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Protein

L-2-hydroxyglutarate dehydrogenase, mitochondrial

Gene

L2hgdh

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

FADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiREACT_321825. 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 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:2384968. L2hgdh.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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.
GenevisibleiQ91YP0. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000021370.

Structurei

3D structure databases

ProteinModelPortaliQ91YP0.
SMRiQ91YP0. Positions 48-329.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the L2HGDH family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0579.
GeneTreeiENSGT00490000043421.
HOGENOMiHOG000245180.
HOVERGENiHBG081883.
InParanoidiQ91YP0.
KOiK00109.
OMAiHFTRMID.
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

        10         20         30         40         50
MWPTLRYVGG VCGLARYCVA GGFLRASGPA SGVPGLLCGG GRRSSSTSSF
60 70 80 90 100
DIVIVGGGIV GLASARTLIL KHPGLSIGVV EKEKDLALHQ TGHNSGVIHS
110 120 130 140 150
GIYYKPESLK AKLCVEGAAL IYEYCNLKGI PYRQCGKLIV AVEQEEIPRL
160 170 180 190 200
QALYERGLQN GVEGLRLIQQ EDIKKKEPYC RGLMAIDCPY TGIVNYQQVA
210 220 230 240 250
LSFAQDFQEA GGSILRDFEV KGIEIAKENS SRSKDGMNYP IAVKNSKGKE
260 270 280 290 300
IRCRYVVTCA GLYSDRISEL SGCNPDPQIV PFRGDYLVLK PEKGYLVKGN
310 320 330 340 350
IYPVPDSRFP FLGVHFTPRL DGTIWLGPNA VLAFKREGYR PFDFDARDVM
360 370 380 390 400
EVILKSGFIN LVFQHFSYGV NEMYKACFLS ETVKHLQKFI PEITISDVLR
410 420 430 440 450
GPAGVRAQAL DRDGNLVEDF VFDGGTGEIA DRVLHVRNAP SPAATSSLAI
460
SRMIAEEAQQ RFKL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ91YP0.
SMRiQ91YP0. Positions 48-329.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000021370.

PTM databases

PhosphoSiteiQ91YP0.

Proteomic databases

MaxQBiQ91YP0.
PaxDbiQ91YP0.
PRIDEiQ91YP0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi79944.
MGIiMGI:2384968. L2hgdh.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_321825. Interconversion of 2-oxoglutarate and 2-hydroxyglutarate.

Miscellaneous databases

NextBioi375942.
PROiQ91YP0.
SOURCEiSearch...

Gene expression databases

BgeeiQ91YP0.
CleanExiMM_L2HGDH.
GenevisibleiQ91YP0. MM.

Family and domain databases

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

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: June 24, 2015
This is version 103 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.