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Protein

Glutamate decarboxylase 1

Gene

GAD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 5'-phosphate1 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: InterPro

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.
BRENDAi4.1.1.15. 2681.
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 Componenti: 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)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:603513
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.

Polymorphism and mutation databases

BioMutaiGAD1.
DMDMi1352213.

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.
HPA031949.
HPA048871.
HPA058412.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AGTRAPQ6RW133EBI-743184,EBI-741181
CMTM5Q96DZ94EBI-743184,EBI-2548702
HAAOP469524EBI-743184,EBI-743215
NCK1P163332EBI-743184,EBI-389883
STK3Q131883EBI-743184,EBI-992580

Protein-protein interaction databases

BioGridi108845. 9 interactions.
DIPiDIP-29292N.
IntActiQ99259. 9 interactions.
MINTiMINT-3058814.
STRINGi9606.ENSP00000350928.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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. AlignAdd to basket

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 (Ref. 7) Curated
Sequence conflicti16 – 172GA → EP in AAB59427 (PubMed:1339255).Curated
Sequence conflicti16 – 172GA → EP in CAA80435 (PubMed:1339255).Curated
Sequence conflicti17 – 171A → Q in AAA35900 (Ref. 7) Curated
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 (Ref. 7) Curated
Sequence conflicti140 – 1401D → E in AAA35900 (Ref. 7) Curated
Sequence conflicti142 – 1421H → R in AAA35900 (Ref. 7) Curated
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:
EMBLi
GenBanki
DDBJi
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_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 and mutation databases

BioMutaiGAD1.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Glutamate decarboxylase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005246501.1. XM_005246444.2. [Q99259-3]
UniGeneiHs.420036.

3D structure databases

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

Protein-protein interaction databases

BioGridi108845. 9 interactions.
DIPiDIP-29292N.
IntActiQ99259. 9 interactions.
MINTiMINT-3058814.
STRINGi9606.ENSP00000350928.

Chemistry

ChEMBLiCHEMBL2614.
GuidetoPHARMACOLOGYi1272.

PTM databases

PhosphoSiteiQ99259.

Polymorphism and mutation databases

BioMutaiGAD1.
DMDMi1352213.

Proteomic databases

PaxDbiQ99259.
PRIDEiQ99259.

Protocols and materials databases

DNASUi2571.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi2571.
GeneCardsiGC02P171669.
HGNCiHGNC:4092. GAD1.
HPAiCAB004415.
HPA031949.
HPA048871.
HPA058412.
MIMi603513. phenotype.
605363. gene.
neXtProtiNX_Q99259.
Orphaneti210141. Inherited congenital spastic tetraplegia.
PharmGKBiPA28507.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciMetaCyc:HS05215-MONOMER.
BRENDAi4.1.1.15. 2681.
ReactomeiREACT_23947. GABA synthesis, release, reuptake and degradation.
REACT_24020. GABA synthesis.

Miscellaneous databases

ChiTaRSiGAD1. human.
EvolutionaryTraceiQ99259.
GenomeRNAii2571.
NextBioi10169.
PROiQ99259.
SOURCEiSearch...

Gene expression databases

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

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]
ProtoNetiSearch...

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: April 29, 2015
This is version 149 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.