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Q04609

- FOLH1_HUMAN

UniProt

Q04609 - FOLH1_HUMAN

Protein

Glutamate carboxypeptidase 2

Gene

FOLH1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    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. Isoform PSM-4 and isoform PSM-5 would appear to be physiologically irrelevant. Involved in prostate tumor progression.
    Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC.

    Catalytic activityi

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

    Cofactori

    Binds 2 zinc ions per subunit. Required for NAALADase activity.1 Publication

    Enzyme 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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei210 – 2101Substrate1 Publication
    Binding sitei257 – 2571Substrate1 Publication
    Metal bindingi269 – 2691Calcium1 Publication
    Metal bindingi272 – 2721Calcium; via carbonyl oxygen1 Publication
    Metal bindingi377 – 3771Zinc 1
    Metal bindingi387 – 3871Zinc 1
    Metal bindingi387 – 3871Zinc 2
    Active sitei424 – 4241For NAALADase activity
    Metal bindingi425 – 4251Zinc 2
    Metal bindingi433 – 4331Calcium1 Publication
    Metal bindingi436 – 4361Calcium1 Publication
    Metal bindingi453 – 4531Zinc 1
    Binding sitei519 – 5191Substrate1 Publication
    Binding sitei552 – 5521Substrate1 Publication
    Metal bindingi553 – 5531Zinc 2
    Active sitei628 – 6281Charge relay systemSequence Analysis
    Active sitei666 – 6661Charge relay systemSequence Analysis
    Active sitei689 – 6891Charge relay systemSequence Analysis

    GO - Molecular functioni

    1. carboxypeptidase activity Source: UniProtKB-KW
    2. dipeptidase activity Source: UniProtKB-KW
    3. metal ion binding Source: UniProtKB-KW
    4. metallopeptidase activity Source: UniProtKB-KW
    5. peptidase activity Source: UniProtKB

    GO - Biological processi

    1. folic acid-containing compound metabolic process Source: Ensembl
    2. proteolysis Source: UniProtKB

    Keywords - Molecular functioni

    Carboxypeptidase, Dipeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    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
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:3788. FOLH1.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type II membrane protein 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. integral component of plasma membrane Source: ProtInc
    3. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi51 – 511N → A: Loss of glycosylation. Reduces enzyme activity. 2 Publications
    Mutagenesisi76 – 761N → A: Loss of glycosylation. Reduces enzyme activity. 2 Publications
    Mutagenesisi121 – 1211N → A: Loss of glycosylation. Severely reduced enzyme activity. 2 Publications
    Mutagenesisi140 – 1401N → A: Loss of glycosylation. Severely reduced enzyme activity. 2 Publications
    Mutagenesisi153 – 1531N → A: Loss of glycosylation. Severely reduced enzyme activity. 2 Publications
    Mutagenesisi195 – 1951N → A: Loss of glycosylation. Severely reduced enzyme activity. 2 Publications
    Mutagenesisi336 – 3361N → A: Loss of glycosylation. Reduces enzyme activity. 2 Publications
    Mutagenesisi377 – 3771H → A, G or Q: Complete loss of activity. 1 Publication
    Mutagenesisi379 – 3791D → E or N: Complete loss of activity. 1 Publication
    Mutagenesisi387 – 3871D → E or L: Complete loss of activity. 1 Publication
    Mutagenesisi387 – 3871D → N: No effect on enzyme activity. 1 Publication
    Mutagenesisi388 – 3881P → A: No effect on enzyme activity. 1 Publication
    Mutagenesisi424 – 4241E → A: Complete loss of activity. 2 Publications
    Mutagenesisi424 – 4241E → D: Reduces enzyme activity. 2 Publications
    Mutagenesisi424 – 4241E → Q: Reduces enzyme activity. 2 Publications
    Mutagenesisi425 – 4251E → Q or D: Complete loss of activity. 1 Publication
    Mutagenesisi453 – 4531D → N or L: Complete loss of activity. 1 Publication
    Mutagenesisi453 – 4531D → Q: Reduces enzyme activity. 1 Publication
    Mutagenesisi454 – 4541S → A: Reduces enzyme activity. 1 Publication
    Mutagenesisi459 – 4591N → A: Loss of glycosylation. Reduces enzyme activity. 2 Publications
    Mutagenesisi476 – 4761N → A: Loss of glycosylation. Reduces enzyme activity. 2 Publications
    Mutagenesisi638 – 6381N → A: Loss of glycosylation. Abolishes enzyme activity. 2 Publications
    Mutagenesisi640 – 6401T → A: Abolishes enzyme activity. 2 Publications

    Organism-specific databases

    PharmGKBiPA28205.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 750750Glutamate carboxypeptidase 2PRO_0000174117Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi51 – 511N-linked (GlcNAc...)1 Publication
    Glycosylationi76 – 761N-linked (GlcNAc...)8 Publications
    Glycosylationi121 – 1211N-linked (GlcNAc...)7 Publications
    Glycosylationi140 – 1401N-linked (GlcNAc...)7 Publications
    Glycosylationi153 – 1531N-linked (GlcNAc...)1 Publication
    Glycosylationi195 – 1951N-linked (GlcNAc...)7 Publications
    Glycosylationi336 – 3361N-linked (GlcNAc...)2 Publications
    Glycosylationi459 – 4591N-linked (GlcNAc...)8 Publications
    Glycosylationi476 – 4761N-linked (GlcNAc...)8 Publications
    Glycosylationi638 – 6381N-linked (GlcNAc...)8 Publications

    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

    Proteomic databases

    MaxQBiQ04609.
    PaxDbiQ04609.
    PRIDEiQ04609.

    PTM databases

    PhosphoSiteiQ04609.

    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-2 is also found in normal prostate as well as in brain and liver. Isoform PSMA-9 is specifically expressed in prostate cancer.4 Publications

    Inductioni

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

    Gene expression databases

    ArrayExpressiQ04609.
    BgeeiQ04609.
    CleanExiHS_FOLH1.
    GenevestigatoriQ04609.

    Organism-specific databases

    HPAiCAB001451.
    HPA010593.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi108630. 4 interactions.
    IntActiQ04609. 4 interactions.
    MINTiMINT-3025010.

    Structurei

    Secondary structure

    1
    750
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi58 – 647
    Helixi67 – 7711
    Beta strandi78 – 803
    Helixi87 – 10317
    Beta strandi106 – 11914
    Beta strandi122 – 1243
    Beta strandi127 – 1315
    Beta strandi137 – 1404
    Turni149 – 1513
    Helixi154 – 1563
    Beta strandi174 – 1763
    Helixi182 – 1909
    Beta strandi200 – 2045
    Helixi210 – 21910
    Beta strandi223 – 2286
    Helixi231 – 2344
    Beta strandi244 – 2474
    Beta strandi269 – 2724
    Helixi283 – 2853
    Beta strandi294 – 2974
    Helixi299 – 3068
    Helixi317 – 3193
    Beta strandi322 – 3254
    Beta strandi330 – 3334
    Helixi335 – 3373
    Beta strandi341 – 3466
    Beta strandi349 – 36214
    Beta strandi365 – 37713
    Beta strandi381 – 3833
    Turni385 – 3884
    Helixi389 – 40719
    Beta strandi413 – 42311
    Helixi424 – 4263
    Helixi429 – 44517
    Beta strandi446 – 4516
    Beta strandi455 – 4573
    Beta strandi459 – 4668
    Helixi468 – 4703
    Helixi471 – 4799
    Beta strandi480 – 4823
    Turni486 – 4905
    Helixi493 – 5008
    Beta strandi504 – 5063
    Beta strandi507 – 5104
    Beta strandi517 – 5193
    Helixi521 – 5266
    Beta strandi531 – 5388
    Beta strandi541 – 5433
    Turni545 – 5473
    Turni550 – 5534
    Helixi559 – 5657
    Helixi571 – 58919
    Helixi597 – 61519
    Helixi619 – 6246
    Helixi630 – 65223
    Helixi658 – 67316
    Beta strandi684 – 6863
    Beta strandi689 – 6957
    Beta strandi698 – 7058
    Helixi706 – 7127
    Helixi715 – 7173
    Helixi721 – 74424

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    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[»]
    ProteinModelPortaliQ04609.
    SMRiQ04609. Positions 55-750.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ04609.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1919CytoplasmicCuratedAdd
    BLAST
    Topological domaini44 – 750707ExtracellularCuratedAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei20 – 4324Helical; Signal-anchor for type II membrane proteinCuratedAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni274 – 587314NAALADaseAdd
    BLAST
    Regioni534 – 5363Substrate binding
    Regioni699 – 7002Substrate binding

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi146 – 1494Poly-Pro

    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

    eggNOGiNOG74799.
    HOVERGENiHBG051639.
    KOiK14592.
    OMAiMWNPLHE.
    OrthoDBiEOG7QK0BC.
    PhylomeDBiQ04609.
    TreeFamiTF312981.

    Family and domain databases

    Gene3Di1.20.930.40. 1 hit.
    InterProiIPR007484. Peptidase_M28.
    IPR003137. Protease-assoc_domain.
    IPR007365. TFR-like_dimer_dom.
    [Graphical view]
    PfamiPF02225. PA. 1 hit.
    PF04389. Peptidase_M28. 1 hit.
    PF04253. TFR_dimer. 1 hit.
    [Graphical view]
    SUPFAMiSSF47672. SSF47672. 1 hit.

    Sequences (8)i

    Sequence statusi: Complete.

    This entry describes 8 isoformsi produced by alternative splicing. Align

    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

    MWNLLHETDS AVATARRPRW LCAGALVLAG GFFLLGFLFG WFIKSSNEAT    50
    NITPKHNMKA FLDELKAENI KKFLYNFTQI PHLAGTEQNF QLAKQIQSQW 100
    KEFGLDSVEL AHYDVLLSYP NKTHPNYISI INEDGNEIFN TSLFEPPPPG 150
    YENVSDIVPP FSAFSPQGMP EGDLVYVNYA RTEDFFKLER DMKINCSGKI 200
    VIARYGKVFR GNKVKNAQLA GAKGVILYSD PADYFAPGVK SYPDGWNLPG 250
    GGVQRGNILN LNGAGDPLTP GYPANEYAYR RGIAEAVGLP SIPVHPIGYY 300
    DAQKLLEKMG GSAPPDSSWR GSLKVPYNVG PGFTGNFSTQ KVKMHIHSTN 350
    EVTRIYNVIG TLRGAVEPDR YVILGGHRDS WVFGGIDPQS GAAVVHEIVR 400
    SFGTLKKEGW RPRRTILFAS WDAEEFGLLG STEWAEENSR LLQERGVAYI 450
    NADSSIEGNY TLRVDCTPLM YSLVHNLTKE LKSPDEGFEG KSLYESWTKK 500
    SPSPEFSGMP RISKLGSGND FEVFFQRLGI ASGRARYTKN WETNKFSGYP 550
    LYHSVYETYE LVEKFYDPMF KYHLTVAQVR GGMVFELANS IVLPFDCRDY 600
    AVVLRKYADK IYSISMKHPQ EMKTYSVSFD SLFSAVKNFT EIASKFSERL 650
    QDFDKSNPIV LRMMNDQLMF LERAFIDPLG LPDRPFYRHV IYAPSSHNKY 700
    AGESFPGIYD ALFDIESKVD PSKAWGEVKR QIYVAAFTVQ AAAETLSEVA 750

    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

    Sequence cautioni

    The sequence AAF31167.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti194 – 1941I → V in AAZ66619. 1 PublicationCurated
    Sequence conflicti354 – 3541R → K AA sequence (PubMed:8417812)Curated
    Sequence conflicti398 – 3981I → N in ABO93402. (PubMed:17929272)Curated

    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)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti23 – 231A → T in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036398
    Natural varianti75 – 751Y → H.1 Publication
    Corresponds to variant rs202676 [ dbSNP | Ensembl ].
    VAR_024592
    Natural varianti475 – 4751H → Y Can be associated with lower folate and higher homocysteine levels. 1 Publication
    Corresponds to variant rs61886492 [ dbSNP | Ensembl ].
    VAR_012736
    Natural varianti627 – 6271V → L.
    Corresponds to variant rs2988342 [ dbSNP | Ensembl ].
    VAR_028882

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 585585Missing in isoform PSMA-3. CuratedVSP_040242Add
    BLAST
    Alternative sequencei1 – 308308Missing in isoform 10. 1 PublicationVSP_044287Add
    BLAST
    Alternative sequencei1 – 159159Missing in isoform PSMA-4. CuratedVSP_040241Add
    BLAST
    Alternative sequencei1 – 5757Missing in isoform PSMA'. 1 PublicationVSP_005336Add
    BLAST
    Alternative sequencei1 – 3939MWNLL…LGFLF → MTAGSSYPLFLAAYACTGCL AERL in isoform PSMA-7 and isoform PSMA-9. 2 PublicationsVSP_038058Add
    BLAST
    Alternative sequencei214 – 24330VKNAQ…VKSYP → NMLIGVELQRLLVFQVFLFI QLDTMMHRSS in isoform PSMA-4. CuratedVSP_040243Add
    BLAST
    Alternative sequencei244 – 750507Missing in isoform PSMA-4. CuratedVSP_040244Add
    BLAST
    Alternative sequencei657 – 75094NPIVL…LSEVA → MSSMLQAATTSMQGSHSQEF MMLCLILKAKWTLPRPGEK in isoform PSMA-3. CuratedVSP_040245Add
    BLAST
    Alternative sequencei657 – 68832NPIVL…RPFYR → K in isoform PSMA-8 and isoform PSMA-9. 3 PublicationsVSP_038059Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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]
    CCDS53626.1. [Q04609-10]
    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]
    UniGeneiHs.654487.

    Genome annotation databases

    EnsembliENST00000256999; ENSP00000256999; ENSG00000086205. [Q04609-1]
    ENST00000340334; ENSP00000344131; ENSG00000086205. [Q04609-7]
    ENST00000343844; ENSP00000344086; ENSG00000086205. [Q04609-10]
    ENST00000356696; ENSP00000349129; ENSG00000086205. [Q04609-8]
    ENST00000533034; ENSP00000431463; ENSG00000086205. [Q04609-9]
    GeneIDi2346.
    KEGGihsa:2346.
    UCSCiuc001ngx.3. human. [Q04609-3]
    uc001ngy.3. human. [Q04609-1]
    uc001ngz.3. human. [Q04609-8]
    uc009yly.3. human. [Q04609-7]
    uc009ylz.3. human. [Q04609-9]

    Polymorphism databases

    DMDMi548615.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS31493.1. [Q04609-8 ]
    CCDS53626.1. [Q04609-10 ]
    CCDS53627.1. [Q04609-9 ]
    CCDS53628.1. [Q04609-7 ]
    CCDS7946.1. [Q04609-1 ]
    PIRi A56881.
    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 ]
    UniGenei Hs.654487.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    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 [» ]
    ProteinModelPortali Q04609.
    SMRi Q04609. Positions 55-750.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108630. 4 interactions.
    IntActi Q04609. 4 interactions.
    MINTi MINT-3025010.

    Chemistry

    BindingDBi Q04609.
    ChEMBLi CHEMBL1892.
    DrugBanki DB00089. Capromab.
    DB00142. L-Glutamic Acid.
    GuidetoPHARMACOLOGYi 1606.

    Protein family/group databases

    MEROPSi M28.010.

    PTM databases

    PhosphoSitei Q04609.

    Polymorphism databases

    DMDMi 548615.

    Proteomic databases

    MaxQBi Q04609.
    PaxDbi Q04609.
    PRIDEi Q04609.

    Protocols and materials databases

    DNASUi 2346.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000256999 ; ENSP00000256999 ; ENSG00000086205 . [Q04609-1 ]
    ENST00000340334 ; ENSP00000344131 ; ENSG00000086205 . [Q04609-7 ]
    ENST00000343844 ; ENSP00000344086 ; ENSG00000086205 . [Q04609-10 ]
    ENST00000356696 ; ENSP00000349129 ; ENSG00000086205 . [Q04609-8 ]
    ENST00000533034 ; ENSP00000431463 ; ENSG00000086205 . [Q04609-9 ]
    GeneIDi 2346.
    KEGGi hsa:2346.
    UCSCi uc001ngx.3. human. [Q04609-3 ]
    uc001ngy.3. human. [Q04609-1 ]
    uc001ngz.3. human. [Q04609-8 ]
    uc009yly.3. human. [Q04609-7 ]
    uc009ylz.3. human. [Q04609-9 ]

    Organism-specific databases

    CTDi 2346.
    GeneCardsi GC11M049168.
    H-InvDB HIX0129475.
    HGNCi HGNC:3788. FOLH1.
    HPAi CAB001451.
    HPA010593.
    MIMi 600934. gene.
    neXtProti NX_Q04609.
    PharmGKBi PA28205.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG74799.
    HOVERGENi HBG051639.
    KOi K14592.
    OMAi MWNPLHE.
    OrthoDBi EOG7QK0BC.
    PhylomeDBi Q04609.
    TreeFami TF312981.

    Miscellaneous databases

    EvolutionaryTracei Q04609.
    GeneWikii Glutamate_carboxypeptidase_II.
    GenomeRNAii 2346.
    NextBioi 9513.
    PROi Q04609.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q04609.
    Bgeei Q04609.
    CleanExi HS_FOLH1.
    Genevestigatori Q04609.

    Family and domain databases

    Gene3Di 1.20.930.40. 1 hit.
    InterProi IPR007484. Peptidase_M28.
    IPR003137. Protease-assoc_domain.
    IPR007365. TFR-like_dimer_dom.
    [Graphical view ]
    Pfami PF02225. PA. 1 hit.
    PF04389. Peptidase_M28. 1 hit.
    PF04253. TFR_dimer. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47672. SSF47672. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of a complementary DNA encoding a prostate-specific membrane antigen."
      Israeli R.S., Powell C.T., Fair W.R., Heston W.D.W.
      Cancer Res. 53:227-230(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PSMA-1), PARTIAL PROTEIN SEQUENCE.
      Tissue: Prostatic carcinoma.
    2. "Alternatively spliced variants of prostate-specific membrane antigen RNA: ratio of expression as a potential measurement of progression."
      Su S.L., Huang I.-P., Fair W.R., Powell C.T., Heston W.D.W.
      Cancer Res. 55:1441-1443(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PSMA').
      Tissue: Prostate.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM PSMA-1), VARIANT HIS-75.
    4. "Molecular characterization of human brain N-acetylated alpha-linked acidic dipeptidase (NAALADase)."
      Luthi-Carter R., Barczak A.K., Speno H., Coyle J.T.
      J. Pharmacol. Exp. Ther. 286:1020-1025(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PSMA-1).
      Tissue: Brain.
    5. "Isolation and expression of novel human glutamate carboxypeptidases with N-acetylated alpha-linked acidic dipeptidase and dipeptidyl peptidase IV activity."
      Pangalos M.N., Neefs J.-M., Somers M., Verhasselt P., Bekkers M., van der Helm L., Fraiponts E., Ashton D., Gordon R.D.
      J. Biol. Chem. 274:8470-8483(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PSMA-1), CHARACTERIZATION.
      Tissue: Prostate.
    6. "Glutamate carboxypeptidase II: a polymorphism associated with lower levels of serum folate and hyperhomocysteinemia."
      Devlin A.M., Ling E.-H., Peerson J.M., Fernando S., Clarke R., Smith A.D., Halsted C.H.
      Hum. Mol. Genet. 9:2837-2844(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PSMA-1), VARIANT TYR-475.
      Tissue: Jejunum and Small intestine.
    7. "Cloning and sequencing of Chinese prostate-specific membrane antigen."
      Ye C.Z., Zhang F.L., Zhang Y.K., Chen C.Q.
      Mian Yi Xue Za Zhi 17:328-330(2001)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PSMA-1).
      Tissue: Prostatic carcinoma.
    8. "High expression of PSM-E correlated with tumor grade in prostate cancer: a new alternatively spliced variant of prostate-specific membrane antigen."
      Cao K.Y., Mao X.P., Wang D.H., Xu L., Yuan G.Q., Dai S.Q., Zheng B.J., Qiu S.P.
      Prostate 67:1791-1800(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PSMA-9).
    9. "Identification of three novel splice variants of prostate-specific membrane antigen."
      Peace D.J., Zhang Y., Holt G., Ferrer K.T., Heller M., Sosman J.A., Xue B.H.
      Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    10. "Identification of a cell growth-inhibiting gene."
      Kim J.W., Kim H.K., Shin S.M.
      Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PSMA-8).
    11. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS PSMA-1; PSMA-7 AND 10).
      Tissue: Amygdala, Corpus callosum and Hippocampus.
    12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    13. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    14. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PSMA-8).
      Tissue: Lung.
    15. "Molecular cloning of a peptidase against N-acetylaspartylglutamate from a rat hippocampal cDNA library."
      Bzdega T., Turi T., Wroblewska B., She D., Chung H.S., Kim H., Neale J.H.
      J. Neurochem. 69:2270-2277(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PSMA-3), TISSUE SPECIFICITY.
      Tissue: Prostate.
    16. "Alternative splicing of the prostate-specific membrane antigen."
      Lupold S.E., Criley S.C., Coffey D.S.
      Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PSMA-4).
    17. "Identification, purification, and subcellular localization of prostate-specific membrane antigen PSM' protein in the LNCaP prostatic carcinoma cell line."
      Grauer L.S., Lawler K.D., Marignac J.L., Kumar A., Goel A.S., Wolfert R.L.
      Cancer Res. 58:4787-4789(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 60-74, SUBCELLULAR LOCATION.
      Tissue: Prostatic carcinoma.
    18. "Molecular cloning of alternatively spliced variants of the peptidase against N-acetylaspartylglutamate (NAAG) from human and rat nervous systems."
      Bzdega T., She D., Turi T., Wroblewska B., Neale J.H.
      Abstr. - Soc. Neurosci. 24:579-579(1998)
      Cited for: ALTERNATIVE SPLICING.
    19. "Hydrolysis of the neuropeptide N-acetylaspartylglutamate (NAAG) by cloned human glutamate carboxypeptidase II."
      Luthi-Carter R., Barczak A.K., Speno H.D., Coyle J.T.
      Brain Res. 795:341-348(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    20. "Structure of membrane glutamate carboxypeptidase."
      Rawlings N.D., Barrett A.J.
      Biochim. Biophys. Acta 1339:247-252(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN STRUCTURE.
    21. "Site-directed mutagenesis of predicted active site residues in glutamate carboxypeptidase II."
      Speno H.S., Luthi-Carter R., Macias W.L., Valentine S.L., Joshi A.R.T., Coyle J.T.
      Mol. Pharmacol. 55:179-185(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    22. "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
      Zhang H., Li X.-J., Martin D.B., Aebersold R.
      Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-76; ASN-336; ASN-459; ASN-476 AND ASN-638.
    23. "Identification of the N-glycosylation sites on glutamate carboxypeptidase II necessary for proteolytic activity."
      Barinka C., Sacha P., Sklenar J., Man P., Bezouska K., Slusher B.S., Konvalinka J.
      Protein Sci. 13:1627-1635(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-51; ASN-76; ASN-121; ASN-140; ASN-153; ASN-195; ASN-336; ASN-459; ASN-476 AND ASN-638, MUTAGENESIS OF ASN-51; ASN-76; ASN-121; ASN-140; ASN-153; ASN-195; ASN-336; ASN-459; ASN-476; ASN-638 AND THR-640.
    24. "Comparative analysis of prostate-specific membrane antigen (PSMA) versus a prostate-specific membrane antigen-like gene."
      O'Keefe D.S., Bacich D.J., Heston W.D.W.
      Prostate 58:200-210(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
      Tissue: Liver.
    25. "Expression of prostate-specific membrane antigen in normal and malignant human tissues."
      Kinoshita Y., Kuratsukuri K., Landas S., Imaida K., Rovito P.M. Jr., Wang C.Y., Haas G.P.
      World J. Surg. 30:628-636(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    26. Cited for: TISSUE SPECIFICITY.
    27. "Structure of glutamate carboxypeptidase II, a drug target in neuronal damage and prostate cancer."
      Mesters J.R., Barinka C., Li W., Tsukamoto T., Majer P., Slusher B.S., Konvalinka J., Hilgenfeld R.
      EMBO J. 25:1375-1384(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 44-750 IN COMPLEXES WITH GLUTAMATE; INHIBITORS; CALCIUM AND ZINC IONS, COFACTOR, SUBUNIT, GLYCOSYLATION AT ASN-76; ASN-121; ASN-140; ASN-195; ASN-459; ASN-476 AND ASN-638.
    28. "Human glutamate carboxypeptidase II inhibition: structures of GCPII in complex with two potent inhibitors, quisqualate and 2-PMPA."
      Mesters J.R., Henning K., Hilgenfeld R.
      Acta Crystallogr. D 63:508-513(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 44-750 IN COMPLEXES WITH THE INHIBITORS QUISQUALATE AND 2-PMPA; CALCIUM AND ZINC IONS, GLYCOSYLATION AT ASN-76; ASN-121; ASN-140; ASN-195; ASN-459; ASN-476 AND ASN-638.
    29. "Structural insight into the pharmacophore pocket of human glutamate carboxypeptidase II."
      Barinka C., Rovenska M., Mlcochova P., Hlouchova K., Plechanovova A., Majer P., Tsukamoto T., Slusher B.S., Konvalinka J., Lubkowski J.
      J. Med. Chem. 50:3267-3273(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF 44-750 IN COMPLEXES WITH SUBSTRATE ANALOGS; CALCIUM AND ZINC IONS, ENZYME REGULATION, GLYCOSYLATION AT ASN-76; ASN-121; ASN-140 ASN-195; ASN-459; ASN-476 AND ASN-638.
    30. "Interactions between human glutamate carboxypeptidase II and urea-based inhibitors: structural characterization."
      Barinka C., Byun Y., Dusich C.L., Banerjee S.R., Chen Y., Castanares M., Kozikowski A.P., Mease R.C., Pomper M.G., Lubkowski J.
      J. Med. Chem. 51:7737-7743(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 44-750 IN COMPLEXES WITH UREA-BASED INHIBITORS; CALCIUM AND ZINC IONS, GLYCOSYLATION AT ASN-76; ASN-121; ASN-140; ASN-195; ASN-459; ASN-476 AND ASN-638.
    31. "Structural basis of interactions between human glutamate carboxypeptidase II and its substrate analogs."
      Barinka C., Hlouchova K., Rovenska M., Majer P., Dauter M., Hin N., Ko Y.-S., Tsukamoto T., Slusher B.S., Konvalinka J., Lubkowski J.
      J. Mol. Biol. 376:1438-1450(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 44-750 IN COMPLEXES WITH SUBSTRATE ANALOGS; CALCIUM AND ZINC IONS, GLYCOSYLATION AT ASN-76; ASN-121; ASN-140; ASN-195; ASN-459; ASN-476 AND ASN-638.
    32. "Reaction mechanism of glutamate carboxypeptidase II revealed by mutagenesis, X-ray crystallography, and computational methods."
      Klusak V., Barinka C., Plechanovova A., Mlcochova P., Konvalinka J., Rulisek L., Lubkowski J.
      Biochemistry 48:4126-4138(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 44-750 IN COMPLEX WITH SUBSTRATE; CALCIUM AND ZINC IONS, GLYCOSYLATION AT ASN-76; ASN-121; ASN-140; ASN-195; ASN-459; ASN-476 AND ASN-638, MUTAGENESIS OF GLU-424.
    33. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-23.

    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 historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 162 of the entry and version 1 of the sequence. [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

    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.

    Keywords - Technical termi

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

    Documents

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

    External Data

    Dasty 3