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P20029 (GRP78_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length655 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. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate By similarity.

Subunit structure

Interacts with TMEM132A and TRIM21. May form a complex with ERLEC1, OS9, SEL1L and SYVN1 By similarity. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. Interacts with DNAJC1 (via J domain). Interacts with METTL23 By similarity. Interacts with DNAJC10 and MX1. Ref.11 Ref.12 Ref.14 Ref.17

Subcellular location

Endoplasmic reticulum lumen. Melanosome By similarity. Cytoplasm Ref.17.

Sequence similarities

Belongs to the heat shock protein 70 family.

Ontologies

Keywords
   Cellular componentCytoplasm
Endoplasmic reticulum
   DomainSignal
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
Methylation
Nitration
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processER overload response

Inferred from direct assay PubMed 11854325. Source: MGI

activation of signaling protein activity involved in unfolded protein response

Inferred from mutant phenotype PubMed 19816510. Source: BHF-UCL

cellular response to antibiotic

Inferred from electronic annotation. Source: Ensembl

cellular response to glucose starvation

Inferred from electronic annotation. Source: Ensembl

cellular response to interleukin-4

Inferred from direct assay PubMed 9798653. Source: MGI

cerebellar Purkinje cell layer development

Inferred from mutant phenotype PubMed 19816510. Source: BHF-UCL

cerebellum structural organization

Inferred from mutant phenotype PubMed 19816510. Source: BHF-UCL

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of transforming growth factor beta receptor signaling pathway

Inferred from genetic interaction PubMed 17991893. Source: MGI

positive regulation of embryonic development

Traceable author statement PubMed 19816510. Source: BHF-UCL

positive regulation of protein ubiquitination

Inferred from mutant phenotype PubMed 19816510. Source: BHF-UCL

proteolysis involved in cellular protein catabolic process

Inferred from direct assay PubMed 18923430. Source: BHF-UCL

   Cellular_componentCOP9 signalosome

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from direct assay PubMed 17991893. Source: MGI

endoplasmic reticulum chaperone complex

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum lumen

Inferred from direct assay PubMed 19816510. Source: BHF-UCL

endoplasmic reticulum-Golgi intermediate compartment

Inferred from direct assay PubMed 21187406. Source: MGI

extracellular region

Traceable author statement. Source: Reactome

integral component of endoplasmic reticulum membrane

Inferred from electronic annotation. Source: Ensembl

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

midbody

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

misfolded protein binding

Inferred from direct assay PubMed 18923430. Source: BHF-UCL

ribosome binding

Inferred from direct assay Ref.11. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ERN1O754602EBI-772325,EBI-371750From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.2 Ref.7
Chain20 – 65563678 kDa glucose-regulated protein
PRO_0000013568

Regions

Nucleotide binding37 – 404ATP By similarity
Nucleotide binding228 – 2303ATP By similarity
Nucleotide binding294 – 3018ATP By similarity
Nucleotide binding365 – 3684ATP By similarity
Motif652 – 6554Prevents secretion from ER

Sites

Binding site971ATP By similarity

Amino acid modifications

Modified residue1261N6-acetyllysine
Modified residue1611Nitrated tyrosine Ref.13
Modified residue2141N6-acetyllysine
Modified residue3271N6-acetyllysine
Modified residue3541N6-acetyllysine
Modified residue4481N6-succinyllysine
Modified residue5191Phosphothreonine By similarity
Modified residue5861N6,N6,N6-trimethyllysine; by METTL21A; in vitro Ref.18
Modified residue6501Phosphoserine Ref.15

Experimental info

Sequence conflict431V → F in BAA11462. Ref.3
Sequence conflict2451V → W in BAA11462. Ref.3
Sequence conflict3291E → G in BAA11462. Ref.3
Sequence conflict3611V → A in BAA11462. Ref.3
Sequence conflict4741T → R in CAA05361. Ref.1
Sequence conflict5911D → G in AAA37742. Ref.9
Sequence conflict5961E → K AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P20029 [UniParc].

Last modified November 1, 1997. Version 3.
Checksum: AFB795D15E20FAC2

FASTA65572,422
        10         20         30         40         50         60 
MMKFTVVAAA LLLLGAVRAE EEDKKEDVGT VVGIDLGTTY SCVGVFKNGR VEIIANDQGN 

        70         80         90        100        110        120 
RITPSYVAFT PEGERLIGDA AKNQLTSNPE NTVFDAKRLI GRTWNDPSVQ QDIKFLPFKV 

       130        140        150        160        170        180 
VEKKTKPYIQ VDIGGGQTKT FAPEEISAMV LTKMKETAEA YLGKKVTHAV VTVPAYFNDA 

       190        200        210        220        230        240 
QRQATKDAGT IAGLNVMRII NEPTAAAIAY GLDKREGEKN ILVFDLGGGT FDVSLLTIDN 

       250        260        270        280        290        300 
GVFEVVATNG DTHLGGEDFD QRVMEHFIKL YKKKTGKDVR KDNRAVQKLR REVEKAKRAL 

       310        320        330        340        350        360 
SSQHQARIEI ESFFEGEDFS ETLTRAKFEE LNMDLFRSTM KPVQKVLEDS DLKKSDIDEI 

       370        380        390        400        410        420 
VLVGGSTRIP KIQQLVKEFF NGKEPSRGIN PDEAVAYGAA VQAGVLSGDQ DTGDLVLLDV 

       430        440        450        460        470        480 
CPLTLGIETV GGVMTKLIPR NTVVPTKKSQ IFSTASDNQP TVTIKVYEGE RPLTKDNHLL 

       490        500        510        520        530        540 
GTFDLTGIPP APRGVPQIEV TFEIDVNGIL RVTAEDKGTG NKNKITITND QNRLTPEEIE 

       550        560        570        580        590        600 
RMVNDAEKFA EEDKKLKERI DTRNELESYA YSLKNQIGDK EKLGGKLSSE DKETMEKAVE 

       610        620        630        640        650 
EKIEWLESHQ DADIEDFKAK KKELEEIVQP IISKLYGSGG PPPTGEEDTS EKDEL 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning of the immunoglobulin heavy chain binding protein."
Haas I.G., Meo T.
Proc. Natl. Acad. Sci. U.S.A. 85:2250-2254(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Identification of immunoglobulin heavy chain binding protein as glucose-regulated protein 78 on the basis of amino acid sequence, immunological cross-reactivity, and functional activity."
Kozutsumi Y., Normington K., Press E., Slaughter C., Sambrook J., Gething M.J.
J. Cell Sci. Suppl. 11:115-137(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-46.
[3]"Molecular characterization of seizure-related genes isolated by differential screening."
Kajiwara K., Nagawawa H., Shimizu-Nishikawa K., Ookura T., Kimura M., Sugaya E.
Biochem. Biophys. Res. Commun. 219:795-799(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Brain.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[6]"Structure and regulation of the mouse GRP78 (BiP) promoter by glucose and calcium ionophore."
Tillman J.B., Mote P.L., Walford R.L., Spindler S.R.
Gene 158:225-229(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
Strain: C3B10RF1.
Tissue: Liver.
[7]"Separation and sequencing of familiar and novel murine proteins using preparative two-dimensional gel electrophoresis."
Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.
Electrophoresis 15:735-745(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-36.
Tissue: Fibroblast.
[8]Lubec G., Kang S.U., Klug S., Friebe K., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 51-75; 140-153; 156-164; 166-182; 187-215; 308-337; 354-368; 449-493; 525-541 AND 623-634, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[9]"Differential screening of a cDNA library with cDNA probes amplified in a heterologous host: isolation of murine GRP78 (BiP) and other serum-regulated low-abundance mRNAs."
Parfett C.L.J., Hofbauer R., Brudzynski K., Edwards D.R., Denhardt D.T.
Gene 82:291-303(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 488-655.
[10]"A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins."
Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.
Mol. Biol. Cell 13:4456-4469(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: COMPONENT OF A CHAPERONE COMPLEX.
[11]"A novel type of co-chaperone mediates transmembrane recruitment of DnaK-like chaperones to ribosomes."
Dudek J., Volkmer J., Bies C., Guth S., Mueller A., Lerner M., Feick P., Schaefer K.-H., Morgenstern E., Hennessy F., Blatch G.L., Janoscheck K., Heim N., Scholtes P., Frien M., Nastainczyk W., Zimmermann R.
EMBO J. 21:2958-2967(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNAJC1.
[12]"ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress."
Cunnea P.M., Miranda-Vizuete A., Bertoli G., Simmen T., Damdimopoulos A.E., Hermann S., Leinonen S., Huikko M.P., Gustafsson J.-A., Sitia R., Spyrou G.
J. Biol. Chem. 278:1059-1066(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNAJC10.
[13]"Endogenously nitrated proteins in mouse brain: links to neurodegenerative disease."
Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C., Bigelow D.J.
Biochemistry 45:8009-8022(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[14]"Age-specific CUGBP1-eIF2 complex increases translation of CCAAT/enhancer-binding protein beta in old liver."
Timchenko L.T., Salisbury E., Wang G.-L., Nguyen H., Albrecht J.H., Hershey J.W., Timchenko N.A.
J. Biol. Chem. 281:32806-32819(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN AN EIF2 COMPLEX WITH EIF2S1; EIF2S2; CELF1; CALR; CALR3 AND HSP90B1.
[15]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-650, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[16]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Interferon-inducible antiviral protein MxA enhances cell death triggered by endoplasmic reticulum stress."
Numajiri Haruki A., Naito T., Nishie T., Saito S., Nagata K.
J. Interferon Cytokine Res. 31:847-856(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MX1.
[18]"Identification and characterization of a novel human methyltransferase modulating Hsp70 function through lysine methylation."
Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S., Melki R., Falnes P.O.
J. Biol. Chem. 288:27752-27763(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-586.
[19]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-126; LYS-214; LYS-327 AND LYS-354, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ002387 mRNA. Translation: CAA05361.1.
M19351 mRNA. Translation: AAA37315.1.
D78645 mRNA. Translation: BAA11462.1.
AK076079 mRNA. Translation: BAC36166.1.
AK146647 mRNA. Translation: BAE27328.1.
AK148539 mRNA. Translation: BAE28609.1.
AK151647 mRNA. Translation: BAE30576.1.
AK152020 mRNA. Translation: BAE30882.1.
AK166739 mRNA. Translation: BAE38982.1.
AK169034 mRNA. Translation: BAE40825.1.
BC050927 mRNA. Translation: AAH50927.1.
U16277 Genomic DNA. Translation: AAA76734.1.
M30779 mRNA. Translation: AAA37742.1.
PIRA37048.
RefSeqNP_001156906.1. NM_001163434.1.
NP_071705.3. NM_022310.3.
UniGeneMm.330160.
Mm.470180.

3D structure databases

ProteinModelPortalP20029.
SMRP20029. Positions 27-638.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200078. 41 interactions.
DIPDIP-32341N.
IntActP20029. 25 interactions.
MINTMINT-1177274.

PTM databases

PhosphoSiteP20029.

2D gel databases

COMPLUYEAST-2DPAGEP20029.
REPRODUCTION-2DPAGEIPI00319992.
P20029.
SWISS-2DPAGEP20029.
UCD-2DPAGEP20029.

Proteomic databases

PaxDbP20029.
PRIDEP20029.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028222; ENSMUSP00000028222; ENSMUSG00000026864.
ENSMUST00000100171; ENSMUSP00000097747; ENSMUSG00000026864.
GeneID14828.
KEGGmmu:14828.
UCSCuc008jis.2. mouse.

Organism-specific databases

CTD3309.
MGIMGI:95835. Hspa5.

Phylogenomic databases

eggNOGCOG0443.
GeneTreeENSGT00740000115335.
HOGENOMHOG000228135.
HOVERGENHBG051845.
InParanoidP20029.
KOK09490.
OMADKRAVQK.
OrthoDBEOG780RKX.
TreeFamTF105044.

Gene expression databases

ArrayExpressP20029.
BgeeP20029.
CleanExMM_HSPA5.
GenevestigatorP20029.

Family and domain databases

InterProIPR018181. Heat_shock_70_CS.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHSPA5. mouse.
NextBio287039.
PROP20029.
SOURCESearch...

Entry information

Entry nameGRP78_MOUSE
AccessionPrimary (citable) accession number: P20029
Secondary accession number(s): O35642, Q3UFF2, Q61630
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: November 1, 1997
Last modified: March 19, 2014
This is version 147 of the entry and version 3 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot