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Protein

78 kDa glucose-regulated protein homolog

Gene

KAR2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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

  • ATPase activity Source: SGD
  • ATP binding Source: UniProtKB-KW
  • unfolded protein binding Source: SGD

GO - Biological processi

  • ER-associated ubiquitin-dependent protein catabolic process Source: SGD
  • fungal-type cell wall beta-glucan biosynthetic process Source: SGD
  • karyogamy involved in conjugation with cellular fusion Source: SGD
  • posttranslational protein targeting to membrane, translocation Source: SGD
  • response to unfolded protein Source: SGD
  • 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.
ReactomeiR-SCE-3371453. Regulation of HSF1-mediated heat shock response.
R-SCE-3371568. Attenuation phase.
R-SCE-3371571. HSF1-dependent transactivation.
R-SCE-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-SCE-6798695. Neutrophil degranulation.

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
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL034W.
SGDiS000003571. KAR2.

Subcellular locationi

  • Endoplasmic reticulum lumen PROSITE-ProRule annotation1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 42Sequence analysisAdd BLAST42
ChainiPRO_000001358743 – 68278 kDa glucose-regulated protein homologAdd BLAST640

Proteomic databases

MaxQBiP16474.
PRIDEiP16474.

2D gel databases

SWISS-2DPAGEP16474.

PTM databases

iPTMnetiP16474.

Interactioni

Subunit structurei

Interacts with EPS1, PDI1 and YOS9.2 Publications

Binary interactionsi

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

GO - Molecular functioni

  • unfolded protein binding Source: SGD

Protein-protein interaction databases

BioGridi33726. 442 interactors.
DIPiDIP-2392N.
IntActiP16474. 99 interactors.
MINTiMINT-506436.

Structurei

Secondary structure

1682
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi53 – 57Combined sources5
Beta strandi59 – 67Combined sources9
Beta strandi72 – 74Combined sources3
Beta strandi82 – 85Combined sources4
Beta strandi88 – 90Combined sources3
Beta strandi95 – 98Combined sources4
Helixi99 – 103Combined sources5
Helixi105 – 107Combined sources3
Helixi109 – 111Combined sources3
Helixi116 – 118Combined sources3
Turni119 – 121Combined sources3
Helixi127 – 133Combined sources7
Beta strandi137 – 143Combined sources7
Beta strandi146 – 160Combined sources15
Helixi162 – 181Combined sources20
Beta strandi187 – 192Combined sources6
Helixi198 – 210Combined sources13
Beta strandi214 – 220Combined sources7
Helixi221 – 228Combined sources8
Turni229 – 232Combined sources4
Beta strandi238 – 245Combined sources8
Beta strandi250 – 258Combined sources9
Beta strandi261 – 270Combined sources10
Helixi275 – 294Combined sources20
Helixi298 – 300Combined sources3
Helixi302 – 318Combined sources17
Turni319 – 321Combined sources3
Beta strandi323 – 333Combined sources11
Beta strandi336 – 343Combined sources8
Helixi344 – 357Combined sources14
Helixi359 – 369Combined sources11
Helixi373 – 375Combined sources3
Beta strandi378 – 383Combined sources6
Helixi384 – 387Combined sources4
Helixi389 – 398Combined sources10
Turni399 – 401Combined sources3
Turni410 – 412Combined sources3
Helixi413 – 425Combined sources13
Beta strandi444 – 448Combined sources5
Turni449 – 451Combined sources3
Beta strandi452 – 457Combined sources6
Beta strandi462 – 471Combined sources10
Beta strandi481 – 489Combined sources9
Helixi493 – 495Combined sources3
Beta strandi496 – 504Combined sources9
Beta strandi517 – 523Combined sources7
Beta strandi527 – 535Combined sources9
Turni536 – 538Combined sources3
Beta strandi541 – 547Combined sources7
Helixi555 – 567Combined sources13
Helixi569 – 580Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3H0XX-ray1.92A438-586[»]
3QFPX-ray2.26A43-426[»]
3QFUX-ray1.80A43-426[»]
3QMLX-ray2.31A/B43-426[»]
ProteinModelPortaliP16474.
SMRiP16474.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16474.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi679 – 682Prevents secretion from ER4

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

GeneTreeiENSGT00860000134073.
HOGENOMiHOG000228135.
InParanoidiP16474.
KOiK09490.
OMAiTKDALEW.
OrthoDBiEOG092C1VPN.

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

        10         20         30         40         50
MFFNRLSAGK LLVPLSVVLY ALFVVILPLQ NSFHSSNVLV RGADDVENYG
60 70 80 90 100
TVIGIDLGTT YSCVAVMKNG KTEILANEQG NRITPSYVAF TDDERLIGDA
110 120 130 140 150
AKNQVAANPQ NTIFDIKRLI GLKYNDRSVQ KDIKHLPFNV VNKDGKPAVE
160 170 180 190 200
VSVKGEKKVF TPEEISGMIL GKMKQIAEDY LGTKVTHAVV TVPAYFNDAQ
210 220 230 240 250
RQATKDAGTI AGLNVLRIVN EPTAAAIAYG LDKSDKEHQI IVYDLGGGTF
260 270 280 290 300
DVSLLSIENG VFEVQATSGD THLGGEDFDY KIVRQLIKAF KKKHGIDVSD
310 320 330 340 350
NNKALAKLKR EAEKAKRALS SQMSTRIEID SFVDGIDLSE TLTRAKFEEL
360 370 380 390 400
NLDLFKKTLK PVEKVLQDSG LEKKDVDDIV LVGGSTRIPK VQQLLESYFD
410 420 430 440 450
GKKASKGINP DEAVAYGAAV QAGVLSGEEG VEDIVLLDVN ALTLGIETTG
460 470 480 490 500
GVMTPLIKRN TAIPTKKSQI FSTAVDNQPT VMIKVYEGER AMSKDNNLLG
510 520 530 540 550
KFELTGIPPA PRGVPQIEVT FALDANGILK VSATDKGTGK SESITITNDK
560 570 580 590 600
GRLTQEEIDR MVEEAEKFAS EDASIKAKVE SRNKLENYAH SLKNQVNGDL
610 620 630 640 650
GEKLEEEDKE TLLDAANDVL EWLDDNFETA IAEDFDEKFE SLSKVAYPIT
660 670 680
SKLYGGADGS GAADYDDEDE DDDGDYFEHD EL
Length:682
Mass (Da):74,468
Last modified:August 1, 1990 - v1
Checksum:iA107BD03DF3F30D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3H0XX-ray1.92A438-586[»]
3QFPX-ray2.26A43-426[»]
3QFUX-ray1.80A43-426[»]
3QMLX-ray2.31A/B43-426[»]
ProteinModelPortaliP16474.
SMRiP16474.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33726. 442 interactors.
DIPiDIP-2392N.
IntActiP16474. 99 interactors.
MINTiMINT-506436.

PTM databases

iPTMnetiP16474.

2D gel databases

SWISS-2DPAGEP16474.

Proteomic databases

MaxQBiP16474.
PRIDEiP16474.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YJL034W.
SGDiS000003571. KAR2.

Phylogenomic databases

GeneTreeiENSGT00860000134073.
HOGENOMiHOG000228135.
InParanoidiP16474.
KOiK09490.
OMAiTKDALEW.
OrthoDBiEOG092C1VPN.

Enzyme and pathway databases

BioCyciYEAST:G3O-31501-MONOMER.
ReactomeiR-SCE-3371453. Regulation of HSF1-mediated heat shock response.
R-SCE-3371568. Attenuation phase.
R-SCE-3371571. HSF1-dependent transactivation.
R-SCE-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-SCE-6798695. Neutrophil degranulation.

Miscellaneous databases

EvolutionaryTraceiP16474.
PROiP16474.

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]
ProtoNetiSearch...

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: November 30, 2016
This is version 180 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.1 Publication

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.