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RefGenome Electronic Jamboree 2008-07 GCH1 and HSPD1
See the talk page for tips on editing the tables and for misc. discussion.
Contents |
Participants
| Name | Group | Organism(s)/Genome(s) | Working on |
|---|---|---|---|
|
Ruth Lovering |
BHF-UCL |
Human |
|
|
Debby Siegele |
EcoliWiki |
E. coli |
|
|
Rachael Huntley |
GOA |
Human |
|
|
Victoria Petri |
RGD |
Rat |
|
|
David Hill |
MGI |
mouse |
|
|
Stacia Engel |
SGD |
Saccharomyces cerevisiae |
|
|
Kimberly Van Auken |
WormBase |
Caenorhabditis elegans |
GCH1 = cat-4 = WBGene00000298 |
|
Ranjana Kishore |
WormBase |
C. elegans |
|
|
Petra Fey |
dictyBase |
Dictyostelium discoideum |
gchA |
|
Tanya Berardini |
TAIR |
Arabidopsis thaliana |
|
|
Fiona McCarthy |
AgBase |
Gallus gallus |
|
|
Pascale Gaudet |
dictyBase |
Dictyostelium discoideum |
hspA |
|
Susan Tweedie |
FlyBase |
Drosophila melanogaster |
|
|
Varsha Khodiyar |
BHF-UCL |
Human |
HSPD1 |
|
Emily Dimmer |
GOA |
Human |
GCH1 |
| edit table |
GCH1
| Category | ID | Term | Human | Mouse | Rat | Chicken | Zfish | Fly | Worm | Dicty | Dicot | Yeast | Pombe | Ecoli |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Molecular Function | GO:0003934 | GTP cyclohydrolase I activity | IDA | IDA ISS | IDA | X | X | IDA IMP | IEA | IDA | ISS | IMP | X | IDA |
| Molecular Function | GO:0005525 | GTP binding | IDA | X | IDA | X | X | X | X | X | X | X | X | IDA |
| Molecular Function | GO:0030742 | GTP-dependent protein binding | X | X | IPI | X | X | X | X | X | X | X | X | X |
| Molecular Function | GO:0005509 | calcium ion binding | X | X | IDA | X | X | X | X | X | X | X | X | X |
| Molecular Function | GO:0050662 | coenzyme binding | X | X | IDA | X | X | X | X | X | X | X | X | X |
| Molecular Function | GO:0008270 | zinc ion binding | IDA | X | IDA | X | X | X | X | X | X | X | X | IDA |
| Molecular Function | GO:0005515 | protein binding | IPI | X | IDA | X | X | X | X | X | X | X | X | X |
| Molecular Function | GO:0003933 | GTP cyclohydrolase activity | X | X | X | IDA | X | X | X | X | X | X | X | X |
| Biological Process | GO:0006729 | tetrahydrobiopterin biosynthetic process | IDA | IC | X | IMP IDA | X | X | X | IDA | X | X | X | X |
| Biological Process | GO:0042416 | dopamine biosynthetic process | X | X | X | X | X | IMP | IMP | X | X | X | X | X |
| Biological Process | GO:0045429 | positive regulation of nitric oxide biosynthetic process | X | X | X | IDA | X | X | X | X | X | X | X | X |
| Biological Process | GO:0009396 | folic acid and derivative biosynthetic process | X | X | X | X | X | X | X | X | X | IMP | X | X |
| Biological Process | GO:0042427 | serotonin biosynthetic process | X | X | X | X | X | X | IMP | X | X | X | X | X |
| Biological Process | GO:0014916 | regulation of lung blood pressure | X | IMP | X | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0050884 | neuromuscular process controlling posture | X | ISS | X | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0008217 | regulation of blood pressure | X | IMP | X | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0046656 | folic acid biosynthetic process | X | X | X | X | X | X | X | X | X | X | X | IDA |
| Biological Process | GO:0051066 | dihydrobiopterin metabolic process | X | X | IDA | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0006461 | protein complex assembly | X | X | IDA | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0051291 | protein heterooligomerization | X | X | IDA | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0051260 | protein homooligomerization | IDA | X | IDA | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0046654 | tetrahydrofolate biosynthetic process | X | X | X | X | X | X | X | X | X | X | X | IDA |
| Biological Process | GO:0046662 | regulation of oviposition | X | X | X | X | X | X | IMP IGI | X | X | X | X | X |
| Biological Process | GO:0043051 | regulation of pharyngeal pumping | X | X | X | X | X | X | IMP | X | X | X | X | X |
| Biological Process | GO:0008277 | regulation of G-protein coupled receptor protein signaling pathway | X | X | X | X | X | X | X | IDA | X | X | X | X |
| Biological Process | GO:0060179 | male mating behavior | X | X | X | X | X | X | IMP | X | X | X | X | X |
| Biological Process | GO:0032095 | regulation of response to food | X | X | X | X | X | X | IMP | X | X | X | X | X |
| Biological Process | GO:0009058 | biosynthetic process | X | X | X | X | X | X | X | X | IEA | X | X | X |
| Biological Process | GO:0007626 | locomotory behavior | X | X | X | X | X | X | IMP | X | X | X | X | X |
| Biological Process | GO:0019438 | aromatic compound biosynthetic process | X | X | X | X | X | X | IEA | X | X | X | X | X |
| Biological Process | GO:0040012 | regulation of locomotion | X | X | X | X | X | X | IMP | X | X | X | X | X |
| Biological Process | GO:0042438 | melanin biosynthetic process | X | X | X | X | X | X | IMP | X | X | X | X | X |
| Biological Process | GO:0040002 | collagen and cuticulin-based cuticle development | X | X | X | X | X | X | IMP | X | X | X | X | X |
| Biological Process | GO:0050804 | regulation of synaptic transmission | X | X | X | X | X | X | IMP | X | X | X | X | X |
| Biological Process | GO:0048067 | cuticle pigmentation | X | X | X | X | X | IMP | X | X | X | X | X | X |
| Biological Process | GO:0008363 | larval chitin-based cuticle development | X | X | X | X | X | IMP | X | X | X | X | X | X |
| Biological Process | GO:0042559 | pteridine and derivative biosynthetic process | IDA | X | X | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0006184 | GTP catabolic process | IDA | X | X | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0048265 | response to pain | ISS | X | X | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0035185 | preblastoderm mitotic cell cycle | X | X | X | X | X | IMP | X | X | X | X | X | X |
| Biological Process | GO:0006728 | pteridine biosynthetic process | X | X | X | X | X | IMP IDA | X | X | X | X | X | X |
| Biological Process | GO:0032496 | response to lipopolysaccharide | IDA | X | X | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0034341 | response to interferon-gamma | IDA | X | X | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0007424 | open tracheal system development | X | X | X | X | X | IMP | X | X | X | X | X | X |
| Biological Process | GO:0006809 | nitric oxide biosynthetic process | NAS | X | X | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0048754 | branching morphogenesis of a tube | X | X | X | X | X | IMP | X | X | X | X | X | X |
| Biological Process | GO:0051000 | positive regulation of nitric-oxide synthase activity | IDA | X | X | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0030334 | regulation of cell migration | X | X | X | X | X | IMP | X | X | X | X | X | X |
| Biological Process | GO:0048072 | compound eye pigmentation | X | X | X | X | X | IMP | X | X | X | X | X | X |
| Cellular Component | GO:0005737 | cytoplasm | IDA | X | X | IDA | X | IDA | IEA | X | IEA | IDA | X | X |
| Cellular Component | GO:0005634 | nucleus | IDA | X | X | X | X | X | X | X | X | IDA | X | X |
| Cellular Component | GO:0005829 | cytosol | IDA | X | X | X | X | X | X | X | X | X | X | IDA |
| Cellular Component | GO:0005625 | soluble fraction | X | X | IDA | X | X | X | X | IDA | X | X | X | X |
| Cellular Component | GO:0043234 | protein complex | X | X | IDA | X | X | X | X | X | X | X | X | IDA |
| Cellular Component | GO:0045335 | phagocytic vesicle | X | X | X | X | X | X | X | IDA | X | X | X | X |
| Cellular Component | GO:0005624 | membrane fraction | X | X | X | X | X | X | X | IDA | X | X | X | X |
| Cellular Component | GO:0031410 | cytoplasmic vesicle | IDA | X | X | X | X | X | X | X | X | X | X | X |

This figure should automatically update from the table
| Group | Organism | gene | Qualifier | GO ID | GO term name | Reference(s) | Evidence Code | with/from | Aspect | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|---|
|
EcoliWiki |
E. coli |
folE |
GO:0003934 |
GTP cyclohydrolase I activity |
IDA: Inferred from Direct Assay |
F |
FolE was purified and assayed for GTP cyclohydrolase I activity. |
complete | |||
|
FlyBase |
Drosophila |
FBgn0003162 |
GO:0003934 |
GTP cyclohydrolase I activity |
IDA: Inferred from Direct Assay |
F |
complete | ||||
|
GOA |
Human |
GCH1 (P30793-2) |
NOT |
GO:0003934 |
GTP cyclohydrolase I activity |
IDA: Inferred from Direct Assay |
F |
complete | |||
|
MGI |
Mouse |
Gch1 |
GO:0006729 |
tetrahydrobiopterin biosynthetic process |
IC: Inferred by Curator |
GO:0003934 |
P |
required field missing | |||
|
RGD |
Rat |
Gch1 |
GO:0005525 |
GTP binding |
IDA: Inferred from Direct Assay |
F |
complete | ||||
|
Sanger GeneDB |
S. Pombe |
required field missing | |||||||||
|
SGD |
S. cerevisiae |
FOL2 |
GO:0003934 |
GTP cyclohydrolase I activity |
IMP: Inferred from Mutant Phenotype |
F |
complete | ||||
|
TAIR |
Arabidopsis |
required field missing | |||||||||
|
WormBase |
C.elegans |
cat-4 (WBGene00000298) |
GO:0042416 |
dopamine biosynthetic process |
IMP: Inferred from Mutant Phenotype |
No specific allele given |
P |
complete | |||
|
ZFIN |
Zebrafish |
required field missing | |||||||||
|
AgBase |
Chicken |
P50141 |
GO:0045429 |
positive regulation of nitric oxide biosynthetic process |
IDA: Inferred from Direct Assay |
P |
with macrophage activating factor (no record) |
complete | |||
|
SGD |
S. cerevisiae |
FOL2 |
GO:0009396 |
folic acid and derivative biosynthetic process |
IMP: Inferred from Mutant Phenotype |
P |
complete | ||||
|
SGD |
S. cerevisiae |
FOL2 |
GO:0005737 |
cytoplasm |
IDA: Inferred from Direct Assay |
C |
high-throughput studies |
complete | |||
|
SGD |
S. cerevisiae |
FOL2 |
GO:0005634 |
nucleus |
IDA: Inferred from Direct Assay |
C |
high-throughput study |
complete | |||
|
WormBase |
C.elegans |
cat-4 (WBGene00000298) |
GO:0042427 |
serotonin biosynthetic process |
IMP: Inferred from Mutant Phenotype |
No specific allele stated |
P |
complete | |||
|
EcoliWiki |
E. coli |
folE |
GO:0005829 |
cytosol |
IDA: Inferred from Direct Assay |
C |
FolE was present in the supernatant after subcellular fractionation. |
complete | |||
|
RGD |
Rat |
Gch1 |
GO:0003934 |
GTP cyclohydrolase I activity |
PMID:2557335[6] PMID:8702680[8] PMID:9636709[15] PMID:8486153[7] |
IDA: Inferred from Direct Assay |
F |
complete | |||
|
RGD |
Rat |
Gch1 |
GO:0030742 |
GTP-dependent protein binding |
IPI: Inferred from Physical Interaction |
RGD:1345739 |
F |
complete | |||
|
RGD |
Rat |
Gch1 |
GO:0005509 |
calcium ion binding |
IDA: Inferred from Direct Assay |
RGD:1345739 |
F |
complete | |||
|
RGD |
Rat |
Gch1 |
GO:0050662 |
coenzyme binding |
IDA: Inferred from Direct Assay |
RGD:1345739 |
F |
complete | |||
|
RGD |
Rat |
Gch1 |
GO:0008270 |
zinc ion binding |
IDA: Inferred from Direct Assay |
RGD:1345739 |
F |
complete | |||
|
RGD |
Rat |
Gch1 |
GO:0005515 |
protein binding |
IDA: Inferred from Direct Assay |
F |
complete | ||||
|
MGI |
Mouse |
Gch1 |
GO:0003934 |
GTP cyclohydrolase I activity |
IDA: Inferred from Direct Assay |
F |
complete | ||||
|
MGI |
Mouse |
Gch1 |
GO:0003934 |
GTP cyclohydrolase I activity |
J:73065 |
ISS: Inferred from Sequence or Structural Similarity |
UniProtKB:P30793 |
F |
complete | ||
|
MGI |
Mouse |
Gch1 |
GO:0014916 |
regulation of lung blood pressure |
IMP: Inferred from Mutant Phenotype |
P |
complete | ||||
|
MGI |
Mouse |
Gch1 |
GO:0050884 |
neuromuscular process controlling posture |
J:73065 |
ISS: Inferred from Sequence or Structural Similarity |
UniProtKB:P30793 |
P |
required field missing | ||
|
MGI |
Mouse |
Gch1 |
GO:0008217 |
regulation of blood pressure |
IMP: Inferred from Mutant Phenotype |
P |
complete | ||||
|
EcoliWiki |
E. coli |
folE |
GO:0046656 |
folic acid biosynthetic process |
IDA: Inferred from Direct Assay |
P |
FolE catalyzes the first committed step in folic acid biosynthesis. |
complete | |||
|
RGD |
Rat |
Gch1 |
GO:0005515 |
protein binding |
IDA: Inferred from Direct Assay |
F |
complete | ||||
|
RGD |
Rat |
Gch1 |
GO:0051066 |
dihydrobiopterin metabolic process |
IDA: Inferred from Direct Assay |
P |
complete | ||||
|
RGD |
Rat |
Gch1 |
GO:0006461 |
protein complex assembly |
IDA: Inferred from Direct Assay |
P |
complete | ||||
|
RGD |
Rat |
Gch1 |
GO:0051291 |
protein heterooligomerization |
IDA: Inferred from Direct Assay |
P |
complete | ||||
|
RGD |
Rat |
Gch1 |
GO:0051260 |
protein homooligomerization |
IDA: Inferred from Direct Assay |
P |
complete | ||||
|
RGD |
Rat |
Gch1 |
GO:0005625 |
soluble fraction |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
RGD |
Rat |
Gch1 |
GO:0043234 |
protein complex |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
EcoliWiki |
E. coli |
folE |
GO:0046654 |
tetrahydrofolate biosynthetic process |
IDA: Inferred from Direct Assay |
P |
complete | ||||
|
EcoliWiki |
E. coli |
folE |
GO:0005525 |
GTP binding |
IDA: Inferred from Direct Assay |
F |
complete | ||||
|
WormBase |
C.elegans |
cat-4 (WBGene00000298) |
GO:0046662 |
regulation of oviposition |
IMP: Inferred from Mutant Phenotype |
WB:e1141 |
P |
complete | |||
|
WormBase |
C.elegans |
cat-4 (WBGene00000298) |
GO:0042427 |
serotonin biosynthetic process |
IMP: Inferred from Mutant Phenotype |
WB:e1141 (for all but first reference) |
P |
complete | |||
|
EcoliWiki |
E. coli |
folE |
GO:0008270 |
zinc ion binding |
IDA: Inferred from Direct Assay |
F |
complete | ||||
|
EcoliWiki |
E. coli |
folE |
GO:0043234 |
protein complex |
IDA: Inferred from Direct Assay |
C |
FolE is a homodecamer, based on X-ray crystallography and biochemical characterization. |
complete | |||
|
DictyBase |
Dicty |
gchA |
GO:0003934 |
GTP cyclohydrolase I activity |
IDA: Inferred from Direct Assay |
F |
complete | ||||
|
DictyBase |
Dicty |
gchA |
GO:0006729 |
tetrahydrobiopterin biosynthetic process |
IDA: Inferred from Direct Assay |
P |
complete | ||||
|
AgBase |
Chicken |
P50141 |
GO:0006729 |
tetrahydrobiopterin biosynthetic process |
IMP: Inferred from Mutant Phenotype |
P |
complete | ||||
|
AgBase |
Chicken |
P50141 |
GO:0006729 |
tetrahydrobiopterin biosynthetic process |
IDA: Inferred from Direct Assay |
P |
complete | ||||
|
AgBase |
Chicken |
P50141 |
GO:0003933 |
GTP cyclohydrolase activity |
IDA: Inferred from Direct Assay |
F |
complete | ||||
|
WormBase |
C.elegans |
cat-4 (WBGene00000298) |
GO:0043051 |
regulation of pharyngeal pumping |
IMP: Inferred from Mutant Phenotype |
No allele stated |
P |
complete | |||
|
DictyBase |
Dicty |
gchA |
GO:0008277 |
regulation of G-protein coupled receptor protein signaling pathway |
IDA: Inferred from Direct Assay |
P |
H4dictyopterin and H4biopterin (arising from the GTPCH reaction) regulate the G protein linked signalling pathway |
complete | |||
|
DictyBase |
Dicty |
gchA |
GO:0005625 |
soluble fraction |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
WormBase |
C.elegans |
cat-4 (WBGene00000298) |
GO:0060179 |
male mating behavior |
IMP: Inferred from Mutant Phenotype |
WB:e1141 |
P |
complete | |||
|
DictyBase |
Dicty |
gchA |
GO:0045335 |
phagocytic vesicle |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
WormBase |
C.elegans |
cat-4 (WBGene00000298) |
GO:0046662 |
regulation of oviposition |
IGI: Inferred from Genetic Interaction |
WB:WBGene00006767 |
P |
complete | |||
|
DictyBase |
Dicty |
gchA |
GO:0005624 |
membrane fraction |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
WormBase |
C.elegans |
cat-4 (WBGene00000298) |
GO:0032095 |
regulation of response to food |
IMP: Inferred from Mutant Phenotype |
WB:e1141 |
P |
complete | |||
|
TAIR |
Arabidopsis |
At3g07270 |
GO:0003934 |
GTP cyclohydrolase I activity |
TAIR:Communication:501714663 |
ISS: Inferred from Sequence or Structural Similarity |
INTERPRO:IPR001474 |
F |
TIGR annotation |
complete | |
|
TAIR |
Arabidopsis |
At3g07270 |
GO:0009058 |
biosynthetic process |
TAIR:Communication:501714663 |
IEA: Inferred from Electronic Annotation |
INTERPRO:IPR001474 |
P |
TIGR annotation |
complete | |
|
TAIR |
Arabidopsis |
At3g07270 |
GO:0005737 |
cytoplasm |
TAIR:AnalysisReference:501721077 |
IEA: Inferred from Electronic Annotation |
INTERPRO:IPR001474 |
C |
INTERPRO2GO mapping, TAIR8 release |
complete | |
|
TAIR |
Arabidopsis |
At3g07270 |
GO:0003934 |
GTP cyclohydrolase I activity |
TAIR:Communication:501714663 |
ISS: Inferred from Sequence or Structural Similarity |
INTERPRO:IPR001474 |
F |
TIGR annotation |
complete | |
|
TAIR |
Arabidopsis |
At3g07270 |
GO:0009058 |
biosynthetic process |
TAIR:Communication:501714663 |
IEA: Inferred from Electronic Annotation |
INTERPRO:IPR001474 |
P |
TIGR annotation |
complete | |
|
WormBase |
C.elegans |
cat-4 (WBGene00000298) |
GO:0007626 |
locomotory behavior |
IMP: Inferred from Mutant Phenotype |
WB:e1141 |
P |
complete | |||
|
WormBase |
C.elegans |
cat-4 (WBGene00000298) |
GO:0019438 |
aromatic compound biosynthetic process |
IEA: Inferred from Electronic Annotation |
InterPro:IPR001474 |
P |
required field missing | |||
|
WormBase |
C.elegans |
cat-4 (WBGene00000298) |
GO:0005737 |
cytoplasm |
IEA: Inferred from Electronic Annotation |
InterPro:IPR001474 |
C |
required field missing | |||
|
WormBase |
C.elegans |
cat-4 (WBGene00000298) |
GO:0003934 |
GTP cyclohydrolase I activity |
IEA: Inferred from Electronic Annotation |
InterPro:IPR001474 |
F |
required field missing | |||
|
WormBase |
C.elegans |
cat-4 (WBGene00000298) |
GO:0040012 |
regulation of locomotion |
IMP: Inferred from Mutant Phenotype |
WB:e1141 |
P |
complete | |||
|
WormBase |
C.elegans |
cat-4 (WBGene00000298) |
GO:0042438 |
melanin biosynthetic process |
IMP: Inferred from Mutant Phenotype |
WB:ok342 |
P |
complete | |||
|
WormBase |
C.elegans |
cat-4 (WBGene00000298) |
GO:0040002 |
collagen and cuticulin-based cuticle development |
IMP: Inferred from Mutant Phenotype |
WB:ok342 |
P |
complete | |||
|
WormBase |
C.elegans |
cat-4 (WBGene00000298) |
GO:0050804 |
regulation of synaptic transmission |
IMP: Inferred from Mutant Phenotype |
WB:e1141 |
P |
complete | |||
|
AgBase |
Chicken |
P50141 |
GO:0005737 |
cytoplasm |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
FlyBase |
Drosophila |
FBgn0003162 |
GO:0048067 |
cuticle pigmentation |
IMP: Inferred from Mutant Phenotype |
P |
complete | ||||
|
FlyBase |
Drosophila |
FBgn0003162 |
GO:0008363 |
larval chitin-based cuticle development |
IMP: Inferred from Mutant Phenotype |
P |
complete | ||||
|
GOA |
Human |
GCH1 (P30793) |
GO:0042559 |
pteridine and derivative biosynthetic process |
IDA: Inferred from Direct Assay |
P |
complete | ||||
|
GOA |
Human |
GCH1 (P30793) |
GO:0006184 |
GTP catabolic process |
IDA: Inferred from Direct Assay |
P |
complete | ||||
|
FlyBase |
Drosophila |
FBgn0003162 |
GO:0003934 |
GTP cyclohydrolase I activity |
IDA: Inferred from Direct Assay |
F |
complete | ||||
|
GOA |
Human |
GCH1 (P30793) |
GO:0048265 |
response to pain |
SPTR P22288 |
ISS: Inferred from Sequence or Structural Similarity |
P |
Annotation to Rat made from PMID:17057711[45] and then ISS'ed to Human |
required field missing | ||
|
FlyBase |
Drosophila |
FBgn0003162 |
GO:0035185 |
preblastoderm mitotic cell cycle |
IMP: Inferred from Mutant Phenotype |
P |
complete | ||||
|
GOA |
Human |
GCH1 (P30793) |
GO:0006729 |
tetrahydrobiopterin biosynthetic process |
IDA: Inferred from Direct Assay |
P |
required field missing | ||||
|
FlyBase |
Drosophila |
FBgn0003162 |
GO:0006728 |
pteridine biosynthetic process |
IMP: Inferred from Mutant Phenotype |
P |
complete | ||||
|
GOA |
Human |
GCH1 (P30793) |
GO:0032496 |
response to lipopolysaccharide |
IDA: Inferred from Direct Assay |
P |
required field missing | ||||
|
FlyBase |
Drosophila |
FBgn0003162 |
GO:0006728 |
pteridine biosynthetic process |
IDA: Inferred from Direct Assay |
P |
complete | ||||
|
GOA |
Human |
GCH1 (P30793) |
GO:0034341 |
response to interferon-gamma |
IDA: Inferred from Direct Assay |
P |
complete | ||||
|
FlyBase |
Drosophila |
FBgn0003162 |
GO:0005737 |
cytoplasm |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
GOA |
Human |
GCH1 (P30793) |
GO:0051260 |
protein homooligomerization |
IDA: Inferred from Direct Assay |
P |
required field missing | ||||
|
FlyBase |
Drosophila |
FBgn0003162 |
GO:0007424 |
open tracheal system development |
IMP: Inferred from Mutant Phenotype |
P |
complete | ||||
|
GOA |
Human |
GCH1 (P30793) |
GO:0006809 |
nitric oxide biosynthetic process |
NAS: Non-traceable Author Statement |
P |
required field missing | ||||
|
FlyBase |
Drosophila |
FBgn0003162 |
GO:0048754 |
branching morphogenesis of a tube |
IMP: Inferred from Mutant Phenotype |
P |
complete | ||||
|
GOA |
Human |
GCH1 (P30793) |
GO:0051000 |
positive regulation of nitric-oxide synthase activity |
IDA: Inferred from Direct Assay |
P |
required field missing | ||||
|
FlyBase |
Drosophila |
FBgn0003162 |
GO:0030334 |
regulation of cell migration |
IMP: Inferred from Mutant Phenotype |
P |
Request new term for regulation of tracheal cell migration |
complete | |||
|
GOA |
Human |
GCH1 (P30793) |
GO:0003934 |
GTP cyclohydrolase I activity |
IDA: Inferred from Direct Assay |
F |
required field missing | ||||
|
FlyBase |
Drosophila |
FBgn0003162 |
GO:0042416 |
dopamine biosynthetic process |
IMP: Inferred from Mutant Phenotype |
P |
complete | ||||
|
GOA |
Human |
GCH1 (P30793) |
GO:0005525 |
GTP binding |
IDA: Inferred from Direct Assay |
F |
required field missing | ||||
|
FlyBase |
Drosophila |
FBgn0003162 |
GO:0048072 |
compound eye pigmentation |
IMP: Inferred from Mutant Phenotype |
P |
complete | ||||
|
GOA |
Human |
GCH1 (P30793) |
GO:0008270 |
zinc ion binding |
IDA: Inferred from Direct Assay |
F |
required field missing | ||||
|
FlyBase |
Drosophila |
FBgn0003162 |
GO:0003934 |
GTP cyclohydrolase I activity |
IMP: Inferred from Mutant Phenotype |
F |
complete | ||||
|
GOA |
Human |
GCH1 (P30793) |
GO:0005829 |
cytosol |
IDA: Inferred from Direct Assay |
C |
required field missing | ||||
|
GOA |
Human |
GCH1 (P30793) |
GO:0031410 |
cytoplasmic vesicle |
IDA: Inferred from Direct Assay |
C |
required field missing | ||||
|
GOA |
Human |
GCH1 (P30793) |
GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
P11142, O95433, Q02447, Q13129, Q96F85, Q9ULW5 |
F |
required field missing | |||
|
GOA |
Human |
GCH1 (P30793-1) |
GO:0003934 |
GTP cyclohydrolase I activity |
IDA: Inferred from Direct Assay |
F |
required field missing | ||||
|
GOA |
Human |
GCH1 (P30793) |
GO:0005737 |
cytoplasm |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
GOA |
Human |
GCH1 (P30793) |
GO:0005634 |
nucleus |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
GOA |
Human |
GCH1 (P30793-3) |
NOT |
GO:0003934 |
GTP cyclohydrolase I activity |
IDA: Inferred from Direct Assay |
F |
complete | |||
|
GOA |
Human |
GCH1 (P30793-4) |
NOT |
GO:0003934 |
GTP cyclohydrolase I activity |
IDA: Inferred from Direct Assay |
F |
complete | |||
| edit table |
GCH1 notes
- Debby-EcoliWiki
- InterPro has several IEA annotations for E. coli FolE that I think are incorrect. Would it be useful to include these in the Jamboree with NOT qualifier? For example, InterPro annotates FolE to GO:0006556 S-adenosylmethionine biosynthetic process. Methionine biosynthesis in E. coli requires 5-methyltetrahydropteroyltri-L-glutamate, which is derived from tetrahydrofolate, but FolE is not directly involved in the biosynthesis of methionine.
- Petra DictyBase
- Authors in PMID 8660315 describe their membrane preparation and assay the enzyme function. The dicty gchA gene was originally annotated to GO:0005626 insoluble fraction, and I now found it should be GO:0005624 membrane fraction and changed the annotation. Looking at this, I was surprised to find these two terms as siblings, as I thought 'membrane fraction' should be part of 'insoluble fraction.
- I wonder if those genes that have IDA annotation to GO:0003934, GTP cyclohydrolase I activity, do not have the same experimental annotation to the process GO:0006729, tetrahydrobiopterin biosynthesis because, how were the enzymes assayed? By determining the tetrahydrobiopterin? Just a thought.
- Debby EcoliWiki: As far as I can tell, E. coli doesn't make tetrahydrobiopterin. The GTP cyclohydrolase I reaction produces 7,8-dihydroneopterin triphosphate which goes into tetrahydrofolate biosynthesis. E. coli makes tyrosine from phenylalanine in a reaction that doesn't use tetrahydrobiopterin as a cofactor.
- Jim EcoliWiki There's a NAS in a paper showing reconstitution of a tetrahydrobiopterin synthesis pathway in E. coli that says E. coli and most bacteria don't make tetrahydrobiopterin[59]
- Debby EcoliWiki: As far as I can tell, E. coli doesn't make tetrahydrobiopterin. The GTP cyclohydrolase I reaction produces 7,8-dihydroneopterin triphosphate which goes into tetrahydrofolate biosynthesis. E. coli makes tyrosine from phenylalanine in a reaction that doesn't use tetrahydrobiopterin as a cofactor.
- Doug-ZFIN
- The PPOD cluster for this gene has the zebrafish gch2 gene, while ZFIN has a gch1 gene which shares conserved synteny with the Human and mouse ortholog. Our gch1 gene was created as a result of manual curation, so currently has no sequence associated with it, and thus does not show up in the PPOD cluster. As a result I guess the next best match, gch2, is included in the cluster. It turns out that gch2 in zebrafish has so far only been used as a marker for pigment cell precursors, so there is no functional data. If there were...should it be curated as part of this cluster?
- I think gch2 should not be curated as an ortholog if you know there is a gch1 gene. Petra
- The PPOD cluster for this gene has the zebrafish gch2 gene, while ZFIN has a gch1 gene which shares conserved synteny with the Human and mouse ortholog. Our gch1 gene was created as a result of manual curation, so currently has no sequence associated with it, and thus does not show up in the PPOD cluster. As a result I guess the next best match, gch2, is included in the cluster. It turns out that gch2 in zebrafish has so far only been used as a marker for pigment cell precursors, so there is no functional data. If there were...should it be curated as part of this cluster?
- Becky-Swiss-Prot
- GCH1 N terminus of the protein has a negative regulation activity - should there be a new GO term – for self-regulation when self binding (ST)
GO Terms
Human annotators: Terms requested for 'Response to TNF', 'Protein homodecamerization' and 'Response to laminar shear stress'
HSPD1
| Category | ID | Term | Human | Mouse | Rat | Chicken | Zfish | Fly | Worm | Dicty | Dicot | Yeast | Pombe | Ecoli |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Biological Process | GO:0042026 | protein refolding | IDA | X | X | X | X | X | X | X | X | IMP IDA | X | IDA |
| Biological Process | GO:0002368 | B cell cytokine production | IDA | X | X | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0045041 | protein import into mitochondrial intermembrane space | X | X | X | X | X | X | X | X | X | IMP | X | X |
| Biological Process | GO:0034514 | mitochondrial unfolded protein response | X | X | X | X | X | X | IEP | X | X | X | X | X |
| Biological Process | GO:0031101 | fin regeneration | X | X | X | X | IMP | X | X | X | X | X | X | X |
| Biological Process | GO:0042963 | phage assembly | X | X | X | X | X | X | X | X | X | X | X | IMP |
| Biological Process | GO:0006986 | response to unfolded protein | IDA | X | X | X | X | X | X | X | X | X | X | |
| Biological Process | GO:0006457 | protein folding | X | X | X | X | X | X | X | X | IEA | X | X | IGI |
| Biological Process | GO:0046956 | positive phototaxis | X | X | X | X | X | X | X | IMP | X | X | X | X |
| Biological Process | GO:0031288 | sorocarp morphogenesis | X | X | X | X | X | X | X | IMP | X | X | X | X |
| Biological Process | GO:0008283 | cell proliferation | X | X | X | X | X | X | X | IMP | X | X | X | X |
| Biological Process | GO:0006458 | 'de novo' protein folding | X | X | IC | X | X | X | X | X | X | IMP | X | IGI |
| Biological Process | GO:0051604 | protein maturation | X | X | X | X | X | X | X | X | X | IMP | X | X |
| Biological Process | GO:0051131 | chaperone-mediated protein complex assembly | X | X | X | X | X | X | X | X | X | IMP | X | X |
| Biological Process | GO:0050821 | protein stabilization | IMP | X | X | X | X | X | X | X | X | IMP | X | X |
| Biological Process | GO:0042110 | T cell activation | X | ISS IDA IGI | X | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0032729 | positive regulation of interferon-gamma production | X | IDA IGI ISS | X | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0032727 | positive regulation of interferon-alpha production | X | IDA | X | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0002236 | detection of misfolded protein | X | X | IDA | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0009792 | embryonic development ending in birth or egg hatching | X | X | X | X | X | X | IMP | X | X | X | X | X |
| Biological Process | GO:0002119 | nematode larval development | X | X | X | X | X | X | IMP | X | X | X | X | X |
| Biological Process | GO:0000302 | response to reactive oxygen species | X | X | X | X | X | X | IEP | X | X | X | X | X |
| Biological Process | GO:0007005 | mitochondrion organization | X | X | X | X | X | IMP | IMP | X | X | X | X | X |
| Biological Process | GO:0009408 | response to heat | X | X | X | X | X | IDA | IEP | X | IEP | X | X | IEP |
| Biological Process | GO:0051085 | chaperone cofactor-dependent protein folding | X | X | IDA | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0006916 | anti-apoptosis | X | X | IMP | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0042246 | tissue regeneration | X | X | X | X | IMP | X | X | X | X | X | X | X |
| Biological Process | GO:0010583 | response to cyclopentenone | X | X | X | X | X | X | X | X | IEP | X | X | X |
| Biological Process | GO:0009651 | response to salt stress | X | X | X | X | X | X | X | X | IEP | X | X | X |
| Biological Process | GO:0006954 | inflammatory response | X | X | X | X | X | X | X | X | ISS | X | X | X |
| Biological Process | GO:0008150 | biological process | X | X | X | ND | X | X | X | X | X | X | X | X |
| Biological Process | GO:0044267 | cellular protein metabolic process | X | X | X | X | X | X | X | X | IEA | X | X | X |
| Biological Process | GO:0002755 | MyD88-dependent toll-like receptor signaling pathway | IDA | X | X | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0032733 | positive regulation of interleukin-10 production | IDA | X | X | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0032755 | positive regulation of interleukin-6 production | IDA | X | X | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0042100 | B cell proliferation | IDA | X | X | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0042113 | B cell activation | IDA | X | X | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0048291 | isotype switching to IgG isotypes | IDA | X | X | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0050870 | positive regulation of T cell activation | IDA | X | X | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0006919 | caspase activation | IDA | X | X | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0043065 | positive regulation of apoptosis | IMP | X | X | X | X | X | X | X | X | X | X | X |
| Biological Process | GO:0043066 | negative regulation of apoptosis | IMP | X | X | X | X | X | X | X | X | X | X | X |
| Cellular Component | GO:0005739 | mitochondrion | IDA | IDA | IDA | X | X | IDA | X | IDA | IDA | IDA | X | X |
| Cellular Component | GO:0005737 | cytoplasm | X | X | IDA | X | X | X | X | X | X | X | X | |
| Cellular Component | GO:0042645 | mitochondrial nucleoid | X | X | X | X | X | X | X | X | X | IDA | X | X |
| Cellular Component | GO:0044459 | plasma membrane part | X | IDA | X | X | X | X | X | X | X | X | X | X |
| Cellular Component | GO:0030141 | secretory granule | X | IDA | IDA | X | X | X | X | X | X | X | X | X |
| Cellular Component | GO:0043231 | intracellular membrane-bounded organelle | X | IDA | X | X | X | X | X | X | X | X | X | X |
| Cellular Component | GO:0005743 | mitochondrial inner membrane | X | IDA | X | X | X | X | X | X | X | X | X | X |
| Cellular Component | GO:0009986 | cell surface | IDA | X | IDA | X | X | X | X | X | X | X | X | X |
| Cellular Component | GO:0045121 | membrane raft | X | X | IDA | X | X | X | X | X | X | X | X | X |
| Cellular Component | GO:0030061 | mitochondrial crista | X | X | IDA | X | X | X | X | X | X | X | X | X |
| Cellular Component | GO:0005791 | rough endoplasmic reticulum | X | X | IDA | X | X | X | X | X | X | X | X | X |
| Cellular Component | GO:0005829 | cytosol | IDA | X | IDA | X | X | X | X | X | IEP | X | X | X |
| Cellular Component | GO:0043234 | protein complex | X | X | X | X | X | X | X | X | X | X | X | IDA |
| Cellular Component | GO:0042588 | zymogen granule | X | X | IDA | X | X | X | X | X | X | X | X | X |
| Cellular Component | GO:0005794 | Golgi apparatus | X | X | IDA | X | X | X | X | X | X | X | X | X |
| Cellular Component | GO:0005759 | mitochondrial matrix | X | X | X | X | X | X | X | X | IDA | X | X | X |
| Cellular Component | GO:0005575 | cellular component | X | X | X | ND | X | X | X | X | X | X | X | X |
| Cellular Component | GO:0016465 | chaperonin ATPase complex | X | X | X | X | X | X | X | X | X | X | X | |
| Cellular Component | GO:0005615 | extracellular space | IDA | X | X | X | X | X | X | X | X | X | X | X |
| Cellular Component | GO:0005811 | lipid particle | X | X | X | X | X | IDA | X | X | X | X | X | X |
| Cellular Component | GO:0031305 | integral to mitochondrial inner membrane | X | X | X | X | X | IDA | X | X | X | X | X | X |
| Molecular Function | GO:0005524 | ATP binding | X | X | X | X | X | X | X | X | IEA | X | X | IDA |
| Molecular Function | GO:0051082 | unfolded protein binding | IC | X | X | X | X | X | ISS | X | IEA | IMP | X | IDA |
| Molecular Function | GO:0005515 | protein binding | IPI | X | X | X | X | X | X | X | IEA | X | X | |
| Molecular Function | GO:0016887 | ATPase activity | X | X | X | X | X | X | X | X | X | IDA | X | IDA |
| Molecular Function | GO:0001530 | lipopolysaccharide binding | X | ISS | X | X | X | X | X | X | X | X | X | X |
| Molecular Function | GO:0051787 | misfolded protein binding | X | X | IPI | X | X | X | X | X | X | X | X | IDA |
| Molecular Function | GO:0008134 | transcription factor binding | X | X | X | X | X | X | IPI | X | X | X | X | X |
| Molecular Function | GO:0003674 | molecular function | X | X | X | ND | X | X | X | X | X | X | X | X |
| Molecular Function | GO:0051087 | chaperone binding | IPI | X | X | X | X | X | X | X | X | X | X | X |
| Molecular Function | GO:0002039 | p53 binding | IPI | X | X | X | X | X | X | X | X | X | X | X |
| Molecular Function | GO:0043498 | cell surface binding | IDA | X | X | X | X | X | X | X | X | X | X | X |
| Molecular Function | GO:0003688 | DNA replication origin binding | X | X | X | X | X | X | X | X | X | IDA | X | X |
| Molecular Function | GO:0003697 | single-stranded DNA binding | X | X | X | X | X | X | X | X | X | IDA | X | X |

This figure should automatically update from the table
| Group | Organism | gene | Qualifier | GO ID | GO term name | Reference(s) | Evidence Code | with/from | Aspect | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|---|
|
EcoliWiki |
E. coli |
groL |
GO:0042026 |
protein refolding |
IDA: Inferred from Direct Assay |
P |
GroEL/GroES can reactivate heat-treated RNA polymerase in vitro. |
complete | |||
|
DictyBase |
Dicty |
hspA |
GO:0005739 |
mitochondrion |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
FlyBase |
Drosophila |
Hsp60 FBgn0015245 |
GO:0005739 |
mitochondrion |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0002368 |
B cell cytokine production |
IDA: Inferred from Direct Assay |
P |
required field missing | ||||
|
Sanger GeneDB |
S. Pombe |
required field missing | |||||||||
|
SGD |
S. cerevisiae |
HSP60 |
GO:0045041 |
protein import into mitochondrial intermembrane space |
IMP: Inferred from Mutant Phenotype |
P |
required field missing | ||||
|
TAIR |
Arabidopsis |
AT3G23990/Hsp60-3b |
GO:0005739 |
mitochondrion |
4 different PMIDs |
IDA: Inferred from Direct Assay |
C |
this location has been assayed to death |
complete | ||
|
WormBase |
C.elegans |
hsp-60(WBGene00002025) |
GO:0034514 |
mitochondrial unfolded protein response |
IEP: Inferred from Expression Pattern |
P |
complete | ||||
|
Chicken |
required field missing | ||||||||||
|
ZFIN |
Zebrafish |
hspd1 |
GO:0031101 |
fin regeneration |
IMP: Inferred from Mutant Phenotype |
ZFIN:ZDB-GENO-051101-1 |
P |
complete | |||
|
EcoliWiki |
E. coli |
groL |
GO:0005524 |
ATP binding |
IDA: Inferred from Direct Assay |
F |
Purified GroEL has ATPase activity. |
complete | |||
|
EcoliWiki |
E. coli |
groL |
GO:0051082 |
unfolded protein binding |
IDA: Inferred from Direct Assay |
F |
complete | ||||
|
EcoliWiki |
E. coli |
groL |
GO:0005515 |
protein binding |
F |
required field missing | |||||
|
EcoliWiki |
E. coli |
groL |
GO:0042963 |
phage assembly |
IMP: Inferred from Mutant Phenotype |
P |
complete | ||||
|
EcoliWiki |
E. coli |
groL |
GO:0016887 |
ATPase activity |
IDA: Inferred from Direct Assay |
F |
complete | ||||
|
EcoliWiki |
E. coli |
groL |
GO:0006986 |
response to unfolded protein |
P |
required field missing | |||||
|
EcoliWiki |
E. coli |
groL |
GO:0005737 |
cytoplasm |
C |
required field missing | |||||
|
EcoliWiki |
E. coli |
groL |
GO:0006457 |
protein folding |
IGI: Inferred from Genetic Interaction |
P |
Not sure about evidence code. |
complete | |||
|
DictyBase |
Dicty |
hspA |
GO:0046956 |
positive phototaxis |
IMP: Inferred from Mutant Phenotype |
P |
unsure about making those P annotations (see email discussion from last week) |
complete | |||
|
DictyBase |
Dicty |
hspA |
GO:0031288 |
sorocarp morphogenesis |
IMP: Inferred from Mutant Phenotype |
P |
unsure about making those P annotations (see email discussion from last week) |
complete | |||
|
DictyBase |
Dicty |
hspA |
GO:0008283 |
cell proliferation |
IMP: Inferred from Mutant Phenotype |
P |
unsure about making those P annotations (see email discussion from last week) |
complete | |||
|
SGD |
S. cerevisiae |
HSP60 |
GO:0006458 |
'de novo' protein folding |
IMP: Inferred from Mutant Phenotype |
P |
required field missing | ||||
|
SGD |
S. cerevisiae |
HSP60 |
GO:0051604 |
protein maturation |
IMP: Inferred from Mutant Phenotype |
P |
required field missing | ||||
|
SGD |
S. cerevisiae |
HSP60 |
GO:0051131 |
chaperone-mediated protein complex assembly |
IMP: Inferred from Mutant Phenotype |
P |
required field missing | ||||
|
SGD |
S. cerevisiae |
HSP60 |
GO:0016887 |
ATPase activity |
IDA: Inferred from Direct Assay |
F |
complete | ||||
|
SGD |
S. cerevisiae |
HSP60 |
GO:0051082 |
unfolded protein binding |
IMP: Inferred from Mutant Phenotype |
F |
complete | ||||
|
SGD |
S. cerevisiae |
HSP60 |
GO:0042026 |
protein refolding |
IMP: Inferred from Mutant Phenotype |
P |
complete | ||||
|
SGD |
S. cerevisiae |
HSP60 |
GO:0005739 |
mitochondrion |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
SGD |
S. cerevisiae |
HSP60 |
GO:0050821 |
protein stabilization |
IMP: Inferred from Mutant Phenotype |
P |
complete | ||||
|
SGD |
S. cerevisiae |
HSP60 |
GO:0042645 |
mitochondrial nucleoid |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
MGI |
Mouse |
Hspd1 |
GO:0044459 |
plasma membrane part |
IDA: Inferred from Direct Assay |
C |
required field missing | ||||
|
MGI |
Mouse |
Hspd1 |
GO:0005739 |
mitochondrion |
PMID:8824711[79] PMID:1516759[80] PMID:12931191[81] PMID:16959573[82] PMID:14651853[83] |
IDA: Inferred from Direct Assay |
C |
complete | |||
|
MGI |
Mouse |
Hspd1 |
GO:0030141 |
secretory granule |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
MGI |
Mouse |
Hspd1 |
GO:0043231 |
intracellular membrane-bounded organelle |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
MGI |
Mouse |
Hspd1 |
GO:0005743 |
mitochondrial inner membrane |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
MGI |
Mouse |
Hspd1 |
GO:0001530 |
lipopolysaccharide binding |
J:73065 |
ISS: Inferred from Sequence or Structural Similarity |
UniProtKB:P10809 |
F |
complete | ||
|
MGI |
Mouse |
Hspd1 |
GO:0042110 |
T cell activation |
J:73065 |
ISS: Inferred from Sequence or Structural Similarity |
UniProtKB:P10809 |
P |
required field missing | ||
|
MGI |
Mouse |
Hspd1 |
GO:0042110 |
T cell activation |
IDA: Inferred from Direct Assay |
P |
complete | ||||
|
MGI |
Mouse |
Hspd1 |
GO:0042110 |
T cell activation |
IGI: Inferred from Genetic Interaction |
MGI:107658 |
P |
required field missing | |||
|
MGI |
Mouse |
Hspd1 |
GO:0032729 |
positive regulation of interferon-gamma production |
IDA: Inferred from Direct Assay |
P |
complete | ||||
|
MGI |
Mouse |
Hspd1 |
GO:0032729 |
positive regulation of interferon-gamma production |
IGI: Inferred from Genetic Interaction |
MGI:107658 |
P |
required field missing | |||
|
MGI |
Mouse |
Hspd1 |
GO:0032729 |
positive regulation of interferon-gamma production |
J:73065 |
ISS: Inferred from Sequence or Structural Similarity |
UniProtKB:P10809 |
P |
required field missing | ||
|
MGI |
Mouse |
Hspd1 |
GO:0032727 |
positive regulation of interferon-alpha production |
IDA: Inferred from Direct Assay |
P |
required field missing | ||||
|
RGD |
Rat |
Hspd1 |
GO:0009986 |
cell surface |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
RGD |
Rat |
Hspd1 |
GO:0005737 |
cytoplasm |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
RGD |
Rat |
Hspd1 |
GO:0045121 |
membrane raft |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
RGD |
Rat |
Hspd1 |
GO:0030061 |
mitochondrial crista |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
RGD |
Rat |
Hspd1 |
GO:0005739 |
mitochondrion |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
RGD |
Rat |
Hspd1 |
GO:0005791 |
rough endoplasmic reticulum |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
RGD |
Rat |
Hspd1 |
GO:0030141 |
secretory granule |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
RGD |
Rat |
Hspd1 |
GO:0051787 |
misfolded protein binding |
IPI: Inferred from Physical Interaction |
RGD:1561359 |
F |
complete | |||
|
RGD |
Rat |
Hspd1 |
GO:0002236 |
detection of misfolded protein |
IDA: Inferred from Direct Assay |
P |
complete | ||||
|
SGD |
S. cerevisiae |
HSP60 |
GO:0016887 |
ATPase activity |
IDA: Inferred from Direct Assay |
F |
complete | ||||
|
SGD |
S. cerevisiae |
HSP60 |
GO:0042026 |
protein refolding |
IDA: Inferred from Direct Assay |
P |
complete | ||||
|
WormBase |
C.elegans |
hsp-60(WBGene00002025) |
GO:0009792 |
embryonic development ending in birth or egg hatching |
IMP: Inferred from Mutant Phenotype |
P |
Shown via RNAi; this annotation shows the essential nature of this gene. |
complete | |||
|
WormBase |
C.elegans |
hsp-60(WBGene00002025) |
GO:0002119 |
nematode larval development |
IMP: Inferred from Mutant Phenotype |
P |
Shown via RNAi; |
complete | |||
|
WormBase |
C.elegans |
hsp-60(WBGene00002025) |
GO:0000302 |
response to reactive oxygen species |
IEP: Inferred from Expression Pattern |
P |
Use of Paraquat that results in accumulation of reactive oxygen species leads to hsp-60 induction, thus use of IEP. |
complete | |||
|
WormBase |
C.elegans |
hsp-60(WBGene00002025) |
GO:0007005 |
mitochondrion organization |
IMP: Inferred from Mutant Phenotype |
P |
Shown via RNAi; actually affects morphology of mitochondria (thicker often fragmented mitochondria); chose the term closest to describing this. |
complete | |||
|
WormBase |
C.elegans |
hsp-60(WBGene00002025) |
NOT |
GO:0009408 |
response to heat |
IEP: Inferred from Expression Pattern |
P |
Paper specifically shows that hsp-60 was not activated by heat shock, I think it is worth making the 'NOT' annotation. |
complete | ||
|
WormBase |
C.elegans |
hsp-60(WBGene00002025) |
GO:0051082 |
unfolded protein binding |
ISS: Inferred from Sequence or Structural Similarity |
F |
complete | ||||
|
WormBase |
C.elegans |
hsp-60(WBGene00002025) |
GO:0008134 |
transcription factor binding |
IPI: Inferred from Physical Interaction |
F |
hsp-60 binds dve-1 (ortholog of fly defective proventriculus, dve-1 is a homeodomain transcription factor) |
complete | |||
|
RGD |
Rat |
Hspd1 |
GO:0051787 |
misfolded protein binding |
IPI: Inferred from Physical Interaction |
RGD:1359615 |
F |
complete | |||
|
RGD |
Rat |
Hspd1 |
GO:0005739 |
mitochondrion |
IDA: Inferred from Direct Assay |
RGD:1359615 |
C |
complete | |||
|
RGD |
Rat |
Hspd1 |
GO:0051085 |
chaperone cofactor-dependent protein folding |
IDA: Inferred from Direct Assay |
P |
complete | ||||
|
RGD |
Rat |
Hspd1 |
GO:0006916 |
anti-apoptosis |
IMP: Inferred from Mutant Phenotype |
P |
complete | ||||
|
RGD |
Rat |
Hspd1 |
GO:0005829 |
cytosol |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
EcoliWiki |
E. coli |
groL |
GO:0006458 |
'de novo' protein folding |
IGI: Inferred from Genetic Interaction |
P |
Unsure about the evidence code to use. |
complete | |||
|
RGD |
Rat |
Hspd1 |
GO:0005829 |
cytosol |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
EcoliWiki |
E. coli |
groL |
GO:0043234 |
protein complex |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
RGD |
Rat |
Hspd1 |
GO:0042588 |
zymogen granule |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
RGD |
Rat |
Hspd1 |
GO:0005791 |
rough endoplasmic reticulum |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
RGD |
Rat |
Hspd1 |
GO:0005794 |
Golgi apparatus |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
RGD |
Rat |
Hspd1 |
GO:0006458 |
'de novo' protein folding |
IC: Inferred by Curator |
GO:0042588 |
P |
complete | |||
|
EcoliWiki |
E. coli |
groL |
GO:0009408 |
response to heat |
IEP: Inferred from Expression Pattern |
P |
complete | ||||
|
ZFIN |
Zebrafish |
hspd1 |
GO:0042246 |
tissue regeneration |
IMP: Inferred from Mutant Phenotype |
ZFIN:ZDB-GENO-051101-1 |
P |
complete | |||
|
TAIR |
Arabidopsis |
AT3G23990/Hsp60-3b |
GO:0010583 |
response to cyclopentenone |
IEP: Inferred from Expression Pattern |
P |
hmmm, not my annotation but based only on microarray data |
complete | |||
|
TAIR |
Arabidopsis |
AT3G23990/Hsp60-3b |
GO:0051082 |
unfolded protein binding |
TAIR:AnalysisReference:501721077 |
IEA: Inferred from Electronic Annotation |
INTERPRO:IPR008950|INTERPRO:IPR012723 |
F |
INTERPRO2GO mapping, TAIR8 release |
complete | |
|
TAIR |
Arabidopsis |
AT3G23990/Hsp60-3b |
GO:0005515 |
protein binding |
TAIR:AnalysisReference:501721077 |
IEA: Inferred from Electronic Annotation |
INTERPRO:IPR001844|INTERPRO:IPR002423 |
F |
INTERPRO2GO mapping, TAIR8 release |
complete | |
|
TAIR |
Arabidopsis |
AT3G23990/Hsp60-3b |
GO:0005524 |
ATP binding |
TAIR:AnalysisReference:501721077 |
IEA: Inferred from Electronic Annotation |
INTERPRO:IPR001844|INTERPRO:IPR002423|INTERPRO:IPR008950|INTERPRO:IPR012723 |
F |
INTERPRO2GO mapping, TAIR8 release |
complete | |
|
TAIR |
Arabidopsis |
AT3G23990/Hsp60-3b |
GO:0009408 |
response to heat |
IEP: Inferred from Expression Pattern |
P |
Northern |
complete | |||
|
TAIR |
Arabidopsis |
AT3G23990/Hsp60-3b |
GO:0005829 |
cytosol |
IEP: Inferred from Expression Pattern |
C |
Western |
complete | |||
|
TAIR |
Arabidopsis |
AT3G23990/Hsp60-3b |
GO:0005759 |
mitochondrial matrix |
IDA: Inferred from Direct Assay |
C |
cell fractionation + Western |
complete | |||
|
TAIR |
Arabidopsis |
At2g33210/Hsp60-2 |
GO:0051082 |
unfolded protein binding |
TAIR:AnalysisReference:501721077 |
IEA: Inferred from Electronic Annotation |
INTERPRO:IPR008950|INTERPRO:IPR012723 |
F |
INTERPRO2GO mapping, TAIR8 release |
complete | |
|
TAIR |
Arabidopsis |
At2g33210/Hsp60-2 |
GO:0005515 |
protein binding |
TAIR:AnalysisReference:501721077 |
IEA: Inferred from Electronic Annotation |
INTERPRO:IPR001844|INTERPRO:IPR002423 |
F |
INTERPRO2GO mapping, TAIR8 release |
complete | |
|
TAIR |
Arabidopsis |
At2g33210/Hsp60-2 |
GO:0005524 |
ATP binding |
TAIR:AnalysisReference:501721077 |
IEA: Inferred from Electronic Annotation |
INTERPRO:IPR008950|INTERPRO:IPR012723 |
F |
INTERPRO2GO mapping, TAIR8 release |
complete | |
|
TAIR |
Arabidopsis |
At2g33210/Hsp60-2 |
GO:0009651 |
response to salt stress |
IEP: Inferred from Expression Pattern |
P |
Northern |
complete | |||
|
TAIR |
Arabidopsis |
At2g33210/Hsp60-2 |
GO:0005739 |
mitochondrion |
2 different PMIDs |
IDA: Inferred from Direct Assay |
C |
complete | |||
|
TAIR |
Arabidopsis |
At2g33210/Hsp60-2 |
GO:0006954 |
inflammatory response |
TAIR:Communication:501714663 |
ISS: Inferred from Sequence or Structural Similarity |
SWISS-PROT:Q59322 |
P |
TIGR annotation from 2001 |
complete | |
|
other |
Chicken |
Q5ZL72 |
GO:0003674 |
molecular function |
ND: No biological Data available |
F |
required field missing | ||||
|
other |
Chicken |
Q5ZL72 |
GO:0008150 |
biological process |
ND: No biological Data available |
P |
required field missing | ||||
|
other |
Chicken |
Q5ZL72 |
GO:0005575 |
cellular component |
ND: No biological Data available |
C |
required field missing | ||||
|
EcoliWiki |
E. coli |
groL |
GO:0016465 |
chaperonin ATPase complex |
C |
required field missing | |||||
|
EcoliWiki |
E. coli |
groL |
GO:0051787 |
misfolded protein binding |
IDA: Inferred from Direct Assay |
F |
complete | ||||
|
TAIR |
Arabidopsis |
At3g13860/Hsp60-3a |
GO:0051082 |
unfolded protein binding |
TAIR:AnalysisReference:501721077 |
IEA: Inferred from Electronic Annotation |
INTERPRO:IPR008950|INTERPRO:IPR012723 |
F |
INTERPRO2GO mapping, TAIR8 release |
complete | |
|
TAIR |
Arabidopsis |
At3g13860/Hsp60-3a |
GO:0005515 |
protein binding |
TAIR:AnalysisReference:501721077 |
IEA: Inferred from Electronic Annotation |
INTERPRO:IPR001844|INTERPRO:IPR002423 |
F |
INTERPRO2GO mapping, TAIR8 release |
complete | |
|
TAIR |
Arabidopsis |
At3g13860/Hsp60-3a |
GO:0005524 |
ATP binding |
TAIR:AnalysisReference:501721077 |
IEA: Inferred from Electronic Annotation |
INTERPRO:IPR008950|INTERPRO:IPR012723 |
F |
INTERPRO2GO mapping, TAIR8 release |
complete | |
|
TAIR |
Arabidopsis |
At3g13860/Hsp60-3a |
GO:0044267 |
cellular protein metabolic process |
TAIR:AnalysisReference:501721077 |
IEA: Inferred from Electronic Annotation |
INTERPRO:IPR001844|INTERPRO:IPR002423INTERPRO:IPR001844|INTERPRO:IPR002423 |
P |
INTERPRO2GO mapping, TAIR8 release |
complete | |
|
TAIR |
Arabidopsis |
At3g13860/Hsp60-3a |
GO:0006457 |
protein folding |
TAIR:AnalysisReference:501721077 |
IEA: Inferred from Electronic Annotation |
INTERPRO:IPR008950|INTERPRO:IPR012723 |
P |
INTERPRO2GO mapping, TAIR8 release |
complete | |
|
TAIR |
Arabidopsis |
At3g13860/Hsp60-3a |
GO:0005739 |
mitochondrion |
IDA: Inferred from Direct Assay |
C |
protein separation and fragment identification |
complete | |||
|
TAIR |
Arabidopsis |
At3g13860/Hsp60-3a |
GO:0005739 |
mitochondrion |
4 different PMIDs |
IDA: Inferred from Direct Assay |
C |
this location has been assayed to death |
required field missing | ||
|
TAIR |
Arabidopsis |
At3g13860/Hsp60-3a |
GO:0005739 |
mitochondrion |
4 different PMIDs |
IDA: Inferred from Direct Assay |
C |
this location has been assayed to death |
required field missing | ||
|
TAIR |
Arabidopsis |
At3g13860/Hsp60-3a |
GO:0005739 |
mitochondrion |
4 different PMIDs |
IDA: Inferred from Direct Assay |
C |
this location has been assayed to death |
required field missing | ||
|
TAIR |
Arabidopsis |
At3g13860/Hsp60-3a |
GO:0005739 |
mitochondrion |
4 different PMIDs |
IDA: Inferred from Direct Assay |
C |
this location has been assayed to death |
required field missing | ||
|
EcoliWiki |
E. coli |
groL |
GO:0051787 |
misfolded protein binding |
IDA: Inferred from Direct Assay |
F |
complete | ||||
|
TAIR |
Arabidopsis |
At3g13860/Hsp60-3a |
GO:0005739 |
mitochondrion |
4 different PMIDs |
IDA: Inferred from Direct Assay |
C |
this location has been assayed to death |
required field missing | ||
|
EcoliWiki |
E. coli |
groL |
GO:0016465 |
chaperonin ATPase complex |
C |
required field missing | |||||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0002755 |
MyD88-dependent toll-like receptor signaling pathway |
IDA: Inferred from Direct Assay |
P |
required field missing | ||||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0032733 |
positive regulation of interleukin-10 production |
IDA: Inferred from Direct Assay |
P |
required field missing | ||||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0032755 |
positive regulation of interleukin-6 production |
IDA: Inferred from Direct Assay |
P |
required field missing | ||||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0042100 |
B cell proliferation |
IDA: Inferred from Direct Assay |
P |
required field missing | ||||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0042113 |
B cell activation |
IDA: Inferred from Direct Assay |
P |
required field missing | ||||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0048291 |
isotype switching to IgG isotypes |
IDA: Inferred from Direct Assay |
P |
required field missing | ||||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0050870 |
positive regulation of T cell activation |
IDA: Inferred from Direct Assay |
P |
required field missing | ||||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0050821 |
protein stabilization |
IMP: Inferred from Mutant Phenotype |
P |
required field missing | ||||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0006919 |
caspase activation |
IDA: Inferred from Direct Assay |
P |
required field missing | ||||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0043065 |
positive regulation of apoptosis |
IMP: Inferred from Mutant Phenotype |
P |
required field missing | ||||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0043066 |
negative regulation of apoptosis |
IMP: Inferred from Mutant Phenotype |
P |
required field missing | ||||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0051087 |
chaperone binding |
IPI: Inferred from Physical Interaction |
P61604 |
F |
required field missing | |||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
O15392, P42574 |
F |
required field missing | |||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0005615 |
extracellular space |
IDA: Inferred from Direct Assay |
C |
required field missing | ||||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0005739 |
mitochondrion |
IDA: Inferred from Direct Assay |
C |
required field missing | ||||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0005829 |
cytosol |
IDA: Inferred from Direct Assay |
C |
required field missing | ||||
|
GOA |
Human |
HSPD1 (P10809) |
required field missing | ||||||||
|
FlyBase |
Drosophila |
Hsp60 FBgn0015245 |
GO:0005811 |
lipid particle |
IDA: Inferred from Direct Assay |
C |
HTP proteomics - is this real? |
complete | |||
|
FlyBase |
Drosophila |
Hsp60 FBgn0015245 |
GO:0005811 |
lipid particle |
IDA: Inferred from Direct Assay |
C |
HTP proteomics - is this real? |
complete | |||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0002039 |
p53 binding |
IPI: Inferred from Physical Interaction |
P04637 |
F |
required field missing | |||
|
FlyBase |
Drosophila |
Hsp60 FBgn0015245 |
NOT |
GO:0009408 |
response to heat |
IDA: Inferred from Direct Assay |
P |
complete | |||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0043498 |
cell surface binding |
IDA: Inferred from Direct Assay |
F |
required field missing | ||||
|
FlyBase |
Drosophila |
Hsp60 FBgn0015245 |
GO:0031305 |
integral to mitochondrial inner membrane |
IDA: Inferred from Direct Assay |
C |
complete | ||||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0009986 |
cell surface |
IDA: Inferred from Direct Assay |
C |
required field missing | ||||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0042026 |
protein refolding |
IDA: Inferred from Direct Assay |
P |
required field missing | ||||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0051082 |
unfolded protein binding |
IC: Inferred by Curator |
GO:0042026 |
F |
complete | |||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0043066 |
negative regulation of apoptosis |
IMP: Inferred from Mutant Phenotype |
P |
required field missing | ||||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0043066 |
negative regulation of apoptosis |
IMP: Inferred from Mutant Phenotype |
P |
required field missing | ||||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0005739 |
mitochondrion |
IDA: Inferred from Direct Assay |
C |
required field missing | ||||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0005829 |
cytosol |
IDA: Inferred from Direct Assay |
C |
required field missing | ||||
|
GOA |
Human |
HSPD1 (P10809) |
GO:0006986 |
response to unfolded protein |
IDA: Inferred from Direct Assay |
P |
complete | ||||
|
FlyBase |
Drosophila |
Hsp60 FBgn0015245 |
GO:0007005 |
mitochondrion organization |
IMP: Inferred from Mutant Phenotype |
P |
complete | ||||
|
SGD |
S. cerevisiae |
HSP60 |
GO:0003688 |
DNA replication origin binding |
IDA: Inferred from Direct Assay |
F |
complete | ||||
|
SGD |
S. cerevisiae |
HSP60 |
GO:0003697 |
single-stranded DNA binding |
IDA: Inferred from Direct Assay |
F |
complete | ||||
| edit table |
HSPD1 notes
Dicty hspA
- Pascale
- In PMID 12952082, they show that Dicty hspA is *not* up-regulated by heat shock. Do we put a NOT annotation?
- In PMID 12952082, the use a helix prediction software to assess that the gene is likely mitochondrial; how to annotate that ? ISS? ISM?
- Debby: I would use ISM.
ZFIN hspd1
- Doug
- In PMID 12416612, they show that expression of zebrafish hspd1, unlike dicty and worm, IS upregulated by heat shock. Should we make an annotation to 'response to heat' by IDA? Worm has a similar "NOT" annotation using IEP.
GO terms
- Victoria
GO has 'chaperone activity' as a synonym for 'unfolded protein binding' but not for 'misfolded protein binding' or otherwise damaged/modified/abnormal which the chaperone(s) recognize as well. I had an annotation for 'unfolded protein binding' because I was looking for chaperone activity and the misfolded term was not pulled out. I removed the annotation and replaced it with the 'misfolded' term which is closer to an abnormal state than unfolded; in my case the proteins recognized by the chaperone were modified proteins.
References
- Debby
I took commas out of some of the reference entries and put the PMID's on separate lines in order to reduce the width of this column.
Arabidopsis Hsp60
- Tanya
- Hsp60 is usually mitochondrial (at 26 and 37 F) but is released to cytosol upon drastic heat shock (50 F). Cells assayed were from a cell culture derived from 14 day old seedlings.
- In PMID: 14730085, the expression of all three genes (Arabidopsis Hsp60-3a, Hsp60-3b, and Hsp6-3c) is affected by rotenone treatment. Rotenone is a mitochondrial electron transport chain inhibitor. Expression levels of all three genes increase about 2 fold with respect to no treatment. The only assay for this is a microarray experiment. There is no follow-up assay of a different sort. I've chosen not to annotate this.
- We also have some TAS annotations (that trace to textbooks) that I haven't entered in the table that I'm eager to get rid of and replace with something better via ISS, if possible.
UK curators
HSPD1 When to annotate to apoptosis? (UK curators)
HSPD1 – should protein stabilization be under ‘regulation of gene expression’ – should be regulation of protein expression.?? There is a qualifier in the definition – but this seems quite artificial. Could the GO term name change, so that protein changes do not appear so much as an after thought? (RL)
e.g. HSPD1 – only a TAS that it is a chaperone, therefore while you could assume it has a protein stability function – currently thinking you could only annotate to ‘regulation of gene expression’.
HSPD1 – is internalized by dendritic cells and then presented to T cells to raise an immune response. – where to annotate the CC term? Should we annotate to cell surface binding and receptor binding? have cell surface receptor binding?? Suggest a child term for eukaryotic cell surface binding.
HSPD1 is thought of as a chaperone protein however only TAS annotations available in many papers; for something that binds to it, can we use the ‘chaperone protein binding’ GO term? (RF)
HSPD1 psychological stress –the level of HSPD1 in plasma in patients, increases when patients are under emotional stress, do we want to annotate to ‘response to psychological stress’ term, and therefore what term/where should it go?ant to annotate to response to stress? (RL)
HSPD1 is located by high-throughput experiments as being in lipid particles in serum. Whereas found in mitochondria by in-depth papers. Would this be another reason supporting the addition of the HTP tags to evidence codes, as was concern that function/localization can sometimes be skewed due to HTP data (ST)
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 1.2 1.3 1.4 1.5 Yim JJ & Brown GM (1976) Characteristics of guanosine triphosphate cyclohydrolase I purified from Escherichia coli. J Biol Chem 251: 5087-94 PubMed GONUTS page
- ↑ 2.0 2.1 Funderburk CD et al. (2006) A typical N-terminal extensions confer novel regulatory properties on GTP cyclohydrolase isoforms in Drosophila melanogaster. J Biol Chem 281: 33302-12 PubMed GONUTS page
- ↑ 3.0 3.1 3.2 Gütlich M et al. (1994) Human GTP cyclohydrolase I: only one out of three cDNA isoforms gives rise to the active enzyme. Biochem J 302 ( Pt 1): 215-21 PubMed GONUTS page
- ↑ 4.0 4.1 4.2 Golderer G et al. (2001) GTP cyclohydrolase I mRNA: novel splice variants in the slime mould Physarum polycephalum and in human monocytes (THP-1) indicate conservation of mRNA processing. Biochem J 355: 499-507 PubMed GONUTS page
- ↑ 5.0 5.1 Gütlich M et al. (1994) Molecular characterization of HPH-1: a mouse mutant deficient in GTP cyclohydrolase I activity. Biochem Biophys Res Commun 203: 1675-81 PubMed GONUTS page
- ↑ 6.0 6.1 6.2 6.3 6.4 Hatakeyama K et al. (1989) Purification and characterization of rat liver GTP cyclohydrolase I. Cooperative binding of GTP to the enzyme. J Biol Chem 264: 21660-4 PubMed GONUTS page
- ↑ 7.0 7.1 7.2 7.3 Werner-Felmayer G et al. (1993) Induction of GTP cyclohydrolase I by bacterial lipopolysaccharide in the rat. FEBS Lett 322: 223-6 PubMed GONUTS page
- ↑ 8.0 8.1 8.2 8.3 8.4 8.5 8.6 Milstien S et al. (1996) Purification and cloning of the GTP cyclohydrolase I feedback regulatory protein, GFRP. J Biol Chem 271: 19743-51 PubMed GONUTS page
- ↑ 9.0 9.1 Nardese V et al. (1996) Disruption of the GTP-cyclohydrolase I gene in Saccharomyces cerevisiae. Biochem Biophys Res Commun 218: 273-9 PubMed GONUTS page
- ↑ Sulston J et al. (1975) Dopaminergic neurons in the nematode Caenorhabditis elegans. J Comp Neurol 163: 215-26 PubMed GONUTS page
- ↑ 11.0 11.1 11.2 11.3 Kaspers B et al. (1997) Coordinate induction of tetrahydrobiopterin synthesis and nitric oxide synthase activity in chicken macrophages: upregulation of GTP-cyclohydrolase I activity. Comp Biochem Physiol B Biochem Mol Biol 117: 209-15 PubMed GONUTS page
- ↑ Kumar A et al. (2002) Subcellular localization of the yeast proteome. Genes Dev 16: 707-19 PubMed GONUTS page
- ↑ 13.0 13.1 Huh WK et al. (2003) Global analysis of protein localization in budding yeast. Nature 425: 686-91 PubMed GONUTS page
- ↑ 14.0 14.1 Desai C et al. (1988) A genetic pathway for the development of the Caenorhabditis elegans HSN motor neurons. Nature 336: 638-46 PubMed GONUTS page
- ↑ 15.0 15.1 15.2 Steinmetz MO et al. (1998) Rat GTP cyclohydrolase I is a homodecameric protein complex containing high-affinity calcium-binding sites. J Mol Biol 279: 189-99 PubMed GONUTS page
- ↑ 16.0 16.1 16.2 Yoneyama T & Hatakeyama K (1998) Decameric GTP cyclohydrolase I forms complexes with two pentameric GTP cyclohydrolase I feedback regulatory proteins in the presence of phenylalanine or of a combination of tetrahydrobiopterin and GTP. J Biol Chem 273: 20102-8 PubMed GONUTS page
- ↑ 17.0 17.1 17.2 17.3 17.4 Maita N et al. (2004) Structural basis of biopterin-induced inhibition of GTP cyclohydrolase I by GFRP, its feedback regulatory protein. J Biol Chem 279: 51534-40 PubMed GONUTS page
- ↑ 18.0 18.1 18.2 Maita N et al. (2002) Crystal structure of the stimulatory complex of GTP cyclohydrolase I and its feedback regulatory protein GFRP. Proc Natl Acad Sci U S A 99: 1212-7 PubMed GONUTS page
- ↑ 19.0 19.1 Nandi M et al. (2005) Pulmonary hypertension in a GTP-cyclohydrolase 1-deficient mouse. Circulation 111: 2086-90 PubMed GONUTS page
- ↑ Constable PD et al. (1990) Atrial fibrillation associated with neostigmine administration in three cows. J Am Vet Med Assoc 196: 329-32 PubMed GONUTS page
- ↑ 21.0 21.1 Weinshenker D et al. (1995) Genetic and pharmacological analysis of neurotransmitters controlling egg laying in C. elegans. J Neurosci 15: 6975-85 PubMed GONUTS page
- ↑ Waggoner LE et al. (1998) Control of alternative behavioral states by serotonin in Caenorhabditis elegans. Neuron 21: 203-14 PubMed GONUTS page
- ↑ Waggoner LE et al. (2000) Effect of a neuropeptide gene on behavioral states in Caenorhabditis elegans egg-laying. Genetics 154: 1181-92 PubMed GONUTS page
- ↑ Ranganathan R et al. (2001) Mutations in the Caenorhabditis elegans serotonin reuptake transporter MOD-5 reveal serotonin-dependent and -independent activities of fluoxetine. J Neurosci 21: 5871-84 PubMed GONUTS page
- ↑ Rebelo J et al. (2003) Biosynthesis of pteridines. Reaction mechanism of GTP cyclohydrolase I. J Mol Biol 326: 503-16 PubMed GONUTS page
- ↑ Nar H et al. (1995) Atomic structure of GTP cyclohydrolase I. Structure 3: 459-66 PubMed GONUTS page
- ↑ 27.0 27.1 27.2 27.3 Gütlich M et al. (1996) Control of 6-(D-threo-1',2'-dihydroxypropyl) pterin (dictyopterin) synthesis during aggregation of Dictyostelium discoideum. Involvement of the G-protein-linked signalling pathway in the regulation of GTP cyclohydrolase I activity. Biochem J 314 ( Pt 1): 95-101 PubMed GONUTS page
- ↑ 28.0 28.1 Witter K et al. (1996) Molecular cloning of a cDNA coding for GTP cyclohydrolase I from Dictyostelium discoideum. Biochem J 319 ( Pt 1): 27-32 PubMed GONUTS page
- ↑ 29.0 29.1 29.2 Choi YK et al. (2006) Functional role of sepiapterin reductase in the biosynthesis of tetrahydropteridines in Dictyostelium discoideum Ax2. Biochim Biophys Acta 1760: 877-82 PubMed GONUTS page
- ↑ Avery L & Horvitz HR (1990) Effects of starvation and neuroactive drugs on feeding in Caenorhabditis elegans. J Exp Zool 253: 263-70 PubMed GONUTS page
- ↑ Ziegler I & Gütlich M (1996) Tetrahydropterins interfere with the G protein pathway in Dictyostelium discoideum. Biochem Biophys Res Commun 221: 368-73 PubMed GONUTS page
- ↑ Loer CM & Kenyon CJ (1993) Serotonin-deficient mutants and male mating behavior in the nematode Caenorhabditis elegans. J Neurosci 13: 5407-17 PubMed GONUTS page
- ↑ Gotthardt D et al. (2006) Proteomics fingerprinting of phagosome maturation and evidence for the role of a Galpha during uptake. Mol Cell Proteomics 5: 2228-43 PubMed GONUTS page
- ↑ Avery L et al. (1993) The Caenorhabditis elegans unc-31 gene affects multiple nervous system-controlled functions. Genetics 134: 455-64 PubMed GONUTS page
- ↑ 35.0 35.1 Sawin ER et al. (2000) C. elegans locomotory rate is modulated by the environment through a dopaminergic pathway and by experience through a serotonergic pathway. Neuron 26: 619-31 PubMed GONUTS page
- ↑ Karbowski J et al. (2006) Conservation rules, their breakdown, and optimality in Caenorhabditis sinusoidal locomotion. J Theor Biol 242: 652-69 PubMed GONUTS page
- ↑ Cronin CJ et al. (2005) An automated system for measuring parameters of nematode sinusoidal movement. BMC Genet 6: 5 PubMed GONUTS page
- ↑ 38.0 38.1 Calvo AC et al. (2008) Anabolic function of phenylalanine hydroxylase in Caenorhabditis elegans. FASEB J 22: 3046-58 PubMed GONUTS page
- ↑ Nurrish S et al. (1999) Serotonin inhibition of synaptic transmission: Galpha(0) decreases the abundance of UNC-13 at release sites. Neuron 24: 231-42 PubMed GONUTS page
- ↑ Holdengreber V et al. (2002) Localization of two enzymes of the tetrahydrobiopterin biosynthetic pathway in embryonic chick retina. J Histochem Cytochem 50: 265-74 PubMed GONUTS page
- ↑ 41.0 41.1 Reynolds ER & O'Donnell JM (1987) An analysis of the embryonic defects in Punch mutants of Drosophila melanogaster. Dev Biol 123: 430-41 PubMed GONUTS page
- ↑ 42.0 42.1 42.2 42.3 Blau N & Niederwieser A (1986) The application of 8-aminoguanosine triphosphate, a new inhibitor of GTP cyclohydrolase I, to the purification of the enzyme from human liver. Biochim Biophys Acta 880: 26-31 PubMed GONUTS page
- ↑ 43.0 43.1 43.2 Schoedon G et al. (1989) Purification of GTP cyclohydrolase I from human liver and production of specific monoclonal antibodies. Eur J Biochem 178: 627-34 PubMed GONUTS page
- ↑ Weisberg EP & O'Donnell JM (1986) Purification and characterization of GTP cyclohydrolase I from Drosophila melanogaster. J Biol Chem 261: 1453-8 PubMed GONUTS page
- ↑ Tegeder I et al. (2006) GTP cyclohydrolase and tetrahydrobiopterin regulate pain sensitivity and persistence. Nat Med 12: 1269-77 PubMed GONUTS page
- ↑ 46.0 46.1 46.2 Chen X et al. (1994) A maternal product of the Punch locus of Drosophila melanogaster is required for precellular blastoderm nuclear divisions. J Cell Sci 107 ( Pt 12): 3501-13 PubMed GONUTS page
- ↑ 47.0 47.1 47.2 Werner-Felmayer G et al. (1993) Pteridine biosynthesis in human endothelial cells. Impact on nitric oxide-mediated formation of cyclic GMP. J Biol Chem 268: 1842-6 PubMed GONUTS page
- ↑ 48.0 48.1 48.2 48.3 Katusic ZS et al. (1998) Cytokines stimulate GTP cyclohydrolase I gene expression in cultured human umbilical vein endothelial cells. Arterioscler Thromb Vasc Biol 18: 27-32 PubMed GONUTS page
- ↑ Gesierich A et al. (2003) Role of human GTP cyclohydrolase I and its regulatory protein in tetrahydrobiopterin metabolism. Basic Res Cardiol 98: 69-75 PubMed GONUTS page
- ↑ 50.0 50.1 Lauderdale JD et al. (2000) 3' deletions cause aniridia by preventing PAX6 gene expression. Proc Natl Acad Sci U S A 97: 13755-9 PubMed GONUTS page
- ↑ 51.0 51.1 51.2 51.3 Hsouna A et al. (2007) Drosophila dopamine synthesis pathway genes regulate tracheal morphogenesis. Dev Biol 308: 30-43 PubMed GONUTS page
- ↑ Cai S et al. (2002) GTP cyclohydrolase I gene transfer augments intracellular tetrahydrobiopterin in human endothelial cells: effects on nitric oxide synthase activity, protein levels and dimerisation. Cardiovasc Res 55: 838-49 PubMed GONUTS page
- ↑ 53.0 53.1 Suzuki T et al. (2004) GTP cyclohydrolase I utilizes metal-free GTP as its substrate. Eur J Biochem 271: 349-55 PubMed GONUTS page
- ↑ 54.0 54.1 Reynolds ER & O'Donnell JM (1988) Characterization of new Punch mutations: identification of two additional mutant classes. Genetics 119: 609-17 PubMed GONUTS page
- ↑ 55.0 55.1 Schoedon G et al. (1987) Localization of GTP cyclohydrolase I in human peripheral blood smears using a specific monoclonal antibody and an immune-alkaline phosphatase labeling technique. Biochem Biophys Res Commun 148: 1232-6 PubMed GONUTS page
- ↑ Swick L & Kapatos G (2006) A yeast 2-hybrid analysis of human GTP cyclohydrolase I protein interactions. J Neurochem 97: 1447-55 PubMed GONUTS page
- ↑ Nagatsu I et al. (1999) Specific localization of the guanosine triphosphate (GTP) cyclohydrolase I-immunoreactivity in the human brain. J Neural Transm 106: 607-17 PubMed GONUTS page
- ↑ Chavan B et al. (2006) GTP cyclohydrolase feedback regulatory protein controls cofactor 6-tetrahydrobiopterin synthesis in the cytosol and in the nucleus of epidermal keratinocytes and melanocytes. J Invest Dermatol 126: 2481-9 PubMed GONUTS page
- ↑ Yamamoto K et al. (2003) Genetic engineering of Escherichia coli for production of tetrahydrobiopterin. Metab Eng 5: 246-54 PubMed GONUTS page
- ↑ 60.0 60.1 60.2 Ziemienowicz A et al. (1993) Both the Escherichia coli chaperone systems, GroEL/GroES and DnaK/DnaJ/GrpE, can reactivate heat-treated RNA polymerase. Different mechanisms for the same activity. J Biol Chem 268: 25425-31 PubMed GONUTS page
- ↑ 61.0 61.1 61.2 61.3 Kotsifas M et al. (2002) Chaperonin 60 and mitochondrial disease in Dictyostelium. J Muscle Res Cell Motil 23: 839-52 PubMed GONUTS page
- ↑ Martin CS et al. (1995) Cpn60 is exclusively localized into mitochondria of rat liver and embryonic Drosophila cells. J Cell Biochem 59: 235-45 PubMed GONUTS page
- ↑ 63.0 63.1 63.2 63.3 63.4 63.5 63.6 63.7 Cohen-Sfady M et al. (2005) Heat shock protein 60 activates B cells via the TLR4-MyD88 pathway. J Immunol 175: 3594-602 PubMed GONUTS page
- ↑ Koll H et al. (1992) Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space. Cell 68: 1163-75 PubMed GONUTS page
- ↑ 65.0 65.1 65.2 65.3 65.4 65.5 Yoneda T et al. (2004) Compartment-specific perturbation of protein handling activates genes encoding mitochondrial chaperones. J Cell Sci 117: 4055-66 PubMed GONUTS page
- ↑ 66.0 66.1 Makino S et al. (2005) Heat-shock protein 60 is required for blastema formation and maintenance during regeneration. Proc Natl Acad Sci U S A 102: 14599-604 PubMed GONUTS page
- ↑ 67.0 67.1 Hendrix RW (1979) Purification and properties of groE, a host protein involved in bacteriophage assembly. J Mol Biol 129: 375-92 PubMed GONUTS page
- ↑ Martin J et al. (1991) Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature 352: 36-42 PubMed GONUTS page
- ↑ Tilly K et al. (1981) Identification of a second Escherichia coli groE gene whose product is necessary for bacteriophage morphogenesis. Proc Natl Acad Sci U S A 78: 1629-33 PubMed GONUTS page
- ↑ Parsell DA & Sauer RT (1989) Induction of a heat shock-like response by unfolded protein in Escherichia coli: dependence on protein level not protein degradation. Genes Dev 3: 1226-32 PubMed GONUTS page
- ↑ 71.0 71.1 Gragerov A et al. (1992) Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli. Proc Natl Acad Sci U S A 89: 10341-4 PubMed GONUTS page
- ↑ Cheng MY et al. (1990) The mitochondrial chaperonin hsp60 is required for its own assembly. Nature 348: 455-8 PubMed GONUTS page
- ↑ 73.0 73.1 Hallberg EM et al. (1993) Loss of mitochondrial hsp60 function: nonequivalent effects on matrix-targeted and intermembrane-targeted proteins. Mol Cell Biol 13: 3050-7 PubMed GONUTS page
- ↑ Cheng MY et al. (1989) Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature 337: 620-5 PubMed GONUTS page
- ↑ Rospert S et al. (1993) Identification and functional analysis of chaperonin 10, the groES homolog from yeast mitochondria. Proc Natl Acad Sci U S A 90: 10967-71 PubMed GONUTS page
- ↑ 76.0 76.1 76.2 Martin J et al. (1992) Prevention of protein denaturation under heat stress by the chaperonin Hsp60. Science 258: 995-8 PubMed GONUTS page
- ↑ 77.0 77.1 77.2 Kaufman BA et al. (2000) In organello formaldehyde crosslinking of proteins to mtDNA: identification of bifunctional proteins. Proc Natl Acad Sci U S A 97: 7772-7 PubMed GONUTS page
- ↑ Asquith KL et al. (2004) Tyrosine phosphorylation activates surface chaperones facilitating sperm-zona recognition. J Cell Sci 117: 3645-57 PubMed GONUTS page
- ↑ 79.0 79.1 Brudzynski K et al. (1995) A family of hsp60-related proteins in pancreatic beta cells of non-obese diabetic (NOD) mice. J Autoimmun 8: 859-74 PubMed GONUTS page
- ↑ 80.0 80.1 Brudzynski K et al. (1992) Immunocytochemical localization of heat-shock protein 60-related protein in beta-cell secretory granules and its altered distribution in non-obese diabetic mice. Diabetologia 35: 316-24 PubMed GONUTS page
- ↑ Danial NN et al. (2003) BAD and glucokinase reside in a mitochondrial complex that integrates glycolysis and apoptosis. Nature 424: 952-6 PubMed GONUTS page
- ↑ Haigis MC et al. (2006) SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells. Cell 126: 941-54 PubMed GONUTS page
- ↑ Mootha VK et al. (2003) Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria. Cell 115: 629-40 PubMed GONUTS page
- ↑ Zhu Y et al. (2004) Constitutive association of the proapoptotic protein Bim with Bcl-2-related proteins on mitochondria in T cells. Proc Natl Acad Sci U S A 101: 7681-6 PubMed GONUTS page
- ↑ Chen W et al. (2006) Efficient induction of antitumor T cell immunity by exosomes derived from heat-shocked lymphoma cells. Eur J Immunol 36: 1598-607 PubMed GONUTS page
- ↑ Da Cruz S et al. (2003) Proteomic analysis of the mouse liver mitochondrial inner membrane. J Biol Chem 278: 41566-71 PubMed GONUTS page
- ↑ 87.0 87.1 Osterloh A et al. (2004) Lipopolysaccharide-free heat shock protein 60 activates T cells. J Biol Chem 279: 47906-11 PubMed GONUTS page
- ↑ Osterloh A et al. (2008) Hsp60-mediated T cell stimulation is independent of TLR4 and IL-12. Int Immunol 20: 433-43 PubMed GONUTS page
- ↑ 89.0 89.1 89.2 89.3 89.4 Osterloh A et al. (2007) Synergistic and differential modulation of immune responses by Hsp60 and lipopolysaccharide. J Biol Chem 282: 4669-80 PubMed GONUTS page
- ↑ 90.0 90.1 Xu Q et al. (1994) Surface staining and cytotoxic activity of heat-shock protein 60 antibody in stressed aortic endothelial cells. Circ Res 75: 1078-85 PubMed GONUTS page
- ↑ Chen S et al. (2005) Association of heat shock proteins and neuronal membrane components with lipid rafts from the rat brain. J Neurosci Res 81: 522-9 PubMed GONUTS page
- ↑ Meinhardt A et al. (1995) Expression of mitochondrial heat shock protein 60 in distinct cell types and defined stages of rat seminiferous epithelium. Biol Reprod 52: 798-807 PubMed GONUTS page
- ↑ Kim HS et al. (2006) Heat shock protein 60 modified with O-linked N-acetylglucosamine is involved in pancreatic beta-cell death under hyperglycemic conditions. FEBS Lett 580: 2311-6 PubMed GONUTS page
- ↑ 94.0 94.1 94.2 Arias AE et al. (2000) Colocalization of chaperone Cpn60, proinsulin and convertase PC1 within immature secretory granules of insulin-secreting cells suggests a role for Cpn60 in insulin processing. J Cell Sci 113 ( Pt 11): 2075-83 PubMed GONUTS page
- ↑ 95.0 95.1 95.2 95.3 Bruschi SA et al. (1998) Mitochondrial stress protein recognition of inactivated dehydrogenases during mammalian cell death. Proc Natl Acad Sci U S A 95: 13413-8 PubMed GONUTS page
- ↑ 96.0 96.1 Dubaquié Y et al. (1997) Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60. Proc Natl Acad Sci U S A 94: 9011-6 PubMed GONUTS page
- ↑ Benedetti C et al. (2006) Ubiquitin-like protein 5 positively regulates chaperone gene expression in the mitochondrial unfolded protein response. Genetics 174: 229-39 PubMed GONUTS page
- ↑ Haynes CM et al. (2007) ClpP mediates activation of a mitochondrial unfolded protein response in C. elegans. Dev Cell 13: 467-80 PubMed GONUTS page
- ↑ 99.0 99.1 Saijo T & Tanaka K (1995) Isoalloxazine ring of FAD is required for the formation of the core in the Hsp60-assisted folding of medium chain acyl-CoA dehydrogenase subunit into the assembly competent conformation in mitochondria. J Biol Chem 270: 1899-907 PubMed GONUTS page
- ↑ 100.0 100.1 100.2 Kirchhoff SR et al. (2002) Cytosolic heat shock protein 60, apoptosis, and myocardial injury. Circulation 105: 2899-904 PubMed GONUTS page
- ↑ Sigler PB & Horwich AL (1995) Unliganded GroEL at 2.8 A: structure and functional implications. Philos Trans R Soc Lond B Biol Sci 348: 113-9 PubMed GONUTS page
- ↑ 102.0 102.1 102.2 102.3 Drummond AE et al. (1996) Application of a chromogenic bioassay procedure for the measurement of the proliferation of endothelial cells in vitro under the influence of the effects of steroid hormones and growth factors. J Biochem Biophys Methods 31: 123-34 PubMed GONUTS page
- ↑ Yamamori T et al. (1978) Transient regulation of protein synthesis in Escherichia coli upon shift-up of growth temperature. J Bacteriol 134: 1133-40 PubMed GONUTS page
- ↑ Lemaux PG et al. (1978) Transient rates of synthesis of individual polypeptides in E. coli following temperature shifts. Cell 13: 427-34 PubMed GONUTS page
- ↑ Mueller S et al. (2008) General detoxification and stress responses are mediated by oxidized lipids through TGA transcription factors in Arabidopsis. Plant Cell 20: 768-85 PubMed GONUTS page
- ↑ Prasad TK & Stewart CR (1992) cDNA clones encoding Arabidopsis thaliana and Zea mays mitochondrial chaperonin HSP60 and gene expression during seed germination and heat shock. Plant Mol Biol 18: 873-85 PubMed GONUTS page
- ↑ Rikhvanov EG et al. (2007) Nuclear-mitochondrial cross-talk during heat shock in Arabidopsis cell culture. Plant J 52: 763-78 PubMed GONUTS page
- ↑ 108.0 108.1 Sunderhaus S et al. (2006) Carbonic anhydrase subunits form a matrix-exposed domain attached to the membrane arm of mitochondrial complex I in plants. J Biol Chem 281: 6482-8 PubMed GONUTS page
- ↑ Heazlewood JL et al. (2004) Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins. Plant Cell 16: 241-56 PubMed GONUTS page
- ↑ 110.0 110.1 110.2 110.3 110.4 110.5 Ghosh JC et al. (2008) Hsp60 regulation of tumor cell apoptosis. J Biol Chem 283: 5188-94 PubMed GONUTS page
- ↑ 111.0 111.1 111.2 111.3 111.4 111.5 111.6 111.7 111.8 111.9 Chandra D et al. (2007) Cytosolic accumulation of HSP60 during apoptosis with or without apparent mitochondrial release: evidence that its pro-apoptotic or pro-survival functions involve differential interactions with caspase-3. J Biol Chem 282: 31289-301 PubMed GONUTS page
- ↑ Samali A et al. (1999) Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells. EMBO J 18: 2040-8 PubMed GONUTS page
- ↑ Shamaei-Tousi A et al. (2007) Plasma heat shock protein 60 and cardiovascular disease risk: the role of psychosocial, genetic, and biological factors. Cell Stress Chaperones 12: 384-92 PubMed GONUTS page
- ↑ 114.0 114.1 114.2 114.3 Trapasso F et al. (2008) Fhit interaction with ferredoxin reductase triggers generation of reactive oxygen species and apoptosis of cancer cells. J Biol Chem 283: 13736-44 PubMed GONUTS page
- ↑ Beller M et al. (2006) Characterization of the Drosophila lipid droplet subproteome. Mol Cell Proteomics 5: 1082-94 PubMed GONUTS page
- ↑ Cermelli S et al. (2006) The lipid-droplet proteome reveals that droplets are a protein-storage depot. Curr Biol 16: 1783-95 PubMed GONUTS page
- ↑ Karunanithi S et al. (1999) Neuroprotection at Drosophila synapses conferred by prior heat shock. J Neurosci 19: 4360-9 PubMed GONUTS page
- ↑ 118.0 118.1 Lipsker D et al. (2002) Heat shock proteins 70 and 60 share common receptors which are expressed on human monocyte-derived but not epidermal dendritic cells. Eur J Immunol 32: 322-32 PubMed GONUTS page
- ↑ 119.0 119.1 Baena-López LA et al. (2008) The expression of heat shock protein HSP60A reveals a dynamic mitochondrial pattern in Drosophila melanogaster embryos. J Proteome Res 7: 2780-8 PubMed GONUTS page
- ↑ Soltys BJ & Gupta RS (1997) Cell surface localization of the 60 kDa heat shock chaperonin protein (hsp60) in mammalian cells. Cell Biol Int 21: 315-20 PubMed GONUTS page
- ↑ Thomas ML et al. (2000) gammadelta T cells lyse autologous and allogenic oesophageal tumours: involvement of heat-shock proteins in the tumour cell lysis. Cancer Immunol Immunother 48: 653-9 PubMed GONUTS page
- ↑ 122.0 122.1 122.2 Richardson A et al. (2001) The importance of a mobile loop in regulating chaperonin/ co-chaperonin interaction: humans versus Escherichia coli. J Biol Chem 276: 4981-7 PubMed GONUTS page