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O75874

- IDHC_HUMAN

UniProt

O75874 - IDHC_HUMAN

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Protein

Isocitrate dehydrogenase [NADP] cytoplasmic

Gene
IDH1, PICD
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH.1 Publication

Cofactori

Binds 1 magnesium or manganese ion per subunit.1 Publication

Kineticsi

  1. KM=49 µM for NADP1 Publication
  2. KM=29 µM for magnesium chloride
  3. KM=65 µM for isocitrate

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei77 – 771Substrate
Binding sitei82 – 821NADP
Binding sitei109 – 1091Substrate
Binding sitei132 – 1321Substrate
Sitei139 – 1391Critical for catalysis
Sitei212 – 2121Critical for catalysis
Metal bindingi252 – 2521Magnesium or manganese
Binding sitei260 – 2601NADP
Metal bindingi275 – 2751Magnesium or manganese
Binding sitei328 – 3281NADP; via amide nitrogen and carbonyl oxygen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi75 – 773NADP
Nucleotide bindingi310 – 3156NADP

GO - Molecular functioni

  1. isocitrate dehydrogenase (NADP+) activity Source: UniProtKB
  2. magnesium ion binding Source: UniProtKB
  3. NAD binding Source: InterPro
  4. NADP binding Source: Ensembl
  5. protein homodimerization activity Source: UniProtKB
  6. receptor binding Source: UniProtKB

GO - Biological processi

  1. 2-oxoglutarate metabolic process Source: UniProtKB
  2. cellular lipid metabolic process Source: Reactome
  3. female gonad development Source: Ensembl
  4. glutathione metabolic process Source: Ensembl
  5. glyoxylate cycle Source: UniProtKB-KW
  6. isocitrate metabolic process Source: UniProtKB
  7. NADPH regeneration Source: Reactome
  8. response to oxidative stress Source: Ensembl
  9. response to steroid hormone Source: Ensembl
  10. small molecule metabolic process Source: Reactome
  11. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glyoxylate bypass, Tricarboxylic acid cycle

Keywords - Ligandi

Magnesium, Manganese, Metal-binding, NADP

Enzyme and pathway databases

BioCyciMetaCyc:HS06502-MONOMER.
ReactomeiREACT_160183. Abnormal conversion of 2-oxoglutarate to 2-hydroxyglutarate.
REACT_16904. NADPH regeneration.
SABIO-RKO75874.

Names & Taxonomyi

Protein namesi
Recommended name:
Isocitrate dehydrogenase [NADP] cytoplasmic (EC:1.1.1.42)
Short name:
IDH
Alternative name(s):
Cytosolic NADP-isocitrate dehydrogenase
IDP
NADP(+)-specific ICDH
Oxalosuccinate decarboxylase
Gene namesi
Name:IDH1
Synonyms:PICD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:5382. IDH1.

Subcellular locationi

Cytoplasm. Peroxisome 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: LIFEdb
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
  4. mitochondrion Source: Ensembl
  5. peroxisomal matrix Source: Reactome
  6. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Peroxisome

Pathology & Biotechi

Involvement in diseasei

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.

Organism-specific databases

MIMi137800. phenotype.
Orphaneti296. Enchondromatosis.
251579. Giant cell glioblastoma.
251576. Gliosarcoma.
163634. Maffucci syndrome.
99646. Metaphyseal chondromatosis with D-2-hydroxyglutaric aciduria.
PharmGKBiPA29630.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 414413Isocitrate dehydrogenase [NADP] cytoplasmicPRO_0000083575Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei81 – 811N6-acetyllysine By similarity
Modified residuei126 – 1261N6-succinyllysine By similarity
Modified residuei224 – 2241N6-acetyllysine By similarity
Modified residuei233 – 2331N6-acetyllysine By similarity
Modified residuei243 – 2431N6-acetyllysine By similarity
Modified residuei321 – 3211N6-acetyllysine1 Publication
Modified residuei400 – 4001N6-succinyllysine By similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO75874.
PaxDbiO75874.
PeptideAtlasiO75874.
PRIDEiO75874.

2D gel databases

OGPiO75874.
REPRODUCTION-2DPAGEIPI00027223.
UCD-2DPAGEO75874.

PTM databases

PhosphoSiteiO75874.

Expressioni

Gene expression databases

ArrayExpressiO75874.
BgeeiO75874.
CleanExiHS_IDH1.
GenevestigatoriO75874.

Organism-specific databases

HPAiCAB033218.
CAB062556.
HPA035248.
HPA057936.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi109643. 34 interactions.
DIPiDIP-59311N.
IntActiO75874. 4 interactions.
MINTiMINT-4998878.
STRINGi9606.ENSP00000260985.

Structurei

Secondary structure

1
414
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 1410
Helixi17 – 2913
Turni30 – 345
Beta strandi35 – 439
Helixi46 – 516
Turni52 – 543
Helixi55 – 6713
Beta strandi68 – 725
Helixi80 – 867
Helixi95 – 1039
Beta strandi106 – 1116
Beta strandi128 – 1336
Helixi137 – 1404
Beta strandi142 – 1465
Beta strandi148 – 15811
Beta strandi165 – 1728
Beta strandi177 – 1859
Helixi186 – 20318
Beta strandi207 – 2115
Turni213 – 2153
Helixi219 – 23416
Helixi236 – 2416
Beta strandi246 – 2505
Helixi251 – 26010
Beta strandi265 – 2695
Helixi271 – 28515
Beta strandi290 – 2967
Beta strandi303 – 3097
Helixi313 – 3208
Helixi330 – 34718
Helixi350 – 36920
Helixi374 – 3818
Helixi383 – 3853
Helixi388 – 3903
Helixi394 – 40916

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliO75874.
SMRiO75874. Positions 3-414.

Miscellaneous databases

EvolutionaryTraceiO75874.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni94 – 1007Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0538.
HOGENOMiHOG000019858.
HOVERGENiHBG006119.
InParanoidiO75874.
KOiK00031.
OMAiSCGGVAM.
OrthoDBiEOG7QNVKS.
PhylomeDBiO75874.
TreeFamiTF300428.

Family and domain databases

Gene3Di3.40.718.10. 1 hit.
InterProiIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR004790. Isocitrate_DH_NADP.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERiPTHR11822. PTHR11822. 1 hit.
PfamiPF00180. Iso_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000108. IDH_NADP. 1 hit.
TIGRFAMsiTIGR00127. nadp_idh_euk. 1 hit.
PROSITEiPS00470. IDH_IMDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O75874-1 [UniParc]FASTAAdd to Basket

« Hide

MSKKISGGSV VEMQGDEMTR IIWELIKEKL IFPYVELDLH SYDLGIENRD    50
ATNDQVTKDA AEAIKKHNVG VKCATITPDE KRVEEFKLKQ MWKSPNGTIR 100
NILGGTVFRE AIICKNIPRL VSGWVKPIII GRHAYGDQYR ATDFVVPGPG 150
KVEITYTPSD GTQKVTYLVH NFEEGGGVAM GMYNQDKSIE DFAHSSFQMA 200
LSKGWPLYLS TKNTILKKYD GRFKDIFQEI YDKQYKSQFE AQKIWYEHRL 250
IDDMVAQAMK SEGGFIWACK NYDGDVQSDS VAQGYGSLGM MTSVLVCPDG 300
KTVEAEAAHG TVTRHYRMYQ KGQETSTNPI ASIFAWTRGL AHRAKLDNNK 350
ELAFFANALE EVSIETIEAG FMTKDLAACI KGLPNVQRSD YLNTFEFMDK 400
LGENLKIKLA QAKL 414
Length:414
Mass (Da):46,659
Last modified:July 11, 2002 - v2
Checksum:i60428B0B6E5851DC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti132 – 1321R → 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. 3 Publications
VAR_036013
Natural varianti132 – 1321R → G in a glioma sample; glioblastoma multiforme; somatic mutation. 1 Publication
VAR_055454
Natural varianti132 – 1321R → 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. 2 Publications
VAR_055455
Natural varianti132 – 1321R → 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. 2 Publications
VAR_055456
Natural varianti132 – 1321R → 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. 2 Publications
VAR_055457
Natural varianti178 – 1781V → I.
Corresponds to variant rs34218846 [ dbSNP | Ensembl ].
VAR_049780

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321F → I in CAB66637. 1 Publication
Sequence conflicti126 – 1261K → E in CAB66637. 1 Publication
Sequence conflicti172 – 1721F → S in CAD97653. 1 Publication
Sequence conflicti174 – 1741E → G in CAD97653. 1 Publication
Sequence conflicti218 – 2181K → I in AAD02918. 1 Publication
Sequence conflicti307 – 3071A → S in AAH93020. 1 Publication
Sequence conflicti329 – 3291P → L in AAD02918. 1 Publication
Sequence conflicti381 – 3811K → R in AAD02918. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS2381.1.
PIRiT46280.
RefSeqiNP_001269315.1. NM_001282386.1.
NP_001269316.1. NM_001282387.1.
NP_005887.2. NM_005896.3.
UniGeneiHs.593422.

Genome annotation databases

EnsembliENST00000345146; ENSP00000260985; ENSG00000138413.
ENST00000415913; ENSP00000390265; ENSG00000138413.
ENST00000446179; ENSP00000410513; ENSG00000138413.
GeneIDi3417.
KEGGihsa:3417.
UCSCiuc002vcs.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Isocitrate dehydrogenase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS2381.1.
PIRi T46280.
RefSeqi NP_001269315.1. NM_001282386.1.
NP_001269316.1. NM_001282387.1.
NP_005887.2. NM_005896.3.
UniGenei Hs.593422.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1T09 X-ray 2.70 A/B 1-414 [» ]
1T0L X-ray 2.41 A/B/C/D 1-414 [» ]
3INM X-ray 2.10 A/B/C 1-414 [» ]
3MAP X-ray 2.80 A/B 1-414 [» ]
3MAR X-ray 3.41 A/B 1-414 [» ]
3MAS X-ray 3.20 A/B 1-414 [» ]
4I3K X-ray 3.31 A/B 1-414 [» ]
4I3L X-ray 3.29 A/B 1-414 [» ]
4KZO X-ray 2.20 A/B/C 1-414 [» ]
4L03 X-ray 2.10 A/B/C 1-414 [» ]
4L04 X-ray 2.87 A/B/C/D/E/F 1-414 [» ]
4L06 X-ray 2.28 A/B/C/D/E/F 1-414 [» ]
ProteinModelPortali O75874.
SMRi O75874. Positions 3-414.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109643. 34 interactions.
DIPi DIP-59311N.
IntActi O75874. 4 interactions.
MINTi MINT-4998878.
STRINGi 9606.ENSP00000260985.

Chemistry

ChEMBLi CHEMBL2007625.

PTM databases

PhosphoSitei O75874.

2D gel databases

OGPi O75874.
REPRODUCTION-2DPAGE IPI00027223.
UCD-2DPAGE O75874.

Proteomic databases

MaxQBi O75874.
PaxDbi O75874.
PeptideAtlasi O75874.
PRIDEi O75874.

Protocols and materials databases

DNASUi 3417.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000345146 ; ENSP00000260985 ; ENSG00000138413 .
ENST00000415913 ; ENSP00000390265 ; ENSG00000138413 .
ENST00000446179 ; ENSP00000410513 ; ENSG00000138413 .
GeneIDi 3417.
KEGGi hsa:3417.
UCSCi uc002vcs.3. human.

Organism-specific databases

CTDi 3417.
GeneCardsi GC02M209100.
H-InvDB HIX0161877.
HGNCi HGNC:5382. IDH1.
HPAi CAB033218.
CAB062556.
HPA035248.
HPA057936.
MIMi 137800. phenotype.
147700. gene.
neXtProti NX_O75874.
Orphaneti 296. Enchondromatosis.
251579. Giant cell glioblastoma.
251576. Gliosarcoma.
163634. Maffucci syndrome.
99646. Metaphyseal chondromatosis with D-2-hydroxyglutaric aciduria.
PharmGKBi PA29630.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0538.
HOGENOMi HOG000019858.
HOVERGENi HBG006119.
InParanoidi O75874.
KOi K00031.
OMAi SCGGVAM.
OrthoDBi EOG7QNVKS.
PhylomeDBi O75874.
TreeFami TF300428.

Enzyme and pathway databases

BioCyci MetaCyc:HS06502-MONOMER.
Reactomei REACT_160183. Abnormal conversion of 2-oxoglutarate to 2-hydroxyglutarate.
REACT_16904. NADPH regeneration.
SABIO-RK O75874.

Miscellaneous databases

ChiTaRSi IDH1. human.
EvolutionaryTracei O75874.
GeneWikii IDH1.
GenomeRNAii 3417.
NextBioi 13470.
PROi O75874.
SOURCEi Search...

Gene expression databases

ArrayExpressi O75874.
Bgeei O75874.
CleanExi HS_IDH1.
Genevestigatori O75874.

Family and domain databases

Gene3Di 3.40.718.10. 1 hit.
InterProi IPR019818. IsoCit/isopropylmalate_DH_CS.
IPR004790. Isocitrate_DH_NADP.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view ]
PANTHERi PTHR11822. PTHR11822. 1 hit.
Pfami PF00180. Iso_dh. 1 hit.
[Graphical view ]
PIRSFi PIRSF000108. IDH_NADP. 1 hit.
TIGRFAMsi TIGR00127. nadp_idh_euk. 1 hit.
PROSITEi PS00470. IDH_IMDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. 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. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-132.
  17. 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.

Entry informationi

Entry nameiIDHC_HUMAN
AccessioniPrimary (citable) accession number: O75874
Secondary accession number(s): Q567U4
, Q6FHQ6, Q7Z3V0, Q93090, Q9NTJ9, Q9UKW8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 11, 2002
Last modified: September 3, 2014
This is version 155 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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