Genomic_DNA
EMBLU75878; AAC51518.1; JOINED; Genomic_DNA
EMBLU75879; AAC51518.1; JOINED; Genomic_DNA
EMBLU75880; AAC51518.1; JOINED; Genomic_DNA
EMBLU75881; AAC51518.1; JOINED; Genomic_DNA
EMBLU75882; AAC51518.1; JOINED; Genomic_DNA
EMBLU75883; AAC51518.1; JOINED; Genomic_DNA
EMBLU75884; AAC51518.1; JOINED; Genomic_DNA
EMBLD83485; BAA11928.1; -; mRNA
EMBLBC014433; AAH14433.1; -; mRNA
EMBLBC036000; AAH36000.4; -; mRNA
EMBLBC071878; AAH71878.1; -; mRNA
CCDSCCDS10101.1; -; .
PIRJC5704; JC5704; .
PIRS55507; S55507; .
PIRS63994; S63994; .
PIRS68363; S68363; .
RefSeqNP_005304.3; NM_005313.4; .
UniGeneHs.591095; -; .
PDB2ALB; NMR; -; A=25-137
PDB2DMM; NMR; -; A=357-485
PDB2H8L; X-ray; 2.00 A; A/B/C=134-376
PDB3F8U; X-ray; 2.60 A; A/C=25-505
PDBsum2ALB; -; .
PDBsum2DMM; -; .
PDBsum2H8L; -; .
PDBsum3F8U; -; .
ProteinModelPortalP30101; -; .
SMRP30101; -; .
BioGrid109180; 125; .
DIPDIP-29132N; -; .
IntActP30101; 76; .
MINTMINT-5000005; -; .
STRING9606.ENSP00000300289; -; .
iPTMnetP30101; -; .
PhosphoSitePlusP30101; -; .
SwissPalmP30101; -; .
BioMutaPDIA3; -; .
DMDM2507461; -; .
DOSAC-COBS-2DPAGEP30101; -; .
REPRODUCTION-2DPAGEP30101; -; .
SWISS-2DPAGEP30101; -; .
UCD-2DPAGEP30101; -; .
EPDP30101; -; .
PaxDbP30101; -; .
PeptideAtlasP30101; -; .
PRIDEP30101; -; .
TopDownProteomicsP30101; -; .
DNASU2923; -; .
EnsemblENST00000300289; ENSP00000300289; ENSG00000167004; .
GeneID2923; -; .
KEGGhsa:2923; -; .
CTD2923; -; .
DisGeNET2923; -; .
GeneCardsPDIA3; -; .
HGNCHGNC:4606; PDIA3; .
HPACAB011199; -; .
HPACAB015181; -; .
HPAHPA002645; -; .
HPAHPA003230; -; .
MIM602046; gene; .
neXtProtNX_P30101; -; .
OpenTargetsENSG00000167004; -; .
PharmGKBPA29000; -; .
eggNOGKOG0190; Eukaryota; .
eggNOGCOG0526; LUCA; .
GeneTreeENSGT00860000133691; -; .
HOGENOMHOG000162459; -; .
HOVERGENHBG005920; -; .
InParanoidP30101; -; .
KOK08056; -; .
OMAQINFAIA; -; .
OrthoDBEOG091G05J9; -; .
PhylomeDBP30101; -; .
TreeFamTF106382; -; .
BRENDA5.3.4.1; 2681; .
ReactomeR-HSA-1236974; ER-Phagosome pathway; .
ReactomeR-HSA-901042; Calnexin/calreticulin cycle; .
ReactomeR-HSA-983170; Antigen Presentation: Folding; assembly and peptide loading of class I MHC; .
ChiTaRSPDIA3; human; .
EvolutionaryTraceP30101; -; .
GenomeRNAi2923; -; .
PROPR:P30101; -; .
ProteomesUP000005640; Chromosome 15; .
BgeeENSG00000167004; -; .
CleanExHS_PDIA3; -; .
ExpressionAtlasP30101; baseline and differential; .
GenevisibleP30101; HS; .
GOGO:0009986; C:cell surface; IDA:MGI; .
GOGO:0005783; C:endoplasmic reticulum; IDA:UniProtKB; .
GOGO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome; .
GOGO:0070062; C:extracellular exosome; IDA:UniProtKB; .
GOGO:0005925; C:focal adhesion; IDA:UniProtKB; .
GOGO:0042470; C:melanosome; IEA:UniProtKB-SubCell; .
GOGO:0043209; C:myelin sheath; IEA:Ensembl; .
GOGO:0005634; C:nucleus; IDA:UniProtKB; .
GOGO:0045335; C:phagocytic vesicle; TAS:Reactome; .
GOGO:0055038; C:recycling endosome membrane; TAS:Reactome; .
GOGO:0004197; F:cysteine-type endopeptidase activity; TAS:ProtInc; .
GOGO:0015036; F:disulfide oxidoreductase activity; TAS:ParkinsonsUK-UCL; .
GOGO:0004629; F:phospholipase C activity; TAS:ProtInc; .
GOGO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central; .
GOGO:0003723; F:RNA binding; IDA:UniProtKB; .
GOGO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; TAP-dependent; TAS:Reactome
GOGO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome; .
GOGO:0045454; P:cell redox homeostasis; IEA:InterPro; .
GOGO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl; .
GOGO:0006457; P:protein folding; TAS:Reactome; .
GOGO:0034975; P:protein folding in endoplasmic reticulum; TAS:ParkinsonsUK-UCL; .
GOGO:0006606; P:protein import into nucleus; TAS:ProtInc; .
GOGO:0006621; P:protein retention in ER lumen; TAS:ProtInc; .
GOGO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central; .
GOGO:0007165; P:signal transduction; TAS:ProtInc; .
Gene3D3.40.30.10; -; 3; .
InterProIPR005788; Disulphide_isomerase; .
InterProIPR005792; Prot_disulphide_isomerase; .
InterProIPR012336; Thioredoxin-like_fold; .
InterProIPR017937; Thioredoxin_CS; .
InterProIPR013766; Thioredoxin_domain; .
PfamPF00085; Thioredoxin; 2; .
SUPFAMSSF52833; SSF52833; 4; .
TIGRFAMsTIGR01130; ER_PDI_fam; 1; .
TIGRFAMsTIGR01126; pdi_dom; 2; .
PROSITEPS00194; THIOREDOXIN_1; 2; .
PROSITEPS51352; THIOREDOXIN_2; 2; .



USC-OGP 2-DE database image


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Database constructed and maintained by Angel Garcia, using the Make2D-DB II package (ver. 3.10.2) from the World-2DPAGE Constellation of the ExPASy web server

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