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Q05329

- DCE2_HUMAN

UniProt

Q05329 - DCE2_HUMAN

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Protein
Glutamate decarboxylase 2
Gene
GAD2, GAD65
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

Kineticsi

  1. KM=2.15 mM for glutamate1 Publication

Sites

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

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
Complete GO annotation...

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

GO - Cellular componenti

  1. Golgi membrane Source: UniProtKB-SubCell
  2. anchored component of membrane Source: Ensembl
  3. axon Source: Ensembl
  4. cell junction Source: UniProtKB-KW
  5. clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane Source: Reactome
  6. cytosol 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
Complete GO annotation...

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 2
PRO_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.1 Publication

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ05329.

Family & Domainsi

Region

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

Sequence similaritiesi

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

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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: September 3, 2014
This is version 128 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

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