FOLH1
entrez
2346
canonical
uniprot
Q04609
canonical
ensembl
ENSG00000086205
resolver
ensp
ENSP00000256999
resolver
ensp
ENSP00000344131
resolver
ensp
ENSP00000349129
resolver
ensp
ENSP00000431463
resolver
ensp
ENSP00000647996
resolver
genesymbol
FOLH1
resolver
genesymbol_syn
FOLH
resolver
genesymbol_syn
NAALAD1
resolver
genesymbol_syn
PSM
resolver
genesymbol_syn
PSMA
resolver
hgnc
HGNC:3788
resolver
uniprot
A4UU12
resolver
uniprot
A9CB79
resolver
uniprot
B7Z312
resolver
uniprot
B7Z343
resolver
uniprot
D3DQS5
resolver
uniprot
E9PDX8
resolver
uniprot
O43748
resolver
uniprot
Q16305
resolver
uniprot
Q541A4
resolver
uniprot
Q8TAY3
resolver
uniprot
Q9NP15
resolver
uniprot
Q9NYE2
resolver
uniprot
Q9P1P8
resolver
uniprot_entry
FOLH1_HUMAN
resolver
uniprot_sec
A4UU12
resolver
uniprot_sec
A9CB79
resolver
uniprot_sec
B7Z312
resolver
uniprot_sec
B7Z343
resolver
uniprot_sec
D3DQS5
resolver
uniprot_sec
E9PDX8
resolver
uniprot_sec
O43748
resolver
uniprot_sec
Q16305
resolver
uniprot_sec
Q541A4
resolver
uniprot_sec
Q8TAY3
resolver
uniprot_sec
Q9NP15
resolver
uniprot_sec
Q9NYE2
resolver
uniprot_sec
Q9P1P8
resolver
activity_regulation
ACTIVITY REGULATION: The NAALADase activity is inhibited by beta-NAAG, quisqualic acid, 2-(phosphonomethyl) pentanedioic acid (PMPA) and EDTA. Activated by cobalt. {ECO:0000269|PubMed:17567119}.
uniprot
proteins
amino_acid_sequence
MWNLLHETDSAVATARRPRWLCAGALVLAGGFFLLGFLFGWFIKSSNEATNITPKHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTHPNYISIINEDGNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIARYGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA
uniprot
proteins
ec_number
3.4.17.21
uniprot
proteins
function
FUNCTION: 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.; FUNCTION: Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC.
uniprot
proteins
mass_dalton
84331
uniprot
proteins
mutagenesis
MUTAGEN 51; /note="N->A: Loss of glycosylation. Reduces enzyme activity."; /evidence="ECO:0000269|PubMed:15152093"; MUTAGEN 76; /note="N->A: Loss of glycosylation. Reduces enzyme activity."; /evidence="ECO:0000269|PubMed:15152093"; MUTAGEN 121; /note="N->A: Loss of glycosylation. Severely reduced enzyme activity."; /evidence="ECO:0000269|PubMed:15152093"; MUTAGEN 140; /note="N->A: Loss of glycosylation. Severely reduced enzyme activity."; /evidence="ECO:0000269|PubMed:15152093"; MUTAGEN 153; /note="N->A: Loss of glycosylation. Severely reduced enzyme activity."; /evidence="ECO:0000269|PubMed:15152093"; MUTAGEN 195; /note="N->A: Loss of glycosylation. Severely reduced enzyme activity."; /evidence="ECO:0000269|PubMed:15152093"; MUTAGEN 336; /note="N->A: Loss of glycosylation. Reduces enzyme activity."; /evidence="ECO:0000269|PubMed:15152093"; MUTAGEN 377; /note="H->A,G,Q: Complete loss of activity."; /evidence="ECO:0000269|PubMed:9882712"; MUTAGEN 379; /note="D->E,N: Complete loss of activity."; /evidence="ECO:0000269|PubMed:9882712"; MUTAGEN 387; /note="D->E,L: Complete loss of activity."; /evidence="ECO:0000269|PubMed:9882712"; MUTAGEN 387; /note="D->N: No effect on enzyme activity."; /evidence="ECO:0000269|PubMed:9882712"; MUTAGEN 388; /note="P->A: No effect on enzyme activity."; /evidence="ECO:0000269|PubMed:9882712"; MUTAGEN 424; /note="E->A: Complete loss of activity."; /evidence="ECO:0000269|PubMed:19301871"; MUTAGEN 424; /note="E->D: Reduces enzyme activity."; /evidence="ECO:0000269|PubMed:19301871"; MUTAGEN 424; /note="E->Q: Reduces enzyme activity."; /evidence="ECO:0000269|PubMed:19301871"; MUTAGEN 425; /note="E->Q,D: Complete loss of activity."; /evidence="ECO:0000269|PubMed:9882712"; MUTAGEN 453; /note="D->N,L: Complete loss of activity."; /evidence="ECO:0000269|PubMed:9882712"; MUTAGEN 453; /note="D->Q: Reduces enzyme activity."; /evidence="ECO:0000269|PubMed:9882712"; MUTAGEN 454; /note="S->A: Reduces enzyme activity."; /evidence="ECO:0000269|PubMed:9882712"; MUTAGEN 459; /note="N->A: Loss of glycosylation. Reduces enzyme activity."; /evidence="ECO:0000269|PubMed:15152093"; MUTAGEN 476; /note="N->A: Loss of glycosylation. Reduces enzyme activity."; /evidence="ECO:0000269|PubMed:15152093"; MUTAGEN 638; /note="N->A: Loss of glycosylation. Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:15152093"; MUTAGEN 640; /note="T->A: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:15152093
uniprot
proteins
post_translational_modification
PTM: The first two amino acids at the N-terminus of isoform PSMA' appear to be cleaved by limited proteolysis.; PTM: The N-terminus is blocked.
uniprot
proteins
protein_family
M28B subfamily
uniprot
proteins
protein_family
Peptidase M28 family
uniprot
proteins
pubmed
10085079
uniprot
proteins
pubmed
11092759
uniprot
proteins
pubmed
12754519
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14716746
uniprot
proteins
pubmed
15152093
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16467855
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
16555021
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17150306
uniprot
proteins
pubmed
17372356
uniprot
proteins
pubmed
17567119
uniprot
proteins
pubmed
17929272
uniprot
proteins
pubmed
18234225
uniprot
proteins
pubmed
19053759
uniprot
proteins
pubmed
19301871
uniprot
proteins
pubmed
7882349
uniprot
proteins
pubmed
8417812
uniprot
proteins
pubmed
9187245
uniprot
proteins
pubmed
9622670
uniprot
proteins
pubmed
9694964
uniprot
proteins
pubmed
9809977
uniprot
proteins
pubmed
9838072
uniprot
proteins
pubmed
9882712
uniprot
proteins
sequence_length
750
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9809977}; Single-pass type II membrane protein {ECO:0000269|PubMed:9809977}.; SUBCELLULAR LOCATION: [Isoform PSMA']: Cytoplasm {ECO:0000269|PubMed:9809977}.
uniprot
proteins
transmembrane_region
TRANSMEM 20..43; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000305
uniprot
proteins