ASpdb: an integrative knowledgebase of human protein isoforms from experimental and AI-predicted structures

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	Protein Summary
	AS Summary
	Protein Functional Features
	Gene Isoform Structures and Expression Levels
	Protein Structures
	pLDDT Score Distribution
	Ramachandran Plot of Protein Structures
	Potential Active Site Information
	Protein Structure and Feature Comparision
	Protein-Protein Interaction
	Related Drugs
	Related Diseases
	Clinically Important Variants

Protein:FOLH1

Protein Summary

Gene summary

Gene name: FOLH1
ASpdb.0 ID: 2346
	Gene
Gene symbol	FOLH1
Gene ID	2346
Gene name	folate hydrolase 1
Synonyms	FGCP\|FOLH\|GCP2\|GCPII\|NAALAD1\|PSM\|PSMA\|mGCP
Cytomap	11p11.12
Type of gene	protein-coding
Description	glutamate carboxypeptidase 2N-acetylated alpha-linked acidic dipeptidase 1N-acetylated-alpha-linked acidic dipeptidase INAALADase Icell growth-inhibiting gene 27 proteinfolylpoly-gamma-glutamate carboxypeptidaseglutamate carboxylase IIglutamate car
Modification date	20240403
UniProtAcc	Q04609

Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez

Partner	Gene	GO ID	GO term	PubMed ID
Gene	FOLH1	GO:0004181	metallocarboxypeptidase activity	12949938\|17241121\|24863754
Gene	FOLH1	GO:0005886	plasma membrane	12949938
Gene	FOLH1	GO:0006508	proteolysis	12949938
Gene	FOLH1	GO:0009986	cell surface	12949938
Gene	FOLH1	GO:0035609	C-terminal protein deglutamylation	12949938\|17241121\|24863754
Gene	FOLH1	GO:1904492	Ac-Asp-Glu binding	24863754
Gene	FOLH1	GO:1904493	tetrahydrofolyl-poly(glutamate) polymer binding	24863754

AS Summary

Information of the canonical protein with experimentally identified structure from PDB (2023).

UniProt Acc	File name	PDB ID	Method	Resolution	Chain	Start	End
Q04609-1	Q04609-1_5o5t_A.pdb	5O5T	X-ray	1.43	A	55	750

ASpdb's canonical and alternatively spliced isoform information.

accession_id	gene_name	canonical_id	alternative_id	canonical_length	alternative_length	canonical_start	canonical_end	type	originalSEQ	variationSEQ	alternative_start	alternative_end
Q04609	FOLH1	Q04609-1	Q04609-10	750	442	1	308	Deletion	none	none	0	0
Q04609	FOLH1	Q04609-1	Q04609-3	750	110	1	585	Deletion	none	none	0	0
Q04609	FOLH1	Q04609-1	Q04609-3	750	110	657	750	Substitution	NPIVLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA	MSSMLQAATTSMQGSHSQEFMMLCLILKAKWTLPRPGEK	72	110
Q04609	FOLH1	Q04609-1	Q04609-4	750	84	1	159	Deletion	none	none	0	0
Q04609	FOLH1	Q04609-1	Q04609-4	750	84	214	243	Substitution	VKNAQLAGAKGVILYSDPADYFAPGVKSYP	NMLIGVELQRLLVFQVFLFIQLDTMMHRSS	55	84
Q04609	FOLH1	Q04609-1	Q04609-4	750	84	244	750	Deletion	none	none	84	84
Q04609	FOLH1	Q04609-1	Q04609-6	750	693	1	57	Deletion	none	none	0	0
Q04609	FOLH1	Q04609-1	Q04609-7	750	735	1	39	Substitution	MWNLLHETDSAVATARRPRWLCAGALVLAGGFFLLGFLF	MTAGSSYPLFLAAYACTGCLAERL	1	24
Q04609	FOLH1	Q04609-1	Q04609-8	750	719	657	688	Substitution	NPIVLRMMNDQLMFLERAFIDPLGLPDRPFYR	K	657	657
Q04609	FOLH1	Q04609-1	Q04609-9	750	704	1	39	Substitution	MWNLLHETDSAVATARRPRWLCAGALVLAGGFFLLGFLF	MTAGSSYPLFLAAYACTGCLAERL	1	24
Q04609	FOLH1	Q04609-1	Q04609-9	750	704	657	688	Substitution	NPIVLRMMNDQLMFLERAFIDPLGLPDRPFYR	K	642	642

Multiple sequence alignment of our canonical and alternatively spliced FOLH1

Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of FOLH1

UniProt-id	ENSG	ENST	ENSP
Q04609-1	ENSG00000086205.18	ENST00000256999.7	ENSP00000256999.2
Q04609-7	ENSG00000086205.18	ENST00000340334.11	ENSP00000344131.7
Q04609-8	ENSG00000086205.18	ENST00000356696.7	ENSP00000349129.3
Q04609-9	ENSG00000086205.18	ENST00000533034.1	ENSP00000431463.1

UniProt-id	NM ID	NP ID
Q04609-1	NM_004476.1	NP_004467.1
Q04609-10	NM_001193473.1	NP_001180402.1
Q04609-7	NM_001193471.1	NP_001180400.1
Q04609-7	XM_017017434.1	XP_016872923.1
Q04609-8	NM_001014986.1	NP_001014986.1
Q04609-9	NM_001193472.1	NP_001180401.1

Amino acid sequences of our canonical and alternatively spliced FOLH1

accession_id	Protein sequence
Q04609-1	MWNLLHETDSAVATARRPRWLCAGALVLAGGFFLLGFLFGWFIKSSNEATNITPKHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNF QLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTHPNYISIINEDGNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYA RTEDFFKLERDMKINCSGKIVIARYGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTP GYPANEYAYRRGIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIG TLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQERGVAYI NADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKN WETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYSISMKHPQEMKTYSVSFD SLFSAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVD
Q04609-10	MGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEI VRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGF EGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQ VRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQL
Q04609-3	ELANSIVLPFDCRDYAVVLRKYADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSMSSMLQAATTSMQGSHSQE
Q04609-4
Q04609-6	MKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTHPNYISIINEDGNEIFNTSLFEPP PPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIARYGKVFRGNKVKNAQLAGAKGVILYSDPADYFAP GVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPY NVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTIL FASWDAEEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFS GMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDC RDYAVVLRKYADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPDRPFY
Q04609-7	MTAGSSYPLFLAAYACTGCLAERLGWFIKSSNEATNITPKHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGL DSVELAHYDVLLSYPNKTHPNYISIINEDGNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKIN CSGKIVIARYGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGIAE AVGLPSIPVHPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILG GHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVD CTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWETNKFSGYPLYHSV YETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASK FSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVDPSKAWGEVKRQIYVA
Q04609-8	MWNLLHETDSAVATARRPRWLCAGALVLAGGFFLLGFLFGWFIKSSNEATNITPKHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNF QLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTHPNYISIINEDGNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYA RTEDFFKLERDMKINCSGKIVIARYGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTP GYPANEYAYRRGIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIG TLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQERGVAYI NADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKN WETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYSISMKHPQEMKTYSVSFD
Q04609-9	MTAGSSYPLFLAAYACTGCLAERLGWFIKSSNEATNITPKHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGL DSVELAHYDVLLSYPNKTHPNYISIINEDGNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKIN CSGKIVIARYGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGIAE AVGLPSIPVHPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILG GHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVD CTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWETNKFSGYPLYHSV YETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASK

Protein Functional Features

Main function of this protein. (from UniProt)

FOLH1 (go to UniProt):Q04609

Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at
download page
* Minus value of BPloci means that the break pointn is located before the CDS.

- Retained protein feature among the 13 regional features.

Accession_id	Subsection	Start	End	Funcitonal feature	Splicing information
Q04609	Topological domain	1	19	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	Type=Deletion;Start=1;End=308
Q04609	Topological domain	1	19	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	Type=Deletion;Start=1;End=585
Q04609	Topological domain	1	19	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	Type=Deletion;Start=1;End=159
Q04609	Topological domain	1	19	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	Type=Deletion;Start=1;End=57
Q04609	Topological domain	1	19	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	Type=Substitution;Start=1;End=39
Q04609	Topological domain	1	19	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	Type=Substitution;Start=1;End=39
Q04609	Transmembrane	20	43	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000305;evidence=ECO:0000305	Type=Deletion;Start=1;End=308
Q04609	Transmembrane	20	43	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000305;evidence=ECO:0000305	Type=Deletion;Start=1;End=585
Q04609	Transmembrane	20	43	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000305;evidence=ECO:0000305	Type=Deletion;Start=1;End=159
Q04609	Transmembrane	20	43	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000305;evidence=ECO:0000305	Type=Deletion;Start=1;End=57
Q04609	Transmembrane	20	43	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000305;evidence=ECO:0000305	Type=Substitution;Start=1;End=39
Q04609	Transmembrane	20	43	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000305;evidence=ECO:0000305	Type=Substitution;Start=1;End=39
Q04609	Topological domain	44	750	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	Type=Deletion;Start=1;End=308
Q04609	Topological domain	44	750	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	Type=Deletion;Start=1;End=585
Q04609	Topological domain	44	750	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	Type=Substitution;Start=657;End=750
Q04609	Topological domain	44	750	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	Type=Deletion;Start=1;End=159
Q04609	Topological domain	44	750	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	Type=Substitution;Start=214;End=243
Q04609	Topological domain	44	750	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	Type=Deletion;Start=244;End=750
Q04609	Topological domain	44	750	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	Type=Deletion;Start=1;End=57
Q04609	Topological domain	44	750	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	Type=Substitution;Start=657;End=688
Q04609	Topological domain	44	750	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	Type=Substitution;Start=657;End=688
Q04609	Region	274	587	Note=NAALADase	Type=Deletion;Start=1;End=308
Q04609	Region	274	587	Note=NAALADase	Type=Deletion;Start=1;End=585
Q04609	Region	274	587	Note=NAALADase	Type=Deletion;Start=244;End=750

Gene Isoform Structures and Expression Levels for FOLH1

Gene structures of our canonical and alternative spliced genes of FOLH1
* Click on the image to open the UCSC genome browser with custom track showing this image in a new window.

Expression levels of gene isoforms across GTEx.

Expression levels of gene isoforms across TCGA.

Protein Structures

PDB and CIF files of the predicted protein structures
* Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format.

3D view using mol* of Q04609-1

3D view using mol* of Q04609-10

3D view using mol* of Q04609-3

3D view using mol* of Q04609-4

3D view using mol* of Q04609-6

3D view using mol* of Q04609-7

3D view using mol* of Q04609-8

3D view using mol* of Q04609-9

pLDDT Score Distribution

pLDDT score distribution of the predicted protein structures from AlphaFold2
* AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100.

pLDDT distribution across the protein length of Q04609-1

pLDDT distribution across the protein length of Q04609-10

pLDDT distribution across the protein length of Q04609-3

pLDDT distribution across the protein length of Q04609-4

pLDDT distribution across the protein length of Q04609-6

pLDDT distribution across the protein length of Q04609-7

pLDDT distribution across the protein length of Q04609-8

pLDDT distribution across the protein length of Q04609-9

Ramachandran Plot of Protein Structures

Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide.

Ramachandran plot of Q04609-1

Ramachandran plot of Q04609-10

Ramachandran plot of Q04609-3

Ramachandran plot of Q04609-6

Ramachandran plot of Q04609-7

Ramachandran plot of Q04609-9

Potential Active Site Information

The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite.

UniProt-id	Site score	Size	D score	Volume	Exposure	Enclosure	Contact	Phobic	Philic	Balance	Don/Acc	Residues
Q04609-1	1.08	296	0.941	720.3	0.482	0.818	1.07	0.367	1.503	0.244	0.613	205,206,207,208,209,210,213,234,254,256,257,259,26 0,261,262,263,264,265,377,381,387,424,425,427,428, 432,453,454,457,463,465,466,468,471,503,504,505,50 6,510,511,512,513,514,515,516,517,518,519,521,522, 523,527,534,536,538,539,541,545,546,547,548,549,55 2,553,603,607,687,692,698,699,700,701,702
Q04609-10	1.024	226	0.897	570.752	0.51	0.734	1.011	0.186	1.482	0.125	0.754	69,73,79,116,117,119,120,145,146,149,152,153,154,1 55,156,157,158,160,163,189,192,193,194,195,196,197 ,198,203,204,205,206,207,208,209,210,211,213,226,2 28,230,231,232,233,234,239,240,241,244,245,299,302 ,384,391,392,393,394,395
Q04609-3	0.911	66	0.976	176.988	0.732	0.603	0.716	1.317	0.459	2.87	1.027	65,68,69,72,73,75,76,79,83,89,92,93,96,97,100,101, 104
Q04609-4	1.023	117	1.073	273.371	0.536	0.672	0.971	0.897	0.829	1.083	0.948	1,2,3,6,7,8,9,11,12,37,38,39,40,41,59,60,61,62,63, 65,66,68,69,72,73,76
Q04609-6	1.026	366	0.976	905.863	0.557	0.737	0.945	0.355	1.246	0.285	0.677	124,125,126,148,149,150,151,152,153,155,156,159,17 7,197,199,200,202,204,320,324,330,367,368,370,371, 396,397,400,403,404,405,406,407,408,414,415,418,41 9,422,437,440,443,444,445,446,447,448,449,452,453, 454,455,456,457,458,459,460,461,462,464,477,479,48 1,482,483,484,485,487,488,489,490,491,495,496,542, 545,546,550,553,638,640,641,642,643,644,645,646,65 2,656
Q04609-7	1.077	322	0.953	796.446	0.511	0.813	1.069	0.331	1.455	0.228	0.617	190,191,192,193,194,195,198,219,239,241,242,244,24 5,246,247,248,249,250,362,366,372,409,410,412,413, 417,438,439,442,448,450,451,452,453,456,460,488,48 9,490,491,494,495,496,497,498,499,500,501,502,503, 504,506,507,508,519,521,523,524,526,529,530,531,53 2,533,534,537,538,584,588,592,672,677,684,685,686, 687
Q04609-8	1.063	214	0.914	528.22	0.458	0.792	1.008	0.427	1.536	0.278	0.607	205,206,207,208,209,210,212,213,215,234,254,255,25 6,257,259,260,261,262,263,264,265,377,381,386,387, 424,425,427,428,453,454,456,457,463,517,518,519,52 2,534,536,541,547,548,549,552,553
Q04609-9	1.054	205	0.971	523.418	0.476	0.779	0.965	0.553	1.337	0.414	0.795	190,191,192,193,194,195,198,219,239,240,241,242,24 4,245,246,248,249,250,362,366,371,372,409,410,412, 413,438,439,441,442,448,502,503,504,507,519,521,52 6,532,533,534,537,538

Protein Structure and Feature Comparision

Protein Structure Comparision Using Template Modeling Scores (TM-score).

Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green)

3D view using mol* of Q04609-1_Q04609-1_5o5t_A.pdb

Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green)

3D view using mol* of Q04609-1_5o5t_A_Q04609-10.pdb

3D view using mol* of Q04609-1_5o5t_A_Q04609-3.pdb

3D view using mol* of Q04609-1_5o5t_A_Q04609-4.pdb

3D view using mol* of Q04609-1_5o5t_A_Q04609-6.pdb

3D view using mol* of Q04609-1_5o5t_A_Q04609-7.pdb

3D view using mol* of Q04609-1_5o5t_A_Q04609-8.pdb

3D view using mol* of Q04609-1_5o5t_A_Q04609-9.pdb

Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green)

3D view using mol* of Q04609-1_Q04609-10.pdb

3D view using mol* of Q04609-1_Q04609-3.pdb

3D view using mol* of Q04609-1_Q04609-4.pdb

3D view using mol* of Q04609-1_Q04609-6.pdb

3D view using mol* of Q04609-1_Q04609-7.pdb

3D view using mol* of Q04609-1_Q04609-8.pdb

3D view using mol* of Q04609-1_Q04609-9.pdb

Protein Feature Comparison of the protein sequendary structures among the protiens.

./stats/secondary_structure/figure/Q04609-1_vs_Q04609-10.png

./stats/secondary_structure/figure/Q04609-1_vs_Q04609-3.png

./stats/secondary_structure/figure/Q04609-1_vs_Q04609-4.png

./stats/secondary_structure/figure/Q04609-1_vs_Q04609-6.png

./stats/secondary_structure/figure/Q04609-1_vs_Q04609-7.png

./stats/secondary_structure/figure/Q04609-1_vs_Q04609-8.png

./stats/secondary_structure/figure/Q04609-1_vs_Q04609-9.png

Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens.

./stats/relative_asa/Q04609-1_vs_Q04609-10.png

./stats/relative_asa/Q04609-1_vs_Q04609-3.png

./stats/relative_asa/Q04609-1_vs_Q04609-4.png

./stats/relative_asa/Q04609-1_vs_Q04609-6.png

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Protein-Protein Interaction

Interactors from UniProt.

Accession_id

Subsection

Start

End

Funcitonal feature

Splicing information

Interactors from STRING.

Gene name

Interactors

Related Drugs to FOLH1

Drugs targeting this gene/protein.
(DrugBank)

UniProt accession	Gene name	DrugBank ID	Drug name	Drug group	Actions
Q04609	FOLH1	DB17851	Flotufolastat F-18	approved, investigational	binder
Q04609	FOLH1	DB00142	Glutamic acid	approved, nutraceutical
Q04609	FOLH1	DB14805	Piflufolastat F 18	approved, investigational	binder
Q04609	FOLH1	DB07754	DCFBC	experimental
Q04609	FOLH1	DB08835	Spaglumic acid	experimental	ligand
Q04609	FOLH1	DB06928	(2S)-2-{[HYDROXY(4-IODOBENZYL)PHOSPHORYL]METHYL}PENTANEDIOIC ACID	experimental
Q04609	FOLH1	DB00089	Capromab pendetide	approved	other/unknown

Related Diseases to FOLH1

Previous studies relating to the alternative splicing of FOLH1 and disease information from the MeSH term (PubMed)

Gene	PMID	Title	Abstract	MeSH ID	MeSH term
FOLH1	12949815	Expression of prostate specific membrane antigen and three alternatively spliced variants of PSMA in prostate cancer patients.	Prostate specific membrane antigen (PSMA) is a folate gamma glutamyl carboxypeptidase that is oriented on the plasma membrane of normal and prostate cancer cells. A cytosolic version of PSMA, PSM', results from alternative splicing of the PSMA gene. Two additional alternatively spliced variants of PSMA, PSM-C and PSM-D, have been described recently. The ratio of PSMA to PSM' mRNA was higher in a small number of prostate cancer specimens compared to normal prostate cancer and benign prostatic hypertrophy (Su et al. Cancer Res 1995;55:1441). The intent of our study was to measure the gene expression of PSMA and the 3 PSMA splice variants in a large number of patient's tissues. A real-time, quantitative PCR assay was developed to quantify PSMA, PSM', PSM-C and PSM-D. Discrimination among the variants was achieved by designing unique primers and TaqMan probes for each gene. Amplification and detection was specific for the desired splice variant and was sensitive to one gene copy per reaction. The assay was used to quantify the gene expression in specimens of normal, benign, primary and metastatic prostate cancer from 72 patients. The mean PSMA expression (relative to 18S rRNA) was 2- to 3-fold lower in normal prostate (n = 4) compared to primary (n = 55, p = 0.31) and metastatic (n = 20, p = 0.33) prostate cancer. There was no difference in the PSMA expression between benign and cancerous prostate tissue from the same patients (n = 35). The ratio of PSMA to PSM' was lowest in the normal prostate and increased with increasing Gleason score (p < 0.001). The increased ratio in these tissues was a reflection of both increasing PSMA levels and decreasing PSM' mRNA. The expression of PSM-C did not differ in any of the tissue categories studied. The expression of PSM-D was similar in normal and primary prostate cancer but was 2-fold higher in lymph node (p < 0.005) and bone metastases (p < 0.05) compared to the primary tumors. Our results of the first detailed quantitative analysis of PSMA mRNA expression in patient's tissues demonstrate that PSMA and the 3 PSMA splice variants are expressed in normal, benign, cancerous and metastatic prostate cancer. We note increased PSMA expression in some malignant tissues, however, these increases are modest in magnitude. We also report that the expression of a novel splice variant, PSM-D, is elevated in prostate cancer metastases.	D001859	Bone Neoplasms
FOLH1	12949815	Expression of prostate specific membrane antigen and three alternatively spliced variants of PSMA in prostate cancer patients.	Prostate specific membrane antigen (PSMA) is a folate gamma glutamyl carboxypeptidase that is oriented on the plasma membrane of normal and prostate cancer cells. A cytosolic version of PSMA, PSM', results from alternative splicing of the PSMA gene. Two additional alternatively spliced variants of PSMA, PSM-C and PSM-D, have been described recently. The ratio of PSMA to PSM' mRNA was higher in a small number of prostate cancer specimens compared to normal prostate cancer and benign prostatic hypertrophy (Su et al. Cancer Res 1995;55:1441). The intent of our study was to measure the gene expression of PSMA and the 3 PSMA splice variants in a large number of patient's tissues. A real-time, quantitative PCR assay was developed to quantify PSMA, PSM', PSM-C and PSM-D. Discrimination among the variants was achieved by designing unique primers and TaqMan probes for each gene. Amplification and detection was specific for the desired splice variant and was sensitive to one gene copy per reaction. The assay was used to quantify the gene expression in specimens of normal, benign, primary and metastatic prostate cancer from 72 patients. The mean PSMA expression (relative to 18S rRNA) was 2- to 3-fold lower in normal prostate (n = 4) compared to primary (n = 55, p = 0.31) and metastatic (n = 20, p = 0.33) prostate cancer. There was no difference in the PSMA expression between benign and cancerous prostate tissue from the same patients (n = 35). The ratio of PSMA to PSM' was lowest in the normal prostate and increased with increasing Gleason score (p < 0.001). The increased ratio in these tissues was a reflection of both increasing PSMA levels and decreasing PSM' mRNA. The expression of PSM-C did not differ in any of the tissue categories studied. The expression of PSM-D was similar in normal and primary prostate cancer but was 2-fold higher in lymph node (p < 0.005) and bone metastases (p < 0.05) compared to the primary tumors. Our results of the first detailed quantitative analysis of PSMA mRNA expression in patient's tissues demonstrate that PSMA and the 3 PSMA splice variants are expressed in normal, benign, cancerous and metastatic prostate cancer. We note increased PSMA expression in some malignant tissues, however, these increases are modest in magnitude. We also report that the expression of a novel splice variant, PSM-D, is elevated in prostate cancer metastases.	D011470	Prostatic Hyperplasia
FOLH1	12949815	Expression of prostate specific membrane antigen and three alternatively spliced variants of PSMA in prostate cancer patients.	Prostate specific membrane antigen (PSMA) is a folate gamma glutamyl carboxypeptidase that is oriented on the plasma membrane of normal and prostate cancer cells. A cytosolic version of PSMA, PSM', results from alternative splicing of the PSMA gene. Two additional alternatively spliced variants of PSMA, PSM-C and PSM-D, have been described recently. The ratio of PSMA to PSM' mRNA was higher in a small number of prostate cancer specimens compared to normal prostate cancer and benign prostatic hypertrophy (Su et al. Cancer Res 1995;55:1441). The intent of our study was to measure the gene expression of PSMA and the 3 PSMA splice variants in a large number of patient's tissues. A real-time, quantitative PCR assay was developed to quantify PSMA, PSM', PSM-C and PSM-D. Discrimination among the variants was achieved by designing unique primers and TaqMan probes for each gene. Amplification and detection was specific for the desired splice variant and was sensitive to one gene copy per reaction. The assay was used to quantify the gene expression in specimens of normal, benign, primary and metastatic prostate cancer from 72 patients. The mean PSMA expression (relative to 18S rRNA) was 2- to 3-fold lower in normal prostate (n = 4) compared to primary (n = 55, p = 0.31) and metastatic (n = 20, p = 0.33) prostate cancer. There was no difference in the PSMA expression between benign and cancerous prostate tissue from the same patients (n = 35). The ratio of PSMA to PSM' was lowest in the normal prostate and increased with increasing Gleason score (p < 0.001). The increased ratio in these tissues was a reflection of both increasing PSMA levels and decreasing PSM' mRNA. The expression of PSM-C did not differ in any of the tissue categories studied. The expression of PSM-D was similar in normal and primary prostate cancer but was 2-fold higher in lymph node (p < 0.005) and bone metastases (p < 0.05) compared to the primary tumors. Our results of the first detailed quantitative analysis of PSMA mRNA expression in patient's tissues demonstrate that PSMA and the 3 PSMA splice variants are expressed in normal, benign, cancerous and metastatic prostate cancer. We note increased PSMA expression in some malignant tissues, however, these increases are modest in magnitude. We also report that the expression of a novel splice variant, PSM-D, is elevated in prostate cancer metastases.	D011471	Prostatic Neoplasms
FOLH1	12949815	Expression of prostate specific membrane antigen and three alternatively spliced variants of PSMA in prostate cancer patients.	Prostate specific membrane antigen (PSMA) is a folate gamma glutamyl carboxypeptidase that is oriented on the plasma membrane of normal and prostate cancer cells. A cytosolic version of PSMA, PSM', results from alternative splicing of the PSMA gene. Two additional alternatively spliced variants of PSMA, PSM-C and PSM-D, have been described recently. The ratio of PSMA to PSM' mRNA was higher in a small number of prostate cancer specimens compared to normal prostate cancer and benign prostatic hypertrophy (Su et al. Cancer Res 1995;55:1441). The intent of our study was to measure the gene expression of PSMA and the 3 PSMA splice variants in a large number of patient's tissues. A real-time, quantitative PCR assay was developed to quantify PSMA, PSM', PSM-C and PSM-D. Discrimination among the variants was achieved by designing unique primers and TaqMan probes for each gene. Amplification and detection was specific for the desired splice variant and was sensitive to one gene copy per reaction. The assay was used to quantify the gene expression in specimens of normal, benign, primary and metastatic prostate cancer from 72 patients. The mean PSMA expression (relative to 18S rRNA) was 2- to 3-fold lower in normal prostate (n = 4) compared to primary (n = 55, p = 0.31) and metastatic (n = 20, p = 0.33) prostate cancer. There was no difference in the PSMA expression between benign and cancerous prostate tissue from the same patients (n = 35). The ratio of PSMA to PSM' was lowest in the normal prostate and increased with increasing Gleason score (p < 0.001). The increased ratio in these tissues was a reflection of both increasing PSMA levels and decreasing PSM' mRNA. The expression of PSM-C did not differ in any of the tissue categories studied. The expression of PSM-D was similar in normal and primary prostate cancer but was 2-fold higher in lymph node (p < 0.005) and bone metastases (p < 0.05) compared to the primary tumors. Our results of the first detailed quantitative analysis of PSMA mRNA expression in patient's tissues demonstrate that PSMA and the 3 PSMA splice variants are expressed in normal, benign, cancerous and metastatic prostate cancer. We note increased PSMA expression in some malignant tissues, however, these increases are modest in magnitude. We also report that the expression of a novel splice variant, PSM-D, is elevated in prostate cancer metastases.	D012983	Soft Tissue Neoplasms
FOLH1	19107881	Prostate-specific membrane antigen and its truncated form PSM'.	Prostate specific membrane antigen (PSMA) is a type II transmembrane protein overexpressed in prostate cancer as well as in the neovasculature of several non-prostatic solid tumors. In addition to full-length PSMA, several splice variants exist in prostatic tissue. Notably, the N-terminally truncated PSMA variant, termed PSM', is prevalent in healthy prostate, and the ratio of PSMA/PSM' mRNA has been shown to correlate with cancer progression. The widely accepted hypothesis is that the PSM' protein is a translation product arising from the alternatively spliced PSM' mRNA.	D000230	Adenocarcinoma
FOLH1	19107881	Prostate-specific membrane antigen and its truncated form PSM'.	Prostate specific membrane antigen (PSMA) is a type II transmembrane protein overexpressed in prostate cancer as well as in the neovasculature of several non-prostatic solid tumors. In addition to full-length PSMA, several splice variants exist in prostatic tissue. Notably, the N-terminally truncated PSMA variant, termed PSM', is prevalent in healthy prostate, and the ratio of PSMA/PSM' mRNA has been shown to correlate with cancer progression. The widely accepted hypothesis is that the PSM' protein is a translation product arising from the alternatively spliced PSM' mRNA.	D011471	Prostatic Neoplasms

Clinically important variants in FOLH1

(ClinVar, 04/20/2024)

accession_id

uniprot_id

gene_name

Type

Variant

Clinical_significance