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Q05329

- DCE2_HUMAN

UniProt

Q05329 - DCE2_HUMAN

Protein

Glutamate decarboxylase 2

Gene

GAD2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (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

    Kineticsi

    1. KM=2.15 mM for glutamate1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei558 – 5581Substrate1 Publication

    GO - Molecular functioni

    1. glutamate binding Source: Ensembl
    2. glutamate decarboxylase activity Source: UniProtKB-EC
    3. protein binding Source: UniProtKB
    4. pyridoxal phosphate binding Source: Ensembl

    GO - Biological processi

    1. glutamate decarboxylation to succinate Source: ProtInc
    2. neurotransmitter biosynthetic process Source: UniProtKB-KW
    3. neurotransmitter secretion Source: Reactome
    4. response to drug Source: Ensembl
    5. synaptic transmission Source: Reactome

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Biological processi

    Neurotransmitter biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06208-MONOMER.
    ReactomeiREACT_23947. GABA synthesis, release, reuptake and degradation.
    REACT_24020. GABA synthesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate decarboxylase 2 (EC:4.1.1.15)
    Alternative name(s):
    65 kDa glutamic acid decarboxylase
    Short name:
    GAD-65
    Glutamate decarboxylase 65 kDa isoform
    Gene namesi
    Name:GAD2
    Synonyms:GAD65
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:4093. GAD2.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication. Cytoplasmic vesicle 1 Publication. Cell junctionsynapsepresynaptic cell membrane 1 Publication; Lipid-anchor 1 Publication. Golgi apparatus membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication
    Note: Associated to cytoplasmic vesicles. In neurons, cytosolic leaflet of Golgi membranes and presynaptic clusters.

    GO - Cellular componenti

    1. anchored component of membrane Source: Ensembl
    2. axon Source: Ensembl
    3. cell junction Source: UniProtKB-KW
    4. clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane Source: Reactome
    5. cytosol Source: UniProtKB-SubCell
    6. Golgi membrane Source: UniProtKB-SubCell
    7. perinuclear region of cytoplasm Source: Ensembl
    8. plasma membrane Source: Reactome
    9. presynaptic membrane Source: UniProtKB-SubCell
    10. synaptic vesicle membrane Source: Ensembl

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane, Synapse

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28508.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 585585Glutamate decarboxylase 2PRO_0000146968Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31Phosphoserine1 Publication
    Modified residuei6 – 61Phosphoserine1 Publication
    Modified residuei10 – 101Phosphoserine1 Publication
    Modified residuei13 – 131Phosphoserine1 Publication
    Lipidationi30 – 301S-palmitoyl cysteine1 Publication
    Lipidationi45 – 451S-palmitoyl cysteine1 Publication
    Modified residuei396 – 3961N6-(pyridoxal phosphate)lysine

    Post-translational modificationi

    Phosphorylated; which does not affect kinetic parameters or subcellular location.1 Publication
    Palmitoylated; which is required for presynaptic clustering.1 Publication

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    PaxDbiQ05329.
    PeptideAtlasiQ05329.
    PRIDEiQ05329.

    PTM databases

    PhosphoSiteiQ05329.

    Expressioni

    Gene expression databases

    ArrayExpressiQ05329.
    BgeeiQ05329.
    CleanExiHS_GAD2.
    GenevestigatoriQ05329.

    Organism-specific databases

    HPAiCAB002682.
    HPA044637.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi108846. 3 interactions.
    DIPiDIP-29293N.
    STRINGi9606.ENSP00000259271.

    Structurei

    Secondary structure

    1
    585
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi89 – 913
    Helixi94 – 963
    Helixi104 – 12623
    Helixi138 – 1447
    Helixi156 – 16914
    Beta strandi178 – 1836
    Helixi188 – 20013
    Turni207 – 2093
    Helixi211 – 22818
    Helixi231 – 2333
    Beta strandi235 – 2428
    Helixi243 – 25816
    Helixi262 – 2654
    Helixi267 – 2693
    Beta strandi273 – 2786
    Helixi284 – 2918
    Helixi296 – 2983
    Beta strandi299 – 3024
    Helixi312 – 32413
    Beta strandi328 – 33710
    Turni339 – 3413
    Helixi347 – 35711
    Beta strandi360 – 3656
    Helixi368 – 3736
    Turni375 – 3773
    Helixi378 – 3814
    Helixi384 – 3863
    Beta strandi388 – 3925
    Beta strandi405 – 4117
    Helixi414 – 4196
    Helixi435 – 4373
    Helixi440 – 4423
    Helixi452 – 48635
    Beta strandi491 – 4977
    Beta strandi500 – 5023
    Beta strandi504 – 5085
    Turni511 – 5155
    Helixi523 – 5264
    Helixi529 – 54012
    Beta strandi544 – 5507
    Beta strandi553 – 5597
    Helixi568 – 58114

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ES0X-ray2.60B207-220[»]
    2OKKX-ray2.30A88-584[»]
    ProteinModelPortaliQ05329.
    SMRiQ05329. Positions 88-584.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ05329.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni181 – 1833Substrate binding

    Sequence similaritiesi

    Belongs to the group II decarboxylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0076.
    HOGENOMiHOG000005382.
    HOVERGENiHBG004980.
    InParanoidiQ05329.
    KOiK01580.
    OMAiWRAKGTT.
    OrthoDBiEOG7H1JM3.
    PhylomeDBiQ05329.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q05329-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASPGSGFWS FGSEDGSGDS ENPGTARAWC QVAQKFTGGI GNKLCALLYG    50
    DAEKPAESGG SQPPRAAARK AACACDQKPC SCSKVDVNYA FLHATDLLPA 100
    CDGERPTLAF LQDVMNILLQ YVVKSFDRST KVIDFHYPNE LLQEYNWELA 150
    DQPQNLEEIL MHCQTTLKYA IKTGHPRYFN QLSTGLDMVG LAADWLTSTA 200
    NTNMFTYEIA PVFVLLEYVT LKKMREIIGW PGGSGDGIFS PGGAISNMYA 250
    MMIARFKMFP EVKEKGMAAL PRLIAFTSEH SHFSLKKGAA ALGIGTDSVI 300
    LIKCDERGKM IPSDLERRIL EAKQKGFVPF LVSATAGTTV YGAFDPLLAV 350
    ADICKKYKIW MHVDAAWGGG LLMSRKHKWK LSGVERANSV TWNPHKMMGV 400
    PLQCSALLVR EEGLMQNCNQ MHASYLFQQD KHYDLSYDTG DKALQCGRHV 450
    DVFKLWLMWR AKGTTGFEAH VDKCLELAEY LYNIIKNREG YEMVFDGKPQ 500
    HTNVCFWYIP PSLRTLEDNE ERMSRLSKVA PVIKARMMEY GTTMVSYQPL 550
    GDKVNFFRMV ISNPAATHQD IDFLIEEIER LGQDL 585
    Length:585
    Mass (Da):65,411
    Last modified:February 1, 1996 - v1
    Checksum:i0322509F0E2C32EE
    GO

    Sequence cautioni

    The sequence CAA49554.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti12 – 121G → R.1 Publication
    Corresponds to variant rs8190591 [ dbSNP | Ensembl ].
    VAR_018821
    Natural varianti124 – 1241K → N.1 Publication
    Corresponds to variant rs8190600 [ dbSNP | Ensembl ].
    VAR_018822
    Natural varianti153 – 1531P → Q.
    Corresponds to variant rs2839672 [ dbSNP | Ensembl ].
    VAR_029176
    Natural varianti232 – 2321G → E.
    Corresponds to variant rs2839673 [ dbSNP | Ensembl ].
    VAR_029177
    Natural varianti286 – 2861K → R.1 Publication
    Corresponds to variant rs8190671 [ dbSNP | Ensembl ].
    VAR_018823
    Natural varianti326 – 3261G → A.
    Corresponds to variant rs2839678 [ dbSNP | Ensembl ].
    VAR_029178
    Natural varianti375 – 3751R → Q.1 Publication
    Corresponds to variant rs8190730 [ dbSNP | Ensembl ].
    VAR_018824

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M81882 mRNA. Translation: AAA62367.1.
    M74826 mRNA. Translation: AAA58491.1.
    AY340073 Genomic DNA. Translation: AAP88040.1.
    X69936 mRNA. Translation: CAA49554.1. Different initiation.
    M70435 mRNA. Translation: AAA52513.1.
    CCDSiCCDS7149.1.
    PIRiA41935. A41292.
    RefSeqiNP_000809.1. NM_000818.2.
    NP_001127838.1. NM_001134366.1.
    UniGeneiHs.231829.

    Genome annotation databases

    EnsembliENST00000259271; ENSP00000259271; ENSG00000136750.
    ENST00000376261; ENSP00000365437; ENSG00000136750.
    GeneIDi2572.
    KEGGihsa:2572.
    UCSCiuc001isp.2. human.

    Polymorphism databases

    DMDMi1352216.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M81882 mRNA. Translation: AAA62367.1 .
    M74826 mRNA. Translation: AAA58491.1 .
    AY340073 Genomic DNA. Translation: AAP88040.1 .
    X69936 mRNA. Translation: CAA49554.1 . Different initiation.
    M70435 mRNA. Translation: AAA52513.1 .
    CCDSi CCDS7149.1.
    PIRi A41935. A41292.
    RefSeqi NP_000809.1. NM_000818.2.
    NP_001127838.1. NM_001134366.1.
    UniGenei Hs.231829.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ES0 X-ray 2.60 B 207-220 [» ]
    2OKK X-ray 2.30 A 88-584 [» ]
    ProteinModelPortali Q05329.
    SMRi Q05329. Positions 88-584.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108846. 3 interactions.
    DIPi DIP-29293N.
    STRINGi 9606.ENSP00000259271.

    Chemistry

    BindingDBi Q05329.
    ChEMBLi CHEMBL2952.
    DrugBanki DB00142. L-Glutamic Acid.

    PTM databases

    PhosphoSitei Q05329.

    Polymorphism databases

    DMDMi 1352216.

    Proteomic databases

    PaxDbi Q05329.
    PeptideAtlasi Q05329.
    PRIDEi Q05329.

    Protocols and materials databases

    DNASUi 2572.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000259271 ; ENSP00000259271 ; ENSG00000136750 .
    ENST00000376261 ; ENSP00000365437 ; ENSG00000136750 .
    GeneIDi 2572.
    KEGGi hsa:2572.
    UCSCi uc001isp.2. human.

    Organism-specific databases

    CTDi 2572.
    GeneCardsi GC10P026545.
    HGNCi HGNC:4093. GAD2.
    HPAi CAB002682.
    HPA044637.
    MIMi 138275. gene.
    neXtProti NX_Q05329.
    PharmGKBi PA28508.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0076.
    HOGENOMi HOG000005382.
    HOVERGENi HBG004980.
    InParanoidi Q05329.
    KOi K01580.
    OMAi WRAKGTT.
    OrthoDBi EOG7H1JM3.
    PhylomeDBi Q05329.
    TreeFami TF314688.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS06208-MONOMER.
    Reactomei REACT_23947. GABA synthesis, release, reuptake and degradation.
    REACT_24020. GABA synthesis.

    Miscellaneous databases

    EvolutionaryTracei Q05329.
    GeneWikii GAD2.
    GenomeRNAii 2572.
    NextBioi 10175.
    PROi Q05329.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q05329.
    Bgeei Q05329.
    CleanExi HS_GAD2.
    Genevestigatori Q05329.

    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. "Cloning and primary structure of a human islet isoform of glutamic acid decarboxylase from chromosome 10."
      Karlsen A.E., Hagopian W.A., Grubin C.E., Dube S., Disteche C.M., Adler D.A., Barmeier H., Mathewes S., Grant F.J., Foster D., Lernmark A.
      Proc. Natl. Acad. Sci. U.S.A. 88:8337-8341(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Pancreatic islet.
    2. "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].
    3. "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].
    4. NIEHS SNPs program
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-12; ASN-124; ARG-286 AND GLN-375.
    5. "Characterization of a linear epitope within the human pancreatic 64-kDa glutamic acid decarboxylase and its autoimmune recognition by sera from insulin-dependent diabetes mellitus patients."
      Mauch L., Abney C.C., Berg H., Scherbaum W.A., Liedvogel B., Northemann W.
      Eur. J. Biochem. 212:597-603(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-585.
      Tissue: Pancreas.
    6. "Differential expression of GAD65 and GAD67 in human, rat, and mouse pancreatic islets."
      Kim J., Richter W., Aanstoot H.-J., Shi Y., Fu Q., Rajotte R., Warnock G., Baekkeskov S.
      Diabetes 42:1799-1808(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 245-585.
    7. "Phosphorylation of serine residues 3, 6, 10, and 13 distinguishes membrane anchored from soluble glutamic acid decarboxylase 65 and is restricted to glutamic acid decarboxylase 65alpha."
      Namchuk M., Lindsay L., Turck C.W., Kanaani J., Baekkeskov S.
      J. Biol. Chem. 272:1548-1557(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-3; SER-6; SER-10 AND SER-13, BIOPHYSICOCHEMICAL PROPERTIES.
    8. "A combination of three distinct trafficking signals mediates axonal targeting and presynaptic clustering of GAD65."
      Kanaani J., El-Din El-Husseini A., Aguilera-Moreno A., Diacovo J.M., Bredt D.S., Baekkeskov S.
      J. Cell Biol. 158:1229-1238(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-30 AND CYS-45.
    9. "A structural framework for deciphering the link between I-Ag7 and autoimmune diabetes."
      Corper A.L., Stratmann T., Apostolopoulos V., Scott C.A., Garcia K.C., Kang A.S., Wilson I.A., Teyton L.
      Science 288:505-511(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 222-235 IN COMPLEX WITH MHC.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 88-584 IN COMPLEX WITH SUBSTRATE, SUBUNIT, COFACTOR.

    Entry informationi

    Entry nameiDCE2_HUMAN
    AccessioniPrimary (citable) accession number: Q05329
    Secondary accession number(s): Q9UD87
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 129 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 10
      Human chromosome 10: 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