FOLH1_HUMAN - dbPTM
FOLH1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FOLH1_HUMAN
UniProt AC Q04609
Protein Name Glutamate carboxypeptidase 2
Gene Name FOLH1
Organism Homo sapiens (Human).
Sequence Length 750
Subcellular Localization Cell membrane
Single-pass type II membrane protein .
Isoform PSMA': Cytoplasm .
Protein Description Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. Involved in prostate tumor progression.; Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC..
Protein Sequence MWNLLHETDSAVATARRPRWLCAGALVLAGGFFLLGFLFGWFIKSSNEATNITPKHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTHPNYISIINEDGNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIARYGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA
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
8PhosphorylationMWNLLHETDSAVATA
CCCHHCCCCCHHHHC		25.2224043423
10PhosphorylationNLLHETDSAVATARR
CHHCCCCCHHHHCCC		31.8724043423
14PhosphorylationETDSAVATARRPRWL
CCCCHHHHCCCCHHH		17.6924043423
51N-linked_GlycosylationKSSNEATNITPKHNM
CCCCCCCCCCCCCCH		43.0912949938
51N-linked_GlycosylationKSSNEATNITPKHNM
CCCCCCCCCCCCCCH		43.0912949938
53PhosphorylationSNEATNITPKHNMKA
CCCCCCCCCCCCHHH		28.4928787133
71 (in isoform 3)Phosphorylation-49.4024043423
73 (in isoform 3)Phosphorylation-8.1124043423
74 (in isoform 3)Phosphorylation-4.7324043423
76N-linked_GlycosylationNIKKFLYNFTQIPHL
HHHHHHHHHHCCCCC		35.32UniProtKB CARBOHYD
76N-linked_GlycosylationNIKKFLYNFTQIPHL
HHHHHHHHHHCCCCC		35.3212949938
80 (in isoform 3)Phosphorylation-1.7924043423
81 (in isoform 3)Phosphorylation-13.4624043423
82 (in isoform 3)Phosphorylation-29.9124043423
86 (in isoform 3)Phosphorylation-28.8824043423
88 (in isoform 3)Phosphorylation-56.7424043423
121N-linked_GlycosylationDVLLSYPNKTHPNYI
HHHHCCCCCCCCCEE		54.33UniProtKB CARBOHYD
121N-linked_GlycosylationDVLLSYPNKTHPNYI
HHHHCCCCCCCCCEE		54.3312949938
140N-linked_GlycosylationEDGNEIFNTSLFEPP
CCCCCCCCCCCCCCC		34.13UniProtKB CARBOHYD
140N-linked_GlycosylationEDGNEIFNTSLFEPP
CCCCCCCCCCCCCCC		34.1312949938
153N-linked_GlycosylationPPPPGYENVSDIVPP
CCCCCCCCHHHCCCC		30.0612949938
153N-linked_GlycosylationPPPPGYENVSDIVPP
CCCCCCCCHHHCCCC		30.0612949938
195N-linked_GlycosylationLERDMKINCSGKIVI
CCCCCCCCCCCCEEE		14.3712949938
195N-linked_GlycosylationLERDMKINCSGKIVI
CCCCCCCCCCCCEEE		14.37UniProtKB CARBOHYD
312PhosphorylationLLEKMGGSAPPDSSW
HHHHCCCCCCCCCCC		31.69-
336N-linked_GlycosylationVGPGFTGNFSTQKVK
CCCCCCCCCCCCEEE		25.3312754519
336N-linked_GlycosylationVGPGFTGNFSTQKVK
CCCCCCCCCCCCEEE		25.3312949938
401PhosphorylationVVHEIVRSFGTLKKE
HHHHHHHHHCCHHCC		19.6828152594
404PhosphorylationEIVRSFGTLKKEGWR
HHHHHHCCHHCCCCC		33.1328152594
449PhosphorylationLQERGVAYINADSSI
HHHHCCEEECCCCCC		7.7227542207
454PhosphorylationVAYINADSSIEGNYT
CEEECCCCCCCCCEE		30.7027542207
455PhosphorylationAYINADSSIEGNYTL
EEECCCCCCCCCEEE		25.8027542207
459N-linked_GlycosylationADSSIEGNYTLRVDC
CCCCCCCCEEEEEEC		17.5212949938
459N-linked_GlycosylationADSSIEGNYTLRVDC
CCCCCCCCEEEEEEC		17.52UniProtKB CARBOHYD
460PhosphorylationDSSIEGNYTLRVDCT
CCCCCCCEEEEEECH		20.2927542207
461PhosphorylationSSIEGNYTLRVDCTP
CCCCCCEEEEEECHH		16.4624719451
467PhosphorylationYTLRVDCTPLMYSLV
EEEEEECHHHHHHHH		18.26-
476N-linked_GlycosylationLMYSLVHNLTKELKS
HHHHHHHHHHHHCCC		41.76UniProtKB CARBOHYD
476N-linked_GlycosylationLMYSLVHNLTKELKS
HHHHHHHHHHHHCCC		41.7612949938
532PhosphorylationFQRLGIASGRARYTK
HHHHCCCCCCEEECC		27.22-
537PhosphorylationIASGRARYTKNWETN
CCCCCEEECCCCCCC		22.5330576142
538PhosphorylationASGRARYTKNWETNK
CCCCEEECCCCCCCC		16.6130576142
549PhosphorylationETNKFSGYPLYHSVY
CCCCCCCCCCCCCHH		6.72-
607PhosphorylationYAVVLRKYADKIYSI
HHHHHHHHHHHEEEE		17.3824719451
615PhosphorylationADKIYSISMKHPQEM
HHHEEEEECCCCCCC		18.8124719451
624PhosphorylationKHPQEMKTYSVSFDS
CCCCCCCEEEECHHH		21.5122468782
638N-linked_GlycosylationSLFSAVKNFTEIASK
HHHHHHHHHHHHHHH		42.34UniProtKB CARBOHYD
638N-linked_GlycosylationSLFSAVKNFTEIASK
HHHHHHHHHHHHHHH		42.3412949938
640PhosphorylationFSAVKNFTEIASKFS
HHHHHHHHHHHHHHH		35.5622468782
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 FOLH1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FOLH1_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 FOLH1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RS3_HUMANRPS3physical
21988832
MTAP_HUMANMTAPphysical
21988832
CGL_HUMANCTHphysical
26344197
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
D03372 Capromab pendetide (USAN); Prostascint (TN)
D04525 Indium In 111 capromab pendetide (USP)
D10070 Iofolastat I123 (USAN); Trofex (TN)
DrugBank
DB00089Capromab
Regulatory Network of FOLH1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Reaction mechanism of glutamate carboxypeptidase II revealed bymutagenesis, X-ray crystallography, and computational methods.";
Klusak V., Barinka C., Plechanovova A., Mlcochova P., Konvalinka J.,Rulisek L., Lubkowski J.;
Biochemistry 48:4126-4138(2009).
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 44-750 IN COMPLEX WITHSUBSTRATE; CALCIUM AND ZINC IONS, GLYCOSYLATION AT ASN-76; ASN-121;ASN-140; ASN-195; ASN-459; ASN-476 AND ASN-638, AND MUTAGENESIS OFGLU-424.
"Structural basis of interactions between human glutamatecarboxypeptidase II and its substrate analogs.";
Barinka C., Hlouchova K., Rovenska M., Majer P., Dauter M., Hin N.,Ko Y.-S., Tsukamoto T., Slusher B.S., Konvalinka J., Lubkowski J.;
J. Mol. Biol. 376:1438-1450(2008).
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 44-750 IN COMPLEXES WITHSUBSTRATE ANALOGS; CALCIUM AND ZINC IONS, AND GLYCOSYLATION AT ASN-76;ASN-121; ASN-140; ASN-195; ASN-459; ASN-476 AND ASN-638.
"Interactions between human glutamate carboxypeptidase II and urea-based inhibitors: structural characterization.";
Barinka C., Byun Y., Dusich C.L., Banerjee S.R., Chen Y.,Castanares M., Kozikowski A.P., Mease R.C., Pomper M.G., Lubkowski J.;
J. Med. Chem. 51:7737-7743(2008).
Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 44-750 IN COMPLEXES WITHUREA-BASED INHIBITORS; CALCIUM AND ZINC IONS, AND GLYCOSYLATION ATASN-76; ASN-121; ASN-140; ASN-195; ASN-459; ASN-476 AND ASN-638.
"Structural insight into the pharmacophore pocket of human glutamatecarboxypeptidase II.";
Barinka C., Rovenska M., Mlcochova P., Hlouchova K., Plechanovova A.,Majer P., Tsukamoto T., Slusher B.S., Konvalinka J., Lubkowski J.;
J. Med. Chem. 50:3267-3273(2007).
Cited for: X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF 44-750 IN COMPLEXES WITHSUBSTRATE ANALOGS; CALCIUM AND ZINC IONS, ENZYME REGULATION, ANDGLYCOSYLATION AT ASN-76; ASN-121; ASN-140 ASN-195; ASN-459; ASN-476AND ASN-638.
"Human glutamate carboxypeptidase II inhibition: structures of GCPIIin complex with two potent inhibitors, quisqualate and 2-PMPA.";
Mesters J.R., Henning K., Hilgenfeld R.;
Acta Crystallogr. D 63:508-513(2007).
Cited for: X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 44-750 IN COMPLEXES WITH THEINHIBITORS QUISQUALATE AND 2-PMPA; CALCIUM AND ZINC IONS, ANDGLYCOSYLATION AT ASN-76; ASN-121; ASN-140; ASN-195; ASN-459; ASN-476AND ASN-638.
"Structure of glutamate carboxypeptidase II, a drug target in neuronaldamage and prostate cancer.";
Mesters J.R., Barinka C., Li W., Tsukamoto T., Majer P., Slusher B.S.,Konvalinka J., Hilgenfeld R.;
EMBO J. 25:1375-1384(2006).
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 44-750 IN COMPLEXES WITHGLUTAMATE; INHIBITORS; CALCIUM AND ZINC IONS, COFACTOR, SUBUNIT, ANDGLYCOSYLATION AT ASN-76; ASN-121; ASN-140; ASN-195; ASN-459; ASN-476AND ASN-638.
"Identification of the N-glycosylation sites on glutamatecarboxypeptidase II necessary for proteolytic activity.";
Barinka C., Sacha P., Sklenar J., Man P., Bezouska K., Slusher B.S.,Konvalinka J.;
Protein Sci. 13:1627-1635(2004).
Cited for: GLYCOSYLATION AT ASN-51; ASN-76; ASN-121; ASN-140; ASN-153; ASN-195;ASN-336; ASN-459; ASN-476 AND ASN-638, AND MUTAGENESIS OF ASN-51;ASN-76; ASN-121; ASN-140; ASN-153; ASN-195; ASN-336; ASN-459; ASN-476;ASN-638 AND THR-640.
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-76; ASN-336; ASN-459; ASN-476 AND ASN-638.

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