GCH1_HUMAN - dbPTM
GCH1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GCH1_HUMAN
UniProt AC P30793
Protein Name GTP cyclohydrolase 1
Gene Name GCH1
Organism Homo sapiens (Human).
Sequence Length 250
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Positively regulates nitric oxide synthesis in umbilical vein endothelial cells (HUVECs). May be involved in dopamine synthesis. May modify pain sensitivity and persistence. Isoform GCH-1 is the functional enzyme, the potential function of the enzymatically inactive isoforms remains unknown..
Protein Sequence MEKGPVRAPAEKPRGARCSNGFPERDPPRPGPSRPAEKPPRPEAKSAQPADGWKGERPRSEEDNELNLPNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLIRS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
38UbiquitinationGPSRPAEKPPRPEAK
CCCCCCCCCCCCCCC
63.53-
54UbiquitinationAQPADGWKGERPRSE
CCCCCCCCCCCCCCH
57.32-
60PhosphorylationWKGERPRSEEDNELN
CCCCCCCCHHCCCCC
48.2828258704
60 (in isoform 2)Phosphorylation-48.2824719451
81PhosphorylationAYSSILSSLGENPQR
HHHHHHHHCCCCHHH
36.6311284739
93UbiquitinationPQRQGLLKTPWRAAS
HHHCCCCCCHHHHHH
58.55-
94PhosphorylationQRQGLLKTPWRAASA
HHCCCCCCHHHHHHH
28.2222210691
106PhosphorylationASAMQFFTKGYQETI
HHHHHHHHHHHHHHH
25.5022985185
160UbiquitinationHIGYLPNKQVLGLSK
EEEECCCCHHHCHHH
39.58-
175PhosphorylationLARIVEIYSRRLQVQ
HHHHHHHHHHHHHHH
5.21-
176PhosphorylationARIVEIYSRRLQVQE
HHHHHHHHHHHHHHH
19.3124719451
194 (in isoform 2)Phosphorylation-12.8824719451
210 (in isoform 2)Phosphorylation-17.9424719451
214 (in isoform 4)Phosphorylation-1.69-
223 (in isoform 4)Phosphorylation-26.63-
224 (in isoform 4)Phosphorylation-41.85-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
81SPhosphorylationKinaseCK2A1P68400
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
81SPhosphorylation

17704208

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of GCH1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GCH1_HUMANGCH1physical
16696853
GFRP_HUMANGCHFRphysical
16696853
AHSA1_HUMANAHSA1physical
16696853
RLF_HUMANRLFphysical
16696853
HSP7C_HUMANHSPA8physical
16696853
SP3_HUMANSP3physical
16696853
CNRP1_HUMANCNRIP1physical
16696853
RAB26_HUMANRAB26physical
16696853
AT1B1_HUMANATP1B1physical
16696853
PACN3_HUMANPACSIN3physical
19294699
CALL5_HUMANCALML5physical
19294699
CALL6_HUMANCALML6physical
19294699
RGS19_HUMANRGS19physical
19294699
PPM1B_HUMANPPM1Bphysical
19294699
MP2K4_HUMANMAP2K4physical
19294699
MP2K5_HUMANMAP2K5physical
19294699
MK12_HUMANMAPK12physical
19294699
MK10_HUMANMAPK10physical
19294699
KKCC1_HUMANCAMKK1physical
19294699
KC1G1_HUMANCSNK1G1physical
19294699
CSK21_HUMANCSNK2A1physical
19294699
CSK2B_HUMANCSNK2Bphysical
19294699
KAP2_HUMANPRKAR2Aphysical
19294699
KAP3_HUMANPRKAR2Bphysical
19294699
GCH1_HUMANGCH1physical
2463916
1433Z_HUMANYWHAZphysical
21988832
GIT2_HUMANGIT2physical
21988832
GCH1_HUMANGCH1physical
11087827

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
233910Hyperphenylalaninemia, BH4-deficient, B (HPABH4B)
128230Dystonia, dopa-responsive (DRD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GCH1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND MASSSPECTROMETRY.
"Regulation of tetrahydrobiopterin biosynthesis by shear stress.";
Widder J.D., Chen W., Li L., Dikalov S., Thony B., Hatakeyama K.,Harrison D.G.;
Circ. Res. 101:830-838(2007).
Cited for: PHOSPHORYLATION AT SER-81.

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