GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

RefGenome Electronic Jamboree 2008-07 GCH1 and HSPD1

From GONUTS
Jump to: navigation, search

See the talk page for tips on editing the tables and for misc. discussion.

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

GCH1_Graph

<ejamb>573c5f77b3a094817c4e1c4a6f9b2c99.0.V4873c8ee0cab7

GCH1</ejamb>

[back to top]


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

PMID:821948[1]

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

PMID:16966327[2]

IDA: Inferred from Direct Assay

F

complete

GOA

Human

GCH1 (P30793-2)

NOT

GO:0003934

GTP cyclohydrolase I activity

PMID:8068008[3] PMID:11284739[4]

IDA: Inferred from Direct Assay

F

complete

MGI

Mouse

Gch1

GO:0006729

tetrahydrobiopterin biosynthetic process

PMID:7524491[5]

IC: Inferred by Curator

GO:0003934

P

required field missing

RGD

Rat

Gch1

GO:0005525

GTP binding

PMID:2557335[6] PMID:8486153[7] PMID:8702680[8]

IDA: Inferred from Direct Assay

F

complete

Sanger GeneDB

S. Pombe

required field missing

SGD

S. cerevisiae

FOL2

GO:0003934

GTP cyclohydrolase I activity

PMID:8573145[9]

IMP: Inferred from Mutant Phenotype

F

complete

TAIR

Arabidopsis

required field missing

WormBase

C.elegans

cat-4 (WBGene00000298)

GO:0042416

dopamine biosynthetic process

PMID:240872[10]

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

PMID:9226880[11]

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

PMID:8573145[9]

IMP: Inferred from Mutant Phenotype

P

complete

SGD

S. cerevisiae

FOL2

GO:0005737

cytoplasm

PMID:11914276[12] PMID:14562095[13]

IDA: Inferred from Direct Assay

C

high-throughput studies

complete

SGD

S. cerevisiae

FOL2

GO:0005634

nucleus

PMID:14562095[13]

IDA: Inferred from Direct Assay

C

high-throughput study

complete

WormBase

C.elegans

cat-4 (WBGene00000298)

GO:0042427

serotonin biosynthetic process

PMID:3200316[14]

IMP: Inferred from Mutant Phenotype

No specific allele stated

P

complete

EcoliWiki

E. coli

folE

GO:0005829

cytosol

PMID:821948[1]

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

PMID:9685352[16]

IPI: Inferred from Physical Interaction

RGD:1345739

F

complete

RGD

Rat

Gch1

GO:0005509

calcium ion binding

PMID:9636709[15]

IDA: Inferred from Direct Assay

RGD:1345739

F

complete

RGD

Rat

Gch1

GO:0050662

coenzyme binding

PMID:15448133[17]

IDA: Inferred from Direct Assay

RGD:1345739

F

complete

RGD

Rat

Gch1

GO:0008270

zinc ion binding

PMID:11818540[18] PMID:15448133[17]

IDA: Inferred from Direct Assay

RGD:1345739

F

complete

RGD

Rat

Gch1

GO:0005515

protein binding

PMID:8702680[8]

IDA: Inferred from Direct Assay

F

complete

MGI

Mouse

Gch1

GO:0003934

GTP cyclohydrolase I activity

PMID:7524491[5]

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

PMID:15824199[19]

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

PMID:15824199[19]

IMP: Inferred from Mutant Phenotype

P

complete

EcoliWiki

E. coli

folE

GO:0046656

folic acid biosynthetic process

PMID:821948[1]

IDA: Inferred from Direct Assay

P

FolE catalyzes the first committed step in folic acid biosynthesis.

complete

RGD

Rat

Gch1

GO:0005515

protein binding

PMID:8702680[8]

IDA: Inferred from Direct Assay

F

complete

RGD

Rat

Gch1

GO:0051066

dihydrobiopterin metabolic process

PMID:8702680[8] PMID:2557335[6] PMID:8486153[7]

IDA: Inferred from Direct Assay

P

complete

RGD

Rat

Gch1

GO:0006461

protein complex assembly

PMID:11818540[18] PMID:9685352[16] PMID:15448133[17]

IDA: Inferred from Direct Assay

P

complete

RGD

Rat

Gch1

GO:0051291

protein heterooligomerization

PMID:11818540[18] PMID:9685352[16] PMID:15448133[17]

IDA: Inferred from Direct Assay

P

complete

RGD

Rat

Gch1

GO:0051260

protein homooligomerization

PMID:2557335[6] PMID:9636709[15]

IDA: Inferred from Direct Assay

P

complete

RGD

Rat

Gch1

GO:0005625

soluble fraction

PMID:8486153[7] PMID:8702680[8] PMID:2557335[6]

IDA: Inferred from Direct Assay

C

complete

RGD

Rat

Gch1

GO:0043234

protein complex

PMID:2298660[20] PMID:8702680[8] PMID:15448133[17]

IDA: Inferred from Direct Assay

C

complete

EcoliWiki

E. coli

folE

GO:0046654

tetrahydrofolate biosynthetic process

PMID:821948[1]

IDA: Inferred from Direct Assay

P

complete

EcoliWiki

E. coli

folE

GO:0005525

GTP binding

PMID:821948[1]

IDA: Inferred from Direct Assay

F

complete

WormBase

C.elegans

cat-4 (WBGene00000298)

GO:0046662

regulation of oviposition

PMID:7472454[21] PMID:9697864[22] PMID:10757762[23]

IMP: Inferred from Mutant Phenotype

WB:e1141

P

complete

WormBase

C.elegans

cat-4 (WBGene00000298)

GO:0042427

serotonin biosynthetic process

PMID:3200316[14] PMID:7472454[21] PMID:11487610[24]

IMP: Inferred from Mutant Phenotype

WB:e1141 (for all but first reference)

P

complete

EcoliWiki

E. coli

folE

GO:0008270

zinc ion binding

PMID:12559918[25]

IDA: Inferred from Direct Assay

F

complete

EcoliWiki

E. coli

folE

GO:0043234

protein complex

PMID:7663943[26] PMID:821948[1]

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

PMID:8660315[27] PMID:8870645[28] PMID:16527408[29]

IDA: Inferred from Direct Assay

F

complete

DictyBase

Dicty

gchA

GO:0006729

tetrahydrobiopterin biosynthetic process

PMID:8660315[27] PMID:8870645[28] PMID:16527408[29]

IDA: Inferred from Direct Assay

P

complete

AgBase

Chicken

P50141

GO:0006729

tetrahydrobiopterin biosynthetic process

PMID:9226880[11]

IMP: Inferred from Mutant Phenotype

P

complete

AgBase

Chicken

P50141

GO:0006729

tetrahydrobiopterin biosynthetic process

PMID:9226880[11]

IDA: Inferred from Direct Assay

P

complete

AgBase

Chicken

P50141

GO:0003933

GTP cyclohydrolase activity

PMID:9226880[11]

IDA: Inferred from Direct Assay

F

complete

WormBase

C.elegans

cat-4 (WBGene00000298)

GO:0043051

regulation of pharyngeal pumping

PMID:2181052[30]

IMP: Inferred from Mutant Phenotype

No allele stated

P

complete

DictyBase

Dicty

gchA

GO:0008277

regulation of G-protein coupled receptor protein signaling pathway

PMID:8619862[31]

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

PMID:8660315[27] PMID:16527408[29]

IDA: Inferred from Direct Assay

C

complete

WormBase

C.elegans

cat-4 (WBGene00000298)

GO:0060179

male mating behavior

PMID:8254383[32]

IMP: Inferred from Mutant Phenotype

WB:e1141

P

complete

DictyBase

Dicty

gchA

GO:0045335

phagocytic vesicle

PMID:16926386[33]

IDA: Inferred from Direct Assay

C

complete

WormBase

C.elegans

cat-4 (WBGene00000298)

GO:0046662

regulation of oviposition

PMID:8325482[34]

IGI: Inferred from Genetic Interaction

WB:WBGene00006767

P

complete

DictyBase

Dicty

gchA

GO:0005624

membrane fraction

PMID:8660315[27]

IDA: Inferred from Direct Assay

C

complete

WormBase

C.elegans

cat-4 (WBGene00000298)

GO:0032095

regulation of response to food

PMID:10896158[35]

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

PMID:10896158[35]

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

PMID:16759670[36] PMID:15698479[37]

IMP: Inferred from Mutant Phenotype

WB:e1141

P

complete

WormBase

C.elegans

cat-4 (WBGene00000298)

GO:0042438

melanin biosynthetic process

PMID:18460651[38]

IMP: Inferred from Mutant Phenotype

WB:ok342

P

complete

WormBase

C.elegans

cat-4 (WBGene00000298)

GO:0040002

collagen and cuticulin-based cuticle development

PMID:18460651[38]

IMP: Inferred from Mutant Phenotype

WB:ok342

P

complete

WormBase

C.elegans

cat-4 (WBGene00000298)

GO:0050804

regulation of synaptic transmission

PMID:10677040[39]

IMP: Inferred from Mutant Phenotype

WB:e1141

P

complete

AgBase

Chicken

P50141

GO:0005737

cytoplasm

PMID:11799145[40]

IDA: Inferred from Direct Assay

C

complete

FlyBase

Drosophila

FBgn0003162

GO:0048067

cuticle pigmentation

PMID:3115849[41]

IMP: Inferred from Mutant Phenotype

P

complete

FlyBase

Drosophila

FBgn0003162

GO:0008363

larval chitin-based cuticle development

PMID:3115849[41]

IMP: Inferred from Mutant Phenotype

P

complete

GOA

Human

GCH1 (P30793)

GO:0042559

pteridine and derivative biosynthetic process

PMID:3753653[42] PMID:2463916[43]

IDA: Inferred from Direct Assay

P

complete

GOA

Human

GCH1 (P30793)

GO:0006184

GTP catabolic process

PMID:2463916[43]

IDA: Inferred from Direct Assay

P

complete

FlyBase

Drosophila

FBgn0003162

GO:0003934

GTP cyclohydrolase I activity

PMID:3080426[44]

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

PMID:7706401[46]

IMP: Inferred from Mutant Phenotype

P

complete

GOA

Human

GCH1 (P30793)

GO:0006729

tetrahydrobiopterin biosynthetic process

PMID:7678411[47] PMID:9445252[48]

IDA: Inferred from Direct Assay

P

required field missing

FlyBase

Drosophila

FBgn0003162

GO:0006728

pteridine biosynthetic process

PMID:7706401[46]

IMP: Inferred from Mutant Phenotype

P

complete

GOA

Human

GCH1 (P30793)

GO:0032496

response to lipopolysaccharide

PMID:7678411[47] PMID:9445252[48]

IDA: Inferred from Direct Assay

P

required field missing

FlyBase

Drosophila

FBgn0003162

GO:0006728

pteridine biosynthetic process

PMID:16966327[2]

IDA: Inferred from Direct Assay

P

complete

GOA

Human

GCH1 (P30793)

GO:0034341

response to interferon-gamma

PMID:7678411[47] PMID:9445252[48] PMID:12607127[49]

IDA: Inferred from Direct Assay

P

complete

FlyBase

Drosophila

FBgn0003162

GO:0005737

cytoplasm

PMID:7706401[46]

IDA: Inferred from Direct Assay

C

complete

GOA

Human

GCH1 (P30793)

GO:0051260

protein homooligomerization

PMID:11087823[50]

IDA: Inferred from Direct Assay

P

required field missing

FlyBase

Drosophila

FBgn0003162

GO:0007424

open tracheal system development

PMID:17585895[51]

IMP: Inferred from Mutant Phenotype

P

complete

GOA

Human

GCH1 (P30793)

GO:0006809

nitric oxide biosynthetic process

PMID:9445252[48]

NAS: Non-traceable Author Statement

P

required field missing

FlyBase

Drosophila

FBgn0003162

GO:0048754

branching morphogenesis of a tube

PMID:17585895[51]

IMP: Inferred from Mutant Phenotype

P

complete

GOA

Human

GCH1 (P30793)

GO:0051000

positive regulation of nitric-oxide synthase activity

PMID:12176133[52]

IDA: Inferred from Direct Assay

P

required field missing

FlyBase

Drosophila

FBgn0003162

GO:0030334

regulation of cell migration

PMID:17585895[51]

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

PMID:3753653[42]

IDA: Inferred from Direct Assay

F

required field missing

FlyBase

Drosophila

FBgn0003162

GO:0042416

dopamine biosynthetic process

PMID:17585895[51]

IMP: Inferred from Mutant Phenotype

P

complete

GOA

Human

GCH1 (P30793)

GO:0005525

GTP binding

PMID:3753653[42] PMID:14717702[53]

IDA: Inferred from Direct Assay

F

required field missing

FlyBase

Drosophila

FBgn0003162

GO:0048072

compound eye pigmentation

PMID:3136053[54]

IMP: Inferred from Mutant Phenotype

P

complete

GOA

Human

GCH1 (P30793)

GO:0008270

zinc ion binding

PMID:14717702[53] PMID:11087823[50]

IDA: Inferred from Direct Assay

F

required field missing

FlyBase

Drosophila

FBgn0003162

GO:0003934

GTP cyclohydrolase I activity

PMID:3136053[54]

IMP: Inferred from Mutant Phenotype

F

complete

GOA

Human

GCH1 (P30793)

GO:0005829

cytosol

PMID:2463916[43] PMID:3318829[55]

IDA: Inferred from Direct Assay

C

required field missing

GOA

Human

GCH1 (P30793)

GO:0031410

cytoplasmic vesicle

PMID:3318829[55]

IDA: Inferred from Direct Assay

C

required field missing

GOA

Human

GCH1 (P30793)

GO:0005515

protein binding

PMID:16696853[56]

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

PMID:3753653[42]

IDA: Inferred from Direct Assay

F

required field missing

GOA

Human

GCH1 (P30793)

GO:0005737

cytoplasm

PMID:10907721[57]

IDA: Inferred from Direct Assay

C

complete

GOA

Human

GCH1 (P30793)

GO:0005634

nucleus

PMID:16778797[58]

IDA: Inferred from Direct Assay

C

complete

GOA

Human

GCH1 (P30793-3)

NOT

GO:0003934

GTP cyclohydrolase I activity

PMID:8068008[3] PMID:11284739[4]

IDA: Inferred from Direct Assay

F

complete

GOA

Human

GCH1 (P30793-4)

NOT

GO:0003934

GTP cyclohydrolase I activity

PMID:8068008[3] PMID:11284739[4]

IDA: Inferred from Direct Assay

F

complete

edit table

GCH1 notes

[back to top]


  • 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]
  • 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
  • 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

HSPD1_Graph <ejamb>573c5f77b3a094817c4e1c4a6f9b2c99.197349.W4873c9d899a70

HSPD1</ejamb>

[back to top]


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

PMID:7902351[60]

IDA: Inferred from Direct Assay

P

GroEL/GroES can reactivate heat-treated RNA polymerase in vitro.

complete

DictyBase

Dicty

hspA

GO:0005739

mitochondrion

PMID:12952082[61]

IDA: Inferred from Direct Assay

C

complete

FlyBase

Drosophila

Hsp60 FBgn0015245

GO:0005739

mitochondrion

PMID:8904317[62]

IDA: Inferred from Direct Assay

C

complete

GOA

Human

HSPD1 (P10809)

GO:0002368

B cell cytokine production

PMID:16148103[63]

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

PMID:1347713[64]

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

PMID:15280428[65]

IEP: Inferred from Expression Pattern

P

complete

Chicken

required field missing

ZFIN

Zebrafish

hspd1

GO:0031101

fin regeneration

PMID:16204379[66]

IMP: Inferred from Mutant Phenotype

ZFIN:ZDB-GENO-051101-1

P

complete

EcoliWiki

E. coli

groL

GO:0005524

ATP binding

PMID:379350[67]

IDA: Inferred from Direct Assay

F

Purified GroEL has ATPase activity.

complete

EcoliWiki

E. coli

groL

GO:0051082

unfolded protein binding

PMID:1676490[68]

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

PMID:7015340[69]

IMP: Inferred from Mutant Phenotype

P

complete

EcoliWiki

E. coli

groL

GO:0016887

ATPase activity

PMID:379350[67]

IDA: Inferred from Direct Assay

F

complete

EcoliWiki

E. coli

groL

GO:0006986

response to unfolded protein

PMID:2676724[70]

P

required field missing

EcoliWiki

E. coli

groL

GO:0005737

cytoplasm

C

required field missing

EcoliWiki

E. coli

groL

GO:0006457

protein folding

PMID:1359538[71]

IGI: Inferred from Genetic Interaction

P

Not sure about evidence code.

complete

DictyBase

Dicty

hspA

GO:0046956

positive phototaxis

PMID:12952082[61]

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

PMID:12952082[61]

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

PMID:12952082[61]

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

PMID:1978929[72]

IMP: Inferred from Mutant Phenotype

P

required field missing

SGD

S. cerevisiae

HSP60

GO:0051604

protein maturation

PMID:8097278[73]

IMP: Inferred from Mutant Phenotype

P

required field missing

SGD

S. cerevisiae

HSP60

GO:0051131

chaperone-mediated protein complex assembly

PMID:2645524[74]

IMP: Inferred from Mutant Phenotype

P

required field missing

SGD

S. cerevisiae

HSP60

GO:0016887

ATPase activity

PMID:7902576[75]

IDA: Inferred from Direct Assay

F

complete

SGD

S. cerevisiae

HSP60

GO:0051082

unfolded protein binding

PMID:1359644[76]

IMP: Inferred from Mutant Phenotype

F

complete

SGD

S. cerevisiae

HSP60

GO:0042026

protein refolding

PMID:1359644[76]

IMP: Inferred from Mutant Phenotype

P

complete

SGD

S. cerevisiae

HSP60

GO:0005739

mitochondrion

PMID:8097278[73]

IDA: Inferred from Direct Assay

C

complete

SGD

S. cerevisiae

HSP60

GO:0050821

protein stabilization

PMID:1359644[76]

IMP: Inferred from Mutant Phenotype

P

complete

SGD

S. cerevisiae

HSP60

GO:0042645

mitochondrial nucleoid

PMID:10869431[77]

IDA: Inferred from Direct Assay

C

complete

MGI

Mouse

Hspd1

GO:0044459

plasma membrane part

PMID:15252132[78]

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

PMID:1516759[80] PMID:8824711[79]

IDA: Inferred from Direct Assay

C

complete

MGI

Mouse

Hspd1

GO:0043231

intracellular membrane-bounded organelle

PMID:15136728[84], PMID:16708399[85]

IDA: Inferred from Direct Assay

C

complete

MGI

Mouse

Hspd1

GO:0005743

mitochondrial inner membrane

PMID:12865426[86]

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

PMID:15371451[87] PMID:18256040[88] PMID:17164250[89]

IDA: Inferred from Direct Assay

P

complete

MGI

Mouse

Hspd1

GO:0042110

T cell activation

PMID:17164250[89]

IGI: Inferred from Genetic Interaction

MGI:107658

P

required field missing

MGI

Mouse

Hspd1

GO:0032729

positive regulation of interferon-gamma production

PMID:17164250[89] PMID:15371451[87]

IDA: Inferred from Direct Assay

P

complete

MGI

Mouse

Hspd1

GO:0032729

positive regulation of interferon-gamma production

PMID:17164250[89]

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

PMID:17164250[89]

IDA: Inferred from Direct Assay

P

required field missing

RGD

Rat

Hspd1

GO:0009986

cell surface

PMID:7525102[90]

IDA: Inferred from Direct Assay

C

complete

RGD

Rat

Hspd1

GO:0005737

cytoplasm

PMID:7525102[90]

IDA: Inferred from Direct Assay

C

complete

RGD

Rat

Hspd1

GO:0045121

membrane raft

PMID:15948182[91]

IDA: Inferred from Direct Assay

C

complete

RGD

Rat

Hspd1

GO:0030061

mitochondrial crista

PMID:7780001[92]

IDA: Inferred from Direct Assay

C

complete

RGD

Rat

Hspd1

GO:0005739

mitochondrion

PMID:16579988[93] PMID:10806118[94]

IDA: Inferred from Direct Assay

C

complete

RGD

Rat

Hspd1

GO:0005791

rough endoplasmic reticulum

PMID:10806118[94]

IDA: Inferred from Direct Assay

C

complete

RGD

Rat

Hspd1

GO:0030141

secretory granule

PMID:10806118[94]

IDA: Inferred from Direct Assay

C

complete

RGD

Rat

Hspd1

GO:0051787

misfolded protein binding

PMID:9811814[95]

IPI: Inferred from Physical Interaction

RGD:1561359

F

complete

RGD

Rat

Hspd1

GO:0002236

detection of misfolded protein

PMID:9811814[95]

IDA: Inferred from Direct Assay

P

complete

SGD

S. cerevisiae

HSP60

GO:0016887

ATPase activity

PMID:9256426[96]

IDA: Inferred from Direct Assay

F

complete

SGD

S. cerevisiae

HSP60

GO:0042026

protein refolding

PMID:9256426[96]

IDA: Inferred from Direct Assay

P

complete

WormBase

C.elegans

hsp-60(WBGene00002025)

GO:0009792

embryonic development ending in birth or egg hatching

PMID:15280428[65]

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

PMID:15280428[65]

IMP: Inferred from Mutant Phenotype

P

Shown via RNAi;

complete

WormBase

C.elegans

hsp-60(WBGene00002025)

GO:0000302

response to reactive oxygen species

PMID:15280428[65]

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

PMID:16816413[97]

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

PMID:15280428[65]

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

PMID:15280428[65]

ISS: Inferred from Sequence or Structural Similarity

F

complete

WormBase

C.elegans

hsp-60(WBGene00002025)

GO:0008134

transcription factor binding

PMID:17925224[98]

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

PMID:9811814[95]

IPI: Inferred from Physical Interaction

RGD:1359615

F

complete

RGD

Rat

Hspd1

GO:0005739

mitochondrion

PMID:9811814[95] PMID:7829528[99]

IDA: Inferred from Direct Assay

RGD:1359615

C

complete

RGD

Rat

Hspd1

GO:0051085

chaperone cofactor-dependent protein folding

PMID:7829528[99]

IDA: Inferred from Direct Assay

P

complete

RGD

Rat

Hspd1

GO:0006916

anti-apoptosis

PMID:12070120[100]

IMP: Inferred from Mutant Phenotype

P

complete

RGD

Rat

Hspd1

GO:0005829

cytosol

PMID:12070120[100]

IDA: Inferred from Direct Assay

C

complete

EcoliWiki

E. coli

groL

GO:0006458

'de novo' protein folding

PMID:1359538[71]

IGI: Inferred from Genetic Interaction

P

Unsure about the evidence code to use.

complete

RGD

Rat

Hspd1

GO:0005829

cytosol

PMID:12070120[100]

IDA: Inferred from Direct Assay

C

complete

EcoliWiki

E. coli

groL

GO:0043234

protein complex

PMID:7770481[101]

IDA: Inferred from Direct Assay

C

complete

RGD

Rat

Hspd1

GO:0042588

zymogen granule

PMID:8675955[102]

IDA: Inferred from Direct Assay

C

complete

RGD

Rat

Hspd1

GO:0005791

rough endoplasmic reticulum

PMID:8675955[102]

IDA: Inferred from Direct Assay

C

complete

RGD

Rat

Hspd1

GO:0005794

Golgi apparatus

PMID:8675955[102]

IDA: Inferred from Direct Assay

C

complete

RGD

Rat

Hspd1

GO:0006458

'de novo' protein folding

PMID:8675955[102]

IC: Inferred by Curator

GO:0042588

P

complete

EcoliWiki

E. coli

groL

GO:0009408

response to heat

PMID:149109[103] PMID:350413[104]

IEP: Inferred from Expression Pattern

P

complete

ZFIN

Zebrafish

hspd1

GO:0042246

tissue regeneration

PMID:16204379[66]

IMP: Inferred from Mutant Phenotype

ZFIN:ZDB-GENO-051101-1

P

complete

TAIR

Arabidopsis

AT3G23990/Hsp60-3b

GO:0010583

response to cyclopentenone

PMID:18334669[105]

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

PMID:1349837[106]

IEP: Inferred from Expression Pattern

P

Northern

complete

TAIR

Arabidopsis

AT3G23990/Hsp60-3b

GO:0005829

cytosol

PMID:17883376[107]

IEP: Inferred from Expression Pattern

C

Western

complete

TAIR

Arabidopsis

AT3G23990/Hsp60-3b

GO:0005759

mitochondrial matrix

PMID:16407270[108]

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

PMID:16407270[108]

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

PMID:7902351[60]

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

PMID:14671022[109]

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

PMID:7902351[60]

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

PMID:16148103[63]

IDA: Inferred from Direct Assay

P

required field missing

GOA

Human

HSPD1 (P10809)

GO:0032733

positive regulation of interleukin-10 production

PMID:16148103[63]

IDA: Inferred from Direct Assay

P

required field missing

GOA

Human

HSPD1 (P10809)

GO:0032755

positive regulation of interleukin-6 production

PMID:16148103[63]

IDA: Inferred from Direct Assay

P

required field missing

GOA

Human

HSPD1 (P10809)

GO:0042100

B cell proliferation

PMID:16148103[63]

IDA: Inferred from Direct Assay

P

required field missing

GOA

Human

HSPD1 (P10809)

GO:0042113

B cell activation

PMID:16148103[63]

IDA: Inferred from Direct Assay

P

required field missing

GOA

Human

HSPD1 (P10809)

GO:0048291

isotype switching to IgG isotypes

PMID:16148103[63]

IDA: Inferred from Direct Assay

P

required field missing

GOA

Human

HSPD1 (P10809)

GO:0050870

positive regulation of T cell activation

PMID:16148103[63]

IDA: Inferred from Direct Assay

P

required field missing

GOA

Human

HSPD1 (P10809)

GO:0050821

protein stabilization

PMID:18086682[110]

IMP: Inferred from Mutant Phenotype

P

required field missing

GOA

Human

HSPD1 (P10809)

GO:0006919

caspase activation

PMID:17823127[111]

IDA: Inferred from Direct Assay

P

required field missing

GOA

Human

HSPD1 (P10809)

GO:0043065

positive regulation of apoptosis

PMID:17823127[111]

IMP: Inferred from Mutant Phenotype

P

required field missing

GOA

Human

HSPD1 (P10809)

GO:0043066

negative regulation of apoptosis

PMID:17823127[111] PMID:18086682[110]

IMP: Inferred from Mutant Phenotype

P

required field missing

GOA

Human

HSPD1 (P10809)

GO:0051087

chaperone binding

PMID:10205158[112]

IPI: Inferred from Physical Interaction

P61604

F

required field missing

GOA

Human

HSPD1 (P10809)

GO:0005515

protein binding

PMID:18086682[110] PMID:17823127[111]

IPI: Inferred from Physical Interaction

O15392, P42574

F

required field missing

GOA

Human

HSPD1 (P10809)

GO:0005615

extracellular space

PMID:18229457[113]

IDA: Inferred from Direct Assay

C

required field missing

GOA

Human

HSPD1 (P10809)

GO:0005739

mitochondrion

PMID:18319262[114] PMID:17823127[111]

IDA: Inferred from Direct Assay

C

required field missing

GOA

Human

HSPD1 (P10809)

GO:0005829

cytosol

PMID:18319262[114] PMID:17823127[111]

IDA: Inferred from Direct Assay

C

required field missing

GOA

Human

HSPD1 (P10809)

required field missing

FlyBase

Drosophila

Hsp60 FBgn0015245

GO:0005811

lipid particle

PMID:16543254[115]

IDA: Inferred from Direct Assay

C

HTP proteomics - is this real?

complete

FlyBase

Drosophila

Hsp60 FBgn0015245

GO:0005811

lipid particle

PMID:16979555[116]

IDA: Inferred from Direct Assay

C

HTP proteomics - is this real?

complete

GOA

Human

HSPD1 (P10809)

GO:0002039

p53 binding

PMID:18086682[110]

IPI: Inferred from Physical Interaction

P04637

F

required field missing

FlyBase

Drosophila

Hsp60 FBgn0015245

NOT

GO:0009408

response to heat

PMID:10341239[117]

IDA: Inferred from Direct Assay

P

complete

GOA

Human

HSPD1 (P10809)

GO:0043498

cell surface binding

PMID:11807771[118]

IDA: Inferred from Direct Assay

F

required field missing

FlyBase

Drosophila

Hsp60 FBgn0015245

GO:0031305

integral to mitochondrial inner membrane

PMID:18549261[119]

IDA: Inferred from Direct Assay

C

complete

GOA

Human

HSPD1 (P10809)

GO:0009986

cell surface

PMID:9243807[120] PMID:11807771[118] PMID:10663613[121]

IDA: Inferred from Direct Assay

C

required field missing

GOA

Human

HSPD1 (P10809)

GO:0042026

protein refolding

PMID:11050098[122]

IDA: Inferred from Direct Assay

P

required field missing

GOA

Human

HSPD1 (P10809)

GO:0051082

unfolded protein binding

PMID:11050098[122]

IC: Inferred by Curator

GO:0042026

F

complete

GOA

Human

HSPD1 (P10809)

GO:0043066

negative regulation of apoptosis

PMID:17823127[111] PMID:18086682[110]

IMP: Inferred from Mutant Phenotype

P

required field missing

GOA

Human

HSPD1 (P10809)

GO:0043066

negative regulation of apoptosis

PMID:17823127[111] PMID:18086682[110]

IMP: Inferred from Mutant Phenotype

P

required field missing

GOA

Human

HSPD1 (P10809)

GO:0005739

mitochondrion

PMID:18319262[114] PMID:17823127[111]

IDA: Inferred from Direct Assay

C

required field missing

GOA

Human

HSPD1 (P10809)

GO:0005829

cytosol

PMID:18319262[114] PMID:17823127[111]

IDA: Inferred from Direct Assay

C

required field missing

GOA

Human

HSPD1 (P10809)

GO:0006986

response to unfolded protein

PMID:11050098[122]

IDA: Inferred from Direct Assay

P

complete

FlyBase

Drosophila

Hsp60 FBgn0015245

GO:0007005

mitochondrion organization

PMID:18549261[119]

IMP: Inferred from Mutant Phenotype

P

complete

SGD

S. cerevisiae

HSP60

GO:0003688

DNA replication origin binding

PMID:10869431[77]

IDA: Inferred from Direct Assay

F

complete

SGD

S. cerevisiae

HSP60

GO:0003697

single-stranded DNA binding

PMID:10869431[77]

IDA: Inferred from Direct Assay

F

complete

edit table

HSPD1 notes

[back to top]


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.

[back to top]


  1. 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. 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. 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. 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. 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. 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. 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. 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. 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
  10. Sulston, J et al. (1975) Dopaminergic neurons in the nematode Caenorhabditis elegans. J. Comp. Neurol. 163 215-26 PubMed GONUTS page
  11. 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
  12. Kumar, A et al. (2002) Subcellular localization of the yeast proteome. Genes Dev. 16 707-19 PubMed GONUTS page
  13. 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. 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. 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. 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. 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. 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. 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
  20. 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. 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
  22. Waggoner, LE et al. (1998) Control of alternative behavioral states by serotonin in Caenorhabditis elegans. Neuron 21 203-14 PubMed GONUTS page
  23. 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
  24. 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
  25. Rebelo, J et al. (2003) Biosynthesis of pteridines. Reaction mechanism of GTP cyclohydrolase I. J. Mol. Biol. 326 503-16 PubMed GONUTS page
  26. Nar, H et al. (1995) Atomic structure of GTP cyclohydrolase I. Structure 3 459-66 PubMed GONUTS page
  27. 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. 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. 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
  30. 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
  31. 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
  32. 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
  33. 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
  34. 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. 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
  36. Karbowski, J et al. (2006) Conservation rules, their breakdown, and optimality in Caenorhabditis sinusoidal locomotion. J. Theor. Biol. 242 652-69 PubMed GONUTS page
  37. Cronin, CJ et al. (2005) An automated system for measuring parameters of nematode sinusoidal movement. BMC Genet. 6 5 PubMed GONUTS page
  38. 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
  39. 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
  40. 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. 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. 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. 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
  44. 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
  45. Tegeder, I et al. (2006) GTP cyclohydrolase and tetrahydrobiopterin regulate pain sensitivity and persistence. Nat. Med. 12 1269-77 PubMed GONUTS page
  46. 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. 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. 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
  49. 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. 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. 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
  52. 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. 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. 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. 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
  56. 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
  57. Nagatsu, I et al. (1999) Specific localization of the guanosine triphosphate (GTP) cyclohydrolase I-immunoreactivity in the human brain. J Neural Transm (Vienna) 106 607-17 PubMed GONUTS page
  58. 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
  59. Yamamoto, K et al. (2003) Genetic engineering of Escherichia coli for production of tetrahydrobiopterin. Metab. Eng. 5 246-54 PubMed GONUTS page
  60. 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. 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
  62. 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. 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
  64. 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. 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. 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. 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
  68. 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
  69. 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
  70. 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. 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
  72. Cheng, MY et al. (1990) The mitochondrial chaperonin hsp60 is required for its own assembly. Nature 348 455-8 PubMed GONUTS page
  73. 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
  74. 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
  75. 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. 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. 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
  78. Asquith, KL et al. (2004) Tyrosine phosphorylation activates surface chaperones facilitating sperm-zona recognition. J. Cell. Sci. 117 3645-57 PubMed GONUTS page
  79. 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. 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
  81. 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
  82. 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
  83. 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
  84. 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
  85. 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
  86. 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. 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
  88. 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. 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. 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
  91. 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
  92. 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
  93. 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. 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. 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. 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
  97. 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
  98. 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. 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. 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
  101. 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. 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
  103. 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
  104. 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
  105. 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
  106. 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
  107. 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. 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
  109. 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. 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. 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
  112. 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
  113. 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. 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
  115. Beller, M et al. (2006) Characterization of the Drosophila lipid droplet subproteome. Mol. Cell Proteomics 5 1082-94 PubMed GONUTS page
  116. 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
  117. Karunanithi, S et al. (1999) Neuroprotection at Drosophila synapses conferred by prior heat shock. J. Neurosci. 19 4360-9 PubMed GONUTS page
  118. 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. 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
  120. 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
  121. 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. 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