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Q90593 (GRP78_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
78 kDa glucose-regulated protein

Short name=GRP-78
Alternative name(s):
Heat shock 70 kDa protein 5
Immunoglobulin heavy chain-binding protein
Short name=BiP
Gene names
Name:HSPA5
Synonyms:GRP78
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length652 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probably plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum By similarity.

Subcellular location

Endoplasmic reticulum lumen.

Sequence similarities

Belongs to the heat shock protein 70 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   DomainSignal
   LigandATP-binding
Nucleotide-binding
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processER overload response

Inferred from electronic annotation. Source: Ensembl

activation of signaling protein activity involved in unfolded protein response

Inferred from electronic annotation. Source: Ensembl

cellular response to glucose starvation

Inferred from electronic annotation. Source: Ensembl

cellular response to interleukin-4

Inferred from electronic annotation. Source: Ensembl

cerebellar Purkinje cell layer development

Inferred from electronic annotation. Source: Ensembl

cerebellum structural organization

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein ubiquitination

Inferred from electronic annotation. Source: Ensembl

proteolysis involved in cellular protein catabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentCOP9 signalosome

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum chaperone complex

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum-Golgi intermediate compartment

Inferred from electronic annotation. Source: Ensembl

integral component of endoplasmic reticulum membrane

Inferred from electronic annotation. Source: Ensembl

midbody

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 22174833. Source: IntAct

ribosome binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

KCNMA1Q8AYS83EBI-1635886,EBI-1635766

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 65263678 kDa glucose-regulated protein
PRO_0000013570

Regions

Nucleotide binding34 – 374ATP By similarity
Nucleotide binding225 – 2273ATP By similarity
Nucleotide binding291 – 2988ATP By similarity
Nucleotide binding362 – 3654ATP By similarity
Motif649 – 6524Prevents secretion from ER By similarity

Sites

Binding site941ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q90593 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 4E4BB58A3EEFAF6F

FASTA65272,019
        10         20         30         40         50         60 
MRHLLLALLL LGGARADDEE KKEDVGTVVG IDLGTTYSCV GVFKNGRVEI IANDQGNRIT 

        70         80         90        100        110        120 
PSYVAFTPEG ERLIGDAAKN QLTSNPENTV FDAKRLIGRT WNDPSVQQDI KYLPFKVVEK 

       130        140        150        160        170        180 
KAKPHIQVDV GGGQTKTFAP EEISAMVLTK MKETAEAYLG KKVTHAVVTV PAYFNDAQRQ 

       190        200        210        220        230        240 
ATKDAGTIAG LNVMRIINEP TAAAIAYGLD KREGEKNILV FDLGGGTFDV SLLTIDNGVF 

       250        260        270        280        290        300 
EVVATNGDTH LGGEDFDQRV MEHFIKLYKK KTGKDVRKDN RAVQKLRREV EKAKRALSSQ 

       310        320        330        340        350        360 
HQARIEIESF FEGEDFSETL TRAKFEELNM DLFRSTMKPV QKVLEDSDLK KSDIDEIVLV 

       370        380        390        400        410        420 
GGSTRIPKIQ QLVKEFFNGK EPSRGINPDE AVAYGAAVQA GVLSGDQDTG DLVLLDVCPL 

       430        440        450        460        470        480 
TLGIETVGGV MTKLIPRNTV VPTKKSQIFS TASDNQPTVT IKVYEGERPL TKDNHLLGTF 

       490        500        510        520        530        540 
DLTGIPPAPR GVPQIEVTFE IDVNGILRVT AEDKGTGNKN KITITNDQNR LTPEEIERMV 

       550        560        570        580        590        600 
NDAEKFAEED KKLKERIDAR NELESYAYSL KNQIGDKEKL GGKLSSEDKE TIEKAVEEKI 

       610        620        630        640        650 
EWLESHQDAD IEDFKSKKKE LEEVVQPIVS KLYGSAGPPP TGEEEAAEKD EL 

« Hide

References

[1]"78-kilodalton glucose-regulated protein is induced in Rous sarcoma virus-transformed cells independently of glucose deprivation."
Stoeckle M.Y., Sugano S., Hampe A., Vashishtha A., Pellman D., Hanafusa H.
Mol. Cell. Biol. 8:2675-2680(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M27260 mRNA. Translation: AAA48785.1.
PIRI50242.
RefSeqNP_990822.1. NM_205491.1.
UniGeneGga.4219.

3D structure databases

ProteinModelPortalQ90593.
SMRQ90593. Positions 26-568.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid676734. 2 interactions.
IntActQ90593. 1 interaction.
STRING9031.ENSGALP00000001474.

Proteomic databases

PaxDbQ90593.
PRIDEQ90593.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSGALT00000001476; ENSGALP00000001474; ENSGALG00000001000.
GeneID396487.
KEGGgga:396487.

Organism-specific databases

CTD3309.

Phylogenomic databases

eggNOGCOG0443.
GeneTreeENSGT00750000117237.
HOGENOMHOG000228135.
HOVERGENHBG051845.
InParanoidQ90593.
KOK09490.
OMADKRAVQK.
OrthoDBEOG780RKX.
PhylomeDBQ90593.
TreeFamTF105044.

Family and domain databases

Gene3D1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
SUPFAMSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20816526.
PROQ90593.

Entry information

Entry nameGRP78_CHICK
AccessionPrimary (citable) accession number: Q90593
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families