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Q04609

- FOLH1_HUMAN

UniProt

Q04609 - FOLH1_HUMAN

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Protein

Glutamate carboxypeptidase 2

Gene
FOLH1, FOLH, NAALAD1, PSM, PSMA, GIG27
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - 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. 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 – 2101Substrate
Binding sitei257 – 2571Substrate
Metal bindingi269 – 2691Calcium
Metal bindingi272 – 2721Calcium; via carbonyl oxygen
Metal bindingi377 – 3771Zinc 1
Metal bindingi387 – 3871Zinc 1
Metal bindingi387 – 3871Zinc 2
Active sitei424 – 4241For NAALADase activity
Metal bindingi425 – 4251Zinc 2
Metal bindingi433 – 4331Calcium
Metal bindingi436 – 4361Calcium
Metal bindingi453 – 4531Zinc 1
Binding sitei519 – 5191Substrate
Binding sitei552 – 5521Substrate
Metal bindingi553 – 5531Zinc 2
Active sitei628 – 6281Charge relay system Reviewed prediction
Active sitei666 – 6661Charge relay system Reviewed prediction
Active sitei689 – 6891Charge relay system Reviewed prediction

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
Complete GO annotation...

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; Single-pass type II membrane protein 1 Publication
Isoform PSMA' : Cytoplasm 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1919Cytoplasmic InferredAdd
BLAST
Transmembranei20 – 4324Helical; Signal-anchor for type II membrane protein; InferredAdd
BLAST
Topological domaini44 – 750707Extracellular InferredAdd
BLAST

GO - Cellular componenti

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

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

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.1 Publication

Gene expression databases

ArrayExpressiQ04609.
BgeeiQ04609.
CleanExiHS_FOLH1.
GenevestigatoriQ04609.

Organism-specific databases

HPAiCAB001451.
HPA010593.

Interactioni

Subunit structurei

Homodimer.1 Publication

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.

Miscellaneous databases

EvolutionaryTraceiQ04609.

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

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.

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. VSP_040242Add
BLAST
Alternative sequencei1 – 308308Missing in isoform 10. VSP_044287Add
BLAST
Alternative sequencei1 – 159159Missing in isoform PSMA-4. VSP_040241Add
BLAST
Alternative sequencei1 – 5757Missing in isoform PSMA'. VSP_005336Add
BLAST
Alternative sequencei1 – 3939MWNLL…LGFLF → MTAGSSYPLFLAAYACTGCL AERL in isoform PSMA-7 and isoform PSMA-9. VSP_038058Add
BLAST
Alternative sequencei214 – 24330VKNAQ…VKSYP → NMLIGVELQRLLVFQVFLFI QLDTMMHRSS in isoform PSMA-4. VSP_040243Add
BLAST
Alternative sequencei244 – 750507Missing in isoform PSMA-4. VSP_040244Add
BLAST
Alternative sequencei657 – 75094NPIVL…LSEVA → MSSMLQAATTSMQGSHSQEF MMLCLILKAKWTLPRPGEK in isoform PSMA-3. VSP_040245Add
BLAST
Alternative sequencei657 – 68832NPIVL…RPFYR → K in isoform PSMA-8 and isoform PSMA-9. VSP_038059Add
BLAST

Sequence conflict

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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 161 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

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