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UniProtKB/Swiss-Prot entry O75874


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IDHC_HUMAN
Primary accession number O75874
Secondary accession numbers Q93090 Q9NTJ9 Q9UKW8
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on July 11, 2002 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 92)
Name and origin of the protein
Protein name Isocitrate dehydrogenase [NADP] cytoplasmic
Synonyms IDH
EC 1.1.1.42
Cytosolic NADP-isocitrate dehydrogenase
Oxalosuccinate decarboxylase
NADP(+)-specific ICDH
IDP
Gene name
Name: IDH1
Synonyms: PICD
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9866202 [NCBI, ExPASy, EBI, Israel, Japan]
Nekrutenko A., Hillis D.M., Patton J.C., Bradley R.D., Baker R.J.;
"Cytosolic isocitrate dehydrogenase in humans, mice, and voles and phylogenetic analysis of the enzyme family.";
Mol. Biol. Evol. 15:1674-1684(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
DOI=10.1074/jbc.274.43.30527; PubMed=10521434 [NCBI, ExPASy, EBI, Israel, Japan]
Geisbrecht B.V., Gould S.J.;
"The human PICD gene encodes a cytoplasmic and peroxisomal NADP(+)-dependent isocitrate dehydrogenase.";
J. Biol. Chem. 274:30527-30533(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
DOI=10.1101/gr.GR1547R; PubMed=11230166 [NCBI, ExPASy, EBI, Israel, Japan]
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., Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 30-49; 188-203 AND 322-338, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Afjehi-Sadat L.;
Submitted (MAR-2007) to UniProtKB.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 100-253.
Kullmann F., Vogt T., Welsh J., McClelland M.;
"Differential gene expression in epithelial cells induced by bile salts: identification by RNA arbitrarily primed PCR.";
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
[7]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEXES WITH NADP; ISOCITRATE AND CALCIUM IONS, AND SUBUNIT.
DOI=10.1074/jbc.M404298200; PubMed=15173171 [NCBI, ExPASy, EBI, Israel, Japan]
Xu X., Zhao J., Xu Z., Peng B., Huang Q., Arnold E., Ding J.;
"Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity.";
J. Biol. Chem. 279:33946-33957(2004).
[8]
VARIANT [LARGE SCALE ANALYSIS] CYS-132.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF020038; AAD02918.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF113917; AAD29284.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136702; CAB66637.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012846; AAH12846.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U62389; AAB17375.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T46280; T46280.
RefSeq NP_005887.2; -.
UniGene Hs.593422
3D structure databases
PDB
1T09; X-ray; 2.70 A; A/B=1-414.[ExPASy / RCSB / EBI]
1T0L; X-ray; 2.41 A; A/B/C/D=1-414.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1T09; -.
1T0L; -.
ModBase O75874.
Protein-protein interaction databases
IntAct O75874; 1.
PTM databases
PhosphoSite O75874; -.
2D gel databases
OGP O75874; -.
REPRODUCTION-2DPAGE IPI00027223; -.
Organism-specific databases
GeneCards GC02M208809; -.
H-InvDB HIX0002783; -.
HIX0033384; -.
HGNC HGNC:5382; IDH1.
GenAtlas IDH1.
MIM 147700; gene. [NCBI / EBI]
PharmGKB PA29630; -.
GeneCards O75874.
Gene expression databases
ArrayExpress O75874; -.
CleanEx HS_IDH1; -.
GermOnline ENSG00000138413; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (traceable author statement from ProtInc).
GO:0005777; Cellular component: peroxisome (inferred from electronic annotation from UniProtKB-KW).
GO:0004450; Molecular function: isocitrate dehydrogenase (NADP+) activity (traceable author statement from ProtInc).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145; Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006097; Biological process: glyoxylate cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0006102; Biological process: isocitrate metabolic process (traceable author statement from ProtInc).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006099; Biological process: tricarboxylic acid cycle (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR004790; IsoCit_DHase_NADP-dep_euk.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.718.10; IDH_IMDH; 1.
PANTHER PTHR11822; IDH_NADP_euk; 1.
Pfam PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000108; IDH_NADP; 1.
TIGRFAMs TIGR00127; nadp_idh_euk; 1.
PROSITE PS00470; IDH_IMDH; 1.
Proteomic databases
PeptideAtlas O75874; -.
Proteomics databases
PRIDE O75874; -.
Genome annotation databases
Ensembl ENSG00000138413; Homo sapiens. [Contig view]
GeneID 3417; -.
KEGG hsa:3417; -.
Phylogenomic databases
HOGENOM O75874; -.
HOVERGEN O75874; -.
Other
LinkHub O75874; -.
NextBio 13470; -.
SOURCE IDH1; Homo sapiens.
ProtoNet O75874.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Direct protein sequencing; Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP; Oxidoreductase; Peroxisome; Polymorphism; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   414  414     Isocitrate dehydrogenase [NADP] cytoplasmic. PRO_0000083575
NP_BIND   75    77  3     NADP. 
NP_BIND   310   315  6     NADP. 
REGION   94   100  7     Substrate binding. 
METAL   252   252        Magnesium or manganese. 
METAL   275   275        Magnesium or manganese. 
BINDING   77    77        Substrate. 
BINDING   82    82        NADP. 
BINDING   109   109        Substrate. 
BINDING   132   132        Substrate. 
BINDING   260   260        NADP. 
BINDING   328   328        NADP; via amide nitrogen and carbonyl oxygen. 
SITE   139   139  1     Critical for catalysis. 
SITE   212   212  1     Critical for catalysis. 
VARIANT   132   132  1     R -> C (in a colorectal cancer sample; somatic mutation). VAR_036013 [3D]
VARIANT   178   178  1     V -> I (in dbSNP:rs34218846 [NCBI]). VAR_049780 [3D]
CONFLICT   32    32        F -> I (in Ref. 3; CAB66637). 
CONFLICT   126   126        K -> E (in Ref. 3; CAB66637). 
CONFLICT   218   218        K -> I (in Ref. 1; AAD02918). 
CONFLICT   329   329        P -> L (in Ref. 1; AAD02918). 
CONFLICT   381   381        K -> R (in Ref. 1; AAD02918). 
STRAND   5    14  10      
HELIX   17    29  13      
TURN   30    34  5      
STRAND   35    43  9      
HELIX   46    51  6      
TURN   52    54  3      
HELIX   55    67  13      
STRAND   68    72  5      
HELIX   80    86  7      
HELIX   95   103  9      
STRAND   106   111  6      
STRAND   128   133  6      
HELIX   137   140  4      
STRAND   142   146  5      
STRAND   148   158  11      
STRAND   165   172  8      
STRAND   177   185  9      
HELIX   186   203  18      
STRAND   207   211  5      
TURN   213   215  3      
HELIX   219   234  16      
HELIX   236   241  6      
STRAND   246   250  5      
HELIX   251   260  10      
STRAND   265   269  5      
HELIX   271   285  15      
STRAND   290   296  7      
STRAND   303   306  4      
HELIX   313   320  8      
HELIX   330   347  18      
HELIX   350   368  19      
HELIX   374   380  7      
HELIX   383   385  3      
HELIX   388   390  3      
HELIX   394   411  18      
Sequence information
Length: 414 AA [This is the length of the unprocessed precursor] Molecular weight: 46659 Da [This is the MW of the unprocessed precursor] CRC64: 60428B0B6E5851DC [This is a checksum on the sequence]
        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 

O75874 in FASTA format

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