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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: GRP78_HUMAN




USC-OGP 2-DE database:  GRP78_HUMAN


GRP78_HUMAN


General information about the entry
View entry in simple text format
Entry nameGRP78_HUMAN
Primary accession numberP11021
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=78 kDa glucose-regulated protein; Short=GRP-78; AltName: Full=Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78; AltName: Full=Heat shock 70 kDa protein 5; AltName: Full=Immunoglobulin heavy chain-binding protein; Short=BiP; Flags: Precursor;.
Gene nameName=HSPA5
Synonyms=GRP78
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_4-5 {PLATELET 4-5}
Homo sapiens (Human)
PLATELET_4-5
  map experimental info
 
PLATELET_4-5

MAP LOCATIONS:
pI=4.92; Mw=80083
pI=5.00; Mw=76753
pI=4.69; Mw=44195



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

MAP LOCATIONS:
pI=5.02; Mw=78395



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=6.35; Mw=30714

Cross-references
UniProtKB/Swiss-ProtP11021; GRP78_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 nameGRP78_HUMAN
Primary accession numberP11021
Secondary accession number(s) B0QZ61 Q2EF78 Q9NPF1 Q9UK02
Sequence was last modified on July 11, 2001 (version 2)
Annotations were last modified on March 15, 2017 (version 200)
Name and origin of the protein
DescriptionRecName: Full=78 kDa glucose-regulated protein; Short=GRP-78; AltName: Full=Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78; AltName: Full=Heat shock 70 kDa protein 5; AltName: Full=Immunoglobulin heavy chain-binding protein; Short=BiP; Flags: Precursor;
Gene nameName=HSPA5
Synonyms=GRP78
Encoded onName=HSPA5; Synonyms=GRP78
Keywords3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; Isopeptide bond; Methylation; Nitration; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Signal; Ubl conjugation.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLM19645; AAA52614.1; -; Genomic_DNA
EMBLX87949; CAA61201.1; -; mRNA
EMBLAJ271729; CAB71335.1; -; mRNA
EMBLAF216292; AAF42836.1; -; mRNA
EMBLDQ385847; ABD04090.1; -; Genomic_DNA
EMBLAL354710; CAQ08732.1; -; Genomic_DNA
EMBLCH471090; EAW87620.1; -; Genomic_DNA
EMBLBC020235; AAH20235.1; -; mRNA
EMBLX59969; CAA42595.1; -; Genomic_DNA
EMBLAF188611; AAF13605.1; ALT_SEQ; mRNA
CCDSCCDS6863.1; -; .
PIRA29821; A29821; .
RefSeqNP_005338.1; NM_005347.4; .
UniGeneHs.743241; -; .
PDB3IUC; X-ray; 2.40 A; A/C=26-410
PDB3LDL; X-ray; 2.30 A; A/B=26-407
PDB3LDN; X-ray; 2.20 A; A/B=26-407
PDB3LDO; X-ray; 1.95 A; A/B=26-407
PDB3LDP; X-ray; 2.20 A; A/B=26-407
PDB5E84; X-ray; 2.99 A; A/B/C/D/E/F=25-633
PDB5E85; X-ray; 2.57 A; A=418-637
PDB5E86; X-ray; 2.68 A; A=418-637
PDB5EVZ; X-ray; 1.85 A; A/B=26-407
PDB5EX5; X-ray; 1.90 A; A/B=26-407
PDB5EXW; X-ray; 1.90 A; A/B=26-407
PDB5EY4; X-ray; 1.86 A; A/B=26-407
PDB5F0X; X-ray; 1.60 A; A/B=26-407
PDB5F1X; X-ray; 1.90 A; A/B=26-407
PDB5F2R; X-ray; 2.15 A; A/B=26-407
PDBsum3IUC; -; .
PDBsum3LDL; -; .
PDBsum3LDN; -; .
PDBsum3LDO; -; .
PDBsum3LDP; -; .
PDBsum5E84; -; .
PDBsum5E85; -; .
PDBsum5E86; -; .
PDBsum5EVZ; -; .
PDBsum5EX5; -; .
PDBsum5EXW; -; .
PDBsum5EY4; -; .
PDBsum5F0X; -; .
PDBsum5F1X; -; .
PDBsum5F2R; -; .
ProteinModelPortalP11021; -; .
SMRP11021; -; .
BioGrid109541; 467; .
DIPDIP-33189N; -; .
IntActP11021; 180; .
MINTMINT-1135308; -; .
STRING9606.ENSP00000324173; -; .
BindingDBP11021; -; .
ChEMBLCHEMBL1781865; -; .
DrugBankDB00945; Acetylsalicylic acid; .
DrugBankDB00025; Antihemophilic Factor (Recombinant); .
iPTMnetP11021; -; .
PhosphoSitePlusP11021; -; .
SwissPalmP11021; -; .
BioMutaHSPA5; -; .
DMDM14916999; -; .
DOSAC-COBS-2DPAGEP11021; -; .
OGPP11021; -; .
REPRODUCTION-2DPAGEP11021; -; .
SWISS-2DPAGEP11021; -; .
UCD-2DPAGEP11021; -; .
EPDP11021; -; .
PaxDbP11021; -; .
PeptideAtlasP11021; -; .
PRIDEP11021; -; .
TopDownProteomicsP11021; -; .
DNASU3309; -; .
EnsemblENST00000324460; ENSP00000324173; ENSG00000044574; .
GeneID3309; -; .
KEGGhsa:3309; -; .
CTD3309; -; .
DisGeNET3309; -; .
GeneCardsHSPA5; -; .
HGNCHGNC:5238; HSPA5; .
HPACAB005221; -; .
HPAHPA038845; -; .
HPAHPA038846; -; .
MIM138120; gene; .
neXtProtNX_P11021; -; .
OpenTargetsENSG00000044574; -; .
PharmGKBPA29504; -; .
eggNOGKOG0101; Eukaryota; .
eggNOGCOG0443; LUCA; .
GeneTreeENSGT00870000136409; -; .
HOGENOMHOG000228135; -; .
HOVERGENHBG051845; -; .
InParanoidP11021; -; .
KOK09490; -; .
OMAESHQDGD; -; .
OrthoDBEOG091G0352; -; .
PhylomeDBP11021; -; .
TreeFamTF105044; -; .
ReactomeR-HSA-114608; Platelet degranulation; .
ReactomeR-HSA-3371453; Regulation of HSF1-mediated heat shock response; .
ReactomeR-HSA-381033; ATF6 (ATF6-alpha) activates chaperones; .
ReactomeR-HSA-381042; PERK regulates gene expression; .
ReactomeR-HSA-381070; IRE1alpha activates chaperones; .
ReactomeR-HSA-381183; ATF6 (ATF6-alpha) activates chaperone genes; .
ReactomeR-HSA-983170; Antigen Presentation: Folding; assembly and peptide loading of class I MHC; .
ChiTaRSHSPA5; human; .
EvolutionaryTraceP11021; -; .
GeneWikiBinding_immunoglobulin_protein; -; .
GenomeRNAi3309; -; .
PROPR:P11021; -; .
ProteomesUP000005640; Chromosome 9; .
BgeeENSG00000044574; -; .
CleanExHS_HSPA5; -; .
ExpressionAtlasP11021; baseline and differential; .
GenevisibleP11021; HS; .
GOGO:0009986; C:cell surface; IEA:Ensembl; .
GOGO:0005783; C:endoplasmic reticulum; IMP:UniProtKB; .
GOGO:0034663; C:endoplasmic reticulum chaperone complex; IDA:UniProtKB; .
GOGO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome; .
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:0031012; C:extracellular matrix; IDA:BHF-UCL; .
GOGO:0005925; C:focal adhesion; IDA:UniProtKB; .
GOGO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:BHF-UCL; .
GOGO:0042470; C:melanosome; IEA:UniProtKB-SubCell; .
GOGO:0016020; C:membrane; IDA:UniProtKB; .
GOGO:0030496; C:midbody; IDA:UniProtKB; .
GOGO:0005739; C:mitochondrion; IEA:Ensembl; .
GOGO:0043209; C:myelin sheath; IEA:Ensembl; .
GOGO:0005634; C:nucleus; IDA:UniProtKB; .
GOGO:0005886; C:plasma membrane; IEA:Ensembl; .
GOGO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl; .
GOGO:0005524; F:ATP binding; IEA:UniProtKB-KW; .
GOGO:0016887; F:ATPase activity; ISS:UniProtKB; .
GOGO:0045296; F:cadherin binding; IDA:BHF-UCL; .
GOGO:0005509; F:calcium ion binding; TAS:UniProtKB; .
GOGO:0051087; F:chaperone binding; TAS:BHF-UCL; .
GOGO:0019899; F:enzyme binding; IPI:BHF-UCL; .
GOGO:0001948; F:glycoprotein binding; IPI:UniProtKB; .
GOGO:0051787; F:misfolded protein binding; IDA:UniProtKB; .
GOGO:0019904; F:protein domain specific binding; IPI:UniProtKB; .
GOGO:0043022; F:ribosome binding; IEA:Ensembl; .
GOGO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB; .
GOGO:0051082; F:unfolded protein binding; TAS:UniProtKB; .
GOGO:0006987; P:activation of signaling protein activity involved in unfolded protein response; IEA:Ensembl; .
GOGO:0036500; P:ATF6-mediated unfolded protein response; TAS:Reactome; .
GOGO:0071236; P:cellular response to antibiotic; IEA:Ensembl; .
GOGO:0071277; P:cellular response to calcium ion; IEA:Ensembl; .
GOGO:0071320; P:cellular response to cAMP; IEA:Ensembl; .
GOGO:0035690; P:cellular response to drug; IEA:Ensembl; .
GOGO:0042149; P:cellular response to glucose starvation; IDA:UniProtKB; .
GOGO:0071353; P:cellular response to interleukin-4; IEA:Ensembl; .
GOGO:0071287; P:cellular response to manganese ion; IEA:Ensembl; .
GOGO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl; .
GOGO:0021680; P:cerebellar Purkinje cell layer development; IEA:Ensembl; .
GOGO:0021589; P:cerebellum structural organization; IEA:Ensembl; .
GOGO:0030968; P:endoplasmic reticulum unfolded protein response; TAS:BHF-UCL; .
GOGO:0006983; P:ER overload response; IEA:Ensembl; .
GOGO:0030433; P:ER-associated ubiquitin-dependent protein catabolic process; TAS:BHF-UCL; .
GOGO:0036498; P:IRE1-mediated unfolded protein response; TAS:Reactome; .
GOGO:0035437; P:maintenance of protein localization in endoplasmic reticulum; IMP:UniProtKB; .
GOGO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB; .
GOGO:0090074; P:negative regulation of protein homodimerization activity; TAS:ParkinsonsUK-UCL; .
GOGO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl; .
GOGO:0051402; P:neuron apoptotic process; IEA:Ensembl; .
GOGO:0030182; P:neuron differentiation; IEA:Ensembl; .
GOGO:0036499; P:PERK-mediated unfolded protein response; TAS:Reactome; .
GOGO:0030335; P:positive regulation of cell migration; IMP:UniProtKB; .
GOGO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl; .
GOGO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl; .
GOGO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; TAS:ParkinsonsUK-UCL; .
GOGO:0034975; P:protein folding in endoplasmic reticulum; TAS:ParkinsonsUK-UCL; .
GOGO:1903891; P:regulation of ATF6-mediated unfolded protein response; TAS:ParkinsonsUK-UCL; .
GOGO:1903894; P:regulation of IRE1-mediated unfolded protein response; TAS:ParkinsonsUK-UCL; .
GOGO:1903897; P:regulation of PERK-mediated unfolded protein response; TAS:ParkinsonsUK-UCL; .
GOGO:0060904; P:regulation of protein folding in endoplasmic reticulum; TAS:BHF-UCL; .
GOGO:0042220; P:response to cocaine; IEA:Ensembl; .
GOGO:1904313; P:response to methamphetamine hydrochloride; IEA:Ensembl; .
GOGO:0009314; P:response to radiation; IEA:Ensembl; .
GOGO:0097501; P:stress response to metal ion; IEA:Ensembl; .
GOGO:0021762; P:substantia nigra development; IEP:UniProtKB; .
GOGO:1901998; P:toxin transport; IEA:Ensembl; .
Gene3D1.20.1270.10; -; 1; .
Gene3D2.60.34.10; -; 1; .
InterProIPR018181; Heat_shock_70_CS; .
InterProIPR029048; HSP70_C; .
InterProIPR029047; HSP70_peptide-bd; .
InterProIPR013126; Hsp_70_fam; .
PfamPF00012; HSP70; 1; .
PRINTSPR00301; HEATSHOCK70; .
SUPFAMSSF100920; SSF100920; 1; .
SUPFAMSSF100934; SSF100934; 1; .
PROSITEPS00014; ER_TARGET; 1; .
PROSITEPS00297; HSP70_1; 1; .
PROSITEPS00329; HSP70_2; 1; .
PROSITEPS01036; HSP70_3; 1; .



USC-OGP 2-DE database image


Gateways to other related servers


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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