CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011308
UniProt Accession
Genbank Protein ID
 M72422 
Genbank Nucleotide ID
Protein Name
 Glutamate decarboxylase 2 
Protein Synonyms/Alias
 65 kDa glutamic acid decarboxylase; GAD-65; Glutamate decarboxylase 65 kDa isoform 
Gene Name
 Gad2 
Gene Synonyms/Alias
 Gad65 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
54LLYGDSEKPAESGGSacetylation[1]
286EHSHFSLKKGAAALGacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
 Catalyzes the production of GABA. 
Sequence Annotation
 REGION 181 183 Substrate binding (By similarity).
 BINDING 558 558 Substrate (By similarity).
 MOD_RES 3 3 Phosphoserine.
 MOD_RES 6 6 Phosphoserine.
 MOD_RES 10 10 Phosphoserine.
 MOD_RES 13 13 Phosphoserine.
 MOD_RES 396 396 N6-(pyridoxal phosphate)lysine (By
 LIPID 30 30 S-palmitoyl cysteine.
 LIPID 45 45 S-palmitoyl cysteine.  
Keyword
 Cell junction; Cell membrane; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Decarboxylase; Direct protein sequencing; Golgi apparatus; Lipoprotein; Lyase; Membrane; Neurotransmitter biosynthesis; Palmitate; Phosphoprotein; Pyridoxal phosphate; Reference proteome; Synapse. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 585 AA 
Protein Sequence
MASPGSGFWS FGSEDGSGDP ENPGTARAWC QVAQKFTGGI GNKLCALLYG DSEKPAESGG 60
SVTSRAATRK VACTCDQKPC SCPKGDVNYA LLHATDLLPA CEGERPTLAF LQDVMNILLQ 120
YVVKSFDRST KVIDFHYPNE LLQEYNWELA DQPQNLEEIL THCQTTLKYA IKTGHPRYFN 180
QLSTGLDMVG LAADWLTSTA NTNMFTYEIA PVFVLLEYVT LKKMREIIGW PGGSGDGIFS 240
PGGAISNMYA MLIARYKMFP EVKEKGMAAV PRLIAFTSEH SHFSLKKGAA ALGIGTDSVI 300
LIKCDERGKM IPSDLERRIL EVKQKGFVPF LVSATAGTTV YGAFDPLLAV ADICKKYKIW 360
MHVDAAWGGG LLMSRKHKWK LNGVERANSV TWNPHKMMGV PLQCSALLVR EEGLMQSCNQ 420
MHASYLFQQD KHYDLSYDTG DKALQCGRHV DVFKLWLMWR AKGTTGFEAH IDKCLELAEY 480
LYNIIKNREG YEMVFDGKPQ HTNVCFWFVP PSLRVLEDNE ERMSRLSKVA PVIKARMMEY 540
GTTMVSYQPL GDKVNFFRMV ISNPAATHQD IDFLIEEIER LGQDL 585 
Gene Ontology
 GO:0031225; C:anchored to membrane; IDA:RGD.
 GO:0030424; C:axon; IEA:Compara.
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0005829; C:cytosol; IDA:RGD.
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
 GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
 GO:0030672; C:synaptic vesicle membrane; IDA:RGD.
 GO:0016595; F:glutamate binding; IDA:RGD.
 GO:0004351; F:glutamate decarboxylase activity; IDA:RGD.
 GO:0046982; F:protein heterodimerization activity; IDA:RGD.
 GO:0030170; F:pyridoxal phosphate binding; IDA:RGD.
 GO:0006540; P:glutamate decarboxylation to succinate; IDA:RGD.
 GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
 GO:0042493; P:response to drug; IEP:RGD.
 GO:0007268; P:synaptic transmission; TAS:RGD. 
Interpro
 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. 
Pfam
 PF00282; Pyridoxal_deC 
SMART
  
PROSITE
 PS00392; DDC_GAD_HDC_YDC 
PRINTS