UniProtKB - Q04609 (FOLH1_HUMAN)
Glutamate carboxypeptidase 2
FOLH1
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
Catalytic activityi
- Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates. EC:3.4.17.21
Cofactori
Activity regulationi
pH dependencei
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 210 | SubstrateCombined sources6 Publications | 1 | |
Binding sitei | 257 | SubstrateCombined sources6 Publications | 1 | |
Metal bindingi | 269 | CalciumCombined sources6 Publications | 1 | |
Metal bindingi | 272 | Calcium; via carbonyl oxygenCombined sources6 Publications | 1 | |
Metal bindingi | 377 | Zinc 1; via tele nitrogen; catalyticCombined sources6 Publications | 1 | |
Metal bindingi | 387 | Zinc 1; catalyticCombined sources6 Publications | 1 | |
Metal bindingi | 387 | Zinc 2Combined sources6 Publications | 1 | |
Active sitei | 424 | Nucleophile; for NAALADase activity | 1 | |
Binding sitei | 424 | SubstrateBy similarity | 1 | |
Metal bindingi | 425 | Zinc 2Combined sources6 Publications | 1 | |
Metal bindingi | 433 | CalciumCombined sources6 Publications | 1 | |
Metal bindingi | 436 | CalciumCombined sources6 Publications | 1 | |
Metal bindingi | 453 | Zinc 1; catalyticCombined sources6 Publications | 1 | |
Binding sitei | 519 | SubstrateCombined sources6 Publications | 1 | |
Binding sitei | 552 | SubstrateCombined sources6 Publications | 1 | |
Metal bindingi | 553 | Zinc 2; via tele nitrogenCombined sources6 Publications | 1 | |
Active sitei | 628 | Charge relay systemSequence analysis | 1 | |
Active sitei | 666 | Charge relay systemSequence analysis | 1 | |
Active sitei | 689 | Charge relay systemSequence analysis | 1 |
GO - Molecular functioni
- Ac-Asp-Glu binding Source: BHF-UCL
- carboxypeptidase activity Source: GO_Central
- dipeptidase activity Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
- metallocarboxypeptidase activity Source: BHF-UCL
- peptidase activity Source: UniProtKB
- tetrahydrofolyl-poly(glutamate) polymer binding Source: BHF-UCL
GO - Biological processi
- C-terminal protein deglutamylation Source: BHF-UCL
- folic acid-containing compound metabolic process Source: Ensembl
- proteolysis Source: BHF-UCL
Keywordsi
Molecular function | Carboxypeptidase, Dipeptidase, Hydrolase, Metalloprotease, Multifunctional enzyme, Protease |
Ligand | Calcium, Metal-binding, Zinc |
Enzyme and pathway databases
BRENDAi | 3.4.17.21, 2681 |
PathwayCommonsi | Q04609 |
Reactomei | R-HSA-8963693, Aspartate and asparagine metabolism |
SignaLinki | Q04609 |
Protein family/group databases
MEROPSi | M28.010 |
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 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:3788, FOLH1 |
MIMi | 600934, gene |
neXtProti | NX_Q04609 |
VEuPathDBi | HostDB:ENSG00000086205 |
Subcellular locationi
Plasma membrane
- Cell membrane 1 Publication; Single-pass type II membrane protein 1 Publication
Cytoplasm and Cytosol
- Cytoplasm 1 Publication
Extracellular region or secreted
- extracellular exosome Source: UniProtKB
Plasma Membrane
- integral component of plasma membrane Source: ProtInc
- plasma membrane Source: BHF-UCL
Other locations
- cell surface Source: BHF-UCL
- cytoplasm Source: UniProtKB-SubCell
- membrane Source: ProtInc
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 19 | CytoplasmicCuratedAdd BLAST | 19 | |
Transmembranei | 20 – 43 | Helical; Signal-anchor for type II membrane proteinCuratedAdd BLAST | 24 | |
Topological domaini | 44 – 750 | ExtracellularCuratedAdd BLAST | 707 |
Keywords - Cellular componenti
Cell membrane, Cytoplasm, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 51 | N → A: Loss of glycosylation. Reduces enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 76 | N → A: Loss of glycosylation. Reduces enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 121 | N → A: Loss of glycosylation. Severely reduced enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 140 | N → A: Loss of glycosylation. Severely reduced enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 153 | N → A: Loss of glycosylation. Severely reduced enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 195 | N → A: Loss of glycosylation. Severely reduced enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 336 | N → A: Loss of glycosylation. Reduces enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 377 | H → A, G or Q: Complete loss of activity. 1 Publication | 1 | |
Mutagenesisi | 379 | D → E or N: Complete loss of activity. 1 Publication | 1 | |
Mutagenesisi | 387 | D → E or L: Complete loss of activity. 1 Publication | 1 | |
Mutagenesisi | 387 | D → N: No effect on enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 388 | P → A: No effect on enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 424 | E → A: Complete loss of activity. 1 Publication | 1 | |
Mutagenesisi | 424 | E → D: Reduces enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 424 | E → Q: Reduces enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 425 | E → Q or D: Complete loss of activity. 1 Publication | 1 | |
Mutagenesisi | 453 | D → N or L: Complete loss of activity. 1 Publication | 1 | |
Mutagenesisi | 453 | D → Q: Reduces enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 454 | S → A: Reduces enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 459 | N → A: Loss of glycosylation. Reduces enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 476 | N → A: Loss of glycosylation. Reduces enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 638 | N → A: Loss of glycosylation. Abolishes enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 640 | T → A: Abolishes enzyme activity. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 2346 |
OpenTargetsi | ENSG00000086205 |
PharmGKBi | PA28205 |
Miscellaneous databases
Pharosi | Q04609, Tclin |
Chemistry databases
ChEMBLi | CHEMBL1892 |
DrugBanki | DB06928, (2S)-2-{[HYDROXY(4-IODOBENZYL)PHOSPHORYL]METHYL}PENTANEDIOIC ACID DB00089, Capromab pendetide DB07754, DCFBC DB00142, Glutamic acid DB14805, Piflufolastat F 18 DB08835, Spaglumic acid |
GuidetoPHARMACOLOGYi | 1606 |
Genetic variation databases
BioMutai | FOLH1 |
DMDMi | 548615 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000174117 | 1 – 750 | Glutamate carboxypeptidase 2Add BLAST | 750 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 10 | PhosphoserineBy similarity | 1 | |
Glycosylationi | 51 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 76 | N-linked (GlcNAc...) asparagineCombined sources8 Publications | 1 | |
Glycosylationi | 121 | N-linked (GlcNAc...) asparagineCombined sources7 Publications | 1 | |
Glycosylationi | 140 | N-linked (GlcNAc...) asparagineCombined sources7 Publications | 1 | |
Glycosylationi | 153 | N-linked (GlcNAc...) asparagineCombined sources1 Publication | 1 | |
Glycosylationi | 195 | N-linked (GlcNAc...) asparagineCombined sources7 Publications | 1 | |
Glycosylationi | 336 | N-linked (GlcNAc...) asparagine2 Publications | 1 | |
Glycosylationi | 459 | N-linked (GlcNAc...) asparagineCombined sources8 Publications | 1 | |
Glycosylationi | 476 | N-linked (GlcNAc...) asparagineCombined sources8 Publications | 1 | |
Glycosylationi | 638 | N-linked (GlcNAc...) asparagineCombined sources8 Publications | 1 |
Post-translational modificationi
Keywords - PTMi
Glycoprotein, PhosphoproteinProteomic databases
CPTACi | CPTAC-1491 |
jPOSTi | Q04609 |
MassIVEi | Q04609 |
MaxQBi | Q04609 |
PaxDbi | Q04609 |
PeptideAtlasi | Q04609 |
PRIDEi | Q04609 |
ProteomicsDBi | 58243 [Q04609-1] 58244 [Q04609-3] 58245 [Q04609-4] 58246 [Q04609-6] 58247 [Q04609-7] 58248 [Q04609-8] 58249 [Q04609-9] 6482 |
PTM databases
GlyGeni | Q04609, 13 sites |
iPTMneti | Q04609 |
PhosphoSitePlusi | Q04609 |
SwissPalmi | Q04609 |
Expressioni
Tissue specificityi
Inductioni
Gene expression databases
Bgeei | ENSG00000086205, Expressed in corpus callosum and 164 other tissues |
ExpressionAtlasi | Q04609, baseline and differential |
Genevisiblei | Q04609, HS |
Organism-specific databases
HPAi | ENSG00000086205, Tissue enhanced (intestine, prostate) |
Interactioni
Subunit structurei
Homodimer.
2 PublicationsBinary interactionsi
Isoform PSMA-8 [Q04609-8]
With | #Exp. | IntAct |
---|---|---|
TTMP [Q5BVD1] | 3 | EBI-13060980,EBI-10243654 |
Protein-protein interaction databases
BioGRIDi | 108630, 21 interactors |
IntActi | Q04609, 7 interactors |
MINTi | Q04609 |
STRINGi | 9606.ENSP00000256999 |
Chemistry databases
BindingDBi | Q04609 |
Miscellaneous databases
RNActi | Q04609, protein |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | Q04609 |
SMRi | Q04609 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q04609 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 274 – 587 | NAALADaseAdd BLAST | 314 | |
Regioni | 517 – 518 | Substrate bindingBy similarity | 2 | |
Regioni | 534 – 536 | Substrate bindingCombined sources2 Publications | 3 | |
Regioni | 552 – 553 | Substrate bindingBy similarity | 2 | |
Regioni | 699 – 700 | Substrate bindingCombined sources5 Publications | 2 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Signal-anchor, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG2195, Eukaryota |
GeneTreei | ENSGT01030000234598 |
HOGENOMi | CLU_005688_3_2_1 |
InParanoidi | Q04609 |
OMAi | VFAPGIW |
OrthoDBi | 633642at2759 |
PhylomeDBi | Q04609 |
TreeFami | TF312981 |
Family and domain databases
Gene3Di | 1.20.930.40, 1 hit |
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 |
PANTHERi | PTHR10404, PTHR10404, 1 hit |
Pfami | View protein in Pfam PF02225, PA, 1 hit PF04389, Peptidase_M28, 1 hit PF04253, TFR_dimer, 1 hit |
SUPFAMi | SSF47672, SSF47672, 1 hit |
s (8+)i Sequence
Sequence statusi: Complete.
This entry describes 8 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 8 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
The sequence of this isoform differs from the canonical sequence as follows:
1-585: Missing.
657-750: NPIVLRMMND...AAAETLSEVA → MSSMLQAATT...KWTLPRPGEK
The sequence of this isoform differs from the canonical sequence as follows:
1-159: Missing.
214-243: VKNAQLAGAKGVILYSDPADYFAPGVKSYP → NMLIGVELQRLLVFQVFLFIQLDTMMHRSS
244-750: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
1-57: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
1-39: MWNLLHETDSAVATARRPRWLCAGALVLAGGFFLLGFLF → MTAGSSYPLFLAAYACTGCLAERL
The sequence of this isoform differs from the canonical sequence as follows:
657-688: NPIVLRMMNDQLMFLERAFIDPLGLPDRPFYR → K
The sequence of this isoform differs from the canonical sequence as follows:
1-39: MWNLLHETDSAVATARRPRWLCAGALVLAGGFFLLGFLF → MTAGSSYPLFLAAYACTGCLAERL
657-688: NPIVLRMMNDQLMFLERAFIDPLGLPDRPFYR → K
The sequence of this isoform differs from the canonical sequence as follows:
1-308: Missing.
Computationally mapped potential isoform sequencesi
There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketE9PMK6 | E9PMK6_HUMAN | Glutamate carboxypeptidase 2 | FOLH1 | 74 | Annotation score: | ||
E9PI29 | E9PI29_HUMAN | Glutamate carboxypeptidase 2 | FOLH1 | 46 | Annotation score: | ||
E9PLV0 | E9PLV0_HUMAN | Glutamate carboxypeptidase 2 | FOLH1 | 48 | Annotation score: | ||
E9PKM3 | E9PKM3_HUMAN | Glutamate carboxypeptidase 2 | FOLH1 | 64 | Annotation score: |
Sequence cautioni
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 194 | I → V in AAZ66619 (Ref. 9) Curated | 1 | |
Sequence conflicti | 354 | R → K AA sequence (PubMed:8417812).Curated | 1 | |
Sequence conflicti | 398 | I → N in ABO93402 (PubMed:17929272).Curated | 1 |
Polymorphismi
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_036398 | 23 | A → T in a colorectal cancer sample; somatic mutation. 1 Publication | 1 | |
Natural variantiVAR_024592 | 75 | Y → H1 PublicationCorresponds to variant dbSNP:rs202676Ensembl. | 1 | |
Natural variantiVAR_012736 | 475 | H → Y Can be associated with lower folate and higher homocysteine levels. 1 PublicationCorresponds to variant dbSNP:rs61886492Ensembl. | 1 | |
Natural variantiVAR_028882 | 627 | V → L. Corresponds to variant dbSNP:rs2988342Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_040242 | 1 – 585 | Missing in isoform PSMA-3. CuratedAdd BLAST | 585 | |
Alternative sequenceiVSP_044287 | 1 – 308 | Missing in isoform 10. 1 PublicationAdd BLAST | 308 | |
Alternative sequenceiVSP_040241 | 1 – 159 | Missing in isoform PSMA-4. CuratedAdd BLAST | 159 | |
Alternative sequenceiVSP_005336 | 1 – 57 | Missing in isoform PSMA'. 1 PublicationAdd BLAST | 57 | |
Alternative sequenceiVSP_038058 | 1 – 39 | MWNLL…LGFLF → MTAGSSYPLFLAAYACTGCL AERL in isoform PSMA-7 and isoform PSMA-9. 2 PublicationsAdd BLAST | 39 | |
Alternative sequenceiVSP_040243 | 214 – 243 | VKNAQ…VKSYP → NMLIGVELQRLLVFQVFLFI QLDTMMHRSS in isoform PSMA-4. CuratedAdd BLAST | 30 | |
Alternative sequenceiVSP_040244 | 244 – 750 | Missing in isoform PSMA-4. CuratedAdd BLAST | 507 | |
Alternative sequenceiVSP_040245 | 657 – 750 | NPIVL…LSEVA → MSSMLQAATTSMQGSHSQEF MMLCLILKAKWTLPRPGEK in isoform PSMA-3. CuratedAdd BLAST | 94 | |
Alternative sequenceiVSP_038059 | 657 – 688 | NPIVL…RPFYR → K in isoform PSMA-8 and isoform PSMA-9. 3 PublicationsAdd BLAST | 32 |
Sequence databases
Genome annotation databases
Ensembli | ENST00000256999.7; ENSP00000256999.2; ENSG00000086205.18 ENST00000340334.11; ENSP00000344131.7; ENSG00000086205.18 [Q04609-7] ENST00000356696.7; ENSP00000349129.3; ENSG00000086205.18 [Q04609-8] ENST00000533034.1; ENSP00000431463.1; ENSG00000086205.18 [Q04609-9] |
GeneIDi | 2346 |
KEGGi | hsa:2346 |
MANE-Selecti | ENST00000256999.7; ENSP00000256999.2; NM_004476.3; NP_004467.1 |
UCSCi | uc001ngy.3, human [Q04609-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1Z8L | X-ray | 3.50 | A/B/C/D | 56-750 | [»] | |
2C6C | X-ray | 2.00 | A | 44-750 | [»] | |
2C6G | X-ray | 2.20 | A | 44-750 | [»] | |
2C6P | X-ray | 2.39 | A | 44-750 | [»] | |
2CIJ | X-ray | 2.40 | A | 44-750 | [»] | |
2JBJ | X-ray | 2.19 | A | 44-750 | [»] | |
2JBK | X-ray | 2.99 | A | 44-750 | [»] | |
2OOT | X-ray | 1.64 | A | 44-750 | [»] | |
2OR4 | X-ray | 1.62 | A | 44-750 | [»] | |
2PVV | X-ray | 2.11 | A | 44-750 | [»] | |
2PVW | X-ray | 1.71 | A | 44-750 | [»] | |
2XEF | X-ray | 1.59 | A | 44-750 | [»] | |
2XEG | X-ray | 1.59 | A | 44-750 | [»] | |
2XEI | X-ray | 1.69 | A | 44-750 | [»] | |
2XEJ | X-ray | 1.78 | A | 44-750 | [»] | |
3BHX | X-ray | 1.60 | A | 44-750 | [»] | |
3BI0 | X-ray | 1.67 | A | 44-750 | [»] | |
3BI1 | X-ray | 1.50 | A | 44-750 | [»] | |
3BXM | X-ray | 1.71 | A | 44-750 | [»] | |
3D7D | X-ray | 1.69 | A | 44-750 | [»] | |
3D7F | X-ray | 1.54 | A | 44-750 | [»] | |
3D7G | X-ray | 1.75 | A | 44-750 | [»] | |
3D7H | X-ray | 1.55 | A | 44-750 | [»] | |
3IWW | X-ray | 2.30 | A | 44-750 | [»] | |
3RBU | X-ray | 1.60 | A | 44-750 | [»] | |
3SJE | X-ray | 1.70 | A | 44-750 | [»] | |
3SJF | X-ray | 1.65 | A | 44-750 | [»] | |
3SJG | X-ray | 1.65 | A | 44-750 | [»] | |
3SJX | X-ray | 1.66 | A | 44-750 | [»] | |
4JYW | X-ray | 1.73 | A | 44-750 | [»] | |
4JZ0 | X-ray | 1.83 | A | 44-750 | [»] | |
4LQG | X-ray | 1.77 | A | 44-750 | [»] | |
4MCP | X-ray | 1.65 | A | 44-750 | [»] | |
4MCQ | X-ray | 2.00 | A | 44-750 | [»] | |
4MCR | X-ray | 1.65 | A | 44-750 | [»] | |
4MCS | X-ray | 1.83 | A | 44-750 | [»] | |
4NGM | X-ray | 1.84 | A | 44-750 | [»] | |
4NGN | X-ray | 1.64 | A | 44-750 | [»] | |
4NGP | X-ray | 1.63 | A | 44-750 | [»] | |
4NGQ | X-ray | 2.08 | A | 44-750 | [»] | |
4NGR | X-ray | 1.90 | A | 44-750 | [»] | |
4NGS | X-ray | 1.68 | A | 44-750 | [»] | |
4NGT | X-ray | 2.31 | A | 44-750 | [»] | |
4OC0 | X-ray | 1.85 | A | 44-750 | [»] | |
4OC1 | X-ray | 1.75 | A | 44-750 | [»] | |
4OC2 | X-ray | 1.65 | A | 44-750 | [»] | |
4OC3 | X-ray | 1.79 | A | 44-750 | [»] | |
4OC4 | X-ray | 1.66 | A | 44-750 | [»] | |
4OC5 | X-ray | 1.70 | A | 44-750 | [»] | |
4OME | X-ray | 1.79 | A | 44-750 | [»] | |
4P44 | X-ray | 1.75 | A | 44-750 | [»] | |
4P45 | X-ray | 1.87 | A | 44-750 | [»] | |
4P4B | X-ray | 1.93 | A | 44-750 | [»] | |
4P4D | X-ray | 1.65 | A | 44-750 | [»] | |
4P4E | X-ray | 1.67 | A | 44-750 | [»] | |
4P4F | X-ray | 1.86 | A | 44-750 | [»] | |
4P4I | X-ray | 1.87 | A | 44-750 | [»] | |
4P4J | X-ray | 1.66 | A | 44-750 | [»] | |
4W9Y | X-ray | 1.64 | A | 44-750 | [»] | |
4X3R | X-ray | 1.86 | A | 44-750 | [»] | |
5D29 | X-ray | 1.80 | A | 56-750 | [»] | |
5ELY | X-ray | 1.81 | A | 55-750 | [»] | |
5F09 | X-ray | 1.85 | A | 44-750 | [»] | |
5O5R | X-ray | 1.65 | A | 44-750 | [»] | |
5O5T | X-ray | 1.43 | A | 44-750 | [»] | |
5O5U | X-ray | 1.53 | A | 44-750 | [»] | |
5OF0 | X-ray | 1.48 | A | 44-750 | [»] | |
6ETY | X-ray | 1.68 | A | 44-750 | [»] | |
6EZ9 | X-ray | 1.61 | A | 44-750 | [»] | |
6F5L | X-ray | 1.63 | A | 44-750 | [»] | |
6FE5 | X-ray | 1.52 | A | 44-750 | [»] | |
6H7Y | X-ray | 1.81 | A | 44-750 | [»] | |
6H7Z | X-ray | 2.00 | A | 44-750 | [»] | |
6HKJ | X-ray | 2.09 | A | 44-750 | [»] | |
6HKZ | X-ray | 2.09 | A | 44-750 | [»] | |
6RBC | X-ray | 1.77 | A | 44-750 | [»] | |
6RTI | X-ray | 2.20 | A | 44-750 | [»] | |
6S1X | X-ray | 1.76 | A | 44-750 | [»] | |
6SGP | X-ray | 1.58 | A | 44-750 | [»] | |
6SKH | X-ray | 1.58 | A | 44-750 | [»] | |
7BFZ | X-ray | 1.73 | A | 44-750 | [»] | |
AlphaFoldDBi | Q04609 | |||||
SMRi | Q04609 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 108630, 21 interactors |
IntActi | Q04609, 7 interactors |
MINTi | Q04609 |
STRINGi | 9606.ENSP00000256999 |
Chemistry databases
BindingDBi | Q04609 |
ChEMBLi | CHEMBL1892 |
DrugBanki | DB06928, (2S)-2-{[HYDROXY(4-IODOBENZYL)PHOSPHORYL]METHYL}PENTANEDIOIC ACID DB00089, Capromab pendetide DB07754, DCFBC DB00142, Glutamic acid DB14805, Piflufolastat F 18 DB08835, Spaglumic acid |
GuidetoPHARMACOLOGYi | 1606 |
Protein family/group databases
MEROPSi | M28.010 |
PTM databases
GlyGeni | Q04609, 13 sites |
iPTMneti | Q04609 |
PhosphoSitePlusi | Q04609 |
SwissPalmi | Q04609 |
Genetic variation databases
BioMutai | FOLH1 |
DMDMi | 548615 |
Proteomic databases
CPTACi | CPTAC-1491 |
jPOSTi | Q04609 |
MassIVEi | Q04609 |
MaxQBi | Q04609 |
PaxDbi | Q04609 |
PeptideAtlasi | Q04609 |
PRIDEi | Q04609 |
ProteomicsDBi | 58243 [Q04609-1] 58244 [Q04609-3] 58245 [Q04609-4] 58246 [Q04609-6] 58247 [Q04609-7] 58248 [Q04609-8] 58249 [Q04609-9] 6482 |
Protocols and materials databases
ABCDi | Q04609, 27 sequenced antibodies |
Antibodypediai | 2262, 1311 antibodies from 41 providers |
DNASUi | 2346 |
Genome annotation databases
Ensembli | ENST00000256999.7; ENSP00000256999.2; ENSG00000086205.18 ENST00000340334.11; ENSP00000344131.7; ENSG00000086205.18 [Q04609-7] ENST00000356696.7; ENSP00000349129.3; ENSG00000086205.18 [Q04609-8] ENST00000533034.1; ENSP00000431463.1; ENSG00000086205.18 [Q04609-9] |
GeneIDi | 2346 |
KEGGi | hsa:2346 |
MANE-Selecti | ENST00000256999.7; ENSP00000256999.2; NM_004476.3; NP_004467.1 |
UCSCi | uc001ngy.3, human [Q04609-1] |
Organism-specific databases
CTDi | 2346 |
DisGeNETi | 2346 |
GeneCardsi | FOLH1 |
HGNCi | HGNC:3788, FOLH1 |
HPAi | ENSG00000086205, Tissue enhanced (intestine, prostate) |
MIMi | 600934, gene |
neXtProti | NX_Q04609 |
OpenTargetsi | ENSG00000086205 |
PharmGKBi | PA28205 |
VEuPathDBi | HostDB:ENSG00000086205 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG2195, Eukaryota |
GeneTreei | ENSGT01030000234598 |
HOGENOMi | CLU_005688_3_2_1 |
InParanoidi | Q04609 |
OMAi | VFAPGIW |
OrthoDBi | 633642at2759 |
PhylomeDBi | Q04609 |
TreeFami | TF312981 |
Enzyme and pathway databases
BRENDAi | 3.4.17.21, 2681 |
PathwayCommonsi | Q04609 |
Reactomei | R-HSA-8963693, Aspartate and asparagine metabolism |
SignaLinki | Q04609 |
Miscellaneous databases
BioGRID-ORCSi | 2346, 19 hits in 1068 CRISPR screens |
ChiTaRSi | FOLH1, human |
EvolutionaryTracei | Q04609 |
GeneWikii | Glutamate_carboxypeptidase_II |
GenomeRNAii | 2346 |
Pharosi | Q04609, Tclin |
PROi | PR:Q04609 |
RNActi | Q04609, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000086205, Expressed in corpus callosum and 164 other tissues |
ExpressionAtlasi | Q04609, baseline and differential |
Genevisiblei | Q04609, HS |
Family and domain databases
Gene3Di | 1.20.930.40, 1 hit |
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 |
PANTHERi | PTHR10404, PTHR10404, 1 hit |
Pfami | View protein in Pfam PF02225, PA, 1 hit PF04389, Peptidase_M28, 1 hit PF04253, TFR_dimer, 1 hit |
SUPFAMi | SSF47672, SSF47672, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | FOLH1_HUMAN | |
Accessioni | Q04609Primary (citable) accession number: Q04609 Secondary accession number(s): A4UU12 Q9P1P8 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 1, 1994 |
Last sequence update: | June 1, 1994 | |
Last modified: | May 25, 2022 | |
This is version 217 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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, Direct protein sequencing, Reference proteomeDocuments
- Peptidase families
Classification of peptidase families and list of entries - Human chromosome 11
Human chromosome 11: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families