Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P51553 (IDH3G_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial

EC=1.1.1.41
Alternative name(s):
Isocitric dehydrogenase subunit gamma
NAD(+)-specific ICDH subunit gamma
Gene names
Name:IDH3G
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length393 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 + NAD+ = 2-oxoglutarate + CO2 + NADH.

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity.

Enzyme regulation

Activated by increasing ADP/ATP ratios and by Ca2+ By similarity.

Subunit structure

Heterooligomer of subunits alpha, beta, and gamma in the apparent ratio of 2:1:1 By similarity.

Subcellular location

Mitochondrion Ref.5.

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P51553-1)

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: P51553-2)

The sequence of this isoform differs from the canonical sequence as follows:
     361-393: MHTPDIGGQGTTSEAIQDVIRHIRVINGRAVEA → VRFPSHPTLLPRPVSPCSLL
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3939Mitochondrion By similarity
Chain40 – 393354Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial
PRO_0000014449

Regions

Nucleotide binding56 – 8429NAD Potential
Nucleotide binding309 – 3168ATP Potential

Sites

Metal binding2541Magnesium or manganese By similarity
Binding site1361Substrate By similarity
Binding site1671Substrate By similarity
Binding site2541Substrate By similarity
Site1741Critical for catalysis By similarity
Site2211Critical for catalysis By similarity

Amino acid modifications

Modified residue2061N6-acetyllysine By similarity
Modified residue2261N6-succinyllysine By similarity

Natural variations

Alternative sequence361 – 39333MHTPD…RAVEA → VRFPSHPTLLPRPVSPCSLL in isoform 2.
VSP_046771

Experimental info

Sequence conflict2671F → L in AAH01902. Ref.4

Sequences

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

Last modified October 1, 1996. Version 1.
Checksum: A0870F2B7D228A37

FASTA39342,794
        10         20         30         40         50         60 
MALKVATVAG SAAKAVLGPA LLCRPWEVLG AHEVPSRNIF SEQTIPPSAK YGGRHTVTMI 

        70         80         90        100        110        120 
PGDGIGPELM LHVKSVFRHA CVPVDFEEVH VSSNADEEDI RNAIMAIRRN RVALKGNIET 

       130        140        150        160        170        180 
NHNLPPSHKS RNNILRTSLD LYANVIHCKS LPGVVTRHKD IDILIVRENT EGEYSSLEHE 

       190        200        210        220        230        240 
SVAGVVESLK IITKAKSLRI AEYAFKLAQE SGRKKVTAVH KANIMKLGDG LFLQCCREVA 

       250        260        270        280        290        300 
ARYPQITFEN MIVDNTTMQL VSRPQQFDVM VMPNLYGNIV NNVCAGLVGG PGLVAGANYG 

       310        320        330        340        350        360 
HVYAVFETAT RNTGKSIANK NIANPTATLL ASCMMLDHLK LHSYATSIRK AVLASMDNEN 

       370        380        390 
MHTPDIGGQG TTSEAIQDVI RHIRVINGRA VEA 

« Hide

Isoform 2 [UniParc].

Checksum: 2D5987CC70725245
Show »

FASTA38041,468

References

« Hide 'large scale' references
[1]"Genomic organization of two novel genes on human Xq28: compact head to head arrangement of IDH gamma and TRAP delta is conserved in rat and mouse."
Brenner V., Nyakatura G., Rosenthal A., Platzer M.
Genomics 44:8-14(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Identification and functional characterization of a novel, tissue-specific NAD+-dependent isocitrate dehydrogenase beta subunit isoform."
Kim Y.-O., Koh H.-J., Kim S.-H., Jo S.-H., Huh J.-W., Jeong K.-S., Lee I.J., Song B.J., Huh T.-L.
J. Biol. Chem. 274:36866-36875(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Heart.
[3]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORM 1).
Tissue: Placenta and Skin.
[5]"Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing."
Simpson J.C., Wellenreuther R., Poustka A., Pepperkok R., Wiemann S.
EMBO Rep. 1:287-292(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[6]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z68907 mRNA. Translation: CAA93143.1.
Z68129 Genomic DNA. Translation: CAA92214.1.
U52111 Genomic DNA. No translation available.
U40272 mRNA. Translation: AAD09357.1.
BC000933 mRNA. Translation: AAH00933.1.
BC001902 mRNA. Translation: AAH01902.1.
RefSeqNP_004126.1. NM_004135.3.
NP_777358.1. NM_174869.2.
UniGeneHs.410197.

3D structure databases

ProteinModelPortalP51553.
SMRP51553. Positions 50-386.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109647. 15 interactions.
IntActP51553. 2 interactions.
MINTMINT-3018829.
STRING9606.ENSP00000217901.

Chemistry

DrugBankDB00157. NADH.

PTM databases

PhosphoSiteP51553.

Polymorphism databases

DMDM1708404.

Proteomic databases

PaxDbP51553.
PRIDEP51553.

Protocols and materials databases

DNASU3421.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000217901; ENSP00000217901; ENSG00000067829. [P51553-1]
ENST00000370092; ENSP00000359110; ENSG00000067829. [P51553-2]
ENST00000593996; ENSP00000473196; ENSG00000267989. [P51553-1]
ENST00000600403; ENSP00000469494; ENSG00000267989. [P51553-2]
GeneID3421.
KEGGhsa:3421.
UCSCuc004fip.4. human. [P51553-1]

Organism-specific databases

CTD3421.
GeneCardsGC0XM153051.
HGNCHGNC:5386. IDH3G.
HPAHPA000425.
HPA002017.
MIM300089. gene.
neXtProtNX_P51553.
PharmGKBPA29634.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0473.
HOGENOMHOG000021113.
HOVERGENHBG052080.
InParanoidP51553.
KOK00030.
OMANETRLHT.
OrthoDBEOG75B85R.
PhylomeDBP51553.
TreeFamTF315033.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000067829-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_17015. Metabolism of proteins.
SABIO-RKP51553.

Gene expression databases

ArrayExpressP51553.
BgeeP51553.
CleanExHS_IDH3G.
GenevestigatorP51553.

Family and domain databases

Gene3D3.40.718.10. 1 hit.
InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR004434. Isocitrate_DH_NAD.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERPTHR11835. PTHR11835. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR00175. mito_nad_idh. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiIDH3G.
GenomeRNAi3421.
NextBio13490.
PROP51553.
SOURCESearch...

Entry information

Entry nameIDH3G_HUMAN
AccessionPrimary (citable) accession number: P51553
Secondary accession number(s): E9PDD5, Q9BUU5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 150 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

MIM cross-references

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

Human chromosome X

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