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P48735

- IDHP_HUMAN

UniProt

P48735 - IDHP_HUMAN

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Protein

Isocitrate dehydrogenase [NADP], mitochondrial

Gene

IDH2

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

Functioni

Plays a role in intermediary metabolism and energy production. It may tightly associate or interact with the pyruvate dehydrogenase complex.

Catalytic activityi

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

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 1 Mg(2+) or Mn(2+) ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei117 – 1171SubstrateBy similarity
Binding sitei122 – 1221NADPBy similarity
Binding sitei149 – 1491SubstrateBy similarity
Binding sitei172 – 1721SubstrateBy similarity
Sitei179 – 1791Critical for catalysisBy similarity
Sitei251 – 2511Critical for catalysisBy similarity
Metal bindingi291 – 2911Magnesium or manganeseBy similarity
Binding sitei299 – 2991NADPBy similarity
Metal bindingi314 – 3141Magnesium or manganeseBy similarity
Binding sitei367 – 3671NADP; via amide nitrogen and carbonyl oxygenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi115 – 1173NADPBy similarity
Nucleotide bindingi349 – 3546NADPBy similarity

GO - Molecular functioni

  1. isocitrate dehydrogenase (NADP+) activity Source: UniProtKB
  2. magnesium ion binding Source: UniProtKB
  3. NAD binding Source: InterPro

GO - Biological processi

  1. 2-oxoglutarate metabolic process Source: UniProtKB
  2. carbohydrate metabolic process Source: ProtInc
  3. cellular metabolic process Source: Reactome
  4. glyoxylate cycle Source: UniProtKB-KW
  5. isocitrate metabolic process Source: UniProtKB
  6. small molecule metabolic process Source: Reactome
  7. tricarboxylic acid cycle Source: Reactome
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:HS00021-MONOMER.
ReactomeiREACT_1785. Citric acid cycle (TCA cycle).

Names & Taxonomyi

Protein namesi
Recommended name:
Isocitrate dehydrogenase [NADP], mitochondrial (EC:1.1.1.42)
Short name:
IDH
Alternative name(s):
ICD-M
IDP
NADP(+)-specific ICDH
Oxalosuccinate decarboxylase
Gene namesi
Name:IDH2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:5383. IDH2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. mitochondrial inner membrane Source: Ensembl
  3. mitochondrial matrix Source: Reactome
  4. mitochondrion Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

D-2-hydroxyglutaric aciduria 2 (D2HGA2) [MIM:613657]: A neurometabolic disorder causing developmental delay, epilepsy, hypotonia, and dysmorphic features. Both a mild and a severe phenotype exist. The severe phenotype is homogeneous and is characterized by early infantile-onset epileptic encephalopathy and cardiomyopathy. The mild phenotype has a more variable clinical presentation. Diagnosis is based on the presence of an excess of D-2-hydroxyglutaric acid in the urine.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti140 – 1401R → G in D2HGA2. 1 Publication
VAR_065174
Natural varianti140 – 1401R → Q in D2HGA2. 1 Publication
VAR_065175

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi413 – 4131K → A: 44-fold loss in activity. 1 Publication
Mutagenesisi413 – 4131K → Q: 20-fold decrease in Vmax. 1 Publication
Mutagenesisi413 – 4131K → R: No appreciable difference in Km for isocitrate and NADP. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi613657. phenotype.
Orphaneti79315. D-2-hydroxyglutaric aciduria.
296. Enchondromatosis.
163634. Maffucci syndrome.
PharmGKBiPA29631.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3939MitochondrionBy similarityAdd
BLAST
Chaini40 – 452413Isocitrate dehydrogenase [NADP], mitochondrialPRO_0000014420Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei45 – 451N6-acetyllysineBy similarity
Modified residuei48 – 481N6-acetyllysineBy similarity
Modified residuei67 – 671N6-acetyllysine1 Publication
Modified residuei69 – 691N6-acetyllysineBy similarity
Modified residuei80 – 801N6-acetyllysine; alternateBy similarity
Modified residuei80 – 801N6-succinyllysine; alternateBy similarity
Modified residuei106 – 1061N6-acetyllysine; alternate1 Publication
Modified residuei106 – 1061N6-succinyllysine; alternateBy similarity
Modified residuei155 – 1551N6-acetyllysine1 Publication
Modified residuei166 – 1661N6-acetyllysine; alternate1 Publication
Modified residuei166 – 1661N6-succinyllysine; alternateBy similarity
Modified residuei180 – 1801N6-acetyllysine; alternate1 Publication
Modified residuei180 – 1801N6-succinyllysine; alternateBy similarity
Modified residuei193 – 1931N6-acetyllysine; alternateBy similarity
Modified residuei193 – 1931N6-succinyllysine; alternateBy similarity
Modified residuei199 – 1991N6-acetyllysineBy similarity
Modified residuei256 – 2561N6-acetyllysine; alternate1 Publication
Modified residuei256 – 2561N6-succinyllysine; alternateBy similarity
Modified residuei263 – 2631N6-acetyllysine1 Publication
Modified residuei272 – 2721N6-acetyllysine1 Publication
Modified residuei275 – 2751N6-acetyllysine1 Publication
Modified residuei280 – 2801N6-acetyllysineBy similarity
Modified residuei282 – 2821N6-acetyllysine; alternate1 Publication
Modified residuei282 – 2821N6-succinyllysine; alternateBy similarity
Modified residuei384 – 3841N6-acetyllysine; alternateBy similarity
Modified residuei384 – 3841N6-succinyllysine; alternateBy similarity
Modified residuei400 – 4001N6-acetyllysineBy similarity
Modified residuei413 – 4131N6-acetyllysine1 Publication
Modified residuei442 – 4421N6-acetyllysine1 Publication

Post-translational modificationi

Acetylation at Lys-413 dramatically reduces catalytic activity. Deacetylated by SIRT3.2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP48735.
PaxDbiP48735.
PeptideAtlasiP48735.
PRIDEiP48735.

2D gel databases

OGPiP48735.
UCD-2DPAGEP48735.

PTM databases

PhosphoSiteiP48735.

Expressioni

Gene expression databases

BgeeiP48735.
CleanExiHS_IDH2.
ExpressionAtlasiP48735. baseline and differential.
GenevestigatoriP48735.

Organism-specific databases

HPAiHPA007831.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi109644. 9 interactions.
IntActiP48735. 2 interactions.
MINTiMINT-3016964.
STRINGi9606.ENSP00000331897.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi50 – 545Combined sources
Helixi57 – 6913Combined sources
Turni70 – 745Combined sources
Beta strandi79 – 835Combined sources
Helixi86 – 916Combined sources
Turni92 – 943Combined sources
Helixi95 – 10713Combined sources
Beta strandi108 – 1125Combined sources
Helixi120 – 1267Combined sources
Helixi135 – 1439Combined sources
Beta strandi146 – 1516Combined sources
Beta strandi168 – 1725Combined sources
Helixi177 – 1804Combined sources
Beta strandi182 – 1865Combined sources
Beta strandi190 – 1989Combined sources
Beta strandi205 – 21410Combined sources
Beta strandi216 – 2249Combined sources
Helixi225 – 24218Combined sources
Beta strandi246 – 2505Combined sources
Turni252 – 2543Combined sources
Helixi258 – 27316Combined sources
Helixi275 – 2806Combined sources
Beta strandi285 – 2895Combined sources
Helixi290 – 29910Combined sources
Beta strandi304 – 3085Combined sources
Helixi310 – 32314Combined sources
Helixi327 – 3293Combined sources
Beta strandi330 – 3356Combined sources
Beta strandi342 – 3487Combined sources
Helixi352 – 3598Combined sources
Helixi369 – 38618Combined sources
Helixi389 – 40719Combined sources
Helixi413 – 4208Combined sources
Helixi422 – 4243Combined sources
Turni427 – 4293Combined sources
Helixi434 – 45219Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JA8X-ray1.55A/B41-452[»]
ProteinModelPortaliP48735.
SMRiP48735. Positions 41-452.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni134 – 1407Substrate bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0538.
GeneTreeiENSGT00390000012547.
HOGENOMiHOG000019858.
HOVERGENiHBG006119.
InParanoidiP48735.
KOiK00031.
OMAiCFQYAIG.
OrthoDBiEOG7QNVKS.
PhylomeDBiP48735.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P48735-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAGYLRVVRS LCRASGSRPA WAPAALTAPT SQEQPRRHYA DKRIKVAKPV
60 70 80 90 100
VEMDGDEMTR IIWQFIKEKL ILPHVDIQLK YFDLGLPNRD QTDDQVTIDS
110 120 130 140 150
ALATQKYSVA VKCATITPDE ARVEEFKLKK MWKSPNGTIR NILGGTVFRE
160 170 180 190 200
PIICKNIPRL VPGWTKPITI GRHAHGDQYK ATDFVADRAG TFKMVFTPKD
210 220 230 240 250
GSGVKEWEVY NFPAGGVGMG MYNTDESISG FAHSCFQYAI QKKWPLYMST
260 270 280 290 300
KNTILKAYDG RFKDIFQEIF DKHYKTDFDK NKIWYEHRLI DDMVAQVLKS
310 320 330 340 350
SGGFVWACKN YDGDVQSDIL AQGFGSLGLM TSVLVCPDGK TIEAEAAHGT
360 370 380 390 400
VTRHYREHQK GRPTSTNPIA SIFAWTRGLE HRGKLDGNQD LIRFAQMLEK
410 420 430 440 450
VCVETVESGA MTKDLAGCIH GLSNVKLNEH FLNTTDFLDT IKSNLDRALG

RQ
Length:452
Mass (Da):50,909
Last modified:April 3, 2002 - v2
Checksum:i4DDC830AFC06AB52
GO
Isoform 2 (identifier: P48735-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: Missing.

Note: No experimental confirmation available.

Show »
Length:400
Mass (Da):45,180
Checksum:iF1274A2EC2243D5E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341Q → H in CAA49208. 1 PublicationCurated
Sequence conflicti435 – 4351T → M in CAA49208. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti140 – 1401R → G in D2HGA2. 1 Publication
VAR_065174
Natural varianti140 – 1401R → Q in D2HGA2. 1 Publication
VAR_065175

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5252Missing in isoform 2. 1 PublicationVSP_056278Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69433 mRNA. Translation: CAA49208.1.
AK294148 mRNA. Translation: BAG57473.1.
AK312627 mRNA. Translation: BAG35513.1.
AK316388 mRNA. Translation: BAH14759.1.
AC087284 Genomic DNA. No translation available.
AC092769 Genomic DNA. No translation available.
CH471101 Genomic DNA. Translation: EAX02082.1.
BC009244 mRNA. Translation: AAH09244.1.
BC071828 mRNA. Translation: AAH71828.1.
CCDSiCCDS10359.1. [P48735-1]
PIRiS57499.
RefSeqiNP_001276839.1. NM_001289910.1. [P48735-2]
NP_001277043.1. NM_001290114.1.
NP_002159.2. NM_002168.3. [P48735-1]
UniGeneiHs.596461.

Genome annotation databases

EnsembliENST00000330062; ENSP00000331897; ENSG00000182054. [P48735-1]
ENST00000540499; ENSP00000446147; ENSG00000182054. [P48735-2]
GeneIDi3418.
KEGGihsa:3418.
UCSCiuc002box.3. human. [P48735-1]

Polymorphism databases

DMDMi20141568.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69433 mRNA. Translation: CAA49208.1 .
AK294148 mRNA. Translation: BAG57473.1 .
AK312627 mRNA. Translation: BAG35513.1 .
AK316388 mRNA. Translation: BAH14759.1 .
AC087284 Genomic DNA. No translation available.
AC092769 Genomic DNA. No translation available.
CH471101 Genomic DNA. Translation: EAX02082.1 .
BC009244 mRNA. Translation: AAH09244.1 .
BC071828 mRNA. Translation: AAH71828.1 .
CCDSi CCDS10359.1. [P48735-1 ]
PIRi S57499.
RefSeqi NP_001276839.1. NM_001289910.1. [P48735-2 ]
NP_001277043.1. NM_001290114.1.
NP_002159.2. NM_002168.3. [P48735-1 ]
UniGenei Hs.596461.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4JA8 X-ray 1.55 A/B 41-452 [» ]
ProteinModelPortali P48735.
SMRi P48735. Positions 41-452.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109644. 9 interactions.
IntActi P48735. 2 interactions.
MINTi MINT-3016964.
STRINGi 9606.ENSP00000331897.

PTM databases

PhosphoSitei P48735.

Polymorphism databases

DMDMi 20141568.

2D gel databases

OGPi P48735.
UCD-2DPAGE P48735.

Proteomic databases

MaxQBi P48735.
PaxDbi P48735.
PeptideAtlasi P48735.
PRIDEi P48735.

Protocols and materials databases

DNASUi 3418.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000330062 ; ENSP00000331897 ; ENSG00000182054 . [P48735-1 ]
ENST00000540499 ; ENSP00000446147 ; ENSG00000182054 . [P48735-2 ]
GeneIDi 3418.
KEGGi hsa:3418.
UCSCi uc002box.3. human. [P48735-1 ]

Organism-specific databases

CTDi 3418.
GeneCardsi GC15M090626.
HGNCi HGNC:5383. IDH2.
HPAi HPA007831.
MIMi 147650. gene.
613657. phenotype.
neXtProti NX_P48735.
Orphaneti 79315. D-2-hydroxyglutaric aciduria.
296. Enchondromatosis.
163634. Maffucci syndrome.
PharmGKBi PA29631.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0538.
GeneTreei ENSGT00390000012547.
HOGENOMi HOG000019858.
HOVERGENi HBG006119.
InParanoidi P48735.
KOi K00031.
OMAi CFQYAIG.
OrthoDBi EOG7QNVKS.
PhylomeDBi P48735.
TreeFami TF300428.

Enzyme and pathway databases

BioCyci MetaCyc:HS00021-MONOMER.
Reactomei REACT_1785. Citric acid cycle (TCA cycle).

Miscellaneous databases

ChiTaRSi IDH2. human.
GeneWikii IDH2.
GenomeRNAii 3418.
NextBioi 13474.
PROi P48735.
SOURCEi Search...

Gene expression databases

Bgeei P48735.
CleanExi HS_IDH2.
ExpressionAtlasi P48735. baseline and differential.
Genevestigatori P48735.

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. Huh T.-L., Oh I.-U., Kim Y.O., Huh J.-W., Song B.J.
    Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Heart.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain cortex, Heart and Testis.
  3. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Colon and Skin.
  6. "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-67; LYS-106; LYS-155; LYS-166; LYS-180; LYS-256; LYS-263; LYS-272; LYS-275; LYS-282 AND LYS-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "SIRT3 protein deacetylates isocitrate dehydrogenase 2 (IDH2) and regulates mitochondrial redox status."
    Yu W., Dittenhafer-Reed K.E., Denu J.M.
    J. Biol. Chem. 287:14078-14086(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-413, MUTAGENESIS OF LYS-413.
  9. Cited for: VARIANTS D2HGA2 GLN-140 AND GLY-140.

Entry informationi

Entry nameiIDHP_HUMAN
AccessioniPrimary (citable) accession number: P48735
Secondary accession number(s): B2R6L6, B4DFL2, Q96GT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: April 3, 2002
Last modified: November 26, 2014
This is version 146 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, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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