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P08249

- MDHM_MOUSE

UniProt

P08249 - MDHM_MOUSE

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Protein

Malate dehydrogenase, mitochondrial

Gene

Mdh2

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

Functioni

Catalytic activityi

(S)-malate + NAD+ = oxaloacetate + NADH.PROSITE-ProRule annotation

Enzyme regulationi

Enzyme activity is enhanced by acetylation.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei57 – 571NADBy similarity
Binding sitei104 – 1041Substrate
Binding sitei110 – 1101Substrate
Binding sitei117 – 1171NADBy similarity
Binding sitei142 – 1421Substrate
Binding sitei176 – 1761Substrate
Active sitei200 – 2001Proton acceptorBy similarity
Binding sitei251 – 2511NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi31 – 377NADBy similarity
Nucleotide bindingi140 – 1423NADBy similarity

GO - Molecular functioni

  1. L-malate dehydrogenase activity Source: MGI
  2. malate dehydrogenase (NADP+) activity Source: Ensembl
  3. malate dehydrogenase activity Source: MGI
  4. poly(A) RNA binding Source: Ensembl

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: InterPro
  2. internal protein amino acid acetylation Source: UniProtKB
  3. malate metabolic process Source: MGI
  4. NADH metabolic process Source: Ensembl
  5. oxaloacetate metabolic process Source: Ensembl
  6. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase, mitochondrial (EC:1.1.1.37)
Gene namesi
Name:Mdh2
Synonyms:Mor1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:97050. Mdh2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. mitochondrial inner membrane Source: MGI
  3. mitochondrial matrix Source: Ensembl
  4. mitochondrion Source: MGI
  5. nucleus Source: Ensembl
  6. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2424MitochondrionAdd
BLAST
Chaini25 – 338314Malate dehydrogenase, mitochondrialPRO_0000018629Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi33 – 331O-linked (GlcNAc)By similarity
Modified residuei78 – 781N6-acetyllysine; alternate1 Publication
Modified residuei78 – 781N6-succinyllysine; alternate1 Publication
Modified residuei91 – 911N6-acetyllysine; alternate1 Publication
Modified residuei91 – 911N6-succinyllysine; alternate1 Publication
Modified residuei165 – 1651N6-acetyllysine1 Publication
Modified residuei185 – 1851N6-acetyllysine; alternate1 Publication
Modified residuei185 – 1851N6-succinyllysine; alternate1 Publication
Modified residuei203 – 2031N6-succinyllysine1 Publication
Modified residuei215 – 2151N6-acetyllysine; alternate1 Publication
Modified residuei215 – 2151N6-succinyllysine; alternate1 Publication
Modified residuei239 – 2391N6-acetyllysine; alternate2 Publications
Modified residuei239 – 2391N6-malonyllysine; alternateBy similarity
Modified residuei239 – 2391N6-succinyllysine; alternate1 Publication
Modified residuei269 – 2691N6-succinyllysine1 Publication
Modified residuei296 – 2961N6-acetyllysine; alternate1 Publication
Modified residuei296 – 2961N6-succinyllysine; alternate1 Publication
Modified residuei301 – 3011N6-acetyllysine; alternate1 Publication
Modified residuei301 – 3011N6-succinyllysine; alternate1 Publication
Modified residuei307 – 3071N6-acetyllysine; alternate1 Publication
Modified residuei307 – 3071N6-malonyllysine; alternateBy similarity
Modified residuei307 – 3071N6-succinyllysine; alternate1 Publication
Modified residuei314 – 3141N6-acetyllysine; alternate1 Publication
Modified residuei314 – 3141N6-succinyllysine; alternate1 Publication
Modified residuei324 – 3241N6-acetyllysine; alternate1 Publication
Modified residuei324 – 3241N6-succinyllysine; alternate1 Publication
Modified residuei328 – 3281N6-acetyllysine; alternateBy similarity
Modified residuei328 – 3281N6-succinyllysine; alternateBy similarity
Modified residuei329 – 3291N6-acetyllysine; alternate1 Publication
Modified residuei329 – 3291N6-malonyllysine; alternateBy similarity
Modified residuei335 – 3351N6-acetyllysine; alternate1 Publication
Modified residuei335 – 3351N6-succinyllysine; alternate1 Publication

Post-translational modificationi

Acetylation is enhanced by up to 67% after treatment either with trichostin A (TCA) or with nicotinamide (NAM) with the appearance of tri-and tetraacetylations. Glucose also increases acetylation by about 60% (By similarity). Acetylation of Lys-239 and Lys-314 is observed in liver mitochondria from fasted mice but not from fed mice.By similarity2 Publications

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

MaxQBiP08249.
PaxDbiP08249.
PRIDEiP08249.

2D gel databases

REPRODUCTION-2DPAGEP08249.
SWISS-2DPAGEP08249.
UCD-2DPAGEP08249.

PTM databases

PhosphoSiteiP08249.

Expressioni

Gene expression databases

BgeeiP08249.
CleanExiMM_MDH2.
ExpressionAtlasiP08249. baseline and differential.
GenevestigatoriP08249.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi201467. 3 interactions.
IntActiP08249. 7 interactions.
MINTiMINT-4101644.

Structurei

3D structure databases

ProteinModelPortaliP08249.
SMRiP08249. Positions 25-337.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LDH/MDH superfamily. MDH type 1 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0039.
GeneTreeiENSGT00390000016686.
HOGENOMiHOG000213792.
HOVERGENiHBG001662.
InParanoidiP08249.
KOiK00026.
OMAiVEVKGFA.
OrthoDBiEOG74R1R7.
PhylomeDBiP08249.
TreeFamiTF300834.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProiIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR001252. Malate_DH_AS.
IPR010097. Malate_DH_type1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11540. PTHR11540. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMiSSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01772. MDH_euk_gproteo. 1 hit.
PROSITEiPS00068. MDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P08249 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLSALARPAG AALRRSFSTS AQNNAKVAVL GASGGIGQPL SLLLKNSPLV
60 70 80 90 100
SRLTLYDIAH TPGVAADLSH IETRANVKGY LGPEQLPDCL KGCDVVVIPA
110 120 130 140 150
GVPRKPGMTR DDLFNTNATI VATLTAACAQ HCPEAMVCII ANPVNSTIPI
160 170 180 190 200
TAEVFKKHGV YNPNKIFGVT TLDIVRANTF VAELKGLDPA RVNVPVIGGH
210 220 230 240 250
AGKTIIPLIS QCTPKVDFPQ DQLATLTGRI QEAGTEVVKA KAGAGSATLS
260 270 280 290 300
MAYAGARFVF SLVDAMNGKE GVVECSFVQS KETECTYFST PLLLGKKGLE
310 320 330
KNLGIGKITP FEEKMIAEAI PELKASIKKG EDFVKNMK
Length:338
Mass (Da):35,611
Last modified:May 1, 2007 - v3
Checksum:i99D13BB2099C19F1
GO

Sequence cautioni

The sequence BAC24986.1 differs from that shown. Reason: Frameshift at position 39.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti76 – 761N → K in AAA39509. (PubMed:3038184)Curated
Sequence conflicti269 – 2691K → L in AAA39509. (PubMed:3038184)Curated
Sequence conflicti269 – 2691K → L in CAA30274. (PubMed:3379635)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M16229 mRNA. Translation: AAA39509.1.
X07295
, X07296, X07297, X07298, X07299, X07300, X07301 Genomic DNA. Translation: CAA30274.1.
AK002305 mRNA. Translation: BAC24986.1. Frameshift.
AK167809 mRNA. Translation: BAE39836.1.
AK160553 mRNA. Translation: BAE35869.1.
AK135162 mRNA. Translation: BAE22447.1.
BC023482 mRNA. Translation: AAH23482.1.
DQ402950 mRNA. Translation: ABD77283.1.
CCDSiCCDS19746.1.
PIRiS01350. DEMSMM.
RefSeqiNP_032643.2. NM_008617.2.
UniGeneiMm.297096.

Genome annotation databases

EnsembliENSMUST00000019323; ENSMUSP00000019323; ENSMUSG00000019179.
GeneIDi17448.
KEGGimmu:17448.
UCSCiuc008zyz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M16229 mRNA. Translation: AAA39509.1 .
X07295
, X07296 , X07297 , X07298 , X07299 , X07300 , X07301 Genomic DNA. Translation: CAA30274.1 .
AK002305 mRNA. Translation: BAC24986.1 . Frameshift.
AK167809 mRNA. Translation: BAE39836.1 .
AK160553 mRNA. Translation: BAE35869.1 .
AK135162 mRNA. Translation: BAE22447.1 .
BC023482 mRNA. Translation: AAH23482.1 .
DQ402950 mRNA. Translation: ABD77283.1 .
CCDSi CCDS19746.1.
PIRi S01350. DEMSMM.
RefSeqi NP_032643.2. NM_008617.2.
UniGenei Mm.297096.

3D structure databases

ProteinModelPortali P08249.
SMRi P08249. Positions 25-337.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201467. 3 interactions.
IntActi P08249. 7 interactions.
MINTi MINT-4101644.

PTM databases

PhosphoSitei P08249.

2D gel databases

REPRODUCTION-2DPAGE P08249.
SWISS-2DPAGE P08249.
UCD-2DPAGE P08249.

Proteomic databases

MaxQBi P08249.
PaxDbi P08249.
PRIDEi P08249.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000019323 ; ENSMUSP00000019323 ; ENSMUSG00000019179 .
GeneIDi 17448.
KEGGi mmu:17448.
UCSCi uc008zyz.1. mouse.

Organism-specific databases

CTDi 4191.
MGIi MGI:97050. Mdh2.

Phylogenomic databases

eggNOGi COG0039.
GeneTreei ENSGT00390000016686.
HOGENOMi HOG000213792.
HOVERGENi HBG001662.
InParanoidi P08249.
KOi K00026.
OMAi VEVKGFA.
OrthoDBi EOG74R1R7.
PhylomeDBi P08249.
TreeFami TF300834.

Miscellaneous databases

ChiTaRSi Mdh2. mouse.
NextBioi 292084.
PROi P08249.
SOURCEi Search...

Gene expression databases

Bgeei P08249.
CleanExi MM_MDH2.
ExpressionAtlasi P08249. baseline and differential.
Genevestigatori P08249.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProi IPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR001252. Malate_DH_AS.
IPR010097. Malate_DH_type1.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PANTHERi PTHR11540. PTHR11540. 1 hit.
Pfami PF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMi SSF56327. SSF56327. 1 hit.
TIGRFAMsi TIGR01772. MDH_euk_gproteo. 1 hit.
PROSITEi PS00068. MDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequence analysis of cDNAs encoding mammalian mitochondrial malate dehydrogenase."
    Joh T., Takeshima H., Tsuzuki T., Shimada K., Tanase S., Morino Y.
    Biochemistry 26:2515-2520(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Structural organization of the mouse mitochondrial malate dehydrogenase gene."
    Takeshima H., Joh T., Tsuzuki T., Shimada K., Matsukado Y.
    J. Mol. Biol. 200:1-11(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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: BALB/c and C57BL/6J.
    Tissue: Cerebellum and Kidney.
  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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  5. "Housekeeping genes for phylogenetic analysis of eutherian relationships."
    Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.
    Mol. Biol. Evol. 23:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-322.
    Tissue: Liver.
  6. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 27-45; 53-74; 79-104; 166-185; 192-239; 242-257; 282-296 AND 308-324, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-239, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-78; LYS-91; LYS-185; LYS-203; LYS-215; LYS-239; LYS-269; LYS-296; LYS-301; LYS-307; LYS-314; LYS-324 AND LYS-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  8. "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-78; LYS-91; LYS-165; LYS-185; LYS-215; LYS-239; LYS-296; LYS-301; LYS-307; LYS-314; LYS-324; LYS-329 AND LYS-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMDHM_MOUSE
AccessioniPrimary (citable) accession number: P08249
Secondary accession number(s): Q0QF44, Q8CF79, Q8R1P0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: May 1, 2007
Last modified: October 29, 2014
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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