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UniProtKB - Q04609 (FOLH1_HUMAN)

Entry version 200 (08 May 2019)
Sequence version 1 (01 Jun 1994)
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Protein

Glutamate carboxypeptidase 2

Gene

FOLH1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.

Miscellaneous

PSMA is used as a diagnostic and prognostic indicator of prostate cancer, and as a possible marker for various neurological disorders such as schizophrenia, Alzheimer disease and Huntington disease.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates. EC:3.4.17.21

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+6 PublicationsNote: Binds 2 Zn2+ ions per subunit. Required for NAALADase activity.1 Publication

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The NAALADase activity is inhibited by beta-NAAG, quisqualic acid, 2-(phosphonomethyl) pentanedioic acid (PMPA) and EDTA. Activated by cobalt.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei

Stable at pH greater than 6.5.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei210SubstrateCombined sources6 Publications1
Binding sitei257SubstrateCombined sources6 Publications1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi269CalciumCombined sources6 Publications1
Metal bindingi272Calcium; via carbonyl oxygenCombined sources6 Publications1
Metal bindingi377Zinc 1; via tele nitrogen; catalyticCombined sources6 Publications1
Metal bindingi387Zinc 1; catalyticCombined sources6 Publications1
Metal bindingi387Zinc 2Combined sources6 Publications1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei424Nucleophile; for NAALADase activity1
Binding sitei424SubstrateBy similarity1
Metal bindingi425Zinc 2Combined sources6 Publications1
Metal bindingi433CalciumCombined sources6 Publications1
Metal bindingi436CalciumCombined sources6 Publications1
Metal bindingi453Zinc 1; catalyticCombined sources6 Publications1
Binding sitei519SubstrateCombined sources6 Publications1
Binding sitei552SubstrateCombined sources6 Publications1
Metal bindingi553Zinc 2; via tele nitrogenCombined sources6 Publications1
Active sitei628Charge relay systemSequence analysis1
Active sitei666Charge relay systemSequence analysis1
Active sitei689Charge relay systemSequence analysis1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionCarboxypeptidase, Dipeptidase, Hydrolase, Metalloprotease, Multifunctional enzyme, Protease
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.4.17.21 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-70614 Amino acid synthesis and interconversion (transamination)

Protein family/group databases

MEROPS protease database

More...MEROPSi		M28.010

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Glutamate carboxypeptidase 2 (EC:3.4.17.21)
Alternative name(s):
Cell growth-inhibiting gene 27 protein
Folate hydrolase 1
Folylpoly-gamma-glutamate carboxypeptidase
Short name:
FGCP
Glutamate carboxypeptidase II
Short name:
GCPII
Membrane glutamate carboxypeptidase
Short name:
mGCP
N-acetylated-alpha-linked acidic dipeptidase I
Short name:
NAALADase I
Prostate-specific membrane antigen
Short name:
PSM
Short name:
PSMA
Pteroylpoly-gamma-glutamate carboxypeptidase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:FOLH1
Synonyms:FOLH, NAALAD1, PSM, PSMA
ORF Names:GIG27
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:3788 FOLH1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		600934 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q04609

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 19CytoplasmicCuratedAdd BLAST19
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei20 – 43Helical; Signal-anchor for type II membrane proteinCuratedAdd BLAST24
Topological domaini44 – 750ExtracellularCuratedAdd BLAST707

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi51N → A: Loss of glycosylation. Reduces enzyme activity. 1 Publication1
Mutagenesisi76N → A: Loss of glycosylation. Reduces enzyme activity. 1 Publication1
Mutagenesisi121N → A: Loss of glycosylation. Severely reduced enzyme activity. 1 Publication1
Mutagenesisi140N → A: Loss of glycosylation. Severely reduced enzyme activity. 1 Publication1
Mutagenesisi153N → A: Loss of glycosylation. Severely reduced enzyme activity. 1 Publication1
Mutagenesisi195N → A: Loss of glycosylation. Severely reduced enzyme activity. 1 Publication1
Mutagenesisi336N → A: Loss of glycosylation. Reduces enzyme activity. 1 Publication1
Mutagenesisi377H → A, G or Q: Complete loss of activity. 1 Publication1
Mutagenesisi379D → E or N: Complete loss of activity. 1 Publication1
Mutagenesisi387D → E or L: Complete loss of activity. 1 Publication1
Mutagenesisi387D → N: No effect on enzyme activity. 1 Publication1
Mutagenesisi388P → A: No effect on enzyme activity. 1 Publication1
Mutagenesisi424E → A: Complete loss of activity. 1 Publication1
Mutagenesisi424E → D: Reduces enzyme activity. 1 Publication1
Mutagenesisi424E → Q: Reduces enzyme activity. 1 Publication1
Mutagenesisi425E → Q or D: Complete loss of activity. 1 Publication1
Mutagenesisi453D → N or L: Complete loss of activity. 1 Publication1
Mutagenesisi453D → Q: Reduces enzyme activity. 1 Publication1
Mutagenesisi454S → A: Reduces enzyme activity. 1 Publication1
Mutagenesisi459N → A: Loss of glycosylation. Reduces enzyme activity. 1 Publication1
Mutagenesisi476N → A: Loss of glycosylation. Reduces enzyme activity. 1 Publication1
Mutagenesisi638N → A: Loss of glycosylation. Abolishes enzyme activity. 1 Publication1
Mutagenesisi640T → A: Abolishes enzyme activity. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		2346

Open Targets

More...OpenTargetsi		ENSG00000086205

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA28205

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1892

Drug and drug target database

More...DrugBanki		DB06928 (2S)-2-{[HYDROXY(4-IODOBENZYL)PHOSPHORYL]METHYL}PENTANEDIOIC ACID
DB00089 Capromab
DB00142 L-Glutamic Acid
DB07754 N-({(1R)-1-carboxy-2-[(4-fluorobenzyl)sulfanyl]ethyl}carbamoyl)-L-glutamic acid

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1606

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		FOLH1

Domain mapping of disease mutations (DMDM)

More...DMDMi		548615

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001741171 – 750Glutamate carboxypeptidase 2Add BLAST750

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei10PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi51N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi76N-linked (GlcNAc...) asparagineCombined sources8 Publications1
Glycosylationi121N-linked (GlcNAc...) asparagineCombined sources7 Publications1
Glycosylationi140N-linked (GlcNAc...) asparagineCombined sources7 Publications1
Glycosylationi153N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi195N-linked (GlcNAc...) asparagineCombined sources7 Publications1
Glycosylationi336N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi459N-linked (GlcNAc...) asparagineCombined sources8 Publications1
Glycosylationi476N-linked (GlcNAc...) asparagineCombined sources8 Publications1
Glycosylationi638N-linked (GlcNAc...) asparagineCombined sources8 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The first two amino acids at the N-terminus of isoform PSMA' appear to be cleaved by limited proteolysis.
The N-terminus is blocked.

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q04609

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q04609

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q04609

PeptideAtlas

More...PeptideAtlasi		Q04609

PRoteomics IDEntifications database

More...PRIDEi		Q04609

ProteomicsDB human proteome resource

More...ProteomicsDBi		58243
58244 [Q04609-3]
58245 [Q04609-4]
58246 [Q04609-6]
58247 [Q04609-7]
58248 [Q04609-8]
58249 [Q04609-9]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q04609

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q04609

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Highly expressed in prostate epithelium. Detected in urinary bladder, kidney, testis, ovary, fallopian tube, breast, adrenal gland, liver, esophagus, stomach, small intestine, colon and brain (at protein level). Detected in the small intestine, brain, kidney, liver, spleen, colon, trachea, spinal cord and the capillary endothelium of a variety of tumors. Expressed specifically in jejunum brush border membranes. In the brain, highly expressed in the ventral striatum and brain stem. Also expressed in fetal liver and kidney. Isoform PSMA' is the most abundant form in normal prostate. Isoform PSMA-1 is the most abundant form in primary prostate tumors. Isoform PSMA-3 is also found in normal prostate as well as in brain and liver. Isoform PSMA-9 is specifically expressed in prostate cancer.5 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

In the prostate, up-regulated in response to androgen deprivation.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000086205 Expressed in 149 organ(s), highest expression level in corpus callosum

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q04609 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q04609 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB001451
HPA010593

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		108630, 5 interactors

Protein interaction database and analysis system

More...IntActi		Q04609, 6 interactors

Molecular INTeraction database

More...MINTi		Q04609

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000256999

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q04609

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1750
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Z8LX-ray3.50A/B/C/D56-750[»]
2C6CX-ray2.00A44-750[»]
2C6GX-ray2.20A44-750[»]
2C6PX-ray2.39A44-750[»]
2CIJX-ray2.40A44-750[»]
2JBJX-ray2.19A44-750[»]
2JBKX-ray2.99A44-750[»]
2OOTX-ray1.64A44-750[»]
2OR4X-ray1.62A44-750[»]
2PVVX-ray2.11A44-750[»]
2PVWX-ray1.71A44-750[»]
2XEFX-ray1.59A44-750[»]
2XEGX-ray1.59A44-750[»]
2XEIX-ray1.69A44-750[»]
2XEJX-ray1.78A44-750[»]
3BHXX-ray1.60A44-750[»]
3BI0X-ray1.67A44-750[»]
3BI1X-ray1.50A44-750[»]
3BXMX-ray1.71A44-750[»]
3D7DX-ray1.69A44-750[»]
3D7FX-ray1.54A44-750[»]
3D7GX-ray1.75A44-750[»]
3D7HX-ray1.55A44-750[»]
3IWWX-ray2.30A44-750[»]
3RBUX-ray1.60A44-750[»]
3SJEX-ray1.70A44-750[»]
3SJFX-ray1.65A44-750[»]
3SJGX-ray1.65A44-750[»]
3SJXX-ray1.66A44-750[»]
4JYWX-ray1.73A44-750[»]
4JZ0X-ray1.83A44-750[»]
4LQGX-ray1.77A44-750[»]
4MCPX-ray1.65A44-750[»]
4MCQX-ray2.00A44-750[»]
4MCRX-ray1.65A44-750[»]
4MCSX-ray1.83A44-750[»]
4NGMX-ray1.84A44-750[»]
4NGNX-ray1.64A44-750[»]
4NGPX-ray1.63A44-750[»]
4NGQX-ray2.08A44-750[»]
4NGRX-ray1.90A44-750[»]
4NGSX-ray1.68A44-750[»]
4NGTX-ray2.31A44-750[»]
4OC0X-ray1.85A44-750[»]
4OC1X-ray1.75A44-750[»]
4OC2X-ray1.65A44-750[»]
4OC3X-ray1.79A44-750[»]
4OC4X-ray1.66A44-750[»]
4OC5X-ray1.70A44-750[»]
4OMEX-ray1.79A44-750[»]
4P44X-ray1.75A44-750[»]
4P45X-ray1.87A44-750[»]
4P4BX-ray1.93A44-750[»]
4P4DX-ray1.65A44-750[»]
4P4EX-ray1.67A44-750[»]
4P4FX-ray1.86A44-750[»]
4P4IX-ray1.87A44-750[»]
4P4JX-ray1.66A44-750[»]
4W9YX-ray1.64A44-750[»]
4X3RX-ray1.86A44-750[»]
5D29X-ray1.80A56-750[»]
5ELYX-ray1.81A55-750[»]
5F09X-ray1.85A44-750[»]
5O5RX-ray1.65A44-750[»]
5O5TX-ray1.43A44-750[»]
5O5UX-ray1.53A44-750[»]
5OF0X-ray1.48A44-750[»]
6ETYX-ray1.68A44-750[»]
6EZ9X-ray1.61A44-750[»]
6F5LX-ray1.63A44-750[»]
6FE5X-ray1.52A44-750[»]
6H7YX-ray1.81A44-750[»]
6H7ZX-ray2.00A44-750[»]
6HKJX-ray2.09A44-750[»]
6HKZX-ray2.09A44-750[»]

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q04609

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q04609

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni274 – 587NAALADaseAdd BLAST314
Regioni517 – 518Substrate bindingBy similarity2
Regioni534 – 536Substrate bindingCombined sources2 Publications3
Regioni552 – 553Substrate bindingBy similarity2
Regioni699 – 700Substrate bindingCombined sources5 Publications2

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi146 – 149Poly-ProSequence analysis4

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The NAALADase activity is found in the central region, the dipeptidyl peptidase IV type activity in the C-terminal.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase M28 family. M28B subfamily.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2195 Eukaryota
COG2234 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00950000182766

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000211921

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q04609

KEGG Orthology (KO)

More...KOi		K14592

Identification of Orthologs from Complete Genome Data

More...OMAi		HKYRDFQ

Database of Orthologous Groups

More...OrthoDBi		633642at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q04609

TreeFam database of animal gene trees

More...TreeFami		TF312981

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.20.930.40, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR003137 PA_domain
IPR007484 Peptidase_M28
IPR039373 Peptidase_M28B
IPR007365 TFR-like_dimer_dom
IPR036757 TFR-like_dimer_dom_sf

The PANTHER Classification System

More...PANTHERi		PTHR10404 PTHR10404, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02225 PA, 1 hit
PF04389 Peptidase_M28, 1 hit
PF04253 TFR_dimer, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47672 SSF47672, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (8+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 8 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 8 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform PSMA-1 (identifier: Q04609-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MWNLLHETDS AVATARRPRW LCAGALVLAG GFFLLGFLFG WFIKSSNEAT 
        60         70         80         90        100
NITPKHNMKA FLDELKAENI KKFLYNFTQI PHLAGTEQNF QLAKQIQSQW 
       110        120        130        140        150
KEFGLDSVEL AHYDVLLSYP NKTHPNYISI INEDGNEIFN TSLFEPPPPG 
       160        170        180        190        200
YENVSDIVPP FSAFSPQGMP EGDLVYVNYA RTEDFFKLER DMKINCSGKI 
       210        220        230        240        250
VIARYGKVFR GNKVKNAQLA GAKGVILYSD PADYFAPGVK SYPDGWNLPG 
       260        270        280        290        300
GGVQRGNILN LNGAGDPLTP GYPANEYAYR RGIAEAVGLP SIPVHPIGYY 
       310        320        330        340        350
DAQKLLEKMG GSAPPDSSWR GSLKVPYNVG PGFTGNFSTQ KVKMHIHSTN 
       360        370        380        390        400
EVTRIYNVIG TLRGAVEPDR YVILGGHRDS WVFGGIDPQS GAAVVHEIVR 
       410        420        430        440        450
SFGTLKKEGW RPRRTILFAS WDAEEFGLLG STEWAEENSR LLQERGVAYI 
       460        470        480        490        500
NADSSIEGNY TLRVDCTPLM YSLVHNLTKE LKSPDEGFEG KSLYESWTKK 
       510        520        530        540        550
SPSPEFSGMP RISKLGSGND FEVFFQRLGI ASGRARYTKN WETNKFSGYP 
       560        570        580        590        600
LYHSVYETYE LVEKFYDPMF KYHLTVAQVR GGMVFELANS IVLPFDCRDY 
       610        620        630        640        650
AVVLRKYADK IYSISMKHPQ EMKTYSVSFD SLFSAVKNFT EIASKFSERL 
       660        670        680        690        700
QDFDKSNPIV LRMMNDQLMF LERAFIDPLG LPDRPFYRHV IYAPSSHNKY 
       710        720        730        740        750
AGESFPGIYD ALFDIESKVD PSKAWGEVKR QIYVAAFTVQ AAAETLSEVA
Note: No experimental confirmation available.
Length:750
Mass (Da):84,331
Last modified:June 1, 1994 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iAD8C0A7DBF47901A
GO
Isoform PSMA-3 (identifier: Q04609-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-585: Missing.
     657-750: NPIVLRMMND...AAAETLSEVA → MSSMLQAATT...KWTLPRPGEK

Note: No experimental confirmation available. Incomplete sequence.
Show »
Length:110
Mass (Da):12,603
Checksum:iE35692A0D83A0E53
GO
Isoform PSMA-4 (identifier: Q04609-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-159: Missing.
     214-243: VKNAQLAGAKGVILYSDPADYFAPGVKSYP → NMLIGVELQRLLVFQVFLFIQLDTMMHRSS
     244-750: Missing.

Note: No experimental confirmation available. Incomplete sequence.
Show »
Length:84
Mass (Da):9,754
Checksum:i80FC286A66993939
GO
Isoform PSMA' (identifier: Q04609-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-57: Missing.

Show »
Length:693
Mass (Da):78,000
Checksum:i5F3F6D31A9FECAEC
GO
Isoform PSMA-7 (identifier: Q04609-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: MWNLLHETDSAVATARRPRWLCAGALVLAGGFFLLGFLF → MTAGSSYPLFLAAYACTGCLAERL

Show »
Length:735
Mass (Da):82,519
Checksum:iB8D9D69F67C3ABF2
GO
Isoform PSMA-8 (identifier: Q04609-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     657-688: NPIVLRMMNDQLMFLERAFIDPLGLPDRPFYR → K

Show »
Length:719
Mass (Da):80,597
Checksum:iAF79A10CA2BF9DF4
GO
Isoform PSMA-9 (identifier: Q04609-9) [UniParc]FASTAAdd to basket
Also known as: PSM-E

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: MWNLLHETDSAVATARRPRWLCAGALVLAGGFFLLGFLF → MTAGSSYPLFLAAYACTGCLAERL
     657-688: NPIVLRMMNDQLMFLERAFIDPLGLPDRPFYR → K

Show »
Length:704
Mass (Da):78,785
Checksum:i800DE87726E1328C
GO
Isoform 10 (identifier: Q04609-10) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-308: Missing.

Show »
Length:442
Mass (Da):50,090
Checksum:i444527FF83B757C6
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PMK6E9PMK6_HUMAN
Glutamate carboxypeptidase 2
FOLH1
74Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PI29E9PI29_HUMAN
Glutamate carboxypeptidase 2
FOLH1
46Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PLV0E9PLV0_HUMAN
Glutamate carboxypeptidase 2
FOLH1
48Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PKM3E9PKM3_HUMAN
Glutamate carboxypeptidase 2
FOLH1
64Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAF31167 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti194I → V in AAZ66619 (Ref. 9) Curated1
Sequence conflicti354R → K AA sequence (PubMed:8417812).Curated1
Sequence conflicti398I → N in ABO93402 (PubMed:17929272).Curated1

<p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

Genetic variation in FOLH1 may be associated with low folate levels and consequent hyperhomocysteinemia. This condition can result in increased risk of cardiovascular disease, neural tube defects, and cognitive deficits.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_03639823A → T in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_02459275Y → H1 PublicationCorresponds to variant dbSNP:rs202676Ensembl.1
Natural variantiVAR_012736475H → Y Can be associated with lower folate and higher homocysteine levels. 1 PublicationCorresponds to variant dbSNP:rs61886492Ensembl.1
Natural variantiVAR_028882627V → L. Corresponds to variant dbSNP:rs2988342Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0402421 – 585Missing in isoform PSMA-3. CuratedAdd BLAST585
Alternative sequenceiVSP_0442871 – 308Missing in isoform 10. 1 PublicationAdd BLAST308
Alternative sequenceiVSP_0402411 – 159Missing in isoform PSMA-4. CuratedAdd BLAST159
Alternative sequenceiVSP_0053361 – 57Missing in isoform PSMA'. 1 PublicationAdd BLAST57
Alternative sequenceiVSP_0380581 – 39MWNLL…LGFLF → MTAGSSYPLFLAAYACTGCL AERL in isoform PSMA-7 and isoform PSMA-9. 2 PublicationsAdd BLAST39
Alternative sequenceiVSP_040243214 – 243VKNAQ…VKSYP → NMLIGVELQRLLVFQVFLFI QLDTMMHRSS in isoform PSMA-4. CuratedAdd BLAST30
Alternative sequenceiVSP_040244244 – 750Missing in isoform PSMA-4. CuratedAdd BLAST507
Alternative sequenceiVSP_040245657 – 750NPIVL…LSEVA → MSSMLQAATTSMQGSHSQEF MMLCLILKAKWTLPRPGEK in isoform PSMA-3. CuratedAdd BLAST94
Alternative sequenceiVSP_038059657 – 688NPIVL…RPFYR → K in isoform PSMA-8 and isoform PSMA-9. 3 PublicationsAdd BLAST32

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M99487 mRNA Translation: AAA60209.1
S76978 mRNA Translation: AAB33750.2
AF007544 Genomic DNA Translation: AAC83972.1
AF176574 mRNA Translation: AAD51121.1
EF488811 mRNA Translation: ABO93402.2
AY101595 mRNA Translation: AAM34479.1
AF107214 Genomic DNA Translation: AAF31167.1 Sequence problems.
DQ088979 mRNA Translation: AAZ66619.1
AK312366 mRNA Translation: BAG35284.1
AK295368 mRNA Translation: BAH12048.1
AK295470 mRNA Translation: BAH12079.1
AC110742 Genomic DNA No translation available.
AC118273 Genomic DNA No translation available.
CH471064 Genomic DNA Translation: EAW67858.1
CH471064 Genomic DNA Translation: EAW67861.1
CH471064 Genomic DNA Translation: EAW67857.1
CH471064 Genomic DNA Translation: EAW67859.1
BC025672 mRNA Translation: AAH25672.1
AF254358 mRNA Translation: AAF71358.1
AF254357 mRNA Translation: AAF71357.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS31493.1 [Q04609-8]
CCDS53627.1 [Q04609-9]
CCDS53628.1 [Q04609-7]
CCDS7946.1 [Q04609-1]

Protein sequence database of the Protein Information Resource

More...PIRi		A56881

NCBI Reference Sequences

More...RefSeqi		NP_001014986.1, NM_001014986.1 [Q04609-8]
NP_001180400.1, NM_001193471.1 [Q04609-7]
NP_001180401.1, NM_001193472.1 [Q04609-9]
NP_001180402.1, NM_001193473.1 [Q04609-10]
NP_004467.1, NM_004476.1 [Q04609-1]
XP_016872923.1, XM_017017434.1 [Q04609-7]
XP_016872924.1, XM_017017435.1 [Q04609-9]
XP_016872925.1, XM_017017436.1
XP_016872926.1, XM_017017437.1
XP_016872931.1, XM_017017442.1
XP_016872932.1, XM_017017443.1
XP_016872933.1, XM_017017444.1 [Q04609-10]
XP_016872934.1, XM_017017445.1 [Q04609-10]
XP_016872935.1, XM_017017446.1 [Q04609-10]
XP_016872936.1, XM_017017447.1 [Q04609-10]
XP_016872937.1, XM_017017448.1 [Q04609-10]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000256999; ENSP00000256999; ENSG00000086205 [Q04609-1]
ENST00000340334; ENSP00000344131; ENSG00000086205 [Q04609-7]
ENST00000356696; ENSP00000349129; ENSG00000086205 [Q04609-8]
ENST00000533034; ENSP00000431463; ENSG00000086205 [Q04609-9]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2346

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:2346

UCSC genome browser

More...UCSCi		uc001ngy.3 human [Q04609-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M99487 mRNA Translation: AAA60209.1
S76978 mRNA Translation: AAB33750.2
AF007544 Genomic DNA Translation: AAC83972.1
AF176574 mRNA Translation: AAD51121.1
EF488811 mRNA Translation: ABO93402.2
AY101595 mRNA Translation: AAM34479.1
AF107214 Genomic DNA Translation: AAF31167.1 Sequence problems.
DQ088979 mRNA Translation: AAZ66619.1
AK312366 mRNA Translation: BAG35284.1
AK295368 mRNA Translation: BAH12048.1
AK295470 mRNA Translation: BAH12079.1
AC110742 Genomic DNA No translation available.
AC118273 Genomic DNA No translation available.
CH471064 Genomic DNA Translation: EAW67858.1
CH471064 Genomic DNA Translation: EAW67861.1
CH471064 Genomic DNA Translation: EAW67857.1
CH471064 Genomic DNA Translation: EAW67859.1
BC025672 mRNA Translation: AAH25672.1
AF254358 mRNA Translation: AAF71358.1
AF254357 mRNA Translation: AAF71357.1
CCDSiCCDS31493.1 [Q04609-8]
CCDS53627.1 [Q04609-9]
CCDS53628.1 [Q04609-7]
CCDS7946.1 [Q04609-1]
PIRiA56881
RefSeqiNP_001014986.1, NM_001014986.1 [Q04609-8]
NP_001180400.1, NM_001193471.1 [Q04609-7]
NP_001180401.1, NM_001193472.1 [Q04609-9]
NP_001180402.1, NM_001193473.1 [Q04609-10]
NP_004467.1, NM_004476.1 [Q04609-1]
XP_016872923.1, XM_017017434.1 [Q04609-7]
XP_016872924.1, XM_017017435.1 [Q04609-9]
XP_016872925.1, XM_017017436.1
XP_016872926.1, XM_017017437.1
XP_016872931.1, XM_017017442.1
XP_016872932.1, XM_017017443.1
XP_016872933.1, XM_017017444.1 [Q04609-10]
XP_016872934.1, XM_017017445.1 [Q04609-10]
XP_016872935.1, XM_017017446.1 [Q04609-10]
XP_016872936.1, XM_017017447.1 [Q04609-10]
XP_016872937.1, XM_017017448.1 [Q04609-10]

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Z8LX-ray3.50A/B/C/D56-750[»]
2C6CX-ray2.00A44-750[»]
2C6GX-ray2.20A44-750[»]
2C6PX-ray2.39A44-750[»]
2CIJX-ray2.40A44-750[»]
2JBJX-ray2.19A44-750[»]
2JBKX-ray2.99A44-750[»]
2OOTX-ray1.64A44-750[»]
2OR4X-ray1.62A44-750[»]
2PVVX-ray2.11A44-750[»]
2PVWX-ray1.71A44-750[»]
2XEFX-ray1.59A44-750[»]
2XEGX-ray1.59A44-750[»]
2XEIX-ray1.69A44-750[»]
2XEJX-ray1.78A44-750[»]
3BHXX-ray1.60A44-750[»]
3BI0X-ray1.67A44-750[»]
3BI1X-ray1.50A44-750[»]
3BXMX-ray1.71A44-750[»]
3D7DX-ray1.69A44-750[»]
3D7FX-ray1.54A44-750[»]
3D7GX-ray1.75A44-750[»]
3D7HX-ray1.55A44-750[»]
3IWWX-ray2.30A44-750[»]
3RBUX-ray1.60A44-750[»]
3SJEX-ray1.70A44-750[»]
3SJFX-ray1.65A44-750[»]
3SJGX-ray1.65A44-750[»]
3SJXX-ray1.66A44-750[»]
4JYWX-ray1.73A44-750[»]
4JZ0X-ray1.83A44-750[»]
4LQGX-ray1.77A44-750[»]
4MCPX-ray1.65A44-750[»]
4MCQX-ray2.00A44-750[»]
4MCRX-ray1.65A44-750[»]
4MCSX-ray1.83A44-750[»]
4NGMX-ray1.84A44-750[»]
4NGNX-ray1.64A44-750[»]
4NGPX-ray1.63A44-750[»]
4NGQX-ray2.08A44-750[»]
4NGRX-ray1.90A44-750[»]
4NGSX-ray1.68A44-750[»]
4NGTX-ray2.31A44-750[»]
4OC0X-ray1.85A44-750[»]
4OC1X-ray1.75A44-750[»]
4OC2X-ray1.65A44-750[»]
4OC3X-ray1.79A44-750[»]
4OC4X-ray1.66A44-750[»]
4OC5X-ray1.70A44-750[»]
4OMEX-ray1.79A44-750[»]
4P44X-ray1.75A44-750[»]
4P45X-ray1.87A44-750[»]
4P4BX-ray1.93A44-750[»]
4P4DX-ray1.65A44-750[»]
4P4EX-ray1.67A44-750[»]
4P4FX-ray1.86A44-750[»]
4P4IX-ray1.87A44-750[»]
4P4JX-ray1.66A44-750[»]
4W9YX-ray1.64A44-750[»]
4X3RX-ray1.86A44-750[»]
5D29X-ray1.80A56-750[»]
5ELYX-ray1.81A55-750[»]
5F09X-ray1.85A44-750[»]
5O5RX-ray1.65A44-750[»]
5O5TX-ray1.43A44-750[»]
5O5UX-ray1.53A44-750[»]
5OF0X-ray1.48A44-750[»]
6ETYX-ray1.68A44-750[»]
6EZ9X-ray1.61A44-750[»]
6F5LX-ray1.63A44-750[»]
6FE5X-ray1.52A44-750[»]
6H7YX-ray1.81A44-750[»]
6H7ZX-ray2.00A44-750[»]
6HKJX-ray2.09A44-750[»]
6HKZX-ray2.09A44-750[»]
SMRiQ04609
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108630, 5 interactors
IntActiQ04609, 6 interactors
MINTiQ04609
STRINGi9606.ENSP00000256999

Chemistry databases

BindingDBiQ04609
ChEMBLiCHEMBL1892
DrugBankiDB06928 (2S)-2-{[HYDROXY(4-IODOBENZYL)PHOSPHORYL]METHYL}PENTANEDIOIC ACID
DB00089 Capromab
DB00142 L-Glutamic Acid
DB07754 N-({(1R)-1-carboxy-2-[(4-fluorobenzyl)sulfanyl]ethyl}carbamoyl)-L-glutamic acid
GuidetoPHARMACOLOGYi1606

Protein family/group databases

MEROPSiM28.010

PTM databases

iPTMnetiQ04609
PhosphoSitePlusiQ04609

Polymorphism and mutation databases

BioMutaiFOLH1
DMDMi548615

Proteomic databases

jPOSTiQ04609
MaxQBiQ04609
PaxDbiQ04609
PeptideAtlasiQ04609
PRIDEiQ04609
ProteomicsDBi58243
58244 [Q04609-3]
58245 [Q04609-4]
58246 [Q04609-6]
58247 [Q04609-7]
58248 [Q04609-8]
58249 [Q04609-9]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		2346
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000256999; ENSP00000256999; ENSG00000086205 [Q04609-1]
ENST00000340334; ENSP00000344131; ENSG00000086205 [Q04609-7]
ENST00000356696; ENSP00000349129; ENSG00000086205 [Q04609-8]
ENST00000533034; ENSP00000431463; ENSG00000086205 [Q04609-9]
GeneIDi2346
KEGGihsa:2346
UCSCiuc001ngy.3 human [Q04609-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2346
DisGeNETi2346

GeneCards: human genes, protein and diseases

More...GeneCardsi		FOLH1

H-Invitational Database, human transcriptome db

More...H-InvDBi		HIX0129475
HGNCiHGNC:3788 FOLH1
HPAiCAB001451
HPA010593
MIMi600934 gene
neXtProtiNX_Q04609
OpenTargetsiENSG00000086205
PharmGKBiPA28205

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG2195 Eukaryota
COG2234 LUCA
GeneTreeiENSGT00950000182766
HOGENOMiHOG000211921
InParanoidiQ04609
KOiK14592
OMAiHKYRDFQ
OrthoDBi633642at2759
PhylomeDBiQ04609
TreeFamiTF312981

Enzyme and pathway databases

BRENDAi3.4.17.21 2681
ReactomeiR-HSA-70614 Amino acid synthesis and interconversion (transamination)

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		FOLH1 human
EvolutionaryTraceiQ04609

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Glutamate_carboxypeptidase_II

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		2346

Protein Ontology

More...PROi		PR:Q04609

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000086205 Expressed in 149 organ(s), highest expression level in corpus callosum
ExpressionAtlasiQ04609 baseline and differential
GenevisibleiQ04609 HS

Family and domain databases

Gene3Di1.20.930.40, 1 hit
InterProiView protein in InterPro
IPR003137 PA_domain
IPR007484 Peptidase_M28
IPR039373 Peptidase_M28B
IPR007365 TFR-like_dimer_dom
IPR036757 TFR-like_dimer_dom_sf
PANTHERiPTHR10404 PTHR10404, 1 hit
PfamiView protein in Pfam
PF02225 PA, 1 hit
PF04389 Peptidase_M28, 1 hit
PF04253 TFR_dimer, 1 hit
SUPFAMiSSF47672 SSF47672, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFOLH1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q04609
Secondary accession number(s): A4UU12
, A9CB79, B7Z312, B7Z343, D3DQS5, E9PDX8, O43748, Q16305, Q541A4, Q8TAY3, Q9NP15, Q9NYE2, Q9P1P8
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: May 8, 2019
This is version 200 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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