RAT:GCH1

Species (Taxon ID)	Rattus norvegicus (Rat). (10116)
Gene Name(s)	Gch1 (synonyms: Gch)
Protein Name(s)	GTP cyclohydrolase 1 GTP cyclohydrolase I GTP-CH-I
External Links
UniProt	P22288
EMBL	M58364
PIR	A39080
RefSeq	NP_077332.1
UniGene	Rn.28195
PDB	1IS7 1IS8 1WPL
PDBsum	1IS7 1IS8 1WPL
ProteinModelPortal	P22288
SMR	P22288
BioGrid	247920
IntAct	P22288
STRING	10116.ENSRNOP00000014821
PhosphoSite	P22288
PRIDE	P22288
Ensembl	ENSRNOT00000014821
GeneID	29244
KEGG	rno:29244
UCSC	RGD:61992
CTD	2643
RGD	61992
eggNOG	COG0302
GeneTree	ENSGT00390000013481
HOGENOM	HOG000221222
HOVERGEN	HBG003136
InParanoid	P22288
KO	K01495
OMA	YIPAKDG
OrthoDB	EOG77DJ6T
PhylomeDB	P22288
BRENDA	3.5.4.16
Reactome	REACT_310165
UniPathway	UPA00848
EvolutionaryTrace	P22288
NextBio	608526
PRO	PR:P22288
Proteomes	UP000002494
ExpressionAtlas	P22288
Genevisible	P22288
GO	GO:0005737 GO:0031410 GO:0005829 GO:0031965 GO:0005654 GO:0043234 GO:0005509 GO:0050662 GO:0005525 GO:0003934 GO:0030742 GO:0008270 GO:0035998 GO:0051066 GO:0042416 GO:0045776 GO:0050884 GO:0051000 GO:0006461 GO:0051291 GO:0051260 GO:0014916 GO:0034341 GO:0032496 GO:0048265 GO:0034612 GO:0006729 GO:0046654 GO:0042311
HAMAP	MF_00223
InterPro	IPR001474 IPR018234 IPR020602
PANTHER	PTHR11109
Pfam	PF01227
TIGRFAMs	TIGR00063
PROSITE	PS00859 PS00860

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
involved_in	GO:0048265	response to pain	PMID:17057711^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0065003	protein-containing complex assembly	PMID:9685352^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0065003	protein-containing complex assembly	PMID:15448133^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0065003	protein-containing complex assembly	PMID:11818540^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0051291	protein heterooligomerization	PMID:9685352^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0051291	protein heterooligomerization	PMID:15448133^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0051291	protein heterooligomerization	PMID:11818540^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0051260	protein homooligomerization	PMID:9636709^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0051260	protein homooligomerization	PMID:2557335^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0051066	dihydrobiopterin metabolic process	PMID:8702680^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0051066	dihydrobiopterin metabolic process	PMID:8486153^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0051066	dihydrobiopterin metabolic process	PMID:2557335^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0050662	coenzyme binding	PMID:15448133^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0045776	negative regulation of blood pressure	PMID:12855421^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0042311	vasodilation	PMID:12855421^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:8702680^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:15448133^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:11818540^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0031369	translation initiation factor binding	PMID:22479495^[10]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:1584560	F	Seeded From UniProt	complete
enables	GO:0030742	GTP-dependent protein binding	PMID:9685352^[2]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:621746	F	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:15448133^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:11818540^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0005525	GTP binding	PMID:8702680^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0005525	GTP binding	PMID:8486153^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0005525	GTP binding	PMID:2557335^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0005509	calcium ion binding	PMID:9636709^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003934	GTP cyclohydrolase I activity	PMID:9636709^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003934	GTP cyclohydrolase I activity	PMID:8702680^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003934	GTP cyclohydrolase I activity	PMID:8486153^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003934	GTP cyclohydrolase I activity	PMID:2557335^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003934	GTP cyclohydrolase I activity	PMID:15292175^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003934	GTP cyclohydrolase I activity	PMID:12051753^[12]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG11375 PANTHER:PTN000121833 RGD:61992 UniProtKB:P30793	F	Seeded From UniProt	complete
involved_in	GO:0006729	tetrahydrobiopterin biosynthetic process	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0003162 PANTHER:PTN000121833 UniProtKB:P30793 UniProtKB:P50141 WB:WBGene00000298 dictyBase:DDB_G0288481	P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG11375 FB:FBgn0003162 PANTHER:PTN000121833 UniProtKB:P30793 UniProtKB:P50141 dictyBase:DDB_G0288481	C	Seeded From UniProt	complete
enables	GO:0005525	GTP binding	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG11375 PANTHER:PTN000121833 RGD:61992 UniProtKB:P30793	F	Seeded From UniProt	complete
enables	GO:0003934	GTP cyclohydrolase I activity	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG11375 FB:FBgn0003162 MGI:MGI:95675 PANTHER:PTN000121833 RGD:61992 SGD:S000003499 UniProtKB:P30793 UniProtKB:Q8I5H7 UniProtKB:Q8VYU3 UniProtKB:Q9SFV7 WB:WBGene00000298 dictyBase:DDB_G0288481	F	Seeded From UniProt	complete
involved_in	GO:2000121	regulation of removal of superoxide radicals	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P30793 ensembl:ENSP00000419045	P	Seeded From UniProt	complete
involved_in	GO:0051260	protein homooligomerization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P30793 ensembl:ENSP00000419045	P	Seeded From UniProt	complete
enables	GO:0051019	mitogen-activated protein kinase binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P30793 ensembl:ENSP00000419045	F	Seeded From UniProt	complete
involved_in	GO:0051000	positive regulation of nitric-oxide synthase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P30793 ensembl:ENSP00000419045	P	Seeded From UniProt	complete
involved_in	GO:0050884	neuromuscular process controlling posture	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P30793 ensembl:ENSP00000419045	P	Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P30793 ensembl:ENSP00000419045	F	Seeded From UniProt	complete
involved_in	GO:0042559	pteridine-containing compound biosynthetic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P30793 ensembl:ENSP00000419045	P	Seeded From UniProt	complete
involved_in	GO:0042416	dopamine biosynthetic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P30793 ensembl:ENSP00000419045	P	Seeded From UniProt	complete
involved_in	GO:0034612	response to tumor necrosis factor	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P30793 ensembl:ENSP00000419045	P	Seeded From UniProt	complete
involved_in	GO:0034341	response to interferon-gamma	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P30793 ensembl:ENSP00000419045	P	Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P30793 ensembl:ENSP00000419045	C	Seeded From UniProt	complete
involved_in	GO:0032496	response to lipopolysaccharide	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P30793 ensembl:ENSP00000419045	P	Seeded From UniProt	complete
part_of	GO:0031965	nuclear membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P30793 ensembl:ENSP00000419045	C	Seeded From UniProt	complete
part_of	GO:0031410	cytoplasmic vesicle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P30793 ensembl:ENSP00000419045	C	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P30793 ensembl:ENSP00000419045	F	Seeded From UniProt	complete
involved_in	GO:0008217	regulation of blood pressure	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P30793 ensembl:ENSP00000419045	P	Seeded From UniProt	complete
involved_in	GO:0006729	tetrahydrobiopterin biosynthetic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P30793 ensembl:ENSP00000419045	P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P30793 ensembl:ENSP00000419045	C	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P30793 ensembl:ENSP00000419045	C	Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P30793 ensembl:ENSP00000419045	C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P30793 ensembl:ENSP00000419045	C	Seeded From UniProt	complete
enables	GO:0005525	GTP binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P30793 ensembl:ENSP00000419045	F	Seeded From UniProt	complete
enables	GO:0003934	GTP cyclohydrolase I activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P30793 ensembl:ENSP00000419045	F	Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P30793 ensembl:ENSP00000419045	F	Seeded From UniProt	complete
involved_in	GO:0014916	regulation of lung blood pressure	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q05915 ensembl:ENSMUSP00000087405	P	Seeded From UniProt	complete
involved_in	GO:0010460	positive regulation of heart rate	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q05915 ensembl:ENSMUSP00000087405	P	Seeded From UniProt	complete
involved_in	GO:0008217	regulation of blood pressure	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q05915 ensembl:ENSMUSP00000087405	P	Seeded From UniProt	complete
enables	GO:0003934	GTP cyclohydrolase I activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q05915 ensembl:ENSMUSP00000087405	F	Seeded From UniProt	complete
part_of	GO:0031965	nuclear membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A024R642 ensembl:ENSP00000419045	C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A024R642 ensembl:ENSP00000419045	C	Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A024R642 ensembl:ENSP00000419045	C	Seeded From UniProt	complete
enables	GO:0003934	GTP cyclohydrolase I activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001474 InterPro:IPR018234	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001474 InterPro:IPR018234	C	Seeded From UniProt	complete
involved_in	GO:0046654	tetrahydrofolate biosynthetic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001474 InterPro:IPR018234	P	Seeded From UniProt	complete
enables	GO:0003934	GTP cyclohydrolase I activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.5.4.16	F	Seeded From UniProt	complete
involved_in	GO:0006729	tetrahydrobiopterin biosynthetic process	PMID:12051753^[12]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C	Seeded From UniProt	complete
involved_in	GO:0006729	tetrahydrobiopterin biosynthetic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0783	P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
enables	GO:0005525	GTP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0342	F	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
involved_in	GO:0008152	metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0021	P	Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0021	F	Seeded From UniProt	complete
involved_in	GO:0035998	7,8-dihydroneopterin 3'-triphosphate biosynthetic process	GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniPathway:UPA00848	P	Seeded From UniProt	complete
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Notes

References

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

↑ Tegeder, I et al. (2006) GTP cyclohydrolase and tetrahydrobiopterin regulate pain sensitivity and persistence. Nat. Med. 12 1269-77 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 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
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 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
↑ ^4.0 ^4.1 ^4.2 ^4.3 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
↑ ^5.0 ^5.1 ^5.2 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
↑ ^6.0 ^6.1 ^6.2 ^6.3 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 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
↑ ^8.0 ^8.1 ^8.2 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
↑ ^9.0 ^9.1 Mitchell, BM et al. (2003) GTP cyclohydrolase 1 inhibition attenuates vasodilation and increases blood pressure in rats. Am. J. Physiol. Heart Circ. Physiol. 285 H2165-70 PubMed GONUTS page
↑ Du, J et al. (2012) The protein partners of GTP cyclohydrolase I in rat organs. PLoS ONE 7 e33991 PubMed GONUTS page
↑ Kolinsky, MA & Gross, SS (2004) The mechanism of potent GTP cyclohydrolase I inhibition by 2,4-diamino-6-hydroxypyrimidine: requirement of the GTP cyclohydrolase I feedback regulatory protein. J. Biol. Chem. 279 40677-82 PubMed GONUTS page
↑ ^12.0 ^12.1 Suzuki, T et al. (2002) Enhanced expression of GTP cyclohydrolase I in V-1-overexpressing PC12D cells. Biochem. Biophys. Res. Commun. 293 962-8 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 ^13.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:17057711-1] Tegeder, I et al. (2006) GTP cyclohydrolase and tetrahydrobiopterin regulate pain sensitivity and persistence. Nat. Med. 12 1269-77 PubMed GONUTS page

[PMID:9685352-2] 2.0 ^2.1 ^2.2 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

[PMID:15448133-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 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

[PMID:11818540-4] 4.0 ^4.1 ^4.2 ^4.3 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

[PMID:9636709-5] 5.0 ^5.1 ^5.2 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

[PMID:2557335-6] 6.0 ^6.1 ^6.2 ^6.3 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

[PMID:8702680-7] 7.0 ^7.1 ^7.2 ^7.3 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

[PMID:8486153-8] 8.0 ^8.1 ^8.2 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

[PMID:12855421-9] 9.0 ^9.1 Mitchell, BM et al. (2003) GTP cyclohydrolase 1 inhibition attenuates vasodilation and increases blood pressure in rats. Am. J. Physiol. Heart Circ. Physiol. 285 H2165-70 PubMed GONUTS page

[PMID:22479495-10] Du, J et al. (2012) The protein partners of GTP cyclohydrolase I in rat organs. PLoS ONE 7 e33991 PubMed GONUTS page

[PMID:15292175-11] Kolinsky, MA & Gross, SS (2004) The mechanism of potent GTP cyclohydrolase I inhibition by 2,4-diamino-6-hydroxypyrimidine: requirement of the GTP cyclohydrolase I feedback regulatory protein. J. Biol. Chem. 279 40677-82 PubMed GONUTS page

[PMID:12051753-12] 12.0 ^12.1 Suzuki, T et al. (2002) Enhanced expression of GTP cyclohydrolase I in V-1-overexpressing PC12D cells. Biochem. Biophys. Res. Commun. 293 962-8 PubMed GONUTS page

[PMID:21873635-13] 13.0 ^13.1 ^13.2 ^13.3 ^13.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

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RAT:GCH1

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