HUMAN:GCH1

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	GCH1 (synonyms: DYT5, GCH)
Protein Name(s)	GTP cyclohydrolase 1 GTP cyclohydrolase I GTP-CH-I
External Links
UniProt	P30793
EMBL	S44049 S44053 S43856 Z29433 Z29434 U19523 U66095 U66097 CR536551 CH471061 BC025415 L29478 Z30952 Z16418 U19259 U19256 U19257 U19258
CCDS	CCDS41954.1 CCDS45110.1 CCDS9720.1
PIR	G01630 JC1225
RefSeq	NP_000152.1 NP_001019195.1 NP_001019241.1 NP_001019242.1 XP_005267587.1
UniGene	Hs.86724
PDB	1FB1
PDBsum	1FB1
ProteinModelPortal	P30793
SMR	P30793
BioGrid	108913
IntAct	P30793
MINT	MINT-3011998
STRING	9606.ENSP00000378890
PhosphoSite	P30793
DMDM	399536
MaxQB	P30793
PaxDb	P30793
PRIDE	P30793
DNASU	2643
Ensembl	ENST00000395514 ENST00000491895 ENST00000536224 ENST00000543643 ENST00000622544
GeneID	2643
KEGG	hsa:2643
UCSC	uc001xbh.1 uc001xbj.1 uc001xbk.1
CTD	2643
GeneCards	GC14M055308
GeneReviews	GCH1
HGNC	HGNC:4193
HPA	HPA028612
MIM	128230 233910 600225
neXtProt	NX_P30793
Orphanet	98808 2102
PharmGKB	PA28608
eggNOG	COG0302
GeneTree	ENSGT00390000013481
HOGENOM	HOG000221222
HOVERGEN	HBG003136
InParanoid	P30793
KO	K01495
OMA	VIVVTEC
OrthoDB	EOG77DJ6T
PhylomeDB	P30793
TreeFam	TF105616
BioCyc	MetaCyc:HS05586-MONOMER
Reactome	REACT_111176
SABIO-RK	P30793
UniPathway	UPA00848
ChiTaRS	GCH1
EvolutionaryTrace	P30793
GeneWiki	GTP_cyclohydrolase_I
GenomeRNAi	2643
NextBio	10420
PRO	PR:P30793
Proteomes	UP000005640
Bgee	P30793
CleanEx	HS_GCH1
ExpressionAtlas	P30793
Genevestigator	P30793
GO	GO:0005737 GO:0031410 GO:0005829 GO:0031965 GO:0005634 GO:0043234 GO:0005509 GO:0050662 GO:0005525 GO:0003934 GO:0042803 GO:0008270 GO:0035998 GO:0042416 GO:0006184 GO:0008152 GO:0045776 GO:0050884 GO:0006809 GO:0046209 GO:0051000 GO:0051291 GO:0051260 GO:0042559 GO:0008217 GO:0014916 GO:0050999 GO:0034341 GO:0032496 GO:0048265 GO:0034612 GO:0044281 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	Extension	Notes	Status
enables	GO:0051019	mitogen-activated protein kinase binding	PMID:19294699^[1]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P53779	F	occurs_in:(CL:0000127)	Seeded From UniProt	complete
enables	GO:0051019	mitogen-activated protein kinase binding	PMID:19294699^[1]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P53778	F	occurs_in:(CL:0000127)	Seeded From UniProt	complete
involved_in	GO:2000121	regulation of removal of superoxide radicals	PMID:19666465^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000115)	Seeded From UniProt	complete
involved_in	GO:0051000	positive regulation of nitric-oxide synthase activity	PMID:19666465^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000115)	Seeded From UniProt	complete
involved_in	GO:0006729	tetrahydrobiopterin biosynthetic process	PMID:19666465^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000115)	Seeded From UniProt	complete
involved_in	GO:0051260	protein homooligomerization	PMID:11087827^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051000	positive regulation of nitric-oxide synthase activity	PMID:17717598^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051000	positive regulation of nitric-oxide synthase activity	PMID:12176133^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051000	positive regulation of nitric-oxide synthase activity	PMID:15721862^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0048265	response to pain	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P22288	P		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:11087823^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:16696853^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P30793	F		Seeded From UniProt	complete
involved_in	GO:0042559	pteridine-containing compound biosynthetic process	PMID:3753653^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042559	pteridine-containing compound biosynthetic process	PMID:2463916^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042559	pteridine-containing compound biosynthetic process	PMID:15721862^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042416	dopamine biosynthetic process	PMID:16338639^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034612	response to tumor necrosis factor	PMID:9445252^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034341	response to interferon-gamma	PMID:7678411^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034341	response to interferon-gamma	PMID:12607127^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034341	response to interferon-gamma	PMID:9445252^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032496	response to lipopolysaccharide	PMID:7678411^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032496	response to lipopolysaccharide	PMID:9445252^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
NOT\|involved_in	GO:0032496	response to lipopolysaccharide	PMID:15604419^[15]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0031410	cytoplasmic vesicle	PMID:3318829^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:11087827^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:14717702^[17]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0008217	regulation of blood pressure	PMID:17717598^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006809	nitric oxide biosynthetic process	PMID:9445252^[12]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006729	tetrahydrobiopterin biosynthetic process	PMID:17101830^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006729	tetrahydrobiopterin biosynthetic process	PMID:9445252^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006729	tetrahydrobiopterin biosynthetic process	PMID:7678411^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	PMID:2463916^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:2463916^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:3318829^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:10907721^[19]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:16778797^[20]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	PMID:14717702^[17]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	PMID:3753653^[9]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003934	GTP cyclohydrolase I activity	PMID:16778797^[20]	ECO:0000314	direct assay evidence used in manual assertion		F	occurs_in:(GO:0005634)	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:21873635^[21]	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^[21]	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^[21]	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^[21]	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^[21]	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:0050884	neuromuscular process controlling posture	PMID:7874165^[22]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003934	GTP cyclohydrolase I activity	PMID:7874165^[22]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003934	GTP cyclohydrolase I activity	PMID:7730309^[23]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0031965	nuclear membrane	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0065003	protein-containing complex assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P22288 ensembl:ENSRNOP00000014821	P		Seeded From UniProt	complete
involved_in	GO:0051291	protein heterooligomerization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P22288 ensembl:ENSRNOP00000014821	P		Seeded From UniProt	complete
involved_in	GO:0051260	protein homooligomerization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P22288 ensembl:ENSRNOP00000014821	P		Seeded From UniProt	complete
involved_in	GO:0051066	dihydrobiopterin metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P22288 ensembl:ENSRNOP00000014821	P		Seeded From UniProt	complete
enables	GO:0050662	coenzyme binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P22288 ensembl:ENSRNOP00000014821	F		Seeded From UniProt	complete
involved_in	GO:0048265	response to pain	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P22288 ensembl:ENSRNOP00000014821	P		Seeded From UniProt	complete
involved_in	GO:0045776	negative regulation of blood pressure	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P22288 ensembl:ENSRNOP00000014821	P		Seeded From UniProt	complete
involved_in	GO:0042311	vasodilation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P22288 ensembl:ENSRNOP00000014821	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:P22288 ensembl:ENSRNOP00000014821	C		Seeded From UniProt	complete
enables	GO:0031369	translation initiation factor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P22288 ensembl:ENSRNOP00000014821	F		Seeded From UniProt	complete
enables	GO:0030742	GTP-dependent protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P22288 ensembl:ENSRNOP00000014821	F		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P22288 ensembl:ENSRNOP00000014821	F		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P22288 ensembl:ENSRNOP00000014821	F		Seeded From UniProt	complete
enables	GO:0005509	calcium ion binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P22288 ensembl:ENSRNOP00000014821	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:P22288 ensembl:ENSRNOP00000014821	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
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
enables	GO:0003934	GTP cyclohydrolase I activity	PMID:3753653^[9]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
NOT\|enables	GO:0003934	GTP cyclohydrolase I activity	PMID:8068008^[24]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
NOT\|enables	GO:0003934	GTP cyclohydrolase I activity	PMID:8068008^[24]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
NOT\|enables	GO:0003934	GTP cyclohydrolase I activity	PMID:11284739^[25]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0044306	neuron projection terminus	PMID:23457032^[26]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	part_of:(CL:0000700)	Seeded From UniProt	complete
involved_in	GO:0051186	cofactor metabolic process	Reactome:R-HSA-8978934	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-1474158 Reactome:R-HSA-1474146	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		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: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
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
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
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: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
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
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
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: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.

↑ ^1.0 ^1.1 Chiarini, A et al. (2009) Proteomic analysis of GTP cyclohydrolase 1 multiprotein complexes in cultured normal adult human astrocytes under both basal and cytokine-activated conditions. Proteomics 9 1850-60 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Crabtree, MJ et al. (2009) Critical role for tetrahydrobiopterin recycling by dihydrofolate reductase in regulation of endothelial nitric-oxide synthase coupling: relative importance of the de novo biopterin synthesis versus salvage pathways. J. Biol. Chem. 284 28128-36 PubMed GONUTS page
↑ ^3.0 ^3.1 Auerbach, G et al. (2000) Zinc plays a key role in human and bacterial GTP cyclohydrolase I. Proc. Natl. Acad. Sci. U.S.A. 97 13567-72 PubMed GONUTS page
↑ ^4.0 ^4.1 Zhang, L et al. (2007) Discovery of common human genetic variants of GTP cyclohydrolase 1 (GCH1) governing nitric oxide, autonomic activity, and cardiovascular risk. J. Clin. Invest. 117 2658-71 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
↑ ^6.0 ^6.1 Cai, S et al. (2005) Augmented BH4 by gene transfer restores nitric oxide synthase function in hyperglycemic human endothelial cells. Cardiovasc. Res. 65 823-31 PubMed GONUTS page
↑ 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
↑ 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
↑ ^9.0 ^9.1 ^9.2 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
↑ ^10.0 ^10.1 ^10.2 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
↑ Duan, CL et al. (2005) The assays of activities and function of TH, AADC, and GCH1 and their potential use in ex vivo gene therapy of PD. Brain Res. Brain Res. Protoc. 16 37-43 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 ^12.3 ^12.4 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
↑ ^13.0 ^13.1 ^13.2 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
↑ 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
↑ Huang, A et al. (2005) Cytokine-stimulated GTP cyclohydrolase I expression in endothelial cells requires coordinated activation of nuclear factor-kappaB and Stat1/Stat3. Circ. Res. 96 164-71 PubMed GONUTS page
↑ ^16.0 ^16.1 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
↑ ^17.0 ^17.1 Suzuki, T et al. (2004) GTP cyclohydrolase I utilizes metal-free GTP as its substrate. Eur. J. Biochem. 271 349-55 PubMed GONUTS page
↑ Ohta, E et al. (2006) Novel mutations in the guanosine triphosphate cyclohydrolase 1 gene associated with DYT5 dystonia. Arch. Neurol. 63 1605-10 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 (Vienna) 106 607-17 PubMed GONUTS page
↑ ^20.0 ^20.1 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
↑ ^21.0 ^21.1 ^21.2 ^21.3 ^21.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^22.0 ^22.1 Ichinose, H et al. (1994) Hereditary progressive dystonia with marked diurnal fluctuation caused by mutations in the GTP cyclohydrolase I gene. Nat. Genet. 8 236-42 PubMed GONUTS page
↑ Ichinose, H et al. (1995) Characterization of mouse and human GTP cyclohydrolase I genes. Mutations in patients with GTP cyclohydrolase I deficiency. J. Biol. Chem. 270 10062-71 PubMed GONUTS page
↑ ^24.0 ^24.1 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
↑ 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
↑ Kapatos, G (2013) The neurobiology of tetrahydrobiopterin biosynthesis: a model for regulation of GTP cyclohydrolase I gene transcription within nigrostriatal dopamine neurons. IUBMB Life 65 323-33 PubMed GONUTS page

[PMID:19294699-1] 1.0 ^1.1 Chiarini, A et al. (2009) Proteomic analysis of GTP cyclohydrolase 1 multiprotein complexes in cultured normal adult human astrocytes under both basal and cytokine-activated conditions. Proteomics 9 1850-60 PubMed GONUTS page

[PMID:19666465-2] 2.0 ^2.1 ^2.2 Crabtree, MJ et al. (2009) Critical role for tetrahydrobiopterin recycling by dihydrofolate reductase in regulation of endothelial nitric-oxide synthase coupling: relative importance of the de novo biopterin synthesis versus salvage pathways. J. Biol. Chem. 284 28128-36 PubMed GONUTS page

[PMID:11087827-3] 3.0 ^3.1 Auerbach, G et al. (2000) Zinc plays a key role in human and bacterial GTP cyclohydrolase I. Proc. Natl. Acad. Sci. U.S.A. 97 13567-72 PubMed GONUTS page

[PMID:17717598-4] 4.0 ^4.1 Zhang, L et al. (2007) Discovery of common human genetic variants of GTP cyclohydrolase 1 (GCH1) governing nitric oxide, autonomic activity, and cardiovascular risk. J. Clin. Invest. 117 2658-71 PubMed GONUTS page

[PMID:12176133-5] 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

[PMID:15721862-6] 6.0 ^6.1 Cai, S et al. (2005) Augmented BH4 by gene transfer restores nitric oxide synthase function in hyperglycemic human endothelial cells. Cardiovasc. Res. 65 823-31 PubMed GONUTS page

[PMID:11087823-7] 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

[PMID:16696853-8] 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

[PMID:3753653-9] 9.0 ^9.1 ^9.2 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

[PMID:2463916-10] 10.0 ^10.1 ^10.2 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

[PMID:16338639-11] Duan, CL et al. (2005) The assays of activities and function of TH, AADC, and GCH1 and their potential use in ex vivo gene therapy of PD. Brain Res. Brain Res. Protoc. 16 37-43 PubMed GONUTS page

[PMID:9445252-12] 12.0 ^12.1 ^12.2 ^12.3 ^12.4 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

[PMID:7678411-13] 13.0 ^13.1 ^13.2 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

[PMID:12607127-14] 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

[PMID:15604419-15] Huang, A et al. (2005) Cytokine-stimulated GTP cyclohydrolase I expression in endothelial cells requires coordinated activation of nuclear factor-kappaB and Stat1/Stat3. Circ. Res. 96 164-71 PubMed GONUTS page

[PMID:3318829-16] 16.0 ^16.1 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

[PMID:14717702-17] 17.0 ^17.1 Suzuki, T et al. (2004) GTP cyclohydrolase I utilizes metal-free GTP as its substrate. Eur. J. Biochem. 271 349-55 PubMed GONUTS page

[PMID:17101830-18] Ohta, E et al. (2006) Novel mutations in the guanosine triphosphate cyclohydrolase 1 gene associated with DYT5 dystonia. Arch. Neurol. 63 1605-10 PubMed GONUTS page

[PMID:10907721-19] 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

[PMID:16778797-20] 20.0 ^20.1 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

[PMID:21873635-21] 21.0 ^21.1 ^21.2 ^21.3 ^21.4 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:7874165-22] 22.0 ^22.1 Ichinose, H et al. (1994) Hereditary progressive dystonia with marked diurnal fluctuation caused by mutations in the GTP cyclohydrolase I gene. Nat. Genet. 8 236-42 PubMed GONUTS page

[PMID:7730309-23] Ichinose, H et al. (1995) Characterization of mouse and human GTP cyclohydrolase I genes. Mutations in patients with GTP cyclohydrolase I deficiency. J. Biol. Chem. 270 10062-71 PubMed GONUTS page

[PMID:8068008-24] 24.0 ^24.1 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

[PMID:11284739-25] 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

[PMID:23457032-26] Kapatos, G (2013) The neurobiology of tetrahydrobiopterin biosynthesis: a model for regulation of GTP cyclohydrolase I gene transcription within nigrostriatal dopamine neurons. IUBMB Life 65 323-33 PubMed GONUTS page

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