Q04609 (FOLH1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	FOLH1
Synonyms:	FOLH, NAALAD1, PSM, PSMA
ORF Names:	GIG27

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	750 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. 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 activity	Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.
Cofactor	Binds 2 zinc ions per subunit. Required for NAALADase activity. Ref.27
Enzyme regulation	The NAALADase activity is inhibited by beta-NAAG, quisqualic acid, 2-(phosphonomethyl) pentanedioic acid (PMPA) and EDTA. Activated by cobalt. Ref.29
Subunit structure	Homodimer. Ref.27
Subcellular location	Cell membrane; Single-pass type II membrane protein Ref.17. Isoform PSMA': Cytoplasm Ref.17.
Tissue specificity	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. Ref.15 Ref.24 Ref.25 Ref.26
Induction	In the prostate, up-regulated in response to androgen deprivation. Ref.29
Domain	The NAALADase activity is found in the central region, the dipeptidyl peptidase IV type activity in the C-terminal. Ref.20
Post-translational modification	The first two amino acids at the N-terminus of isoform PSMA' appear to be cleaved by limited proteolysis. The N-terminus is blocked.
Polymorphism	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.
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.
Sequence similarities	Belongs to the peptidase M28 family. M28B subfamily.
Biophysicochemical properties	pH dependence: Stable at pH greater than 6.5.
Sequence caution	The sequence AAF31167.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding Zinc
Molecular function	Carboxypeptidase Dipeptidase Hydrolase Metalloprotease Protease
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	proteolysis Non-traceable author statement Ref.15. Source: UniProtKB
Cellular component	cytoplasm Inferred from direct assay. Source: HPA integral to plasma membrane Traceable author statement. Source: ProtInc membrane fraction Traceable author statement. Source: ProtInc nucleus Inferred from direct assay. Source: HPA
Molecular function	carboxypeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW dipeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Isoform PSMA-1 (identifier: Q04609-1)

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.

Note: No experimental confirmation available.

Isoform PSMA-3 (identifier: Q04609-3)

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.

Isoform PSMA-4 (identifier: Q04609-4)

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.

Isoform PSMA' (identifier: Q04609-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-57: Missing.

Isoform PSMA-7 (identifier: Q04609-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: MWNLLHETDSAVATARRPRWLCAGALVLAGGFFLLGFLF → MTAGSSYPLFLAAYACTGCLAERL

Isoform PSMA-8 (identifier: Q04609-8)

The sequence of this isoform differs from the canonical sequence as follows:
     657-688: NPIVLRMMNDQLMFLERAFIDPLGLPDRPFYR → K

Isoform PSMA-9 (identifier: Q04609-9)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 750

750

Glutamate carboxypeptidase 2

PRO_0000174117

Regions

Topological domain

1 – 19

19

Cytoplasmic Probable

Transmembrane

20 – 43

24

Helical; Signal-anchor for type II membrane protein; Probable

Topological domain

44 – 750

707

Extracellular Probable

Region

274 – 587

314

NAALADase

Region

534 – 536

3

Substrate binding

Region

699 – 700

2

Substrate binding

Compositional bias

146 – 149

4

Poly-Pro

Sites

Active site

424

1

For NAALADase activity

Active site

628

1

Charge relay system Potential

Active site

666

1

Charge relay system Potential

Active site

689

1

Charge relay system Potential

Metal binding

269

1

Calcium

Metal binding

272

1

Calcium; via carbonyl oxygen

Metal binding

377

1

Zinc 1

Metal binding

387

1

Zinc 1

Metal binding

387

1

Zinc 2

Metal binding

425

1

Zinc 2

Metal binding

433

1

Calcium

Metal binding

436

1

Calcium

Metal binding

453

1

Zinc 1

Metal binding

553

1

Zinc 2

Binding site

210

1

Substrate

Binding site

257

1

Substrate

Binding site

519

1

Substrate

Binding site

552

1

Substrate

Amino acid modifications

Glycosylation

51

1

N-linked (GlcNAc...) Ref.23

Glycosylation

76

1

N-linked (GlcNAc...) Ref.22 Ref.23 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32

Glycosylation

121

1

N-linked (GlcNAc...) Ref.23 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32

Glycosylation

140

1

N-linked (GlcNAc...) Ref.23 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32

Glycosylation

153

1

N-linked (GlcNAc...) Ref.23

Glycosylation

195

1

N-linked (GlcNAc...) Ref.23 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32

Glycosylation

336

1

N-linked (GlcNAc...) Ref.22 Ref.23

Glycosylation

459

1

N-linked (GlcNAc...) Ref.22 Ref.23 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32

Glycosylation

476

1

N-linked (GlcNAc...) Ref.22 Ref.23 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32

Glycosylation

638

1

N-linked (GlcNAc...) Ref.22 Ref.23 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32

Natural variations

Alternative sequence

1 – 585

585

Missing in isoform PSMA-3.

VSP_040242

Alternative sequence

1 – 159

159

Missing in isoform PSMA-4.

VSP_040241

Alternative sequence

1 – 57

57

Missing in isoform PSMA'.

VSP_005336

Alternative sequence

1 – 39

39

MWNLL…LGFLF → MTAGSSYPLFLAAYACTGCL AERL in isoform PSMA-7 and isoform PSMA-9.

VSP_038058

Alternative sequence

214 – 243

30

VKNAQ…VKSYP → NMLIGVELQRLLVFQVFLFI QLDTMMHRSS in isoform PSMA-4.

VSP_040243

Alternative sequence

244 – 750

507

Missing in isoform PSMA-4.

VSP_040244

Alternative sequence

657 – 750

94

NPIVL…LSEVA → MSSMLQAATTSMQGSHSQEF MMLCLILKAKWTLPRPGEK in isoform PSMA-3.

VSP_040245

Alternative sequence

657 – 688

32

NPIVL…RPFYR → K in isoform PSMA-8 and isoform PSMA-9.

VSP_038059

Natural variant

23

1

A → T in a colorectal cancer sample; somatic mutation. Ref.33

VAR_036398

Natural variant

75

1

Y → H. Ref.3
Corresponds to variant rs202676 [ dbSNP | Ensembl ].

VAR_024592

Natural variant

475

1

H → Y Can be associated with lower folate and higher homocysteine levels. Ref.6

VAR_012736

Natural variant

627

1

V → L.
Corresponds to variant rs2988342 [ dbSNP | Ensembl ].

VAR_028882

Experimental info

Mutagenesis

51

1

N → A: Loss of glycosylation. Reduces enzyme activity. Ref.23

Mutagenesis

76

1

N → A: Loss of glycosylation. Reduces enzyme activity. Ref.23

Mutagenesis

121

1

N → A: Loss of glycosylation. Severely reduced enzyme activity. Ref.23

Mutagenesis

140

1

N → A: Loss of glycosylation. Severely reduced enzyme activity. Ref.23

Mutagenesis

153

1

N → A: Loss of glycosylation. Severely reduced enzyme activity. Ref.23

Mutagenesis

195

1

N → A: Loss of glycosylation. Severely reduced enzyme activity. Ref.23

Mutagenesis

336

1

N → A: Loss of glycosylation. Reduces enzyme activity. Ref.23

Mutagenesis

377

1

H → A, G or Q: Complete loss of activity.

Mutagenesis

379

1

D → E or N: Complete loss of activity.

Mutagenesis

387

1

D → E or L: Complete loss of activity.

Mutagenesis

387

1

D → N: No effect on enzyme activity.

Mutagenesis

388

1

P → A: No effect on enzyme activity.

Mutagenesis

424

1

E → A: Complete loss of activity. Ref.32

Mutagenesis

424

1

E → D: Reduces enzyme activity. Ref.32

Mutagenesis

424

1

E → Q: Reduces enzyme activity. Ref.32

Mutagenesis

425

1

E → Q or D: Complete loss of activity.

Mutagenesis

453

1

D → N or L: Complete loss of activity.

Mutagenesis

453

1

D → Q: Reduces enzyme activity.

Mutagenesis

454

1

S → A: Reduces enzyme activity.

Mutagenesis

459

1

N → A: Loss of glycosylation. Reduces enzyme activity. Ref.23

Mutagenesis

476

1

N → A: Loss of glycosylation. Reduces enzyme activity. Ref.23

Mutagenesis

638

1

N → A: Loss of glycosylation. Abolishes enzyme activity. Ref.23

Mutagenesis

640

1

T → A: Abolishes enzyme activity. Ref.23

Sequence conflict

194

1

I → V in AAZ66619. Ref.9

Sequence conflict

354

1

R → K AA sequence Ref.1

Sequence conflict

398

1

I → N in ABO93402. Ref.8

Secondary structure

1

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750

Helix Strand Turn

Details...

Helix

58 – 64

7

Helix

67 – 77

11

Beta strand

78 – 80

3

Helix

87 – 102

16

Beta strand

106 – 119

14

Beta strand

127 – 131

5

Beta strand

137 – 140

4

Beta strand

174 – 176

3

Helix

182 – 190

9

Beta strand

200 – 204

5

Helix

210 – 219

10

Beta strand

223 – 228

6

Helix

231 – 234

4

Turn

242 – 244

3

Beta strand

245 – 247

3

Helix

283 – 285

3

Beta strand

294 – 297

4

Helix

299 – 306

8

Helix

317 – 319

3

Beta strand

322 – 325

4

Beta strand

341 – 346

6

Beta strand

349 – 362

14

Beta strand

365 – 377

13

Beta strand

381 – 383

3

Turn

385 – 388

4

Helix

389 – 407

19

Beta strand

413 – 422

10

Helix

424 – 426

3

Helix

429 – 445

17

Beta strand

446 – 451

6

Beta strand

455 – 457

3

Beta strand

459 – 466

8

Helix

468 – 470

3

Helix

471 – 479

9

Beta strand

480 – 482

3

Helix

493 – 500

8

Beta strand

504 – 510

7

Beta strand

517 – 519

3

Helix

521 – 526

6

Beta strand

532 – 538

7

Turn

550 – 553

4

Helix

559 – 565

7

Helix

571 – 589

19

Helix

597 – 615

19

Helix

619 – 624

6

Helix

630 – 650

21

Helix

658 – 673

16

Beta strand

689 – 695

7

Beta strand

698 – 705

8

Helix

706 – 712

7

Helix

715 – 717

3

Helix

721 – 744

24

Sequences

	Sequence		Length	Mass (Da)
	Isoform PSMA-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: AD8C0A7DBF47901A	FASTA	750	84,331
	10 20 30 40 50 60 MWNLLHETDS AVATARRPRW LCAGALVLAG GFFLLGFLFG WFIKSSNEAT NITPKHNMKA 70 80 90 100 110 120 FLDELKAENI KKFLYNFTQI PHLAGTEQNF QLAKQIQSQW KEFGLDSVEL AHYDVLLSYP 130 140 150 160 170 180 NKTHPNYISI INEDGNEIFN TSLFEPPPPG YENVSDIVPP FSAFSPQGMP EGDLVYVNYA 190 200 210 220 230 240 RTEDFFKLER DMKINCSGKI VIARYGKVFR GNKVKNAQLA GAKGVILYSD PADYFAPGVK 250 260 270 280 290 300 SYPDGWNLPG GGVQRGNILN LNGAGDPLTP GYPANEYAYR RGIAEAVGLP SIPVHPIGYY 310 320 330 340 350 360 DAQKLLEKMG GSAPPDSSWR GSLKVPYNVG PGFTGNFSTQ KVKMHIHSTN EVTRIYNVIG 370 380 390 400 410 420 TLRGAVEPDR YVILGGHRDS WVFGGIDPQS GAAVVHEIVR SFGTLKKEGW RPRRTILFAS 430 440 450 460 470 480 WDAEEFGLLG STEWAEENSR LLQERGVAYI NADSSIEGNY TLRVDCTPLM YSLVHNLTKE 490 500 510 520 530 540 LKSPDEGFEG KSLYESWTKK SPSPEFSGMP RISKLGSGND FEVFFQRLGI ASGRARYTKN 550 560 570 580 590 600 WETNKFSGYP LYHSVYETYE LVEKFYDPMF KYHLTVAQVR GGMVFELANS IVLPFDCRDY 610 620 630 640 650 660 AVVLRKYADK IYSISMKHPQ EMKTYSVSFD SLFSAVKNFT EIASKFSERL QDFDKSNPIV 670 680 690 700 710 720 LRMMNDQLMF LERAFIDPLG LPDRPFYRHV IYAPSSHNKY AGESFPGIYD ALFDIESKVD 730 740 750 PSKAWGEVKR QIYVAAFTVQ AAAETLSEVA
	Isoform PSMA-3 [UniParc]. Checksum: E35692A0D83A0E53	FASTA	110	12,603
	10 20 30 40 50 60 ELANSIVLPF DCRDYAVVLR KYADKIYSIS MKHPQEMKTY SVSFDSLFSA VKNFTEIASK 70 80 90 100 110 FSERLQDFDK SMSSMLQAAT TSMQGSHSQE FMMLCLILKA KWTLPRPGEK
	Isoform PSMA-4 [UniParc]. Checksum: 80FC286A66993939	FASTA	84	9,754
	10 20 30 40 50 60 PFSAFSPQGM PEGDLVYVNY ARTEDFFKLE RDMKINCSGK IVIARYGKVF RGNKNMLIGV 70 80 ELQRLLVFQV FLFIQLDTMM HRSS
	Isoform PSMA' [UniParc]. Checksum: 5F3F6D31A9FECAEC	FASTA	693	78,000
	10 20 30 40 50 60 MKAFLDELKA ENIKKFLYNF TQIPHLAGTE QNFQLAKQIQ SQWKEFGLDS VELAHYDVLL 70 80 90 100 110 120 SYPNKTHPNY ISIINEDGNE IFNTSLFEPP PPGYENVSDI VPPFSAFSPQ GMPEGDLVYV 130 140 150 160 170 180 NYARTEDFFK LERDMKINCS GKIVIARYGK VFRGNKVKNA QLAGAKGVIL YSDPADYFAP 190 200 210 220 230 240 GVKSYPDGWN LPGGGVQRGN ILNLNGAGDP LTPGYPANEY AYRRGIAEAV GLPSIPVHPI 250 260 270 280 290 300 GYYDAQKLLE KMGGSAPPDS SWRGSLKVPY NVGPGFTGNF STQKVKMHIH STNEVTRIYN 310 320 330 340 350 360 VIGTLRGAVE PDRYVILGGH RDSWVFGGID PQSGAAVVHE IVRSFGTLKK EGWRPRRTIL 370 380 390 400 410 420 FASWDAEEFG LLGSTEWAEE NSRLLQERGV AYINADSSIE GNYTLRVDCT PLMYSLVHNL 430 440 450 460 470 480 TKELKSPDEG FEGKSLYESW TKKSPSPEFS GMPRISKLGS GNDFEVFFQR LGIASGRARY 490 500 510 520 530 540 TKNWETNKFS GYPLYHSVYE TYELVEKFYD PMFKYHLTVA QVRGGMVFEL ANSIVLPFDC 550 560 570 580 590 600 RDYAVVLRKY ADKIYSISMK HPQEMKTYSV SFDSLFSAVK NFTEIASKFS ERLQDFDKSN 610 620 630 640 650 660 PIVLRMMNDQ LMFLERAFID PLGLPDRPFY RHVIYAPSSH NKYAGESFPG IYDALFDIES 670 680 690 KVDPSKAWGE VKRQIYVAAF TVQAAAETLS EVA
	Isoform PSMA-7 [UniParc]. Checksum: B8D9D69F67C3ABF2	FASTA	735	82,519
	10 20 30 40 50 60 MTAGSSYPLF LAAYACTGCL AERLGWFIKS SNEATNITPK HNMKAFLDEL KAENIKKFLY 70 80 90 100 110 120 NFTQIPHLAG TEQNFQLAKQ IQSQWKEFGL DSVELAHYDV LLSYPNKTHP NYISIINEDG 130 140 150 160 170 180 NEIFNTSLFE PPPPGYENVS DIVPPFSAFS PQGMPEGDLV YVNYARTEDF FKLERDMKIN 190 200 210 220 230 240 CSGKIVIARY GKVFRGNKVK NAQLAGAKGV ILYSDPADYF APGVKSYPDG WNLPGGGVQR 250 260 270 280 290 300 GNILNLNGAG DPLTPGYPAN EYAYRRGIAE AVGLPSIPVH PIGYYDAQKL LEKMGGSAPP 310 320 330 340 350 360 DSSWRGSLKV PYNVGPGFTG NFSTQKVKMH IHSTNEVTRI YNVIGTLRGA VEPDRYVILG 370 380 390 400 410 420 GHRDSWVFGG IDPQSGAAVV HEIVRSFGTL KKEGWRPRRT ILFASWDAEE FGLLGSTEWA 430 440 450 460 470 480 EENSRLLQER GVAYINADSS IEGNYTLRVD CTPLMYSLVH NLTKELKSPD EGFEGKSLYE 490 500 510 520 530 540 SWTKKSPSPE FSGMPRISKL GSGNDFEVFF QRLGIASGRA RYTKNWETNK FSGYPLYHSV 550 560 570 580 590 600 YETYELVEKF YDPMFKYHLT VAQVRGGMVF ELANSIVLPF DCRDYAVVLR KYADKIYSIS 610 620 630 640 650 660 MKHPQEMKTY SVSFDSLFSA VKNFTEIASK FSERLQDFDK SNPIVLRMMN DQLMFLERAF 670 680 690 700 710 720 IDPLGLPDRP FYRHVIYAPS SHNKYAGESF PGIYDALFDI ESKVDPSKAW GEVKRQIYVA 730 AFTVQAAAET LSEVA
	Isoform PSMA-8 [UniParc]. Checksum: AF79A10CA2BF9DF4	FASTA	719	80,597
	10 20 30 40 50 60 MWNLLHETDS AVATARRPRW LCAGALVLAG GFFLLGFLFG WFIKSSNEAT NITPKHNMKA 70 80 90 100 110 120 FLDELKAENI KKFLYNFTQI PHLAGTEQNF QLAKQIQSQW KEFGLDSVEL AHYDVLLSYP 130 140 150 160 170 180 NKTHPNYISI INEDGNEIFN TSLFEPPPPG YENVSDIVPP FSAFSPQGMP EGDLVYVNYA 190 200 210 220 230 240 RTEDFFKLER DMKINCSGKI VIARYGKVFR GNKVKNAQLA GAKGVILYSD PADYFAPGVK 250 260 270 280 290 300 SYPDGWNLPG GGVQRGNILN LNGAGDPLTP GYPANEYAYR RGIAEAVGLP SIPVHPIGYY 310 320 330 340 350 360 DAQKLLEKMG GSAPPDSSWR GSLKVPYNVG PGFTGNFSTQ KVKMHIHSTN EVTRIYNVIG 370 380 390 400 410 420 TLRGAVEPDR YVILGGHRDS WVFGGIDPQS GAAVVHEIVR SFGTLKKEGW RPRRTILFAS 430 440 450 460 470 480 WDAEEFGLLG STEWAEENSR LLQERGVAYI NADSSIEGNY TLRVDCTPLM YSLVHNLTKE 490 500 510 520 530 540 LKSPDEGFEG KSLYESWTKK SPSPEFSGMP RISKLGSGND FEVFFQRLGI ASGRARYTKN 550 560 570 580 590 600 WETNKFSGYP LYHSVYETYE LVEKFYDPMF KYHLTVAQVR GGMVFELANS IVLPFDCRDY 610 620 630 640 650 660 AVVLRKYADK IYSISMKHPQ EMKTYSVSFD SLFSAVKNFT EIASKFSERL QDFDKSKHVI 670 680 690 700 710 YAPSSHNKYA GESFPGIYDA LFDIESKVDP SKAWGEVKRQ IYVAAFTVQA AAETLSEVA
	Isoform PSMA-9 (PSM-E) [UniParc]. Checksum: 800DE87726E1328C	FASTA	704	78,785
	10 20 30 40 50 60 MTAGSSYPLF LAAYACTGCL AERLGWFIKS SNEATNITPK HNMKAFLDEL KAENIKKFLY 70 80 90 100 110 120 NFTQIPHLAG TEQNFQLAKQ IQSQWKEFGL DSVELAHYDV LLSYPNKTHP NYISIINEDG 130 140 150 160 170 180 NEIFNTSLFE PPPPGYENVS DIVPPFSAFS PQGMPEGDLV YVNYARTEDF FKLERDMKIN 190 200 210 220 230 240 CSGKIVIARY GKVFRGNKVK NAQLAGAKGV ILYSDPADYF APGVKSYPDG WNLPGGGVQR 250 260 270 280 290 300 GNILNLNGAG DPLTPGYPAN EYAYRRGIAE AVGLPSIPVH PIGYYDAQKL LEKMGGSAPP 310 320 330 340 350 360 DSSWRGSLKV PYNVGPGFTG NFSTQKVKMH IHSTNEVTRI YNVIGTLRGA VEPDRYVILG 370 380 390 400 410 420 GHRDSWVFGG IDPQSGAAVV HEIVRSFGTL KKEGWRPRRT ILFASWDAEE FGLLGSTEWA 430 440 450 460 470 480 EENSRLLQER GVAYINADSS IEGNYTLRVD CTPLMYSLVH NLTKELKSPD EGFEGKSLYE 490 500 510 520 530 540 SWTKKSPSPE FSGMPRISKL GSGNDFEVFF QRLGIASGRA RYTKNWETNK FSGYPLYHSV 550 560 570 580 590 600 YETYELVEKF YDPMFKYHLT VAQVRGGMVF ELANSIVLPF DCRDYAVVLR KYADKIYSIS 610 620 630 640 650 660 MKHPQEMKTY SVSFDSLFSA VKNFTEIASK FSERLQDFDK SKHVIYAPSS HNKYAGESFP 670 680 690 700 GIYDALFDIE SKVDPSKAWG EVKRQIYVAA FTVQAAAETL SEVA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8417812] [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: 7882349] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PSMA'). Tissue: Prostate.
[3]	"Mapping, genomic organization and promoter analysis of the human prostate-specific membrane antigen gene." O'Keefe D.S., Su S.L., Bacich D.J., Horiguchi Y., Luo Y., Powell C.T., Zandvliet D., Russell P.J., Molloy P.L., Nowak N.J., Shows T.B., Mullins C., Vonder Haar R.A., Fair W.R., Heston W.D.W. Biochim. Biophys. Acta 1443:113-127(1998) [PubMed: 9838072] [Abstract] 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: 9694964] [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: 10085079] [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: 11092759] [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: 17929272] [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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS PSMA-1 AND PSMA-7). Tissue: Amygdala and Hippocampus.
[12]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed: 16554811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [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: 9375657] [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: 9809977] [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: 9622670] [Abstract] Cited for: CHARACTERIZATION.
[20]	"Structure of membrane glutamate carboxypeptidase." Rawlings N.D., Barrett A.J. Biochim. Biophys. Acta 1339:247-252(1997) [PubMed: 9187245] [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: 9882712] [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: 12754519] [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: 15152093] [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: 14716746] [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: 16555021] [Abstract] Cited for: TISSUE SPECIFICITY.
[26]	"Expression of glutamate carboxypeptidase II in human brain." Sacha P., Zamecnik J., Barinka C., Hlouchova K., Vicha A., Mlcochova P., Hilgert I., Eckschlager T., Konvalinka J. Neuroscience 144:1361-1372(2007) [PubMed: 17150306] [Abstract] 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: 16467855] [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: 17372356] [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: 17567119] [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: 19053759] [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: 18234225] [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: 19301871] [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]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-23.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
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.

IPI

IPI00028514.
IPI00216908.
IPI00216910.
IPI00944595.
IPI00944663.
IPI00973065.
IPI01012792.

PIR

A56881.

RefSeq

NP_001014986.1. NM_001014986.1.
NP_001180400.1. NM_001193471.1.
NP_001180401.1. NM_001193472.1.
NP_001180402.1. NM_001193473.1.
NP_004467.1. NM_004476.1.

UniGene

Hs.654487.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
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	[»]

ProteinModelPortal

Q04609.

SMR

Q04609. Positions 55-750.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q04609. 3 interactions.

STRING

Q04609.

Protein family/group databases

MEROPS

M28.010.

PTM databases

PhosphoSite

Q04609.

Polymorphism databases

DMDM

548615.

Proteomic databases

PRIDE

Q04609.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000256999; ENSP00000256999; ENSG00000086205.
ENST00000356696; ENSP00000349129; ENSG00000086205.

GeneID

2346.

KEGG

hsa:2346.

UCSC

uc001ngy.1. human.

Organism-specific databases

CTD

2346.

GeneCards

GC11M049168.

H-InvDB

HIX0009626.

HGNC

HGNC:3788. FOLH1.

HPA

CAB001451.
HPA010593.

MIM

600934. gene.

neXtProt

NX_Q04609.

PharmGKB

PA28205.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG16210.

HOGENOM

HBG713441.

HOVERGEN

HBG051639.

OMA

IGMPRIS.

OrthoDB

EOG48GW2N.

PhylomeDB

Q04609.

Gene expression databases

ArrayExpress

Q04609.

Bgee

Q04609.

CleanEx

HS_FOLH1.

Genevestigator

Q04609.

GermOnline

ENSG00000086205. Homo sapiens.

Family and domain databases

InterPro

IPR007484. Peptidase_M28.
IPR003137. Protease-assoc_domain.
IPR007365. TFR-like_dimer_dom.
[Graphical view]

Gene3D

G3DSA:1.20.930.40. TFR_dimer. 1 hit.

KO

K14592.

Pfam

PF02225. PA. 1 hit.
PF04389. Peptidase_M28. 1 hit.
PF04253. TFR_dimer. 1 hit.
[Graphical view]

SUPFAM

SSF47672. Transferrin_rcpt-like_dimerise. 1 hit.

ProtoNet

Search...

Other

BindingDB

Q04609.

DrugBank

DB00089. Capromab.
DB00142. L-Glutamic Acid.

NextBio

9513.

SOURCE

Search...

Entry information

Entry name

FOLH1_HUMAN

Accession

Primary (citable) accession number: Q04609
Secondary accession number(s): A4UU12 , A9CB79, B7Z343, D3DQS5, O43748, Q16305, Q541A4, Q8TAY3, Q9NP15, Q9NYE2, Q9P1P8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	January 25, 2012
This is version 135 of the entry and version 1 of the sequence. [Complete history]

Entry status

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.