GGH_HUMAN - dbPTM
GGH_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GGH_HUMAN
UniProt AC Q92820
Protein Name Gamma-glutamyl hydrolase
Gene Name GGH
Organism Homo sapiens (Human).
Sequence Length 318
Subcellular Localization Secreted, extracellular space . Lysosome . Melanosome . While its intracellular location is primarily the lysosome, most of the enzyme activity is secreted. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Protein Description Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates. Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha-glutamate (folic acid) and free glutamate. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates..
Protein Sequence MASPGCLLCVLGLLLCGAASLELSRPHGDTAKKPIIGILMQKCRNKVMKNYGRYYIAASYVKYLESAGARVVPVRLDLTEKDYEILFKSINGILFPGGSVDLRRSDYAKVAKIFYNLSIQSFDDGDYFPVWGTCLGFEELSLLISGECLLTATDTVDVAMPLNFTGGQLHSRMFQNFPTELLLSLAVEPLTANFHKWSLSVKNFTMNEKLKKFFNVLTTNTDGKIEFISTMEGYKYPVYGVQWHPEKAPYEWKNLDGISHAPNAVKTAFYLAEFFVNEARKNNHHFKSESEEEKALIYQFSPIYTGNISSFQQCYIFD
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
81UbiquitinationVRLDLTEKDYEILFK
EEEECCHHHHHHHHE		61.4521906983
109UbiquitinationLRRSDYAKVAKIFYN
CCCCHHHHHHHHHHC		36.1729967540
116N-linked_GlycosylationKVAKIFYNLSIQSFD
HHHHHHHCCCCCCCC		19.30UniProtKB CARBOHYD
163N-linked_GlycosylationVDVAMPLNFTGGQLH
CCEEEECCCCCCCHH		26.9411953431
198PhosphorylationTANFHKWSLSVKNFT
CCCHHHCEEEECCCC		18.6424719451
203N-linked_GlycosylationKWSLSVKNFTMNEKL
HCEEEECCCCCCHHH		35.1511953431
209UbiquitinationKNFTMNEKLKKFFNV
CCCCCCHHHHHHHCC		61.6823000965
211UbiquitinationFTMNEKLKKFFNVLT
CCCCHHHHHHHCCCC		59.6123000965
212UbiquitinationTMNEKLKKFFNVLTT
CCCHHHHHHHCCCCC		66.6723000965
235UbiquitinationISTMEGYKYPVYGVQ
EEECCCCCCCEEEEE		54.6721906983
247AcetylationGVQWHPEKAPYEWKN
EEEECCCCCCCCCCC		60.1426822725
253UbiquitinationEKAPYEWKNLDGISH
CCCCCCCCCCCCCCC		35.3721906983
287UbiquitinationRKNNHHFKSESEEEK
HHCCCCCCCCCHHHH		49.2921906983
307N-linked_GlycosylationFSPIYTGNISSFQQC
CCCCCCCCCCCCCEE		24.1416399764
307N-linked_GlycosylationFSPIYTGNISSFQQC
CCCCCCCCCCCCCEE		24.1416399764
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

Oops, there are no upstream regulatory protein records of GGH_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GGH_HUMAN !!
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 GGH_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GGH_HUMANGGHphysical
11953431
ZMYM3_HUMANZMYM3physical
26186194
TXD16_HUMANTXNDC16physical
26186194
LRWD1_HUMANLRWD1physical
26186194
MKLN1_HUMANMKLN1physical
26186194
OS9_HUMANOS9physical
26186194
UGDH_HUMANUGDHphysical
26186194
AT2B2_HUMANATP2B2physical
26186194
DCAF8_HUMANDCAF8physical
26186194
GT253_HUMANCERCAMphysical
26186194
GPR98_HUMANGPR98physical
26186194
TGON2_HUMANTGOLN2physical
26186194
MICA_HUMANMICAphysical
26186194
UGDH_HUMANUGDHphysical
28514442
TGON2_HUMANTGOLN2physical
28514442
ITAV_HUMANITGAVphysical
28514442
MKLN1_HUMANMKLN1physical
28514442
MICA_HUMANMICAphysical
28514442
TXD16_HUMANTXNDC16physical
28514442
OS9_HUMANOS9physical
28514442
GT253_HUMANCERCAMphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00158Folic Acid
DB00563Methotrexate
Regulatory Network of GGH_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Three-dimensional structure of human gamma -glutamyl hydrolase. Aclass I glatamine amidotransferase adapted for a complex substate.";
Li H., Ryan T.J., Chave K.J., Van Roey P.;
J. Biol. Chem. 277:24522-24529(2002).
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 25-318, MASS SPECTROMETRY,GLYCOSYLATION AT ASN-163; ASN-203 AND ASN-307, AND SUBUNIT.

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