Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

78 kDa glucose-regulated protein

Gene

HSPA5

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei94 – 941ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi34 – 374ATPBy similarity
Nucleotide bindingi225 – 2273ATPBy similarity
Nucleotide bindingi291 – 2988ATPBy similarity
Nucleotide bindingi362 – 3654ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ribosome binding Source: Ensembl

GO - Biological processi

  1. activation of signaling protein activity involved in unfolded protein response Source: Ensembl
  2. cellular response to glucose starvation Source: Ensembl
  3. cellular response to interleukin-4 Source: Ensembl
  4. cerebellar Purkinje cell layer development Source: Ensembl
  5. cerebellum structural organization Source: Ensembl
  6. ER overload response Source: Ensembl
  7. maintenance of protein localization in endoplasmic reticulum Source: Ensembl
  8. negative regulation of apoptotic process Source: Ensembl
  9. negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
  10. positive regulation of cell migration Source: Ensembl
  11. positive regulation of protein ubiquitination Source: Ensembl
  12. proteolysis involved in cellular protein catabolic process Source: Ensembl
  13. substantia nigra development Source: Ensembl
  14. toxin transport Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_288861. Platelet degranulation.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:HSPA5
Synonyms:GRP78
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539 Componenti: Chromosome 17

Subcellular locationi

GO - Cellular componenti

  1. cell surface Source: Ensembl
  2. COP9 signalosome Source: Ensembl
  3. endoplasmic reticulum chaperone complex Source: Ensembl
  4. endoplasmic reticulum-Golgi intermediate compartment Source: Ensembl
  5. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  6. extracellular vesicular exosome Source: Ensembl
  7. focal adhesion Source: Ensembl
  8. integral component of endoplasmic reticulum membrane Source: Ensembl
  9. midbody Source: Ensembl
  10. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence AnalysisAdd
BLAST
Chaini17 – 65263678 kDa glucose-regulated proteinPRO_0000013570Add
BLAST

Proteomic databases

PaxDbiQ90593.
PRIDEiQ90593.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
KCNMA1Q8AYS83EBI-1635886,EBI-1635766

Protein-protein interaction databases

BioGridi676734. 2 interactions.
IntActiQ90593. 1 interaction.
STRINGi9031.ENSGALP00000001474.

Structurei

3D structure databases

ProteinModelPortaliQ90593.
SMRiQ90593. Positions 26-568.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi649 – 6524Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0443.
GeneTreeiENSGT00750000117237.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiQ90593.
KOiK09490.
OMAiESHQDGD.
OrthoDBiEOG780RKX.
PhylomeDBiQ90593.
TreeFamiTF105044.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q90593-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRHLLLALLL LGGARADDEE KKEDVGTVVG IDLGTTYSCV GVFKNGRVEI
60 70 80 90 100
IANDQGNRIT PSYVAFTPEG ERLIGDAAKN QLTSNPENTV FDAKRLIGRT
110 120 130 140 150
WNDPSVQQDI KYLPFKVVEK KAKPHIQVDV GGGQTKTFAP EEISAMVLTK
160 170 180 190 200
MKETAEAYLG KKVTHAVVTV PAYFNDAQRQ ATKDAGTIAG LNVMRIINEP
210 220 230 240 250
TAAAIAYGLD KREGEKNILV FDLGGGTFDV SLLTIDNGVF EVVATNGDTH
260 270 280 290 300
LGGEDFDQRV MEHFIKLYKK KTGKDVRKDN RAVQKLRREV EKAKRALSSQ
310 320 330 340 350
HQARIEIESF FEGEDFSETL TRAKFEELNM DLFRSTMKPV QKVLEDSDLK
360 370 380 390 400
KSDIDEIVLV GGSTRIPKIQ QLVKEFFNGK EPSRGINPDE AVAYGAAVQA
410 420 430 440 450
GVLSGDQDTG DLVLLDVCPL TLGIETVGGV MTKLIPRNTV VPTKKSQIFS
460 470 480 490 500
TASDNQPTVT IKVYEGERPL TKDNHLLGTF DLTGIPPAPR GVPQIEVTFE
510 520 530 540 550
IDVNGILRVT AEDKGTGNKN KITITNDQNR LTPEEIERMV NDAEKFAEED
560 570 580 590 600
KKLKERIDAR NELESYAYSL KNQIGDKEKL GGKLSSEDKE TIEKAVEEKI
610 620 630 640 650
EWLESHQDAD IEDFKSKKKE LEEVVQPIVS KLYGSAGPPP TGEEEAAEKD

EL
Length:652
Mass (Da):72,019
Last modified:November 1, 1996 - v1
Checksum:i4E4BB58A3EEFAF6F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27260 mRNA. Translation: AAA48785.1.
PIRiI50242.
RefSeqiNP_990822.1. NM_205491.1.
UniGeneiGga.4219.

Genome annotation databases

EnsembliENSGALT00000001476; ENSGALP00000001474; ENSGALG00000001000.
GeneIDi396487.
KEGGigga:396487.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27260 mRNA. Translation: AAA48785.1.
PIRiI50242.
RefSeqiNP_990822.1. NM_205491.1.
UniGeneiGga.4219.

3D structure databases

ProteinModelPortaliQ90593.
SMRiQ90593. Positions 26-568.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi676734. 2 interactions.
IntActiQ90593. 1 interaction.
STRINGi9031.ENSGALP00000001474.

Proteomic databases

PaxDbiQ90593.
PRIDEiQ90593.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000001476; ENSGALP00000001474; ENSGALG00000001000.
GeneIDi396487.
KEGGigga:396487.

Organism-specific databases

CTDi3309.

Phylogenomic databases

eggNOGiCOG0443.
GeneTreeiENSGT00750000117237.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiQ90593.
KOiK09490.
OMAiESHQDGD.
OrthoDBiEOG780RKX.
PhylomeDBiQ90593.
TreeFamiTF105044.

Enzyme and pathway databases

ReactomeiREACT_288861. Platelet degranulation.

Miscellaneous databases

NextBioi20816526.
PROiQ90593.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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].

Entry informationi

Entry nameiGRP78_CHICK
AccessioniPrimary (citable) accession number: Q90593
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: April 1, 2015
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.