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O75874 (IDHC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 152. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isocitrate dehydrogenase [NADP] cytoplasmic

Short name=IDH
EC=1.1.1.42
Alternative name(s):
Cytosolic NADP-isocitrate dehydrogenase
IDP
NADP(+)-specific ICDH
Oxalosuccinate decarboxylase
Gene names
Name:IDH1
Synonyms:PICD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length414 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH. Ref.15

Cofactor

Binds 1 magnesium or manganese ion per subunit. Ref.15

Subunit structure

Homodimer. Ref.14 Ref.15

Subcellular location

Cytoplasm. Peroxisome Ref.2.

Post-translational modification

Acetylation at Lys-374 dramatically reduces catalytic activity By similarity.

Involvement in disease

Glioma (GLM) [MIM:137800]: Gliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes.
Note: The gene represented in this entry is involved in disease pathogenesis. Mutations affecting Arg-132 are tissue-specific, and suggest that this residue plays a unique role in the development of high-grade gliomas. Mutations of Arg-132 to Cys, His, Leu or Ser abolish magnesium binding and abolish the conversion of isocitrate to alpha-ketoglutarate. Instead, alpha-ketoglutarate is converted to R--2-hydroxyglutarate. Elevated levels of R--2-hydroxyglutarate are correlated with an elevated risk of malignant brain tumors.

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Biophysicochemical properties

Kinetic parameters:

KM=49 µM for NADP Ref.15

KM=29 µM for magnesium chloride

KM=65 µM for isocitrate

Ontologies

Keywords
   Biological processGlyoxylate bypass
Tricarboxylic acid cycle
   Cellular componentCytoplasm
Peroxisome
   Coding sequence diversityPolymorphism
   LigandMagnesium
Manganese
Metal-binding
NADP
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process2-oxoglutarate metabolic process

Inferred from direct assay Ref.15. Source: UniProtKB

NADPH regeneration

Traceable author statement. Source: Reactome

cellular lipid metabolic process

Traceable author statement. Source: Reactome

female gonad development

Inferred from electronic annotation. Source: Ensembl

glutathione metabolic process

Inferred from electronic annotation. Source: Ensembl

glyoxylate cycle

Inferred from electronic annotation. Source: UniProtKB-KW

isocitrate metabolic process

Inferred from direct assay Ref.2Ref.15PubMed 20171178. Source: UniProtKB

response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

response to steroid hormone

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay. Source: LIFEdb

cytosol

Inferred from direct assay Ref.2. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

mitochondrion

Inferred from electronic annotation. Source: Ensembl

peroxisomal matrix

Traceable author statement. Source: Reactome

peroxisome

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: InterPro

NADP binding

Inferred from electronic annotation. Source: Ensembl

isocitrate dehydrogenase (NADP+) activity

Inferred from direct assay Ref.2Ref.15PubMed 20171178. Source: UniProtKB

magnesium ion binding

Inferred from direct assay Ref.15. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.15. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 20178365. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13
Chain2 – 414413Isocitrate dehydrogenase [NADP] cytoplasmic
PRO_0000083575

Regions

Nucleotide binding75 – 773NADP
Nucleotide binding310 – 3156NADP
Region94 – 1007Substrate binding

Sites

Metal binding2521Magnesium or manganese
Metal binding2751Magnesium or manganese
Binding site771Substrate
Binding site821NADP
Binding site1091Substrate
Binding site1321Substrate
Binding site2601NADP
Binding site3281NADP; via amide nitrogen and carbonyl oxygen
Site1391Critical for catalysis
Site2121Critical for catalysis

Amino acid modifications

Modified residue21N-acetylserine Ref.13
Modified residue811N6-acetyllysine By similarity
Modified residue1261N6-succinyllysine By similarity
Modified residue2241N6-acetyllysine By similarity
Modified residue2331N6-acetyllysine By similarity
Modified residue2431N6-acetyllysine By similarity
Modified residue3211N6-acetyllysine Ref.11
Modified residue4001N6-succinyllysine By similarity

Natural variations

Natural variant1321R → C in colorectal cancer and glioma samples; glioblastoma multiforme; somatic mutation; abolishes magnesium binding and alters enzyme activity so that isocitrate is no longer converted to alpha-ketoglutarate but instead alpha-ketoglutarate is converted to R(-)-2-hydroxyglutarate. Ref.15 Ref.16 Ref.18
VAR_036013
Natural variant1321R → G in a glioma sample; glioblastoma multiforme; somatic mutation. Ref.18
VAR_055454
Natural variant1321R → H in a glioma sample; glioblastoma multiforme; somatic mutation; abolishes magnesium binding and alters enzyme activity so that isocitrate is no longer converted to alpha-ketoglutarate but instead alpha-ketoglutarate is converted to R(-)-2-hydroxyglutarate. Ref.15 Ref.17
VAR_055455
Natural variant1321R → L in a glioma sample; glioblastoma multiforme; somatic mutation; abolishes magnesium binding and alters enzyme activity so that isocitrate is no longer converted to alpha-ketoglutarate but instead alpha-ketoglutarate is converted to R(-)-2-hydroxyglutarate. Ref.15 Ref.18
VAR_055456
Natural variant1321R → S in a glioma sample; glioblastoma multiforme; somatic mutation; abolishes magnesium binding and alters enzyme activity so that isocitrate is no longer converted to alpha-ketoglutarate but instead alpha-ketoglutarate is converted to R(-)-2-hydroxyglutarate. Ref.15 Ref.17
VAR_055457
Natural variant1781V → I.
Corresponds to variant rs34218846 [ dbSNP | Ensembl ].
VAR_049780

Experimental info

Sequence conflict321F → I in CAB66637. Ref.3
Sequence conflict1261K → E in CAB66637. Ref.3
Sequence conflict1721F → S in CAD97653. Ref.5
Sequence conflict1741E → G in CAD97653. Ref.5
Sequence conflict2181K → I in AAD02918. Ref.1
Sequence conflict3071A → S in AAH93020. Ref.6
Sequence conflict3291P → L in AAD02918. Ref.1
Sequence conflict3811K → R in AAD02918. Ref.1

Secondary structure

................................................................ 414
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O75874 [UniParc].

Last modified July 11, 2002. Version 2.
Checksum: 60428B0B6E5851DC

FASTA41446,659
        10         20         30         40         50         60 
MSKKISGGSV VEMQGDEMTR IIWELIKEKL IFPYVELDLH SYDLGIENRD ATNDQVTKDA 

        70         80         90        100        110        120 
AEAIKKHNVG VKCATITPDE KRVEEFKLKQ MWKSPNGTIR NILGGTVFRE AIICKNIPRL 

       130        140        150        160        170        180 
VSGWVKPIII GRHAYGDQYR ATDFVVPGPG KVEITYTPSD GTQKVTYLVH NFEEGGGVAM 

       190        200        210        220        230        240 
GMYNQDKSIE DFAHSSFQMA LSKGWPLYLS TKNTILKKYD GRFKDIFQEI YDKQYKSQFE 

       250        260        270        280        290        300 
AQKIWYEHRL IDDMVAQAMK SEGGFIWACK NYDGDVQSDS VAQGYGSLGM MTSVLVCPDG 

       310        320        330        340        350        360 
KTVEAEAAHG TVTRHYRMYQ KGQETSTNPI ASIFAWTRGL AHRAKLDNNK ELAFFANALE 

       370        380        390        400        410 
EVSIETIEAG FMTKDLAACI KGLPNVQRSD YLNTFEFMDK LGENLKIKLA QAKL 

« Hide

References

« Hide 'large scale' references
[1]"Cytosolic isocitrate dehydrogenase in humans, mice, and voles and phylogenetic analysis of the enzyme family."
Nekrutenko A., Hillis D.M., Patton J.C., Bradley R.D., Baker R.J.
Mol. Biol. Evol. 15:1674-1684(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The human PICD gene encodes a cytoplasmic and peroxisomal NADP(+)-dependent isocitrate dehydrogenase."
Geisbrecht B.V., Gould S.J.
J. Biol. Chem. 274:30527-30533(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
[3]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Endometrium.
[6]"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].
[7]Mural R.J., Istrail S., Sutton 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].
[8]"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].
Tissue: Lung and Placenta.
[9]Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 5-20; 30-49; 101-109; 120-132; 141-212; 223-233; 250-270; 322-338 AND 389-400, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[10]"Differential gene expression in epithelial cells induced by bile salts: identification by RNA arbitrarily primed PCR."
Kullmann F., Vogt T., Welsh J., McClelland M.
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 100-253.
[11]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[14]"Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity."
Xu X., Zhao J., Xu Z., Peng B., Huang Q., Arnold E., Ding J.
J. Biol. Chem. 279:33946-33957(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEXES WITH NADP; ISOCITRATE AND CALCIUM IONS, SUBUNIT.
[15]"Cancer-associated IDH1 mutations produce 2-hydroxyglutarate."
Dang L., White D.W., Gross S., Bennett B.D., Bittinger M.A., Driggers E.M., Fantin V.R., Jang H.G., Jin S., Keenan M.C., Marks K.M., Prins R.M., Ward P.S., Yen K.E., Liau L.M., Rabinowitz J.D., Cantley L.C., Thompson C.B., Vander Heiden M.G., Su S.M.
Nature 462:739-744(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF VARIANT GBM HIS-132 IN COMPLEX WITH NADP AND ALPHA-KETOGLUTARATE, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANTS CYS-132; HIS-132; LEU-132 AND SER-132.
[16]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-132.
[17]"An integrated genomic analysis of human glioblastoma multiforme."
Parsons D.W., Jones S., Zhang X., Lin J.C.-H., Leary R.J., Angenendt P., Mankoo P., Carter H., Siu I.-M., Gallia G.L., Olivi A., McLendon R., Rasheed B.A., Keir S., Nikolskaya T., Nikolsky Y., Busam D.A., Tekleab H. expand/collapse author list , Diaz L.A. Jr., Hartigan J., Smith D.R., Strausberg R.L., Marie S.K.N., Shinjo S.M.O., Yan H., Riggins G.J., Bigner D.D., Karchin R., Papadopoulos N., Parmigiani G., Vogelstein B., Velculescu V.E., Kinzler K.W.
Science 321:1807-1812(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HIS-132 AND SER-132.
[18]"IDH1 mutations at residue p.R132 (IDH1(R132)) occur frequently in high-grade gliomas but not in other solid tumors."
Bleeker F.E., Lamba S., Leenstra S., Troost D., Hulsebos T., Vandertop W.P., Frattini M., Molinari F., Knowles M., Cerrato A., Rodolfo M., Scarpa A., Felicioni L., Buttitta F., Malatesta S., Marchetti A., Bardelli A.
Hum. Mutat. 30:7-11(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CYS-132; GLY-132 AND LEU-132, ROLE IN GLIOMAS.
+Additional computationally mapped references.

Web resources

Wikipedia

Isocitrate dehydrogenase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF020038 mRNA. Translation: AAD02918.1.
AF113917 mRNA. Translation: AAD29284.1.
AL136702 mRNA. Translation: CAB66637.1.
CR541695 mRNA. Translation: CAG46496.1.
BX537411 mRNA. Translation: CAD97653.1.
AC016697 Genomic DNA. Translation: AAX93221.1.
CH471063 Genomic DNA. Translation: EAW70439.1.
BC012846 mRNA. Translation: AAH12846.1.
BC093020 mRNA. Translation: AAH93020.1.
U62389 mRNA. Translation: AAB17375.1.
PIRT46280.
RefSeqNP_001269315.1. NM_001282386.1.
NP_001269316.1. NM_001282387.1.
NP_005887.2. NM_005896.3.
UniGeneHs.593422.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1T09X-ray2.70A/B1-414[»]
1T0LX-ray2.41A/B/C/D1-414[»]
3INMX-ray2.10A/B/C1-414[»]
3MAPX-ray2.80A/B1-414[»]
3MARX-ray3.41A/B1-414[»]
3MASX-ray3.20A/B1-414[»]
4I3KX-ray3.31A/B1-414[»]
4I3LX-ray3.29A/B1-414[»]
4KZOX-ray2.20A/B/C1-414[»]
4L03X-ray2.10A/B/C1-414[»]
4L04X-ray2.87A/B/C/D/E/F1-414[»]
4L06X-ray2.28A/B/C/D/E/F1-414[»]
ProteinModelPortalO75874.
SMRO75874. Positions 3-414.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109643. 34 interactions.
DIPDIP-59311N.
IntActO75874. 4 interactions.
MINTMINT-4998878.
STRING9606.ENSP00000260985.

Chemistry

ChEMBLCHEMBL2007625.

PTM databases

PhosphoSiteO75874.

2D gel databases

OGPO75874.
REPRODUCTION-2DPAGEIPI00027223.
UCD-2DPAGEO75874.

Proteomic databases

PaxDbO75874.
PeptideAtlasO75874.
PRIDEO75874.

Protocols and materials databases

DNASU3417.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000345146; ENSP00000260985; ENSG00000138413.
ENST00000415913; ENSP00000390265; ENSG00000138413.
ENST00000446179; ENSP00000410513; ENSG00000138413.
GeneID3417.
KEGGhsa:3417.
UCSCuc002vcs.3. human.

Organism-specific databases

CTD3417.
GeneCardsGC02M209100.
H-InvDBHIX0161877.
HGNCHGNC:5382. IDH1.
HPACAB033218.
CAB062556.
HPA035248.
HPA057936.
MIM137800. phenotype.
147700. gene.
neXtProtNX_O75874.
Orphanet296. Enchondromatosis.
251579. Giant cell glioblastoma.
251576. Gliosarcoma.
163634. Maffucci syndrome.
99646. Metaphyseal chondromatosis with D-2-hydroxyglutaric aciduria.
PharmGKBPA29630.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0538.
HOGENOMHOG000019858.
HOVERGENHBG006119.
InParanoidO75874.
KOK00031.
OMAKELSFFA.
OrthoDBEOG7QNVKS.
PhylomeDBO75874.
TreeFamTF300428.

Enzyme and pathway databases

BioCycMetaCyc:HS06502-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKO75874.

Gene expression databases

ArrayExpressO75874.
BgeeO75874.
CleanExHS_IDH1.
GenevestigatorO75874.

Family and domain databases

Gene3D3.40.718.10. 1 hit.
InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR004790. Isocitrate_DH_NADP.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERPTHR11822. PTHR11822. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000108. IDH_NADP. 1 hit.
TIGRFAMsTIGR00127. nadp_idh_euk. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIDH1. human.
EvolutionaryTraceO75874.
GeneWikiIDH1.
GenomeRNAi3417.
NextBio13470.
PROO75874.
SOURCESearch...

Entry information

Entry nameIDHC_HUMAN
AccessionPrimary (citable) accession number: O75874
Secondary accession number(s): Q567U4 expand/collapse secondary AC list , Q6FHQ6, Q7Z3V0, Q93090, Q9NTJ9, Q9UKW8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 11, 2002
Last modified: April 16, 2014
This is version 152 of the entry and version 2 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