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Protein

Glutamate carboxypeptidase 2

Gene

FOLH1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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.

Catalytic activityi

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

Cofactori

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

Activity regulationi

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

pH dependencei

Stable at pH greater than 6.5.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei210SubstrateCombined sources6 Publications1
Binding sitei257SubstrateCombined sources6 Publications1
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
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

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

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

Protein family/group databases

MEROPSiM28.010

Names & Taxonomyi

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
Gene namesi
Name:FOLH1
Synonyms:FOLH, NAALAD1, PSM, PSMA
ORF Names:GIG27
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000086205.16
HGNCiHGNC:3788 FOLH1
MIMi600934 gene
neXtProtiNX_Q04609

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; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 19CytoplasmicCuratedAdd BLAST19
Transmembranei20 – 43Helical; Signal-anchor for type II membrane proteinCuratedAdd BLAST24
Topological domaini44 – 750ExtracellularCuratedAdd BLAST707

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

DisGeNETi2346
OpenTargetsiENSG00000086205
PharmGKBiPA28205

Chemistry databases

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

Polymorphism and mutation databases

BioMutaiFOLH1
DMDMi548615

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001741171 – 750Glutamate carboxypeptidase 2Add BLAST750

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei10PhosphoserineBy similarity1
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

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

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

PTM databases

GlyConnecti1272
iPTMnetiQ04609
PhosphoSitePlusiQ04609

Expressioni

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

Inductioni

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

Gene expression databases

BgeeiENSG00000086205 Expressed in 149 organ(s), highest expression level in corpus callosum
CleanExiHS_FOLH1
ExpressionAtlasiQ04609 baseline and differential
GenevisibleiQ04609 HS

Organism-specific databases

HPAiCAB001451
HPA010593

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

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

Chemistry databases

BindingDBiQ04609

Structurei

Secondary structure

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

3D structure databases

ProteinModelPortaliQ04609
SMRiQ04609
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04609

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Compositional biasi146 – 149Poly-ProSequence analysis4

Domaini

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

Sequence similaritiesi

Belongs to the peptidase M28 family. M28B subfamily.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2195 Eukaryota
COG2234 LUCA
GeneTreeiENSGT00550000074421
HOGENOMiHOG000211921
HOVERGENiHBG051639
InParanoidiQ04609
KOiK14592
OMAiYHRTMAQ
OrthoDBiEOG091G02ZM
PhylomeDBiQ04609
TreeFamiTF312981

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

Sequences (8+)i

Sequence statusi: Complete.

This entry describes 8 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
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

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:
E9PLV0E9PLV0_HUMAN
Glutamate carboxypeptidase 2
FOLH1
48Annotation score:
E9PI29E9PI29_HUMAN
Glutamate carboxypeptidase 2
FOLH1
46Annotation score:
E9PKM3E9PKM3_HUMAN
Glutamate carboxypeptidase 2
FOLH1
64Annotation score:

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti194I → V in AAZ66619 (Ref. 9) Curated1
Sequence conflicti354R → K AA sequence (PubMed:8417812).Curated1
Sequence conflicti398I → N in ABO93402 (PubMed:17929272).Curated1

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
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
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:
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]
UniGeneiHs.551896
Hs.645352
Hs.654487

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]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

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]
UniGeneiHs.551896
Hs.645352
Hs.654487

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[»]
ProteinModelPortaliQ04609
SMRiQ04609
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108630, 5 interactors
IntActiQ04609, 5 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

GlyConnecti1272
iPTMnetiQ04609
PhosphoSitePlusiQ04609

Polymorphism and mutation databases

BioMutaiFOLH1
DMDMi548615

Proteomic databases

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

DNASUi2346
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

CTDi2346
DisGeNETi2346
EuPathDBiHostDB:ENSG00000086205.16
GeneCardsiFOLH1
H-InvDBiHIX0129475
HGNCiHGNC:3788 FOLH1
HPAiCAB001451
HPA010593
MIMi600934 gene
neXtProtiNX_Q04609
OpenTargetsiENSG00000086205
PharmGKBiPA28205
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2195 Eukaryota
COG2234 LUCA
GeneTreeiENSGT00550000074421
HOGENOMiHOG000211921
HOVERGENiHBG051639
InParanoidiQ04609
KOiK14592
OMAiYHRTMAQ
OrthoDBiEOG091G02ZM
PhylomeDBiQ04609
TreeFamiTF312981

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiFOLH1 human
EvolutionaryTraceiQ04609
GeneWikiiGlutamate_carboxypeptidase_II
GenomeRNAii2346
PROiPR:Q04609
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000086205 Expressed in 149 organ(s), highest expression level in corpus callosum
CleanExiHS_FOLH1
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
ProtoNetiSearch...

Entry informationi

Entry nameiFOLH1_HUMAN
AccessioniPrimary (citable) accession number: Q04609
Secondary accession number(s): A4UU12
, A9CB79, B7Z312, B7Z343, D3DQS5, E9PDX8, O43748, Q16305, Q541A4, Q8TAY3, Q9NP15, Q9NYE2, Q9P1P8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 7, 2018
This is version 195 of the entry and version 1 of the sequence. See complete history.
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.

Miscellaneousi

Keywords - Technical termi

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

Documents

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

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