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Q99259

- DCE1_HUMAN

UniProt

Q99259 - DCE1_HUMAN

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Protein

Glutamate decarboxylase 1

Gene

GAD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the production of GABA.

Catalytic activityi

L-glutamate = 4-aminobutanoate + CO2.

Cofactori

Pyridoxal phosphate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei567 – 5671Substrate

GO - Molecular functioni

  1. glutamate binding Source: Ensembl
  2. glutamate decarboxylase activity Source: UniProtKB
  3. pyridoxal phosphate binding Source: Ensembl

GO - Biological processi

  1. gamma-aminobutyric acid biosynthetic process Source: Ensembl
  2. glutamate catabolic process Source: UniProtKB
  3. glutamate decarboxylation to succinate Source: ProtInc
  4. neurotransmitter biosynthetic process Source: UniProtKB-KW
  5. neurotransmitter secretion Source: Reactome
  6. protein-pyridoxal-5-phosphate linkage Source: UniProtKB
  7. response to drug Source: Ensembl
  8. synaptic transmission Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Neurotransmitter biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:HS05215-MONOMER.
ReactomeiREACT_23947. GABA synthesis, release, reuptake and degradation.
REACT_24020. GABA synthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate decarboxylase 1 (EC:4.1.1.15)
Alternative name(s):
67 kDa glutamic acid decarboxylase
Short name:
GAD-67
Glutamate decarboxylase 67 kDa isoform
Gene namesi
Name:GAD1
Synonyms:GAD, GAD67
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:4092. GAD1.

Subcellular locationi

GO - Cellular componenti

  1. clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane Source: Reactome
  2. intracellular Source: UniProtKB
  3. plasma membrane Source: Reactome
  4. vesicle membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Cerebral palsy, spastic quadriplegic 1 (CPSQ1) [MIM:603513]: A non-progressive disorder of movement and/or posture resulting from defects in the developing central nervous system. Affected individuals manifest symmetrical, non-progressive spasticity and no adverse perinatal history or obvious underlying alternative diagnosis. Developmental delay, mental retardation and sometimes epilepsy can be part of the clinical picture.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121S → C in CPSQ1. 1 Publication
VAR_031021

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi603513. phenotype.
Orphaneti210141. Inherited congenital spastic tetraplegia.
PharmGKBiPA28507.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 594594Glutamate decarboxylase 1PRO_0000146963Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei405 – 4051N6-(pyridoxal phosphate)lysine

Proteomic databases

PaxDbiQ99259.
PRIDEiQ99259.

PTM databases

PhosphoSiteiQ99259.

Expressioni

Tissue specificityi

Isoform 3 is expressed in pancreatic islets, testis, adrenal cortex, and perhaps other endocrine tissues, but not in brain.1 Publication

Gene expression databases

BgeeiQ99259.
CleanExiHS_GAD1.
ExpressionAtlasiQ99259. baseline and differential.
GenevestigatoriQ99259.

Organism-specific databases

HPAiCAB004415.
HPA058412.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NCK1P163332EBI-743184,EBI-389883

Protein-protein interaction databases

BioGridi108845. 4 interactions.
DIPiDIP-29292N.
IntActiQ99259. 7 interactions.
MINTiMINT-3058814.
STRINGi9606.ENSP00000350928.

Structurei

Secondary structure

1
594
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni94 – 974
Helixi100 – 1023
Helixi110 – 13122
Helixi144 – 1496
Helixi165 – 17713
Beta strandi187 – 1926
Helixi197 – 20913
Beta strandi212 – 2143
Turni216 – 2183
Helixi220 – 23718
Beta strandi241 – 2433
Beta strandi245 – 2517
Helixi252 – 26716
Helixi270 – 2745
Helixi276 – 2783
Beta strandi282 – 2876
Helixi293 – 3008
Helixi305 – 3073
Beta strandi308 – 3114
Helixi321 – 33313
Beta strandi337 – 34610
Beta strandi348 – 3503
Helixi356 – 36611
Beta strandi369 – 3746
Helixi377 – 3826
Turni384 – 3863
Helixi387 – 3904
Helixi393 – 3953
Beta strandi397 – 4015
Beta strandi414 – 4207
Helixi423 – 4286
Turni433 – 4353
Helixi444 – 4463
Helixi449 – 4513
Helixi461 – 49535
Beta strandi500 – 5067
Beta strandi509 – 5113
Beta strandi513 – 5175
Helixi520 – 5223
Helixi529 – 54921
Beta strandi553 – 5597
Beta strandi562 – 5687
Helixi577 – 59115

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OKJX-ray2.30A/B93-594[»]
3VP6X-ray2.10A/B90-594[»]
ProteinModelPortaliQ99259.
SMRiQ99259. Positions 93-593.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99259.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni190 – 1923Substrate binding

Sequence similaritiesi

Belongs to the group II decarboxylase family.Curated

Phylogenomic databases

eggNOGiCOG0076.
GeneTreeiENSGT00760000119205.
HOGENOMiHOG000005382.
HOVERGENiHBG004980.
InParanoidiQ99259.
KOiK01580.
OMAiEYLYTKI.
OrthoDBiEOG7H1JM3.
PhylomeDBiQ99259.
TreeFamiTF314688.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR021115. Pyridoxal-P_BS.
[Graphical view]
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q99259-1) [UniParc]FASTAAdd to Basket

Also known as: GAD67

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

        10         20         30         40         50
MASSTPSSSA TSSNAGADPN TTNLRPTTYD TWCGVAHGCT RKLGLKICGF
60 70 80 90 100
LQRTNSLEEK SRLVSAFKER QSSKNLLSCE NSDRDARFRR TETDFSNLFA
110 120 130 140 150
RDLLPAKNGE EQTVQFLLEV VDILLNYVRK TFDRSTKVLD FHHPHQLLEG
160 170 180 190 200
MEGFNLELSD HPESLEQILV DCRDTLKYGV RTGHPRFFNQ LSTGLDIIGL
210 220 230 240 250
AGEWLTSTAN TNMFTYEIAP VFVLMEQITL KKMREIVGWS SKDGDGIFSP
260 270 280 290 300
GGAISNMYSI MAARYKYFPE VKTKGMAAVP KLVLFTSEQS HYSIKKAGAA
310 320 330 340 350
LGFGTDNVIL IKCNERGKII PADFEAKILE AKQKGYVPFY VNATAGTTVY
360 370 380 390 400
GAFDPIQEIA DICEKYNLWL HVDAAWGGGL LMSRKHRHKL NGIERANSVT
410 420 430 440 450
WNPHKMMGVL LQCSAILVKE KGILQGCNQM CAGYLFQPDK QYDVSYDTGD
460 470 480 490 500
KAIQCGRHVD IFKFWLMWKA KGTVGFENQI NKCLELAEYL YAKIKNREEF
510 520 530 540 550
EMVFNGEPEH TNVCFWYIPQ SLRGVPDSPQ RREKLHKVAP KIKALMMESG
560 570 580 590
TTMVGYQPQG DKANFFRMVI SNPAATQSDI DFLIEEIERL GQDL
Length:594
Mass (Da):66,897
Last modified:February 1, 1996 - v1
Checksum:i6D761C471C81FDAE
GO
Isoform 2 (identifier: Q99259-2)

Sequence is not available
Length:
Mass (Da):
Isoform 3 (identifier: Q99259-3) [UniParc]FASTAAdd to Basket

Also known as: GAD25

The sequence of this isoform differs from the canonical sequence as follows:
     214-224: FTYEIAPVFVL → PSDMRECWLLR
     225-594: Missing.

Note: Lacks enzymatic activity.

Show »
Length:224
Mass (Da):25,279
Checksum:i2CDCB04ECD6BC2E9
GO
Isoform 4 (identifier: Q99259-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     374-425: AAWGGGLLMS...ILVKEKGILQ → GFNFSQLANR...WAAHVQEAPP
     426-594: Missing.

Note: No experimental confirmation available.

Show »
Length:425
Mass (Da):47,440
Checksum:iF392B68338CC6800
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91Missing in AAA35900. 1 PublicationCurated
Sequence conflicti16 – 172GA → EP in AAB59427. (PubMed:1339255)Curated
Sequence conflicti16 – 172GA → EP in CAA80435. (PubMed:1339255)Curated
Sequence conflicti17 – 171A → Q in AAA35900. 1 PublicationCurated
Sequence conflicti18 – 181D → N in AAB26938. (PubMed:8507203)Curated
Sequence conflicti31 – 311T → N in AAB26938. (PubMed:8507203)Curated
Sequence conflicti68 – 681K → R in AAA62368. (PubMed:8088791)Curated
Sequence conflicti116 – 1161F → L in AAB26938. (PubMed:8507203)Curated
Sequence conflicti136 – 1361T → A in AAA35900. 1 PublicationCurated
Sequence conflicti140 – 1401D → E in AAA35900. 1 PublicationCurated
Sequence conflicti142 – 1421H → R in AAA35900. 1 PublicationCurated
Sequence conflicti155 – 1551N → T in AAB26938. (PubMed:8507203)Curated
Sequence conflicti206 – 2061T → N in AAB59427. (PubMed:1339255)Curated
Sequence conflicti206 – 2061T → N in CAA80435. (PubMed:1339255)Curated
Sequence conflicti302 – 3021G → C in AAB26938. (PubMed:8507203)Curated
Sequence conflicti436 – 4361F → L in AAB26937. (PubMed:8507202)Curated
Sequence conflicti477 – 4771E → G in AAB26938. (PubMed:8507203)Curated
Sequence conflicti492 – 4921A → G in AAB26938. (PubMed:8507203)Curated
Sequence conflicti512 – 5121N → S in AAB26937. (PubMed:8507202)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121S → C in CPSQ1. 1 Publication
VAR_031021
Natural varianti228 – 2281I → L.1 Publication
Corresponds to variant rs45566933 [ dbSNP | Ensembl ].
VAR_018861
Natural varianti474 – 4741V → G.
Corresponds to variant rs769403 [ dbSNP | Ensembl ].
VAR_011882
Natural varianti532 – 5321R → Q.1 Publication
Corresponds to variant rs769402 [ dbSNP | Ensembl ].
VAR_011883
Natural varianti565 – 5651F → L.
Corresponds to variant rs1049736 [ dbSNP | Ensembl ].
VAR_011884

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei214 – 22411FTYEIAPVFVL → PSDMRECWLLR in isoform 3. 2 PublicationsVSP_009123Add
BLAST
Alternative sequencei225 – 594370Missing in isoform 3. 2 PublicationsVSP_009124Add
BLAST
Alternative sequencei374 – 42552AAWGG…KGILQ → GFNFSQLANRIICLATELMT NKGCVTWHPNYSVNMHHGCL GRWAAHVQEAPP in isoform 4. 1 PublicationVSP_054473Add
BLAST
Alternative sequencei426 – 594169Missing in isoform 4. 1 PublicationVSP_054474Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M81883 mRNA. Translation: AAA62368.1.
L16888 mRNA. Translation: AAB59427.1.
Z22750 mRNA. Translation: CAA80435.1.
S61897 mRNA. Translation: AAB26937.1.
S61898 mRNA. Translation: AAB26938.1.
M86522 Genomic DNA. Translation: AAA35900.1.
AF178853 mRNA. Translation: AAF18390.2.
AY337516 Genomic DNA. Translation: AAP88035.1.
AC007405 Genomic DNA. Translation: AAY24237.1.
CH471058 Genomic DNA. Translation: EAX11228.1.
CH471058 Genomic DNA. Translation: EAX11229.1.
BC002815 mRNA. Translation: AAH02815.1.
BC026349 mRNA. Translation: AAH26349.1.
BC036552 mRNA. Translation: AAH36552.1.
M70434 mRNA. Translation: AAA52512.1.
M55574 mRNA. Translation: AAA72938.1.
CCDSiCCDS2239.1. [Q99259-1]
CCDS2240.1. [Q99259-3]
PIRiB41935.
S48135.
S51775.
S51776.
RefSeqiNP_000808.2. NM_000817.2. [Q99259-1]
NP_038473.2. NM_013445.3. [Q99259-3]
XP_005246500.1. XM_005246443.2. [Q99259-1]
XP_005246501.1. XM_005246444.2. [Q99259-3]
UniGeneiHs.420036.

Genome annotation databases

EnsembliENST00000344257; ENSP00000341167; ENSG00000128683. [Q99259-3]
ENST00000358196; ENSP00000350928; ENSG00000128683. [Q99259-1]
ENST00000375272; ENSP00000364421; ENSG00000128683. [Q99259-3]
ENST00000493875; ENSP00000434696; ENSG00000128683. [Q99259-4]
GeneIDi2571.
KEGGihsa:2571.
UCSCiuc002ugh.3. human. [Q99259-3]
uc002ugi.3. human. [Q99259-1]

Polymorphism databases

DMDMi1352213.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Glutamate decarboxylase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M81883 mRNA. Translation: AAA62368.1 .
L16888 mRNA. Translation: AAB59427.1 .
Z22750 mRNA. Translation: CAA80435.1 .
S61897 mRNA. Translation: AAB26937.1 .
S61898 mRNA. Translation: AAB26938.1 .
M86522 Genomic DNA. Translation: AAA35900.1 .
AF178853 mRNA. Translation: AAF18390.2 .
AY337516 Genomic DNA. Translation: AAP88035.1 .
AC007405 Genomic DNA. Translation: AAY24237.1 .
CH471058 Genomic DNA. Translation: EAX11228.1 .
CH471058 Genomic DNA. Translation: EAX11229.1 .
BC002815 mRNA. Translation: AAH02815.1 .
BC026349 mRNA. Translation: AAH26349.1 .
BC036552 mRNA. Translation: AAH36552.1 .
M70434 mRNA. Translation: AAA52512.1 .
M55574 mRNA. Translation: AAA72938.1 .
CCDSi CCDS2239.1. [Q99259-1 ]
CCDS2240.1. [Q99259-3 ]
PIRi B41935.
S48135.
S51775.
S51776.
RefSeqi NP_000808.2. NM_000817.2. [Q99259-1 ]
NP_038473.2. NM_013445.3. [Q99259-3 ]
XP_005246500.1. XM_005246443.2. [Q99259-1 ]
XP_005246501.1. XM_005246444.2. [Q99259-3 ]
UniGenei Hs.420036.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2OKJ X-ray 2.30 A/B 93-594 [» ]
3VP6 X-ray 2.10 A/B 90-594 [» ]
ProteinModelPortali Q99259.
SMRi Q99259. Positions 93-593.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108845. 4 interactions.
DIPi DIP-29292N.
IntActi Q99259. 7 interactions.
MINTi MINT-3058814.
STRINGi 9606.ENSP00000350928.

Chemistry

BindingDBi Q99259.
ChEMBLi CHEMBL2614.

PTM databases

PhosphoSitei Q99259.

Polymorphism databases

DMDMi 1352213.

Proteomic databases

PaxDbi Q99259.
PRIDEi Q99259.

Protocols and materials databases

DNASUi 2571.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000344257 ; ENSP00000341167 ; ENSG00000128683 . [Q99259-3 ]
ENST00000358196 ; ENSP00000350928 ; ENSG00000128683 . [Q99259-1 ]
ENST00000375272 ; ENSP00000364421 ; ENSG00000128683 . [Q99259-3 ]
ENST00000493875 ; ENSP00000434696 ; ENSG00000128683 . [Q99259-4 ]
GeneIDi 2571.
KEGGi hsa:2571.
UCSCi uc002ugh.3. human. [Q99259-3 ]
uc002ugi.3. human. [Q99259-1 ]

Organism-specific databases

CTDi 2571.
GeneCardsi GC02P171669.
HGNCi HGNC:4092. GAD1.
HPAi CAB004415.
HPA058412.
MIMi 603513. phenotype.
605363. gene.
neXtProti NX_Q99259.
Orphaneti 210141. Inherited congenital spastic tetraplegia.
PharmGKBi PA28507.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0076.
GeneTreei ENSGT00760000119205.
HOGENOMi HOG000005382.
HOVERGENi HBG004980.
InParanoidi Q99259.
KOi K01580.
OMAi EYLYTKI.
OrthoDBi EOG7H1JM3.
PhylomeDBi Q99259.
TreeFami TF314688.

Enzyme and pathway databases

BioCyci MetaCyc:HS05215-MONOMER.
Reactomei REACT_23947. GABA synthesis, release, reuptake and degradation.
REACT_24020. GABA synthesis.

Miscellaneous databases

ChiTaRSi GAD1. human.
EvolutionaryTracei Q99259.
GenomeRNAii 2571.
NextBioi 10169.
PROi Q99259.
SOURCEi Search...

Gene expression databases

Bgeei Q99259.
CleanExi HS_GAD1.
ExpressionAtlasi Q99259. baseline and differential.
Genevestigatori Q99259.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR021115. Pyridoxal-P_BS.
[Graphical view ]
Pfami PF00282. Pyridoxal_deC. 1 hit.
[Graphical view ]
SUPFAMi SSF53383. SSF53383. 1 hit.
PROSITEi PS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are each encoded by a single gene."
    Bu D.-F., Erlander M.G., Hitz B.C., Tillakaratne N.J., Kaufman D.L., Wagner-Mcpherson C.B., Evans G.A., Tobin A.J.
    Proc. Natl. Acad. Sci. U.S.A. 89:2115-2119(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "The exon-intron organization of the genes (GAD1 and GAD2) encoding two human glutamate decarboxylases (GAD67 and GAD65) suggests that they derive from a common ancestral GAD."
    Bu D.-F., Tobin A.J.
    Genomics 21:222-228(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Cloning of large isoform of human brain glutamic acid decarboxylase."
    Kelly C.D., Carter N.D., Johnstone A.P., Nussey S.S.
    Lancet 338:1468-1469(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Nucleotide sequence and chromosomal assignment of a cDNA encoding the large isoform of human glutamate decarboxylase."
    Kelly C.D., Edwards Y., Johnstone A.P., Harfst E., Nogradi A., Nussey S.S., Povey S., Carter N.D.
    Ann. Hum. Genet. 56:255-265(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  5. "Molecular cloning of full-length glutamic acid decarboxylase 67 from human pancreas and islets."
    Yamashita K., Cram D.S., Harrison L.C.
    Biochem. Biophys. Res. Commun. 192:1347-1352(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  6. "Cloning and expression of large isoform of glutamic acid decarboxylase from human pancreatic islet."
    Kawasaki E., Moriuchi R., Watanabe M., Saitoh K., Brunicardi F.C., Watt P.C., Yamaguchi T., Mullen Y., Akazawa S., Miyamoto T.
    Biochem. Biophys. Res. Commun. 192:1353-1359(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Pancreatic islet.
  7. "Sequence of glutamic acid decarboxylase transcripts in human pancreatic islets and brain."
    Giorda R., Peakman M., Vergani D., Trucco M.
    Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  8. "Alternative splicing of GAD67 results in the synthesis of a third form of glutamic-acid decarboxylase in human islets and other non-neural tissues."
    Chessler S.D., Lernmark A.
    J. Biol. Chem. 275:5188-5192(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
    Tissue: Pancreatic islet and Testis.
  9. NIEHS SNPs program
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-228 AND GLN-532.
  10. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  12. "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] (ISOFORMS 1; 3 AND 4).
    Tissue: Brain.
  13. "Cloning and partial nucleotide sequence of human glutamic acid decarboxylase cDNA from brain and pancreatic islets."
    Cram D.S., Barnett L.D., Joseph J.L., Harrison L.C.
    Biochem. Biophys. Res. Commun. 176:1239-1244(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 218-397.
    Tissue: Brain.
  14. "Expression of the neurotransmitter-synthesizing enzyme glutamic acid decarboxylase in male germ cells."
    Persson H., Pelto-Huikko M., Metsis M., Soeder O., Brene S., Skog S., Hoekfelt T., Ritzen E.M.
    Mol. Cell. Biol. 10:4701-4711(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 527-594.
    Tissue: Testis.
  15. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 93-594 IN COMPLEX WITH SUBSTRATE ANALOG, SUBUNIT, COFACTOR.
  16. "Homozygosity for a missense mutation in the 67 kDa isoform of glutamate decarboxylase in a family with autosomal recessive spastic cerebral palsy: parallels with Stiff-Person Syndrome and other movement disorders."
    Lynex C.N., Carr I.M., Leek J.P., Achuthan R., Mitchell S., Maher E.R., Woods C.G., Bonthon D.T., Markham A.F.
    BMC Neurol. 4:20-20(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CPSQ1 CYS-12.

Entry informationi

Entry nameiDCE1_HUMAN
AccessioniPrimary (citable) accession number: Q99259
Secondary accession number(s): Q49AK1
, Q53TQ7, Q9BU91, Q9UHH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: October 29, 2014
This is version 143 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3