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Q99259 (DCE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length594 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processNeurotransmitter biosynthesis
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   LigandPyridoxal phosphate
   Molecular functionDecarboxylase
Lyase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processgamma-aminobutyric acid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

glutamate catabolic process

Traceable author statement Ref.8. Source: UniProtKB

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: Ensembl

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentaxon terminus

Inferred from electronic annotation. Source: Ensembl

cell cortex

Inferred from electronic annotation. Source: Ensembl

clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane

Traceable author statement. Source: Reactome

intracellular

Inferred from direct assay Ref.8. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

presynaptic active zone

Inferred from electronic annotation. Source: Ensembl

vesicle membrane

Non-traceable author statement Ref.8. Source: UniProtKB

   Molecular_functionglutamate binding

Inferred from electronic annotation. Source: Ensembl

glutamate decarboxylase activity

Inferred from direct assay Ref.8. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

pyridoxal phosphate binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NCK1P163332EBI-743184,EBI-389883

Alternative products

This entry describes 4 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.
Isoform 4 (identifier: Q99259-4)

The sequence of this isoform differs from the canonical sequence as follows:
     374-425: AAWGGGLLMS...ILVKEKGILQ → GFNFSQLANR...WAAHVQEAPP
     426-594: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 594594Glutamate decarboxylase 1
PRO_0000146963

Regions

Region190 – 1923Substrate binding

Sites

Binding site5671Substrate

Amino acid modifications

Modified residue4051N6-(pyridoxal phosphate)lysine

Natural variations

Alternative sequence214 – 22411FTYEIAPVFVL → PSDMRECWLLR in isoform 3.
VSP_009123
Alternative sequence225 – 594370Missing in isoform 3.
VSP_009124
Alternative sequence374 – 42552AAWGG…KGILQ → GFNFSQLANRIICLATELMT NKGCVTWHPNYSVNMHHGCL GRWAAHVQEAPP in isoform 4.
VSP_054473
Alternative sequence426 – 594169Missing in isoform 4.
VSP_054474
Natural variant121S → C in CPSQ1. Ref.16
VAR_031021
Natural variant2281I → L. Ref.9
Corresponds to variant rs45566933 [ dbSNP | Ensembl ].
VAR_018861
Natural variant4741V → G.
Corresponds to variant rs769403 [ dbSNP | Ensembl ].
VAR_011882
Natural variant5321R → Q. Ref.9
Corresponds to variant rs769402 [ dbSNP | Ensembl ].
VAR_011883
Natural variant5651F → L.
Corresponds to variant rs1049736 [ dbSNP | Ensembl ].
VAR_011884

Experimental info

Sequence conflict91Missing in AAA35900. Ref.7
Sequence conflict16 – 172GA → EP in AAB59427. Ref.4
Sequence conflict16 – 172GA → EP in CAA80435. Ref.4
Sequence conflict171A → Q in AAA35900. Ref.7
Sequence conflict181D → N in AAB26938. Ref.6
Sequence conflict311T → N in AAB26938. Ref.6
Sequence conflict681K → R in AAA62368. Ref.2
Sequence conflict1161F → L in AAB26938. Ref.6
Sequence conflict1361T → A in AAA35900. Ref.7
Sequence conflict1401D → E in AAA35900. Ref.7
Sequence conflict1421H → R in AAA35900. Ref.7
Sequence conflict1551N → T in AAB26938. Ref.6
Sequence conflict2061T → N in AAB59427. Ref.4
Sequence conflict2061T → N in CAA80435. Ref.4
Sequence conflict3021G → C in AAB26938. Ref.6
Sequence conflict4361F → L in AAB26937. Ref.5
Sequence conflict4771E → G in AAB26938. Ref.6
Sequence conflict4921A → G in AAB26938. Ref.6
Sequence conflict5121N → S in AAB26937. Ref.5

Secondary structure

.................................................................................... 594
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (GAD67) [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 6D761C471C81FDAE

FASTA59466,897
        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 

« Hide

Isoform 2 (Sequence not available).
Isoform 3 (GAD25) [UniParc].

Checksum: 2CDCB04ECD6BC2E9
Show »

FASTA22425,279
Isoform 4 [UniParc].

Checksum: F392B68338CC6800
Show »

FASTA42547,440

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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; 3 AND 4).
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.
BC036552 mRNA. Translation: AAH36552.1.
M70434 mRNA. Translation: AAA52512.1.
M55574 mRNA. Translation: AAA72938.1.
CCDSCCDS2239.1. [Q99259-1]
CCDS2240.1. [Q99259-3]
PIRB41935.
S48135.
S51775.
S51776.
RefSeqNP_000808.2. NM_000817.2. [Q99259-1]
NP_038473.2. NM_013445.3. [Q99259-3]
XP_005246500.1. XM_005246443.2. [Q99259-1]
XP_005246501.1. XM_005246444.2. [Q99259-3]
UniGeneHs.420036.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2OKJX-ray2.30A/B93-594[»]
3VP6X-ray2.10A/B90-594[»]
ProteinModelPortalQ99259.
SMRQ99259. Positions 93-593.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108845. 4 interactions.
DIPDIP-29292N.
IntActQ99259. 7 interactions.
MINTMINT-3058814.
STRING9606.ENSP00000350928.

Chemistry

BindingDBQ99259.
ChEMBLCHEMBL2614.
DrugBankDB00142. L-Glutamic Acid.
DB00114. Pyridoxal Phosphate.

PTM databases

PhosphoSiteQ99259.

Polymorphism databases

DMDM1352213.

Proteomic databases

PaxDbQ99259.
PRIDEQ99259.

Protocols and materials databases

DNASU2571.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344257; ENSP00000341167; ENSG00000128683. [Q99259-3]
ENST00000358196; ENSP00000350928; ENSG00000128683. [Q99259-1]
ENST00000375272; ENSP00000364421; ENSG00000128683. [Q99259-3]
ENST00000493875; ENSP00000434696; ENSG00000128683.
GeneID2571.
KEGGhsa:2571.
UCSCuc002ugh.3. human. [Q99259-3]
uc002ugi.3. human. [Q99259-1]

Organism-specific databases

CTD2571.
GeneCardsGC02P171669.
HGNCHGNC:4092. GAD1.
HPACAB004415.
HPA058412.
MIM603513. phenotype.
605363. gene.
neXtProtNX_Q99259.
Orphanet210141. Inherited congenital spastic tetraplegia.
PharmGKBPA28507.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0076.
HOGENOMHOG000005382.
HOVERGENHBG004980.
InParanoidQ99259.
KOK01580.
OMAEYLYTKI.
OrthoDBEOG7H1JM3.
PhylomeDBQ99259.
TreeFamTF314688.

Enzyme and pathway databases

BioCycMetaCyc:HS05215-MONOMER.
ReactomeREACT_13685. Neuronal System.

Gene expression databases

ArrayExpressQ99259.
BgeeQ99259.
CleanExHS_GAD1.
GenevestigatorQ99259.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR002129. 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]
PfamPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGAD1. human.
EvolutionaryTraceQ99259.
GenomeRNAi2571.
NextBio10169.
PROQ99259.
SOURCESearch...

Entry information

Entry nameDCE1_HUMAN
AccessionPrimary (citable) accession number: Q99259
Secondary accession number(s): Q49AK1 expand/collapse secondary AC list , Q53TQ7, Q9BU91, Q9UHH4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM