CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008011
UniProt Accession
Genbank Protein ID
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
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
54LLYGDSGKPAEGGGSubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
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 (By similarity).
 MOD_RES 6 6 Phosphoserine (By similarity).
 MOD_RES 10 10 Phosphoserine (By similarity).
 MOD_RES 13 13 Phosphoserine (By similarity).
 MOD_RES 396 396 N6-(pyridoxal phosphate)lysine (By
 LIPID 30 30 S-palmitoyl cysteine (By similarity).
 LIPID 45 45 S-palmitoyl cysteine (By similarity).  
Keyword
 Cell junction; Cell membrane; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Decarboxylase; 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 FGSEDGSADP ENPGTARAWC QVAQKFTGGI GNKLCALLYG DSGKPAEGGG 60
SVTSRAATGK VACTCDQKPC NCPKGDVNYA FLHATDLLPA CDGERPTLAF 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 LSGVERANSV TWNPHKMMGV PLQCSALLVR EEGLMQSCNQ 420
MHASYLFQQD KHYDLSYDTG DKALQCGRHV DVFKLWLMWR AKGTTGFEAH IDKCLELAEY 480
LYTIIKNREG YEMVFDGKPQ HTNVCFWFVP PSLRTLEDNE ERMSRLSKVA PVIKARMMEY 540
GTTMVSYQPL GDKVNFFRMV ISNPAATHQD IDFLIEEIER LGQDL 585 
Gene Ontology
 GO:0031225; C:anchored to membrane; IEA:Compara.
 GO:0030424; C:axon; IDA:MGI.
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
 GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
 GO:0045202; C:synapse; IDA:MGI.
 GO:0030672; C:synaptic vesicle membrane; IEA:Compara.
 GO:0016595; F:glutamate binding; IEA:Compara.
 GO:0004351; F:glutamate decarboxylase activity; IEA:EC.
 GO:0030170; F:pyridoxal phosphate binding; IEA:Compara.
 GO:0006540; P:glutamate decarboxylation to succinate; IEA:Compara.
 GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
 GO:0042493; P:response to drug; IEA:Compara. 
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