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Q91YP0

- L2HDH_MOUSE

UniProt

Q91YP0 - L2HDH_MOUSE

Protein

L-2-hydroxyglutarate dehydrogenase, mitochondrial

Gene

L2hgdh

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    (S)-2-hydroxyglutarate + acceptor = 2-oxoglutarate + reduced acceptor.

    Cofactori

    FAD.By similarity

    GO - Molecular functioni

    1. 2-hydroxyglutarate dehydrogenase activity Source: HGNC

    GO - Biological processi

    1. cellular protein metabolic process Source: HGNC

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    ReactomeiREACT_198633. Interconversion of 2-oxoglutarate and 2-hydroxyglutarate.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-2-hydroxyglutarate dehydrogenase, mitochondrial (EC:1.1.99.2)
    Alternative name(s):
    Duranin
    Gene namesi
    Name:L2hgdh
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 12

    Organism-specific databases

    MGIiMGI:2384968. L2hgdh.

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. integral component of membrane Source: HGNC
    2. mitochondrion Source: HGNC

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5252MitochondrionSequence AnalysisAdd
    BLAST
    Chaini53 – 464412L-2-hydroxyglutarate dehydrogenase, mitochondrialPRO_0000228130Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei105 – 1051N6-acetyllysine1 Publication
    Modified residuei174 – 1741N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ91YP0.
    PaxDbiQ91YP0.
    PRIDEiQ91YP0.

    PTM databases

    PhosphoSiteiQ91YP0.

    Expressioni

    Gene expression databases

    BgeeiQ91YP0.
    CleanExiMM_L2HGDH.
    GenevestigatoriQ91YP0.

    Structurei

    3D structure databases

    ProteinModelPortaliQ91YP0.
    SMRiQ91YP0. Positions 46-329.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the L2HGDH family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0579.
    GeneTreeiENSGT00490000043421.
    HOGENOMiHOG000245180.
    HOVERGENiHBG081883.
    InParanoidiQ91YP0.
    KOiK00109.
    OMAiNVCNAPS.
    OrthoDBiEOG7MPRDR.
    PhylomeDBiQ91YP0.
    TreeFamiTF105922.

    Family and domain databases

    InterProiIPR006076. FAD-dep_OxRdtase.
    [Graphical view]
    PfamiPF01266. DAO. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q91YP0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWPTLRYVGG VCGLARYCVA GGFLRASGPA SGVPGLLCGG GRRSSSTSSF    50
    DIVIVGGGIV GLASARTLIL KHPGLSIGVV EKEKDLALHQ TGHNSGVIHS 100
    GIYYKPESLK AKLCVEGAAL IYEYCNLKGI PYRQCGKLIV AVEQEEIPRL 150
    QALYERGLQN GVEGLRLIQQ EDIKKKEPYC RGLMAIDCPY TGIVNYQQVA 200
    LSFAQDFQEA GGSILRDFEV KGIEIAKENS SRSKDGMNYP IAVKNSKGKE 250
    IRCRYVVTCA GLYSDRISEL SGCNPDPQIV PFRGDYLVLK PEKGYLVKGN 300
    IYPVPDSRFP FLGVHFTPRL DGTIWLGPNA VLAFKREGYR PFDFDARDVM 350
    EVILKSGFIN LVFQHFSYGV NEMYKACFLS ETVKHLQKFI PEITISDVLR 400
    GPAGVRAQAL DRDGNLVEDF VFDGGTGEIA DRVLHVRNAP SPAATSSLAI 450
    SRMIAEEAQQ RFKL 464
    Length:464
    Mass (Da):50,899
    Last modified:December 1, 2001 - v1
    Checksum:i27270B28FCCC3762
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti184 – 1841M → I in BAE31229. (PubMed:16141072)Curated
    Sequence conflicti216 – 2161R → K in BAE26312. (PubMed:16141072)Curated
    Sequence conflicti225 – 2251I → V in BAE26312. (PubMed:16141072)Curated
    Sequence conflicti228 – 2281E → G in BAE31229. (PubMed:16141072)Curated
    Sequence conflicti416 – 4161L → P in BAE40337. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK145228 mRNA. Translation: BAE26312.1.
    AK152450 mRNA. Translation: BAE31229.1.
    AK168429 mRNA. Translation: BAE40337.1.
    BC016226 mRNA. Translation: AAH16226.1.
    CCDSiCCDS25953.1.
    RefSeqiNP_663418.1. NM_145443.2.
    UniGeneiMm.103362.

    Genome annotation databases

    EnsembliENSMUST00000021370; ENSMUSP00000021370; ENSMUSG00000020988.
    GeneIDi217666.
    KEGGimmu:217666.
    UCSCiuc011ynb.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK145228 mRNA. Translation: BAE26312.1 .
    AK152450 mRNA. Translation: BAE31229.1 .
    AK168429 mRNA. Translation: BAE40337.1 .
    BC016226 mRNA. Translation: AAH16226.1 .
    CCDSi CCDS25953.1.
    RefSeqi NP_663418.1. NM_145443.2.
    UniGenei Mm.103362.

    3D structure databases

    ProteinModelPortali Q91YP0.
    SMRi Q91YP0. Positions 46-329.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q91YP0.

    Proteomic databases

    MaxQBi Q91YP0.
    PaxDbi Q91YP0.
    PRIDEi Q91YP0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000021370 ; ENSMUSP00000021370 ; ENSMUSG00000020988 .
    GeneIDi 217666.
    KEGGi mmu:217666.
    UCSCi uc011ynb.1. mouse.

    Organism-specific databases

    CTDi 79944.
    MGIi MGI:2384968. L2hgdh.

    Phylogenomic databases

    eggNOGi COG0579.
    GeneTreei ENSGT00490000043421.
    HOGENOMi HOG000245180.
    HOVERGENi HBG081883.
    InParanoidi Q91YP0.
    KOi K00109.
    OMAi NVCNAPS.
    OrthoDBi EOG7MPRDR.
    PhylomeDBi Q91YP0.
    TreeFami TF105922.

    Enzyme and pathway databases

    Reactomei REACT_198633. Interconversion of 2-oxoglutarate and 2-hydroxyglutarate.

    Miscellaneous databases

    NextBioi 375942.
    PROi Q91YP0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q91YP0.
    CleanExi MM_L2HGDH.
    Genevestigatori Q91YP0.

    Family and domain databases

    InterProi IPR006076. FAD-dep_OxRdtase.
    [Graphical view ]
    Pfami PF01266. DAO. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Amnion, Bone marrow and Mammary gland.
    2. "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].
      Strain: FVB/N.
      Tissue: Mammary tumor.
    3. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-105 AND LYS-174, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiL2HDH_MOUSE
    AccessioniPrimary (citable) accession number: Q91YP0
    Secondary accession number(s): Q3TH61, Q3U7Z0, Q3ULY6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 21, 2006
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3