78 kDa glucose-regulated protein homolog precursor - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P16474 (GRP78_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 143. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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

Alternative name(s):
Immunoglobulin heavy chain-binding protein homolog
Short name=BiP

Gene names

Name:	KAR2
Synonyms:	GRP78, SSD1
Ordered Locus Names:	YJL034W
ORF Names:	J1248

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	682 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. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis. Ref.7
Subunit structure	Interacts with EPS1 and PDI1. Ref.7
Subcellular location	Endoplasmic reticulum lumen.
Miscellaneous	Present with 337000 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the heat shock protein 70 family.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Endoplasmic reticulum
Domain	Signal
Ligand	ATP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER-associated protein catabolic process Inferred from mutant phenotype PubMed 11381090. Source: SGD SRP-dependent cotranslational protein targeting to membrane, translocation Inferred from mutant phenotype PubMed 7568189. Source: SGD karyogamy involved in conjugation with cellular fusion Inferred from mutant phenotype PubMed 10069807. Source: SGD posttranslational protein targeting to membrane, translocation Inferred from direct assay PubMed 10367885. Source: SGD response to unfolded protein Inferred from mutant phenotype PubMed 12808051. Source: SGD
Cellular_component	luminal surveillance complex Inferred from direct assay PubMed 16873065. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from direct assay PubMed 1325440. Source: SGD unfolded protein binding Inferred from mutant phenotype PubMed 12808051. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
IDP1	P21954	2	EBI-7876,EBI-8898
YOS9	Q99220	2	EBI-7876,EBI-34938

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 42

Chain

43 – 682

640

78 kDa glucose-regulated protein homolog

PRO_0000013587

Regions

Motif

679 – 682

Prevents secretion from ER

Amino acid modifications

Modified residue

574

Phosphoserine Ref.9

Modified residue

660

Phosphoserine Ref.8 Ref.9

Modified residue

665

Phosphotyrosine Ref.9

Modified residue

676

Phosphotyrosine Ref.9

Secondary structure

682

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P16474 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: A107BD03DF3F30D3
Show »

FASTA

682

74,468

        10         20         30         40         50         60 
MFFNRLSAGK LLVPLSVVLY ALFVVILPLQ NSFHSSNVLV RGADDVENYG TVIGIDLGTT 

        70         80         90        100        110        120 
YSCVAVMKNG KTEILANEQG NRITPSYVAF TDDERLIGDA AKNQVAANPQ NTIFDIKRLI 

       130        140        150        160        170        180 
GLKYNDRSVQ KDIKHLPFNV VNKDGKPAVE VSVKGEKKVF TPEEISGMIL GKMKQIAEDY 

       190        200        210        220        230        240 
LGTKVTHAVV TVPAYFNDAQ RQATKDAGTI AGLNVLRIVN EPTAAAIAYG LDKSDKEHQI 

       250        260        270        280        290        300 
IVYDLGGGTF DVSLLSIENG VFEVQATSGD THLGGEDFDY KIVRQLIKAF KKKHGIDVSD 

       310        320        330        340        350        360 
NNKALAKLKR EAEKAKRALS SQMSTRIEID SFVDGIDLSE TLTRAKFEEL NLDLFKKTLK 

       370        380        390        400        410        420 
PVEKVLQDSG LEKKDVDDIV LVGGSTRIPK VQQLLESYFD GKKASKGINP DEAVAYGAAV 

       430        440        450        460        470        480 
QAGVLSGEEG VEDIVLLDVN ALTLGIETTG GVMTPLIKRN TAIPTKKSQI FSTAVDNQPT 

       490        500        510        520        530        540 
VMIKVYEGER AMSKDNNLLG KFELTGIPPA PRGVPQIEVT FALDANGILK VSATDKGTGK 

       550        560        570        580        590        600 
SESITITNDK GRLTQEEIDR MVEEAEKFAS EDASIKAKVE SRNKLENYAH SLKNQVNGDL 

       610        620        630        640        650        660 
GEKLEEEDKE TLLDAANDVL EWLDDNFETA IAEDFDEKFE SLSKVAYPIT SKLYGGADGS 

       670        680 
GAADYDDEDE DDDGDYFEHD EL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene." Rose M.D., Misra L.M., Vogel J.P. Cell 57:1211-1221(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"An essential member of the HSP70 gene family of Saccharomyces cerevisiae is homologous to immunoglobulin heavy chain binding protein." Nicholson R.C., Williams D.B., Moran L.A. Proc. Natl. Acad. Sci. U.S.A. 87:1159-1163(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: LL20.
[3]	"S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP." Normington K., Kohno K., Kozutsumi Y., Gething M.J., Sambrook J. Cell 57:1223-1236(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. Karpfinger-Hartl L. EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities." Kimura T., Hosoda Y., Sato Y., Kitamura Y., Ikeda T., Horibe T., Kikuchi M. J. Biol. Chem. 280:31438-31441(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH EPS1 AND PDI1.
[8]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-660, MASS SPECTROMETRY.
[9]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-574; SER-660; TYR-665 AND TYR-676, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M25064 Genomic DNA. Translation: AAA34714.1.
M25394 Genomic DNA. Translation: AAA34713.1.
M31006 Genomic DNA. Translation: AAA34454.1.
Z49309 Genomic DNA. Translation: CAA89325.1.
BK006943 Genomic DNA. Translation: DAA08765.1.

PIR

HHBYK2. A32366.

RefSeq

NP_012500.3. NM_001181468.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3H0X	X-ray	1.92	A	438-586	[»]
3QFP	X-ray	2.26	A	43-426	[»]
3QFU	X-ray	1.80	A	43-426	[»]
3QML	X-ray	2.31	A/B	43-426	[»]

ProteinModelPortal

P16474.

SMR

P16474. Positions 48-621.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2392N.

IntAct

P16474. 91 interactions.

MINT

MINT-506436.

STRING

4932.YJL034W.

2D gel databases

SWISS-2DPAGE

P16474.

Proteomic databases

PaxDb

P16474.

PeptideAtlas

P16474.

PRIDE

P16474.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YJL034W; YJL034W; YJL034W.

GeneID

853418.

KEGG

sce:YJL030W.
sce:YJL034W.

Organism-specific databases

CYGD

YJL034w.

SGD

S000003571. KAR2.

Phylogenomic databases

eggNOG

COG0443.

GeneTree

ENSGT00700000104620.

HOGENOM

HOG000228135.

K02537.
K09490.

OMA

DIVANDQ.

OrthoDB

EOG4X0R1M.

Gene expression databases

Genevestigator

P16474.

GermOnline

YJL034W. Saccharomyces cerevisiae.

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

EvolutionaryTrace

P16474.

NextBio

973939.

Entry information

Entry name

GRP78_YEAST

Accession

Primary (citable) accession number: P16474
Secondary accession number(s): D6VWE9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	May 1, 2013
This is version 143 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome X

Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents