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Q99259

- DCE1_HUMAN

UniProt

Q99259 - DCE1_HUMAN

Protein

Glutamate decarboxylase 1

Gene

GAD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    4. 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

    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. axon terminus Source: Ensembl
    2. cell cortex Source: Ensembl
    3. clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane Source: Reactome
    4. intracellular Source: UniProtKB
    5. mitochondrion Source: Ensembl
    6. plasma membrane Source: Reactome
    7. presynaptic active zone Source: Ensembl
    8. vesicle membrane Source: UniProtKB

    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

    ArrayExpressiQ99259.
    BgeeiQ99259.
    CleanExiHS_GAD1.
    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.
    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

    MASSTPSSSA TSSNAGADPN TTNLRPTTYD TWCGVAHGCT RKLGLKICGF    50
    LQRTNSLEEK SRLVSAFKER QSSKNLLSCE NSDRDARFRR TETDFSNLFA 100
    RDLLPAKNGE EQTVQFLLEV VDILLNYVRK TFDRSTKVLD FHHPHQLLEG 150
    MEGFNLELSD HPESLEQILV DCRDTLKYGV RTGHPRFFNQ LSTGLDIIGL 200
    AGEWLTSTAN TNMFTYEIAP VFVLMEQITL KKMREIVGWS SKDGDGIFSP 250
    GGAISNMYSI MAARYKYFPE VKTKGMAAVP KLVLFTSEQS HYSIKKAGAA 300
    LGFGTDNVIL IKCNERGKII PADFEAKILE AKQKGYVPFY VNATAGTTVY 350
    GAFDPIQEIA DICEKYNLWL HVDAAWGGGL LMSRKHRHKL NGIERANSVT 400
    WNPHKMMGVL LQCSAILVKE KGILQGCNQM CAGYLFQPDK QYDVSYDTGD 450
    KAIQCGRHVD IFKFWLMWKA KGTVGFENQI NKCLELAEYL YAKIKNREEF 500
    EMVFNGEPEH TNVCFWYIPQ SLRGVPDSPQ RREKLHKVAP KIKALMMESG 550
    TTMVGYQPQG DKANFFRMVI SNPAATQSDI DFLIEEIERL GQDL 594
    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.
    DrugBanki DB00142. L-Glutamic Acid.
    DB00114. Pyridoxal Phosphate.

    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.
    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

    ArrayExpressi Q99259.
    Bgeei Q99259.
    CleanExi HS_GAD1.
    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

    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 1, 2014
    This is version 142 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