P11021 (GRP78_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
78 kDa glucose-regulated protein
Short name=GRP-78

Alternative name(s):
Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78
Heat shock 70 kDa protein 5
Immunoglobulin heavy chain-binding protein
Short name=BiP

Gene names

Name:	HSPA5
Synonyms:	GRP78

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	654 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. Ref.12
Subunit structure	Interacts with DNAJC1 (via J domain) 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 TMEM132A and TRIM21. May form a complex with ERLEC1, OS9, SEL1L and SYVN1. Interacts with MX1 By similarity. Ref.16 Ref.19 Ref.20
Subcellular location	Endoplasmic reticulum lumen. Melanosome. Cytoplasm By similarity. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.17 Ref.18
Involvement in disease	Autoantigen in rheumatoid arthritis. Ref.10
Sequence similarities	Belongs to the heat shock protein 70 family.

Ontologies

Keywords
Cellular component	Cytoplasm Endoplasmic reticulum
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	ATP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ER overload response Inferred from electronic annotation. Source: Compara ER-associated protein catabolic process Traceable author statement PubMed 19816510. Source: BHF-UCL activation of signaling protein activity involved in unfolded protein response Traceable author statement. Source: Reactome cellular response to glucose starvation Inferred from direct assay PubMed 10085239. Source: UniProtKB cerebellar Purkinje cell layer development Inferred from electronic annotation. Source: Compara cerebellum structural organization Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from mutant phenotype PubMed 10760948PubMed 12665508. Source: UniProtKB negative regulation of transforming growth factor beta receptor signaling pathway Inferred from electronic annotation. Source: Compara platelet activation Traceable author statement. Source: Reactome platelet degranulation Traceable author statement. Source: Reactome positive regulation of protein ubiquitination Inferred from electronic annotation. Source: Compara regulation of protein folding in endoplasmic reticulum Traceable author statement PubMed 19816510. Source: BHF-UCL
Cellular_component	cell surface Inferred from direct assay PubMed 12493773. Source: UniProtKB endoplasmic reticulum chaperone complex Inferred from direct assay PubMed 18400946. Source: UniProtKB endoplasmic reticulum lumen Traceable author statement. Source: Reactome endoplasmic reticulum-Golgi intermediate compartment Inferred from direct assay PubMed 15308636. Source: UniProtKB integral to endoplasmic reticulum membrane Inferred from direct assay PubMed 11181571. Source: BHF-UCL melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell midbody Inferred from direct assay PubMed 15166316. Source: UniProtKB nucleus Inferred from mutant phenotype PubMed 11943137. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from sequence or structural similarity. Source: UniProtKB calcium ion binding Traceable author statement PubMed 16130169. Source: UniProtKB chaperone binding Traceable author statement PubMed 19816510. Source: BHF-UCL misfolded protein binding Inferred from direct assay PubMed 18400946. Source: UniProtKB protein binding, bridging Non-traceable author statement. Source: UniProtKB ribosome binding Inferred from electronic annotation. Source: Compara unfolded protein binding Traceable author statement PubMed 16130169. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PAWR	Q96IZ0	8	EBI-354921,EBI-595869
Pawr	Q62627	4	EBI-354921,EBI-1187240	From a different organism.
RAF1	P04049	4	EBI-354921,EBI-365996

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Ref.12 Ref.13

Chain

19 – 654

636

78 kDa glucose-regulated protein

PRO_0000013566

Regions

Motif

651 – 654

4

Prevents secretion from ER

Amino acid modifications

Modified residue

166

1

Phosphothreonine By similarity

Modified residue

518

1

Phosphothreonine Ref.21

Modified residue

571

1

Phosphoserine By similarity

Natural variations

Natural variant

543

1

N → H. Ref.5
Corresponds to variant rs35356639 [ dbSNP | Ensembl ].

VAR_025815

Experimental info

Sequence conflict

297

1

Missing Ref.1

Sequence conflict

297

1

Missing Ref.2

Sequence conflict

418

1

D → H Ref.1

Sequence conflict

418

1

D → H Ref.2

Sequence conflict

439

1

R → S Ref.1

Sequence conflict

439

1

R → S Ref.2

Sequence conflict

447

1

K → N Ref.1

Sequence conflict

447

1

K → N Ref.2

Secondary structure

1

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654

Helix Strand Turn

Details...

Beta strand

31 – 34

4

Beta strand

37 – 46

10

Beta strand

49 – 52

4

Beta strand

60 – 63

4

Beta strand

66 – 68

3

Beta strand

74 – 76

3

Helix

78 – 82

5

Helix

84 – 86

3

Helix

88 – 90

3

Beta strand

91 – 93

3

Helix

95 – 97

3

Turn

98 – 100

3

Helix

106 – 114

9

Beta strand

116 – 122

7

Beta strand

125 – 131

7

Beta strand

137 – 140

4

Helix

142 – 161

20

Beta strand

167 – 172

6

Helix

178 – 190

13

Beta strand

194 – 200

7

Helix

201 – 208

8

Helix

211 – 213

3

Beta strand

215 – 225

11

Beta strand

230 – 238

9

Beta strand

241 – 250

10

Helix

255 – 273

19

Helix

278 – 280

3

Helix

282 – 298

17

Turn

299 – 301

3

Beta strand

302 – 313

12

Beta strand

316 – 323

8

Helix

324 – 336

13

Helix

339 – 348

10

Helix

353 – 355

3

Beta strand

358 – 363

6

Helix

364 – 367

4

Helix

369 – 378

10

Turn

379 – 381

3

Turn

390 – 392

3

Helix

393 – 406

14

Sequences

	Sequence		Length	Mass (Da)
	P11021 [UniParc]. Last modified July 11, 2001. Version 2. Checksum: 59B7D8D85BC32A00	FASTA	654	72,333
	10 20 30 40 50 60 MKLSLVAAML LLLSAARAEE EDKKEDVGTV VGIDLGTTYS CVGVFKNGRV EIIANDQGNR 70 80 90 100 110 120 ITPSYVAFTP EGERLIGDAA KNQLTSNPEN TVFDAKRLIG RTWNDPSVQQ DIKFLPFKVV 130 140 150 160 170 180 EKKTKPYIQV DIGGGQTKTF APEEISAMVL TKMKETAEAY LGKKVTHAVV TVPAYFNDAQ 190 200 210 220 230 240 RQATKDAGTI AGLNVMRIIN EPTAAAIAYG LDKREGEKNI LVFDLGGGTF DVSLLTIDNG 250 260 270 280 290 300 VFEVVATNGD THLGGEDFDQ RVMEHFIKLY KKKTGKDVRK DNRAVQKLRR EVEKAKRALS 310 320 330 340 350 360 SQHQARIEIE SFYEGEDFSE TLTRAKFEEL NMDLFRSTMK PVQKVLEDSD LKKSDIDEIV 370 380 390 400 410 420 LVGGSTRIPK IQQLVKEFFN GKEPSRGINP DEAVAYGAAV QAGVLSGDQD TGDLVLLDVC 430 440 450 460 470 480 PLTLGIETVG GVMTKLIPRN TVVPTKKSQI FSTASDNQPT VTIKVYEGER PLTKDNHLLG 490 500 510 520 530 540 TFDLTGIPPA PRGVPQIEVT FEIDVNGILR VTAEDKGTGN KNKITITNDQ NRLTPEEIER 550 560 570 580 590 600 MVNDAEKFAE EDKKLKERID TRNELESYAY SLKNQIGDKE KLGGKLSSED KETMEKAVEE 610 620 630 640 650 KIEWLESHQD ADIEDFKAKK KELEEIVQPI ISKLYGSAGP PPTGEEDTAE KDEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: structure, conservation, and regulation." Ting J., Lee A.S. DNA 7:275-286(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Chao C.C.K. Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Cervix carcinoma.
[3]	"Grp78 is involved in the quality control of the LDL-receptor." Hansen J.J., Nielsen M.N., Jorgensen M.M., Gregersen N., Bolund L. Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fibroblast.
[4]	"Sequence differences between human grp78/BiP isolated from HeLa cells and previously reported human sequences." Bermudez-Fajardo A., Llewellyn D.H., Campbell A.K., Errington R.R. Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	NIEHS SNPs program Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-543.
[6]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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]. Tissue: Muscle.
[9]	"A direct-repeat sequence of the human BiP gene is required for A23187-mediated inducibility and an inducible nuclear factor binding." Chao C.C.K., Lin-Chao S. Nucleic Acids Res. 20:6481-6485(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
[10]	"The human endoplasmic reticulum molecular chaperone BiP is an autoantigen for rheumatoid arthritis and prevents the induction of experimental arthritis." Corrigall V.M., Bodman-Smith M.D., Fife M.S., Canas B., Myers L.K., Wooley P., Soh C., Staines N.A., Pappin D.J.C., Berlo S.E., van Eden W., van Der Zee R., Lanchbury J.S., Panayi G.S. J. Immunol. 166:1492-1498(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-650, DISEASE. Tissue: Articular cartilage.
[11]	"Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2." Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E., Simpson R.J., Dorow D.S. Electrophoresis 18:588-598(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-38. Tissue: Mammary carcinoma.
[12]	"Heat shock proteins bind calcitonin." Dana R.C., Welch W.J., Deftos L.J. Endocrinology 126:672-674(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-39, FUNCTION.
[13]	"A two-dimensional gel database of human colon carcinoma proteins." Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J. Electrophoresis 18:605-613(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-40. Tissue: Colon carcinoma.
[14]	Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 61-74; 82-96; 102-113; 124-152; 164-181; 186-214; 307-336; 353-367; 448-464; 475-492; 563-573; 602-617 AND 622-654, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[15]	"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.
[16]	"Association of stress proteins with autoantigens: a possible mechanism for triggering autoimmunity?" Purcell A.W., Todd A., Kinoshita G., Lynch T.A., Keech C.L., Gething M.J., Gordon T.P. Clin. Exp. Immunol. 132:193-200(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TRIM21.
[17]	"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins." Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E. J. Proteome Res. 2:69-79(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Melanoma.
[18]	"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F. J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Melanoma.
[19]	"Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP." Hosokawa N., Wada I., Nagasawa K., Moriyama T., Okawa K., Nagata K. J. Biol. Chem. 283:20914-20924(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ERLEC1; OS9; SEL1L AND SYVN1.
[20]	"OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD." Christianson J.C., Shaler T.A., Tyler R.E., Kopito R.R. Nat. Cell Biol. 10:272-282(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ERLEC1; OS9; SEL1L AND SYVN1.
[21]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-518, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M19645 Genomic DNA. Translation: AAA52614.1.
X87949 mRNA. Translation: CAA61201.1.
AJ271729 mRNA. Translation: CAB71335.1.
AF216292 mRNA. Translation: AAF42836.1.
DQ385847 Genomic DNA. Translation: ABD04090.1.
AL354710 Genomic DNA. Translation: CAQ08732.1.
CH471090 Genomic DNA. Translation: EAW87620.1.
BC020235 mRNA. Translation: AAH20235.1.
X59969 Genomic DNA. Translation: CAA42595.1.
AF188611 mRNA. Translation: AAF13605.1. Sequence problems.

IPI

IPI00003362.

PIR

A29821.

RefSeq

NP_005338.1. NM_005347.4.

UniGene

Hs.605502.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3IUC	X-ray	2.40	A/C	26-410	[»]
3LDL	X-ray	2.30	A/B	26-407	[»]
3LDN	X-ray	2.20	A/B	26-407	[»]
3LDO	X-ray	1.95	A/B	26-407	[»]
3LDP	X-ray	2.20	A/B	26-407	[»]

ProteinModelPortal

P11021.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33189N.

IntAct

P11021. 62 interactions.

MINT

MINT-1135308.

STRING

9606.ENSP00000324173.

PTM databases

PhosphoSite

P11021.

Polymorphism databases

DMDM

14916999.

2D gel databases

DOSAC-COBS-2DPAGE

P11021.

OGP

P11021.

REPRODUCTION-2DPAGE

P11021.

SWISS-2DPAGE

P11021.

UCD-2DPAGE

P11021.

Proteomic databases

PaxDb

P11021.

PRIDE

P11021.

Protocols and materials databases

DNASU

3309.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000324460; ENSP00000324173; ENSG00000044574.

GeneID

3309.

KEGG

hsa:3309.

UCSC

uc004bpn.3. human.

Organism-specific databases

CTD

3309.

GeneCards

GC09M127997.

HGNC

HGNC:5238. HSPA5.

HPA

CAB005221.
HPA038845.
HPA038846.

MIM

138120. gene.

neXtProt

NX_P11021.

PharmGKB

PA29504.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0443.

HOGENOM

HOG000228135.

HOVERGEN

HBG051845.

InParanoid

P11021.

KO

K09490.

OMA

DKRAVQK.

OrthoDB

EOG444KJV.

PhylomeDB

P11021.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

Bgee

P11021.

CleanEx

HS_HSPA5.

Genevestigator

P11021.

GermOnline

ENSG00000044574. Homo sapiens.

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

BindingDB

P11021.

ChEMBL

CHEMBL1781865.

ChiTaRS

HSPA5. human.

DrugBank

DB00025. Antihemophilic Factor.

EvolutionaryTrace

P11021.

GenomeRNAi

3309.

NextBio

13123.

SOURCE

Search...

Entry information

Entry name

GRP78_HUMAN

Accession

Primary (citable) accession number: P11021
Secondary accession number(s): B0QZ61 , Q2EF78, Q9NPF1, Q9UK02

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 11, 2001
Last modified:	May 1, 2013
This is version 157 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.