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This is your chance to make annotations OR challenge other team's annotations. You may also DEFEND or suggest improvements to your own annotations IF they have been challenged. Please note, although we ENCOURAGE challenges, an excess of identical challenges that do not appear to be applicable to the annotation or well thought out will be considered spam and ignored.

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SCHPO:GRP78

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Species (Taxon ID) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). (284812)
Gene Name(s) bip1 (synonyms: bip)
Protein Name(s) 78 kDa glucose-regulated protein homolog

GRP-78 Immunoglobulin heavy chain-binding protein homolog BiP

External Links
UniProt P36604
EMBL X64416
CU329670
PIR S20877
T38155
RefSeq NP_593245.1
ProteinModelPortal P36604
SMR P36604
BioGrid 278306
IntAct P36604
MINT MINT-4688922
STRING 4896.SPAC22A12.15c-1
PaxDb P36604
PRIDE P36604
EnsemblFungi [example_ID SPAC22A12.15c.1]
GeneID 2541815
KEGG spo:SPAC22A12.15c
PomBase SPAC22A12.15c
eggNOG COG0443
HOGENOM HOG000228135
KO K09490
OMA CWIALLF
OrthoDB EOG728916
NextBio 20802903
PRO PR:P36604
GO GO:0005788
GO:0005794
GO:0031965
GO:0005524
GO:0016887
GO:0051082
GO:0051084
GO:0034620
GO:0030433
InterPro IPR018181
IPR013126
Pfam PF00012
PRINTS PR00301
PROSITE PS00014
PS00297
PS00329
PS01036

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0000166

nucleotide binding

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0547

F

Seeded From UniProt

GO:0005515

protein binding

PMID:9860839[1]

IPI: Inferred from Physical Interaction

PomBase:SPAC3C7.11c

F

Seeded From UniProt

GO:0005524

ATP binding

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0067

F

Seeded From UniProt

GO:0005783

endoplasmic reticulum

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0256

C

Seeded From UniProt

GO:0005783

endoplasmic reticulum

PMID:16823372[2]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

GO:0005788

endoplasmic reticulum lumen

GO_REF:0000039

IEA: Inferred from Electronic Annotation

UniProtKB-SubCell:SL-0096

C

Seeded From UniProt

GO:0005788

endoplasmic reticulum lumen

PMID:1373379[3]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

GO:0005794

Golgi apparatus

PMID:16823372[2]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

GO:0006200

ATP catabolic process

GO_REF:0000024

ISO: Inferred from Sequence Orthology

SGD:S000003571

P

Seeded From UniProt

GO:0006950

response to stress

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0346

P

Seeded From UniProt

GO:0016887

ATPase activity

GO_REF:0000024

ISO: Inferred from Sequence Orthology

SGD:S000003571

F

Seeded From UniProt

GO:0030433

ER-associated ubiquitin-dependent protein catabolic process

GO_REF:0000024

ISO: Inferred from Sequence Orthology

SGD:S000003571

P

Seeded From UniProt

GO:0031965

nuclear membrane

PMID:1373379[3]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

GO:0034620

cellular response to unfolded protein

GO_REF:0000024

ISO: Inferred from Sequence Orthology

SGD:S000003571

P

Seeded From UniProt

GO:0051082

unfolded protein binding

GO_REF:0000024

ISO: Inferred from Sequence Orthology

SGD:S000003571

F

Seeded From UniProt

GO:0051084

'de novo' posttranslational protein folding

PMID:9860839[1]

IDA: Inferred from Direct Assay

P

Seeded From UniProt

GO:0005783

endoplasmic reticulum

PMID:8227200[4]

IDA: Inferred from Direct Assay

C

Figure 6E: Confocal immunofluorescence microscopy results indicate that BiP protein is localized in the Endoplasmic Reticulum of S. pombe strain 972.

complete

GO:0005783

endoplasmic reticulum

PMID:10641037[5]

IDA: Inferred from Direct Assay

C

Figure 3A: immunofluorescence microscopy results indicate that BiP1 is localized in the Endoplasmic reticulum.

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Jannatipour, M et al. (1998) Calnexin and BiP interact with acid phosphatase independently of glucose trimming and reglucosylation in Schizosaccharomyces pombe. Biochemistry 37 17253-61 PubMed GONUTS page
  2. 2.0 2.1 Matsuyama, A et al. (2006) ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe. Nat. Biotechnol. 24 841-7 PubMed GONUTS page
  3. 3.0 3.1 Pidoux, AL & Armstrong, J (1992) Analysis of the BiP gene and identification of an ER retention signal in Schizosaccharomyces pombe. EMBO J. 11 1583-91 PubMed GONUTS page
  4. Pidoux, AL & Armstrong, J (1993) The BiP protein and the endoplasmic reticulum of Schizosaccharomyces pombe: fate of the nuclear envelope during cell division. J. Cell. Sci. 105 ( Pt 4) 1115-20 PubMed GONUTS page
  5. Brazer, SC et al. (2000) A fission yeast kinesin affects Golgi membrane recycling. Yeast 16 149-66 PubMed GONUTS page