SubmitCancel

Skip Header

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

P16474

- GRP78_YEAST

UniProt

P16474 - GRP78_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

78 kDa glucose-regulated protein homolog

Gene
KAR2, GRP78, SSD1, YJL034W, J1248
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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 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.1 Publication

GO - Molecular functioni

  1. ATPase activity Source: SGD
  2. ATP binding Source: UniProtKB-KW
  3. protein binding Source: IntAct
  4. unfolded protein binding Source: SGD

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. ER-associated ubiquitin-dependent protein catabolic process Source: SGD
  3. karyogamy involved in conjugation with cellular fusion Source: SGD
  4. posttranslational protein targeting to membrane, translocation Source: SGD
  5. response to unfolded protein Source: SGD
  6. SRP-dependent cotranslational protein targeting to membrane, translocation Source: SGD
Complete GO annotation...

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31501-MONOMER.
ReactomeiREACT_108597. ATF6-alpha activates chaperone genes.

Names & Taxonomyi

Protein namesi
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 namesi
Name:KAR2
Synonyms:GRP78, SSD1
Ordered Locus Names:YJL034W
ORF Names:J1248
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome X

Organism-specific databases

CYGDiYJL034w.
SGDiS000003571. KAR2.

Subcellular locationi

Endoplasmic reticulum lumen 1 Publication

GO - Cellular componenti

  1. endoplasmic reticulum Source: SGD
  2. luminal surveillance complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4242 Reviewed predictionAdd
BLAST
Chaini43 – 68264078 kDa glucose-regulated protein homologPRO_0000013587Add
BLAST

Proteomic databases

MaxQBiP16474.
PaxDbiP16474.
PeptideAtlasiP16474.
PRIDEiP16474.

2D gel databases

SWISS-2DPAGEP16474.

Expressioni

Gene expression databases

GenevestigatoriP16474.

Interactioni

Subunit structurei

Interacts with EPS1, PDI1 and YOS9.

Binary interactionsi

WithEntry#Exp.IntActNotes
IDP1P219542EBI-7876,EBI-8898
YOS9Q992202EBI-7876,EBI-34938

Protein-protein interaction databases

BioGridi33726. 443 interactions.
DIPiDIP-2392N.
IntActiP16474. 99 interactions.
MINTiMINT-506436.
STRINGi4932.YJL034W.

Structurei

Secondary structure

1
682
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi53 – 575
Beta strandi59 – 679
Beta strandi72 – 743
Beta strandi82 – 854
Beta strandi88 – 903
Beta strandi95 – 984
Helixi99 – 1035
Helixi105 – 1073
Helixi109 – 1113
Helixi116 – 1183
Turni119 – 1213
Helixi127 – 1337
Beta strandi137 – 1437
Beta strandi146 – 16015
Helixi162 – 18120
Beta strandi187 – 1926
Helixi198 – 21013
Beta strandi214 – 2207
Helixi221 – 2288
Turni229 – 2324
Beta strandi238 – 2458
Beta strandi250 – 2589
Beta strandi261 – 27010
Helixi275 – 29420
Helixi298 – 3003
Helixi302 – 31817
Turni319 – 3213
Beta strandi323 – 33311
Beta strandi336 – 3438
Helixi344 – 35714
Helixi359 – 36911
Helixi373 – 3753
Beta strandi378 – 3836
Helixi384 – 3874
Helixi389 – 39810
Turni399 – 4013
Turni410 – 4123
Helixi413 – 42513
Beta strandi444 – 4485
Turni449 – 4513
Beta strandi452 – 4576
Beta strandi462 – 47110
Beta strandi481 – 4899
Helixi493 – 4953
Beta strandi496 – 5049
Beta strandi517 – 5237
Beta strandi527 – 5359
Turni536 – 5383
Beta strandi541 – 5477
Helixi555 – 56713
Helixi569 – 58012

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3H0XX-ray1.92A438-586[»]
3QFPX-ray2.26A43-426[»]
3QFUX-ray1.80A43-426[»]
3QMLX-ray2.31A/B43-426[»]
ProteinModelPortaliP16474.
SMRiP16474. Positions 48-621.

Miscellaneous databases

EvolutionaryTraceiP16474.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi679 – 6824Prevents secretion from ER

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0443.
GeneTreeiENSGT00750000117836.
HOGENOMiHOG000228135.
KOiK09490.
OMAiHITITSK.
OrthoDBiEOG728916.

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.

P16474-1 [UniParc]FASTAAdd to Basket

« Hide

MFFNRLSAGK LLVPLSVVLY ALFVVILPLQ NSFHSSNVLV RGADDVENYG    50
TVIGIDLGTT YSCVAVMKNG KTEILANEQG NRITPSYVAF TDDERLIGDA 100
AKNQVAANPQ NTIFDIKRLI GLKYNDRSVQ KDIKHLPFNV VNKDGKPAVE 150
VSVKGEKKVF TPEEISGMIL GKMKQIAEDY LGTKVTHAVV TVPAYFNDAQ 200
RQATKDAGTI AGLNVLRIVN EPTAAAIAYG LDKSDKEHQI IVYDLGGGTF 250
DVSLLSIENG VFEVQATSGD THLGGEDFDY KIVRQLIKAF KKKHGIDVSD 300
NNKALAKLKR EAEKAKRALS SQMSTRIEID SFVDGIDLSE TLTRAKFEEL 350
NLDLFKKTLK PVEKVLQDSG LEKKDVDDIV LVGGSTRIPK VQQLLESYFD 400
GKKASKGINP DEAVAYGAAV QAGVLSGEEG VEDIVLLDVN ALTLGIETTG 450
GVMTPLIKRN TAIPTKKSQI FSTAVDNQPT VMIKVYEGER AMSKDNNLLG 500
KFELTGIPPA PRGVPQIEVT FALDANGILK VSATDKGTGK SESITITNDK 550
GRLTQEEIDR MVEEAEKFAS EDASIKAKVE SRNKLENYAH SLKNQVNGDL 600
GEKLEEEDKE TLLDAANDVL EWLDDNFETA IAEDFDEKFE SLSKVAYPIT 650
SKLYGGADGS GAADYDDEDE DDDGDYFEHD EL 682
Length:682
Mass (Da):74,468
Last modified:August 1, 1990 - v1
Checksum:iA107BD03DF3F30D3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA32366. HHBYK2.
RefSeqiNP_012500.3. NM_001181468.3.

Genome annotation databases

EnsemblFungiiYJL034W; YJL034W; YJL034W.
GeneIDi853418.
KEGGisce:YJL034W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A32366. HHBYK2.
RefSeqi NP_012500.3. NM_001181468.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P16474.
SMRi P16474. Positions 48-621.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33726. 443 interactions.
DIPi DIP-2392N.
IntActi P16474. 99 interactions.
MINTi MINT-506436.
STRINGi 4932.YJL034W.

2D gel databases

SWISS-2DPAGE P16474.

Proteomic databases

MaxQBi P16474.
PaxDbi P16474.
PeptideAtlasi P16474.
PRIDEi P16474.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YJL034W ; YJL034W ; YJL034W .
GeneIDi 853418.
KEGGi sce:YJL034W.

Organism-specific databases

CYGDi YJL034w.
SGDi S000003571. KAR2.

Phylogenomic databases

eggNOGi COG0443.
GeneTreei ENSGT00750000117836.
HOGENOMi HOG000228135.
KOi K09490.
OMAi HITITSK.
OrthoDBi EOG728916.

Enzyme and pathway databases

BioCyci YEAST:G3O-31501-MONOMER.
Reactomei REACT_108597. ATF6-alpha activates chaperone genes.

Miscellaneous databases

EvolutionaryTracei P16474.
NextBioi 973939.
PROi P16474.

Gene expression databases

Genevestigatori P16474.

Family and domain databases

Gene3Di 1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProi IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view ]
Pfami PF00012. HSP70. 1 hit.
[Graphical view ]
PRINTSi PR00301. HEATSHOCK70.
SUPFAMi SSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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], SUBCELLULAR LOCATION.
  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.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. 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. "A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation."
    Denic V., Quan E.M., Weissman J.S.
    Cell 126:349-359(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YOS9.

Entry informationi

Entry nameiGRP78_YEAST
AccessioniPrimary (citable) accession number: P16474
Secondary accession number(s): D6VWE9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: September 3, 2014
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 337000 molecules/cell in log phase SD medium.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

External Data

Dasty 3

Similar proteinsi