Reviewed, UniProtKB/Swiss-Prot P00367 (DHE3_HUMAN)

Names and origin

Protein names

Recommended name:
    Glutamate dehydrogenase 1, mitochondrial
      Short name=GDH
    EC=1.4.1.3

Gene names

Name:	GLUD1
Synonyms:	GLUD

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	558 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate By similarity.
Catalytic activity	L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H.
Enzyme regulation	Subject to allosteric regulation. Activated by ADP. Inhibited by GTP and ATP. ADP can occupy the NADH binding site and activate the enzyme.
Subunit structure	Homohexamer.
Subcellular location	Mitochondrion matrix.
Involvement in disease	Defects in GLUD1 are the cause of hyperinsulinism-hyperammonemia syndrome (HHS) [MIM:606762]. Elevated oxidation rate of glutamate to alpha-ketoglutarate stimulates insulin secretion in the pancreatic beta cells, while they impair detoxification of ammonium in the liver. Ref.20 Ref.21 Ref.22 Ref.23
Sequence similarities	Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

Ontologies

Keywords
Cellular component	Mitochondrion
Disease	Disease mutation
Domain	Transit peptide
Ligand	ATP-binding GTP-binding NADP Nucleotide-binding
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	glutamate biosynthetic process Inferred from direct assay. Source: UniProtKB glutamate deamidation Inferred from direct assay. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of insulin secretion Inferred from mutant phenotype. Source: UniProtKB
Cellular component	mitochondrial matrix Ref.8 Inferred from Experiment. Source: Reactome
Molecular function	ADP binding Inferred from direct assay. Source: UniProtKB ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP binding Inferred from direct assay. Source: UniProtKB NAD binding Inferred from direct assay. Source: UniProtKB glutamate dehydrogenase [NAD(P)+] activity Ref.8 Inferred from direct assay. Source: UniProtKB glutamate dehydrogenase activity Ref.15 Inferred from direct assay. Source: UniProtKB identical protein binding Ref.15 Traceable author statement. Source: UniProtKB leucine binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 53

53

Mitochondrion Ref.8 Ref.9

Chain

54 – 558

505

Glutamate dehydrogenase 1, mitochondrial

PRO_0000007206

Regions

Nucleotide binding

141 – 143

3

NAD By similarity

Sites

Active site

183

1

Binding site

147

1

Substrate By similarity

Binding site

171

1

Substrate By similarity

Binding site

176

1

NAD By similarity

Binding site

252

1

NAD By similarity

Binding site

266

1

GTP By similarity

Binding site

270

1

GTP By similarity

Binding site

319

1

GTP By similarity

Binding site

322

1

GTP By similarity

Binding site

438

1

Substrate By similarity

Binding site

444

1

NAD By similarity

Binding site

450

1

ADP By similarity

Binding site

516

1

ADP By similarity

Amino acid modifications

Modified residue

84

1

N6-acetyllysine Ref.13

Modified residue

135

1

Phosphotyrosine By similarity

Modified residue

227

1

Phosphoserine By similarity

Modified residue

450

1

Phosphoserine By similarity

Modified residue

480

1

N6-acetyllysine Ref.13

Modified residue

503

1

N6-acetyllysine Ref.13

Modified residue

512

1

Phosphotyrosine By similarity

Modified residue

527

1

N6-acetyllysine By similarity

Natural variations

Natural variant

270

1

S → C in HHS; diminished sensitivity to GTP. Ref.23

VAR_016760

Natural variant

274

1

R → C in HHS; diminished sensitivity to GTP. Ref.22 Ref.23

VAR_016761

Natural variant

318

1

R → K in HHS. Ref.21

VAR_009270

Natural variant

318

1

R → T in HHS; diminished sensitivity to GTP. Ref.23

VAR_016762

Natural variant

319

1

Y → C in HHS. Ref.23

VAR_016763

Natural variant

322

1

R → C in HHS; diminished sensitivity to GTP. Ref.23

VAR_016764

Natural variant

322

1

R → H in HHS; diminished sensitivity to GTP. Ref.22 Ref.23

VAR_016765

Natural variant

349

1

E → A in HHS. Ref.21

VAR_009271

Natural variant

498

1

S → L in HHS. Ref.20

VAR_008666

Natural variant

499

1

G → D in HHS. Ref.20

VAR_008667

Natural variant

499

1

G → S in HHS. Ref.20

VAR_008668

Natural variant

501

1

S → P in HHS. Ref.20

VAR_008669

Natural variant

507

1

H → Y in HHS; abolishes inhibition by ATP; no effect on activation by ADP. Ref.20 Ref.14 Ref.15

VAR_008670

Experimental info

Mutagenesis

501

1

S → A: Reduces activity and inhibition by GTP. Ref.15

Mutagenesis

507

1

H → A: Strongly reduces inhibition by GTP.

Mutagenesis

516

1

R → A: Abolishes activation by ADP. Ref.15

Secondary structure

1

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558

Helix Strand Turn

Details...

Helix

66 – 90

25

Helix

91 – 93

3

Helix

95 – 97

3

Helix

99 – 102

4

Helix

104 – 109

6

Beta strand

113 – 123

11

Beta strand

125 – 127

3

Beta strand

129 – 138

10

Beta strand

142 – 152

11

Helix

158 – 174

17

Beta strand

180 – 186

7

Helix

190 – 192

3

Helix

195 – 211

17

Turn

217 – 219

3

Beta strand

220 – 223

4

Helix

230 – 242

13

Turn

243 – 247

5

Helix

251 – 253

3

Helix

260 – 262

3

Helix

271 – 284

14

Helix

287 – 293

7

Beta strand

298 – 300

3

Beta strand

303 – 307

5

Helix

311 – 322

12

Beta strand

326 – 331

6

Helix

345 – 354

10

Beta strand

355 – 358

4

Turn

371 – 373

3

Beta strand

377 – 381

5

Beta strand

383 – 386

4

Turn

390 – 392

3

Helix

393 – 395

3

Beta strand

399 – 402

4

Beta strand

405 – 407

3

Helix

411 – 419

9

Beta strand

423 – 425

3

Helix

427 – 430

4

Helix

433 – 447

15

Turn

451 – 455

5

Helix

456 – 475

20

Turn

476 – 479

4

Helix

491 – 498

8

Helix

502 – 527

26

Helix

534 – 551

18

Sequences

	Sequence		Length	Mass (Da)
	P00367-1 [UniParc]. Last modified January 1, 1990. Version 2. Checksum: A7319A840F57FBB2	FASTA	558	61,398
	10 20 30 40 50 60 MYRYLGEALL LSRAGPAALG SASADSAALL GWARGQPAAA PQPGLALAAR RHYSEAVADR 70 80 90 100 110 120 EDDPNFFKMV EGFFDRGASI VEDKLVEDLR TRESEEQKRN RVRGILRIIK PCNHVLSLSF 130 140 150 160 170 180 PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI RYSTDVSVDE VKALASLMTY KCAVVDVPFG 190 200 210 220 230 240 GAKAGVKINP KNYTDNELEK ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY 250 260 270 280 290 300 ASTIGHYDIN AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG 310 320 330 340 350 360 DKTFVVQGFG NVGLHSMRYL HRFGAKCIAV GESDGSIWNP DGIDPKELED FKLQHGSILG 370 380 390 400 410 420 FPKAKPYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI IAEGANGPTT PEADKIFLER 430 440 450 460 470 480 NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS YGRLTFKYER DSNYHLLMSV QESLERKFGK 490 500 510 520 530 540 HGGTIPIVPT AEFQDRISGA SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV 550 NAIEKVFKVY NEAGVTFT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Comparison of human brain and liver glutamate dehydrogenase cDNAS." Nakatani Y., Banner C., von Herrat M., Schneider M.E., Smith H.H., Freese E. Biochem. Biophys. Res. Commun. 149:405-410(1987) [PubMed: 3426581] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain and Liver.
[2]	"Molecular cloning and nucleotide sequence of the cDNA for human liver glutamate dehydrogenase precursor." Amuro N., Yamaura M., Goto Y., Okazaki T. Biochem. Biophys. Res. Commun. 152:1395-1400(1988) [PubMed: 3377777] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[3]	"Complete nucleotide sequence of human glutamate dehydrogenase cDNA." Nakatani Y., Schneider M.E., Banner C., Freese E. Nucleic Acids Res. 16:6237-6237(1988) [PubMed: 3399399] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Isolation and characterization of cDNA clones encoding human liver glutamate dehydrogenase: evidence for a small gene family." Mavrothalassitis G., Tzimagiorgis G., Mitsialis A., Zannis V., Plaitakis A., Papamatheakis J., Moschonas N. Proc. Natl. Acad. Sci. U.S.A. 85:3494-3498(1988) [PubMed: 3368458] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[5]	"The human glutamate dehydrogenase gene family: gene organization and structural characterization." Michaelidis T.M., Tzimagiorgis G., Moschonas N.K., Papamatheakis J. Genomics 16:150-160(1993) [PubMed: 8486350] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Placenta.
[6]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Duodenum and Eye.
[8]	"Partial amino acid sequence of the glutamate dehydrogenase of human liver and a revision of the sequence of the bovine enzyme." Julliard J.H., Smith E.L. J. Biol. Chem. 254:3427-3438(1979) [PubMed: 429360] [Abstract] Cited for: PROTEIN SEQUENCE OF 54-558. Tissue: Liver.
[9]	"Human liver protein map: a reference database established by microsequencing and gel comparison." Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J. Electrophoresis 13:992-1001(1992) [PubMed: 1286669] [Abstract] Cited for: PROTEIN SEQUENCE OF 54-69. Tissue: Liver.
[10]	"Isolation of a human brain cDNA for glutamate dehydrogenase." Banner C., Silverman S., Thomas J.W., Lampel K.A., Vitkovic L., Huie D., Wenthold R.J. J. Neurochem. 49:246-252(1987) [PubMed: 3585334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 301-558. Tissue: Brain.
[11]	Lubec G., Vishwanath V. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 481-496, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[12]	"Structure and expression analysis of a member of the human glutamate dehydrogenase (GLUD) gene family mapped to chromosome 10p11.2." Tzimagiorgis G., Leversha M.A., Chroniary K., Goulielmos G., Sargent C.A., Ferguson-Smith M., Moschonas N.K. Hum. Genet. 91:433-438(1993) [PubMed: 8314555] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 540-558.
[13]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84; LYS-480 AND LYS-503, MASS SPECTROMETRY.
[14]	"Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation." Smith T.J., Peterson P.E., Schmidt T., Fang J., Stanley C.A. J. Mol. Biol. 307:707-720(2001) [PubMed: 11254391] [Abstract] Cited for: CHARACTERIZATION OF VARIANT TYR-507, ALLOSTERIC REGULATION.
[15]	"Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations." Fang J., Hsu B.Y.L., MacMullen C.M., Poncz M., Smith T.J., Stanley C.A. Biochem. J. 363:81-87(2002) [PubMed: 11903050] [Abstract] Cited for: MUTAGENESIS OF SER-501 AND ARG-516, CHARACTERIZATION OF VARIANT TYR-507, ALLOSTERIC REGULATION.
[16]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[17]	"The structure of apo human glutamate dehydrogenase details subunit communication and allostery." Smith T.J., Schmidt T., Fang J., Wu J., Siuzdak G., Stanley C.A. J. Mol. Biol. 318:765-777(2002) [PubMed: 12054821] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 54-558.
[18]	"Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation." Banerjee S., Schmidt T., Fang J., Stanley C.A., Smith T.J. Biochemistry 42:3446-3456(2003) [PubMed: 12653548] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 63-558 OF MUTANT ALA-516, ALLOSTERIC REGULATION.
[19]	"Congenital hyperinsulinism: molecular basis of a heterogeneous disease." Meissner T., Beinbrech B., Mayatepek E. Hum. Mutat. 13:351-361(1999) [PubMed: 10338089] [Abstract] Cited for: REVIEW ON VARIANTS.
[20]	"Hyperinsulinism and hyperammonemia in infants with regulatory mutations of the glutamate dehydrogenase gene." Stanley C.A., Lieu Y.K., Hsu B.Y.L., Burlina A.B., Greenberg C.R., Hopwood N.J., Perlman K., Rich B.H., Zammarchi E., Poncz M. N. Engl. J. Med. 338:1352-1357(1998) [PubMed: 9571255] [Abstract] Cited for: VARIANTS HHS LEU-498; SER-499; ASP-499; PRO-501 AND TYR-507.
[21]	"Novel missense mutations in the glutamate dehydrogenase gene in the congenital hyperinsulinism-hyperammonemia syndrome." Miki Y., Taki T., Ohura T., Kato H., Yanagisawa M., Hayashi Y. J. Pediatr. 136:69-72(2000) [PubMed: 10636977] [Abstract] Cited for: VARIANTS HHS LYS-318 AND ALA-349.
[22]	"Novel missense mutations outside the allosteric domain of glutamate dehydrogenase are prevalent in European patients with the congenital hyperinsulinism-hyperammonemia syndrome." Santer R., Kinner M., Passarge M., Superti-Furga A., Mayatepek E., Meissner T., Schneppenheim R., Schaub J. Hum. Genet. 108:66-71(2001) [PubMed: 11214910] [Abstract] Cited for: VARIANTS HHS CYS-274 AND HIS-322.
[23]	"Hyperinsulinism/hyperammonemia syndrome in children with regulatory mutations in the inhibitory guanosine triphosphate-binding domain of glutamate dehydrogenase." MacMullen C., Fang J., Hsu B.Y.L., Kelly A., de Lonlay-Debeney P., Saudubray J.-M., Ganguly A., Smith T.J., Stanley C.A., Brown R., Buist N., Dasouki M., Fefferman R., Grange D., Karaviti L., Luedke C., Marriage B., McLaughlin J. , Perlman K., Seashore M., van Vliet G. J. Clin. Endocrinol. Metab. 86:1782-1787(2001) [PubMed: 11297618] [Abstract] Cited for: VARIANTS HHS CYS-270; CYS-274; THR-318; CYS-319; CYS-322 AND HIS-322.
+	Additional computationally mapped references.

Web resources

GeneReviews

Wikipedia

Glutamate dehydrogenase 1 entry

Cross-references

Sequence databases

EMBLGenBankDDBJ

X07674 mRNA. Translation: CAA30521.1.
M20867 mRNA. Translation: AAA52526.1.
M37154 mRNA. Translation: AAA52525.1.
X07769 mRNA. Translation: CAA30598.1.
J03248 mRNA. Translation: AAA52523.1.
X66300 , X66301, X66302, X66303, X66304, X66305, X66306, X66307, X66308, X66309, X66311, X66312 Genomic DNA. Translation: CAA46994.2.
AL136982 Genomic DNA. Translation: CAI17120.1.
BC040132 mRNA. Translation: AAH40132.1.
BC112946 mRNA. Translation: AAI12947.1.
X67491 Genomic DNA. Translation: CAA47830.1.

IPI

IPI00016801.

PIR

DEHUE. A28208.
I37424.
S29331.
S60192.

RefSeq

NP_005262.1.

UniGene

Hs.500409

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1L1F	X-ray	2.70	A/B/C/D/E/F	54-558	[»]
1NR1	X-ray	3.30	A/B/C/D/E/F	63-558	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P00367. 3 interactions.

STRING

P00367.

PTM databases

PhosphoSite

P00367.

2-D gel databases

SWISS-2DPAGE

P00367.

REPRODUCTION-2DPAGE

IPI00016801.

Siena-2DPAGE

P00367.

Proteomic databases

PeptideAtlas

P00367.

PRIDE

P00367.

Genome annotation databases

Ensembl

ENST00000277865; ENSP00000277865; ENSG00000148672; Homo sapiens. [Genome view]
ENST00000394415; ENSP00000377937; ENSG00000148672; Homo sapiens. [Genome view]

GeneID

2746.

KEGG

hsa:2746.

NMPDR

fig|9606.3.peg.4285.

UCSC

uc001keh.1. human.

Organism-specific databases

CTD

2746.

GeneCards

GC10M088800.

H-InvDB

HIX0009003.
HIX0035678.

HGNC

HGNC:4335. GLUD1.

MIM

138130. gene.
606762. phenotype.

Orphanet

657. Persistent hyperinsulinemic hypoglycemia of infancy.

PharmGKB

PA28737.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P00367.

HOVERGEN

P00367.

OMA

RIQAKII.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-11464.

BRENDA

1.4.1.3. 247.

Reactome

REACT_13. Metabolism of amino acids.

Gene expression databases

Bgee

P00367.

CleanEx

HS_GLUD1.

Genevestigator

P00367.

GermOnline

ENSG00000148672. Homo sapiens.

Family and domain databases

InterPro

IPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

PANTHER

PTHR11606:SF2. GLFV_DH. 1 hit.

Pfam

PF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]

PRINTS

PR00082. GLFDHDRGNASE.

PROSITE

PS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00142. L-Glutamic Acid.
DB00157. NADH.

NextBio

10824.

SOURCE

Search...

Entry information

Entry name

DHE3_HUMAN

Accession

Primary (citable) accession number: P00367
Secondary accession number(s): Q5TBU3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 1, 1990
Last modified:	November 3, 2009
This is version 121 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.