P20029 (GRP78_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Hspa5
Synonyms:	Grp78

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	655 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.
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 MX1. Ref.11 Ref.13 Ref.16
Subcellular location	Endoplasmic reticulum lumen. Melanosome By similarity. Cytoplasm Ref.16.
Sequence similarities	Belongs to the heat shock protein 70 family.

Ontologies

Keywords
Cellular component	Cytoplasm Endoplasmic reticulum
Domain	Signal
Ligand	ATP-binding Nucleotide-binding
PTM	Nitration Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ER 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 glucose starvation Inferred from electronic annotation. Source: Compara 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: Compara 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_component	cell surface Inferred from direct assay PubMed 17991893. Source: MGI endoplasmic reticulum chaperone complex Inferred from electronic annotation. Source: Compara endoplasmic reticulum lumen Inferred from direct assay PubMed 19816510. Source: BHF-UCL endoplasmic reticulum-Golgi intermediate compartment Inferred from electronic annotation. Source: Compara extracellular region Traceable author statement. Source: Reactome integral to endoplasmic reticulum membrane Inferred from electronic annotation. Source: Compara melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell midbody Inferred from electronic annotation. Source: Compara perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara signalosome Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cysteine-type endopeptidase inhibitor activity involved in apoptotic process Inferred from electronic annotation. Source: Compara 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
ERN1	O75460	2	EBI-772325,EBI-371750	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Ref.2 Ref.7
	Chain	20 – 655	636	78 kDa glucose-regulated protein		PRO_0000013568
Regions
	Motif	652 – 655	4	Prevents secretion from ER
Amino acid modifications
	Modified residue	161	1	Nitrated tyrosine Ref.12
	Modified residue	167	1	Phosphothreonine Ref.15
	Modified residue	519	1	Phosphothreonine By similarity
	Modified residue	572	1	Phosphoserine Ref.15
	Modified residue	650	1	Phosphoserine Ref.14
Experimental info
	Sequence conflict	43	1	V → F in BAA11462. Ref.3
	Sequence conflict	245	1	V → W in BAA11462. Ref.3
	Sequence conflict	329	1	E → G in BAA11462. Ref.3
	Sequence conflict	361	1	V → A in BAA11462. Ref.3
	Sequence conflict	474	1	T → R in CAA05361. Ref.1
	Sequence conflict	591	1	D → G in AAA37742. Ref.9
	Sequence conflict	596	1	E → K AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P20029 [UniParc]. Last modified November 1, 1997. Version 3. Checksum: AFB795D15E20FAC2	FASTA	655	72,422
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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, MASS SPECTROMETRY. Tissue: Brain.
[13]	"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.
[14]	"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, MASS SPECTROMETRY. Tissue: Liver.
[15]	Lubec G., Kang S. Submitted (APR-2007) to UniProtKB Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-167 AND SER-572, MASS SPECTROMETRY. Tissue: Brain.
[16]	"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.
+	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.
IPI	IPI00319992.
PIR	A37048.
RefSeq	NP_001156906.1. NM_001163434.1. NP_071705.3. NM_022310.3.
UniGene	Mm.330160.
3D structure databases
ProteinModelPortal	P20029.
SMR	P20029. Positions 27-638.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-32341N.
IntAct	P20029. 12 interactions.
MINT	MINT-1177274.
PTM databases
PhosphoSite	P20029.
2D gel databases
COMPLUYEAST-2DPAGE	P20029.
REPRODUCTION-2DPAGE	IPI00319992. P20029.
SWISS-2DPAGE	P20029.
UCD-2DPAGE	P20029.
Proteomic databases
PaxDb	P20029.
PRIDE	P20029.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000028222; ENSMUSP00000028222; ENSMUSG00000026864. ENSMUST00000100171; ENSMUSP00000097747; ENSMUSG00000026864.
GeneID	14828.
KEGG	mmu:14828.
Organism-specific databases
CTD	3309.
MGI	MGI:95835. Hspa5.
Phylogenomic databases
eggNOG	COG0443.
GeneTree	ENSGT00550000074467.
HOGENOM	HOG000228135.
HOVERGEN	HBG051845.
InParanoid	P20029.
KO	K09490.
OMA	DKRAVQK.
OrthoDB	EOG444KJV.
Enzyme and pathway databases
Reactome	REACT_89750. Hemostasis.
Gene expression databases
ArrayExpress	P20029.
Bgee	P20029.
CleanEx	MM_HSPA5.
Genevestigator	P20029.
GermOnline	ENSMUSG00000026864. Mus musculus.
Family and domain databases
InterPro	IPR018181. Heat_shock_70_CS. IPR013126. Hsp_70_fam. [Graphical view]
Pfam	PF00012. HSP70. 1 hit. [Graphical view]
PRINTS	PR00301. HEATSHOCK70.
PROSITE	PS00014. ER_TARGET. 1 hit. PS00297. HSP70_1. 1 hit. PS00329. HSP70_2. 1 hit. PS01036. HSP70_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	HSPA5. mouse.
NextBio	287039.
SOURCE	Search...

Entry information

Entry name

GRP78_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 137 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program