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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: Q15084




USC-OGP 2-DE database:  Q15084


Q15084


General information about the entry
View entry in simple text format
Entry namePDIA6_HUMAN
Primary accession numberQ15084
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 A6; EC=5.3.4.1 {ECO:0000269|PubMed:12204115, ECO:0000269|PubMed:15466936}; AltName: Full=Endoplasmic reticulum protein 5; Short=ER protein 5; Short=ERp5; AltName: Full=Protein disulfide isomerase P5; AltName: Full=Thioredoxin domain-containing protein 7; Flags: Precursor;.
Gene nameName=PDIA6
Synonyms=ERP5, P5, TXNDC7
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=20990
pI=5.33; Mw=20483



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

MAP LOCATIONS:
pI=5.29; Mw=16741

Cross-references
UniProtKB/Swiss-ProtQ15084; PDIA6_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 namePDIA6_HUMAN
Primary accession numberQ15084
Secondary accession number(s) B3KY95 B5MCQ5 B7Z254 B7Z4M8 F8WA83 Q53RC7 Q6ZSH5 Q99778
Sequence was last modified on November 1, 1997 (version 1)
Annotations were last modified on March 15, 2017 (version 187)
Name and origin of the protein
DescriptionRecName: Full=Protein disulfide-isomerase A6; EC=5.3.4.1 {ECO:0000269|PubMed:12204115, ECO:0000269|PubMed:15466936}; AltName: Full=Endoplasmic reticulum protein 5; Short=ER protein 5; Short=ERp5; AltName: Full=Protein disulfide isomerase P5; AltName: Full=Thioredoxin domain-containing protein 7; Flags: Precursor;
Gene nameName=PDIA6
Synonyms=ERP5, P5, TXNDC7
Encoded onName=PDIA6; Synonyms=ERP5, P5, TXNDC7
Keywords3D-structure; Alternative splicing; Cell membrane; Chaperone; Complete proteome; Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; Isomerase; Membrane; 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
EMBLD49489; BAA08450.1; -; mRNA
EMBLAK127433; BAC86977.1; -; mRNA
EMBLAK131234; BAG54757.1; -; mRNA
EMBLAK289428; BAF82117.1; -; mRNA
EMBLAK294347; BAH11740.1; -; mRNA
EMBLAK297547; BAH12614.1; -; mRNA
EMBLAC092687; AAY24070.1; -; Genomic_DNA
EMBLCH471053; EAX00950.1; -; Genomic_DNA
EMBLBC001312; AAH01312.1; -; mRNA
EMBLU79278; AAB50217.1; -; mRNA
CCDSCCDS1675.1; -. [Q15084-1]; .
CCDSCCDS62852.1; -. [Q15084-3]; .
CCDSCCDS62853.1; -. [Q15084-4]; .
CCDSCCDS62854.1; -. [Q15084-2]; .
CCDSCCDS62855.1; -. [Q15084-5]; .
PIRJC4369; JC4369; .
RefSeqNP_001269633.1; NM_001282704.1. [Q15084-2]; .
RefSeqNP_001269634.1; NM_001282705.1. [Q15084-5]; .
RefSeqNP_001269635.1; NM_001282706.1. [Q15084-4]; .
RefSeqNP_001269636.1; NM_001282707.1. [Q15084-3]; .
RefSeqNP_005733.1; NM_005742.3. [Q15084-1]; .
UniGeneHs.212102; -; .
UniGeneHs.580464; -; .
PDB1X5D; NMR; -; A=161-280
PDB3VWW; X-ray; 1.93 A; A/B=25-140
PDB3W8J; X-ray; 2.10 A; A/B=20-140
PDB4EF0; X-ray; 1.50 A; A/B=27-140
PDB4GWR; X-ray; 1.81 A; A/B=160-274
PDBsum1X5D; -; .
PDBsum3VWW; -; .
PDBsum3W8J; -; .
PDBsum4EF0; -; .
PDBsum4GWR; -; .
ProteinModelPortalQ15084; -; .
SMRQ15084; -; .
BioGrid115434; 91; .
IntActQ15084; 38; .
MINTMINT-3030897; -; .
STRING9606.ENSP00000272227; -; .
ChEMBLCHEMBL2146308; -; .
iPTMnetQ15084; -; .
PhosphoSitePlusQ15084; -; .
SwissPalmQ15084; -; .
DMDM2501205; -; .
OGPQ15084; -; .
REPRODUCTION-2DPAGEIPI00644989; -; .
REPRODUCTION-2DPAGEQ15084; -; .
EPDQ15084; -; .
PaxDbQ15084; -; .
PeptideAtlasQ15084; -; .
PRIDEQ15084; -; .
DNASU10130; -; .
EnsemblENST00000272227; ENSP00000272227; ENSG00000143870. [Q15084-1]; .
EnsemblENST00000381611; ENSP00000371024; ENSG00000143870. [Q15084-4]; .
EnsemblENST00000404371; ENSP00000385385; ENSG00000143870. [Q15084-2]; .
EnsemblENST00000404824; ENSP00000384459; ENSG00000143870. [Q15084-5]; .
EnsemblENST00000540494; ENSP00000438778; ENSG00000143870. [Q15084-3]; .
EnsemblENST00000617249; ENSP00000481892; ENSG00000143870. [Q15084-2]; .
GeneID10130; -; .
KEGGhsa:10130; -; .
UCSCuc002rau.5; human. [Q15084-1]; .
CTD10130; -; .
DisGeNET10130; -; .
GeneCardsPDIA6; -; .
HGNCHGNC:30168; PDIA6; .
HPACAB034347; -; .
HPAHPA034652; -; .
HPAHPA034653; -; .
MIM611099; gene; .
neXtProtNX_Q15084; -; .
OpenTargetsENSG00000143870; -; .
PharmGKBPA134977905; -; .
eggNOGKOG0191; Eukaryota; .
eggNOGCOG0526; LUCA; .
GeneTreeENSGT00860000133723; -; .
HOGENOMHOG000012631; -; .
HOVERGENHBG053548; -; .
InParanoidQ15084; -; .
KOK09584; -; .
OMATAHQSKA; -; .
OrthoDBEOG091G07Z0; -; .
PhylomeDBQ15084; -; .
TreeFamTF315231; -; .
ReactomeR-HSA-381038; XBP1(S) activates chaperone genes; .
ChiTaRSPDIA6; human; .
EvolutionaryTraceQ15084; -; .
GenomeRNAi10130; -; .
PROPR:Q15084; -; .
ProteomesUP000005640; Chromosome 2; .
BgeeENSG00000143870; -; .
CleanExHS_PDIA6; -; .
ExpressionAtlasQ15084; baseline and differential; .
GenevisibleQ15084; HS; .
GOGO:0005829; C:cytosol; IDA:HPA; .
GOGO:0005783; C:endoplasmic reticulum; TAS:UniProtKB; .
GOGO:0034663; C:endoplasmic reticulum chaperone complex; ISS:ParkinsonsUK-UCL; .
GOGO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell; .
GOGO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome; .
GOGO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB; .
GOGO:0070062; C:extracellular exosome; IDA:UniProtKB; .
GOGO:0042470; C:melanosome; IEA:UniProtKB-SubCell; .
GOGO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell; .
GOGO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central; .
GOGO:0043277; P:apoptotic cell clearance; IBA:GO_Central; .
GOGO:0045454; P:cell redox homeostasis; IEA:InterPro; .
GOGO:0036498; P:IRE1-mediated unfolded protein response; TAS:Reactome; .
GOGO:0006457; P:protein folding; TAS:ProtInc; .
GOGO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central; .
Gene3D3.40.30.10; -; 2; .
InterProIPR005788; Disulphide_isomerase; .
InterProIPR012336; Thioredoxin-like_fold; .
InterProIPR017937; Thioredoxin_CS; .
InterProIPR013766; Thioredoxin_domain; .
PfamPF00085; Thioredoxin; 2; .
SUPFAMSSF52833; SSF52833; 3; .
TIGRFAMsTIGR01126; pdi_dom; 2; .
PROSITEPS00014; ER_TARGET; 1; .
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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