Q99259 (DCE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	GAD1
Synonyms:	GAD, GAD67

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	594 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the production of GABA.
Catalytic activity	L-glutamate = 4-aminobutanoate + CO2.
Cofactor	Pyridoxal phosphate. Ref.15
Subunit structure	Homodimer. Ref.15
Tissue specificity	Isoform 3 is expressed in pancreatic islets, testis, adrenal cortex, and perhaps other endocrine tissues, but not in brain. Ref.8
Involvement in disease	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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16
Sequence similarities	Belongs to the group II decarboxylase family.

Ontologies

Keywords
Biological process	Neurotransmitter biosynthesis
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Ligand	Pyridoxal phosphate
Molecular function	Decarboxylase Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	gamma-aminobutyric acid biosynthetic process Inferred from electronic annotation. Source: Compara glutamate decarboxylation to succinate Traceable author statement Ref.1. Source: ProtInc neurotransmitter biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW neurotransmitter secretion Traceable author statement. Source: Reactome protein-pyridoxal-5-phosphate linkage Traceable author statement Ref.8. Source: UniProtKB response to drug Inferred from electronic annotation. Source: Compara
Cellular_component	clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane Traceable author statement. Source: Reactome plasma membrane Traceable author statement. Source: Reactome
Molecular_function	glutamate binding Inferred from electronic annotation. Source: Compara glutamate decarboxylase activity Inferred from direct assay Ref.8. Source: UniProtKB pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NCK1	P16333	2	EBI-743184,EBI-389883

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q99259-1)

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.

Isoform 2 (identifier: Q99259-2)

The sequence of this isoform is not available.

Isoform 3 (identifier: Q99259-3)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 594

594

Glutamate decarboxylase 1

PRO_0000146963

Regions

Region

190 – 192

3

Substrate binding

Sites

Binding site

567

1

Substrate

Amino acid modifications

Modified residue

405

1

N6-(pyridoxal phosphate)lysine

Natural variations

Alternative sequence

214 – 224

11

FTYEIAPVFVL → PSDMRECWLLR in isoform 3.

VSP_009123

Alternative sequence

225 – 594

370

Missing in isoform 3.

VSP_009124

Natural variant

12

1

S → C in CPSQ1. Ref.16

VAR_031021

Natural variant

228

1

I → L. Ref.9
Corresponds to variant rs45566933 [ dbSNP | Ensembl ].

VAR_018861

Natural variant

474

1

V → G.
Corresponds to variant rs769403 [ dbSNP | Ensembl ].

VAR_011882

Natural variant

532

1

R → Q. Ref.9
Corresponds to variant rs769402 [ dbSNP | Ensembl ].

VAR_011883

Natural variant

565

1

F → L.
Corresponds to variant rs1049736 [ dbSNP | Ensembl ].

VAR_011884

Experimental info

Sequence conflict

9

1

Missing in AAA35900. Ref.7

Sequence conflict

16 – 17

2

GA → EP in AAB59427. Ref.4

Sequence conflict

16 – 17

2

GA → EP in CAA80435. Ref.4

Sequence conflict

17

1

A → Q in AAA35900. Ref.7

Sequence conflict

18

1

D → N in AAB26938. Ref.6

Sequence conflict

31

1

T → N in AAB26938. Ref.6

Sequence conflict

68

1

K → R in AAA62368. Ref.2

Sequence conflict

116

1

F → L in AAB26938. Ref.6

Sequence conflict

136

1

T → A in AAA35900. Ref.7

Sequence conflict

140

1

D → E in AAA35900. Ref.7

Sequence conflict

142

1

H → R in AAA35900. Ref.7

Sequence conflict

155

1

N → T in AAB26938. Ref.6

Sequence conflict

206

1

T → N in AAB59427. Ref.4

Sequence conflict

206

1

T → N in CAA80435. Ref.4

Sequence conflict

302

1

G → C in AAB26938. Ref.6

Sequence conflict

436

1

F → L in AAB26937. Ref.5

Sequence conflict

477

1

E → G in AAB26938. Ref.6

Sequence conflict

492

1

A → G in AAB26938. Ref.6

Sequence conflict

512

1

N → S in AAB26937. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

594

Helix Strand Turn

Details...

Turn

94 – 97

4

Helix

100 – 102

3

Helix

110 – 131

22

Helix

144 – 149

6

Helix

165 – 177

13

Beta strand

187 – 192

6

Helix

197 – 209

13

Beta strand

212 – 214

3

Turn

216 – 218

3

Helix

220 – 237

18

Beta strand

241 – 243

3

Beta strand

245 – 251

7

Helix

252 – 267

16

Helix

270 – 274

5

Helix

276 – 278

3

Beta strand

282 – 287

6

Helix

293 – 300

8

Helix

305 – 307

3

Beta strand

308 – 311

4

Helix

321 – 333

13

Beta strand

337 – 346

10

Beta strand

348 – 350

3

Helix

356 – 366

11

Beta strand

369 – 374

6

Helix

377 – 382

6

Turn

384 – 386

3

Helix

387 – 390

4

Helix

393 – 395

3

Beta strand

397 – 401

5

Beta strand

414 – 420

7

Helix

423 – 428

6

Turn

433 – 435

3

Helix

444 – 446

3

Helix

449 – 451

3

Helix

461 – 495

35

Beta strand

500 – 506

7

Beta strand

509 – 511

3

Beta strand

513 – 517

5

Helix

520 – 522

3

Helix

529 – 549

21

Beta strand

553 – 559

7

Beta strand

562 – 568

7

Helix

577 – 591

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (GAD67) [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 6D761C471C81FDAE	FASTA	594	66,897
	10 20 30 40 50 60 MASSTPSSSA TSSNAGADPN TTNLRPTTYD TWCGVAHGCT RKLGLKICGF LQRTNSLEEK 70 80 90 100 110 120 SRLVSAFKER QSSKNLLSCE NSDRDARFRR TETDFSNLFA RDLLPAKNGE EQTVQFLLEV 130 140 150 160 170 180 VDILLNYVRK TFDRSTKVLD FHHPHQLLEG MEGFNLELSD HPESLEQILV DCRDTLKYGV 190 200 210 220 230 240 RTGHPRFFNQ LSTGLDIIGL AGEWLTSTAN TNMFTYEIAP VFVLMEQITL KKMREIVGWS 250 260 270 280 290 300 SKDGDGIFSP GGAISNMYSI MAARYKYFPE VKTKGMAAVP KLVLFTSEQS HYSIKKAGAA 310 320 330 340 350 360 LGFGTDNVIL IKCNERGKII PADFEAKILE AKQKGYVPFY VNATAGTTVY GAFDPIQEIA 370 380 390 400 410 420 DICEKYNLWL HVDAAWGGGL LMSRKHRHKL NGIERANSVT WNPHKMMGVL LQCSAILVKE 430 440 450 460 470 480 KGILQGCNQM CAGYLFQPDK QYDVSYDTGD KAIQCGRHVD IFKFWLMWKA KGTVGFENQI 490 500 510 520 530 540 NKCLELAEYL YAKIKNREEF EMVFNGEPEH TNVCFWYIPQ SLRGVPDSPQ RREKLHKVAP 550 560 570 580 590 KIKALMMESG TTMVGYQPQG DKANFFRMVI SNPAATQSDI DFLIEEIERL GQDL
	Isoform 2 (Sequence not available).		–	–
	Isoform 3 (GAD25) [UniParc]. Checksum: 2CDCB04ECD6BC2E9	FASTA	224	25,279
	10 20 30 40 50 60 MASSTPSSSA TSSNAGADPN TTNLRPTTYD TWCGVAHGCT RKLGLKICGF LQRTNSLEEK 70 80 90 100 110 120 SRLVSAFKER QSSKNLLSCE NSDRDARFRR TETDFSNLFA RDLLPAKNGE EQTVQFLLEV 130 140 150 160 170 180 VDILLNYVRK TFDRSTKVLD FHHPHQLLEG MEGFNLELSD HPESLEQILV DCRDTLKYGV 190 200 210 220 RTGHPRFFNQ LSTGLDIIGL AGEWLTSTAN TNMPSDMREC WLLR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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 AND 3). 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]	"GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop." Fenalti G., Law R.H.P., Buckle A.M., Langendorf C., Tuck K., Rosado C.J., Faux N.G., Mahmood K., Hampe C.S., Banga J.P., Wilce M., Schmidberger J., Rossjohn J., El-Kabbani O., Pike R.N., Smith A.I., Mackay I.R., Rowley M.J., Whisstock J.C. Nat. Struct. Mol. Biol. 14:280-286(2007) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Wikipedia

Glutamate decarboxylase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
M70434 mRNA. Translation: AAA52512.1.
M55574 mRNA. Translation: AAA72938.1.

IPI

IPI00292646.
IPI00844138.

PIR

B41935.
S48135.
S51775.
S51776.

RefSeq

NP_000808.2. NM_000817.2.
NP_038473.2. NM_013445.3.

UniGene

Hs.420036.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q99259.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29292N.

IntAct

Q99259. 6 interactions.

MINT

MINT-3058814.

STRING

9606.ENSP00000350928.

PTM databases

PhosphoSite

Q99259.

Polymorphism databases

DMDM

1352213.

Proteomic databases

PaxDb

Q99259.

PRIDE

Q99259.

Protocols and materials databases

DNASU

2571.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000344257; ENSP00000341167; ENSG00000128683.
ENST00000358196; ENSP00000350928; ENSG00000128683.
ENST00000375272; ENSP00000364421; ENSG00000128683.

GeneID

2571.

KEGG

hsa:2571.

UCSC

uc002ugh.3. human.
uc002ugi.3. human.

Organism-specific databases

CTD

2571.

GeneCards

GC02P171669.

HGNC

HGNC:4092. GAD1.

HPA

CAB004415.

MIM

603513. phenotype.
605363. gene.

neXtProt

NX_Q99259.

Orphanet

210141. Inherited congenital spastic tetraplegia.

PharmGKB

PA28507.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0076.

HOGENOM

HOG000005382.

HOVERGEN

HBG004980.

InParanoid

Q99259.

KO

K01580.

OMA

ISMAGEW.

OrthoDB

EOG4QJRMS.

PhylomeDB

Q99259.

Enzyme and pathway databases

BioCyc

MetaCyc:HS05215-MONOMER.

Reactome

REACT_13685. Neuronal System.

Gene expression databases

ArrayExpress

Q99259.

Bgee

Q99259.

CleanEx

HS_GAD1.

Genevestigator

Q99259.

GermOnline

ENSG00000128683. Homo sapiens.

Family and domain databases

Gene3D

3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.

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.
[Graphical view]

Pfam

PF00282. Pyridoxal_deC. 1 hit.
[Graphical view]

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

PROSITE

PS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q99259.

ChEMBL

CHEMBL2614.

ChiTaRS

GAD1. human.

DrugBank

DB00142. L-Glutamic Acid.
DB00114. Pyridoxal Phosphate.

EvolutionaryTrace

Q99259.

GenomeRNAi

2571.

NextBio

10169.

SOURCE

Search...

Entry information

Entry name

DCE1_HUMAN

Accession

Primary (citable) accession number: Q99259
Secondary accession number(s): Q53TQ7, Q9BU91, Q9UHH4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.