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P40926

- MDHM_HUMAN

UniProt

P40926 - MDHM_HUMAN

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Protein

Malate dehydrogenase, mitochondrial

Gene
MDH2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-malate + NAD+ = oxaloacetate + NADH.

Enzyme regulationi

Enzyme activity is enhanced by acetylation.1 Publication

Sites

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

Regions

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

GO - Molecular functioni

  1. L-malate dehydrogenase activity Source: UniProtKB
  2. malate dehydrogenase (NADP+) activity Source: Ensembl
  3. oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: InterPro
  4. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. cellular carbohydrate metabolic process Source: InterPro
  3. cellular metabolic process Source: Reactome
  4. gluconeogenesis Source: Reactome
  5. glucose metabolic process Source: Reactome
  6. internal protein amino acid acetylation Source: UniProtKB
  7. malate metabolic process Source: UniProtKB
  8. NADH metabolic process Source: Ensembl
  9. oxaloacetate metabolic process Source: Ensembl
  10. small molecule metabolic process Source: Reactome
  11. tricarboxylic acid cycle Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:HS07366-MONOMER.
ReactomeiREACT_1520. Gluconeogenesis.
REACT_1785. Citric acid cycle (TCA cycle).

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase, mitochondrial (EC:1.1.1.37)
Gene namesi
Name:MDH2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:6971. MDH2.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi185 – 1851K → R: No activation of enzyme activity on treatment with TSA or NAM; when associated with R-301; R-307 and R-314. 1 Publication
Mutagenesisi301 – 3011K → R: No activation of enzyme activity on treatment with TSA or NAM; when associated with R-185; R-307 and R-314. 1 Publication
Mutagenesisi307 – 3071K → R: No activation of enzyme activity on treatment with TSA or NAM; when associated with R-185; R-301 and R-314. 1 Publication
Mutagenesisi314 – 3141K → R: No activation of enzyme activity on treatment with TSA or NAM; when associated with R-185; R-301 and R-307. 1 Publication

Organism-specific databases

PharmGKBiPA30716.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2424Mitochondrion By similarityAdd
BLAST
Chaini25 – 338314Malate dehydrogenase, mitochondrialPRO_0000018628Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Acetylation is enhanced by up to 67% after treatment either with trichostin A (TSA) or with nicotinamide (NAM) with the appearance of tri-and tetraacetylations. Glucose also increases acetylation by about 60% By similarity.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

MaxQBiP40926.
PaxDbiP40926.
PRIDEiP40926.

2D gel databases

DOSAC-COBS-2DPAGEP40926.
REPRODUCTION-2DPAGEIPI00291006.
P40926.
UCD-2DPAGEP40926.

PTM databases

PhosphoSiteiP40926.

Expressioni

Gene expression databases

ArrayExpressiP40926.
BgeeiP40926.
CleanExiHS_MDH2.
GenevestigatoriP40926.

Organism-specific databases

HPAiHPA019714.
HPA019716.
HPA019848.
HPA026720.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi110356. 28 interactions.
IntActiP40926. 12 interactions.
MINTiMINT-1408946.
STRINGi9606.ENSP00000327070.

Structurei

Secondary structure

1
338
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 306
Turni31 – 333
Helixi37 – 459
Beta strandi50 – 6011
Helixi61 – 699
Beta strandi71 – 744
Beta strandi76 – 827
Turni83 – 853
Helixi86 – 905
Beta strandi94 – 985
Helixi110 – 1134
Helixi114 – 13118
Beta strandi135 – 1395
Helixi144 – 15714
Beta strandi165 – 1684
Helixi171 – 18515
Helixi189 – 1913
Beta strandi196 – 1983
Helixi202 – 2043
Beta strandi205 – 2073
Helixi209 – 2113
Helixi220 – 24122
Helixi249 – 26618
Beta strandi273 – 2797
Beta strandi282 – 29514
Beta strandi298 – 3025
Helixi310 – 33526

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DFDX-ray1.90A/B/C/D20-338[»]
ProteinModelPortaliP40926.
SMRiP40926. Positions 24-337.

Miscellaneous databases

EvolutionaryTraceiP40926.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0039.
HOGENOMiHOG000213792.
HOVERGENiHBG001662.
InParanoidiP40926.
KOiK00026.
OMAiMVAEAMS.
OrthoDBiEOG74R1R7.
PhylomeDBiP40926.
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]

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: P40926-1) [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

MLSALARPAS AALRRSFSTS AQNNAKVAVL GASGGIGQPL SLLLKNSPLV    50
SRLTLYDIAH TPGVAADLSH IETKAAVKGY LGPEQLPDCL KGCDVVVIPA 100
GVPRKPGMTR DDLFNTNATI VATLTAACAQ HCPEAMICVI ANPVNSTIPI 150
TAEVFKKHGV YNPNKIFGVT TLDIVRANTF VAELKGLDPA RVNVPVIGGH 200
AGKTIIPLIS QCTPKVDFPQ DQLTALTGRI QEAGTEVVKA KAGAGSATLS 250
MAYAGARFVF SLVDAMNGKE GVVECSFVKS QETECTYFST PLLLGKKGIE 300
KNLGIGKVSS FEEKMISDAI PELKASIKKG EDFVKTLK 338
Length:338
Mass (Da):35,503
Last modified:November 25, 2008 - v3
Checksum:iAAB9F5E5B2FBC8CA
GO
Isoform 2 (identifier: P40926-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     144-185: Missing.

Note: No experimental confirmation available.

Show »
Length:296
Mass (Da):30,875
Checksum:i309B55235F0097F7
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91A → V.2 Publications
Corresponds to variant rs17849553 [ dbSNP | Ensembl ].
VAR_047787

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei144 – 18542Missing in isoform 2. VSP_055312Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti301 – 3011K → R in BAG56955. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF047470 mRNA. Translation: AAC03787.1.
AK290779 mRNA. Translation: BAF83468.1.
AK293460 mRNA. Translation: BAG56955.1.
AK316587 mRNA. Translation: BAG38175.1.
AC005077 Genomic DNA. No translation available.
AC006330 Genomic DNA. No translation available.
CH471220 Genomic DNA. Translation: EAW71796.1.
BC001917 mRNA. Translation: AAH01917.1.
CCDSiCCDS5581.1. [P40926-1]
RefSeqiNP_001269332.1. NM_001282403.1.
NP_001269333.1. NM_001282404.1.
NP_005909.2. NM_005918.3.
UniGeneiHs.520967.

Genome annotation databases

EnsembliENST00000315758; ENSP00000327070; ENSG00000146701.
ENST00000432020; ENSP00000408649; ENSG00000146701.
ENST00000573193; ENSP00000459911; ENSG00000262847.
GeneIDi4191.
KEGGihsa:4191.
UCSCiuc003ueo.3. human. [P40926-1]

Polymorphism databases

DMDMi215274114.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Malate dehydrogenase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF047470 mRNA. Translation: AAC03787.1 .
AK290779 mRNA. Translation: BAF83468.1 .
AK293460 mRNA. Translation: BAG56955.1 .
AK316587 mRNA. Translation: BAG38175.1 .
AC005077 Genomic DNA. No translation available.
AC006330 Genomic DNA. No translation available.
CH471220 Genomic DNA. Translation: EAW71796.1 .
BC001917 mRNA. Translation: AAH01917.1 .
CCDSi CCDS5581.1. [P40926-1 ]
RefSeqi NP_001269332.1. NM_001282403.1.
NP_001269333.1. NM_001282404.1.
NP_005909.2. NM_005918.3.
UniGenei Hs.520967.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DFD X-ray 1.90 A/B/C/D 20-338 [» ]
ProteinModelPortali P40926.
SMRi P40926. Positions 24-337.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110356. 28 interactions.
IntActi P40926. 12 interactions.
MINTi MINT-1408946.
STRINGi 9606.ENSP00000327070.

Chemistry

BindingDBi P40926.
ChEMBLi CHEMBL5917.
DrugBanki DB00157. NADH.

PTM databases

PhosphoSitei P40926.

Polymorphism databases

DMDMi 215274114.

2D gel databases

DOSAC-COBS-2DPAGE P40926.
REPRODUCTION-2DPAGE IPI00291006.
P40926.
UCD-2DPAGE P40926.

Proteomic databases

MaxQBi P40926.
PaxDbi P40926.
PRIDEi P40926.

Protocols and materials databases

DNASUi 4191.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000315758 ; ENSP00000327070 ; ENSG00000146701 .
ENST00000432020 ; ENSP00000408649 ; ENSG00000146701 .
ENST00000573193 ; ENSP00000459911 ; ENSG00000262847 .
GeneIDi 4191.
KEGGi hsa:4191.
UCSCi uc003ueo.3. human. [P40926-1 ]

Organism-specific databases

CTDi 4191.
GeneCardsi GC07P075677.
HGNCi HGNC:6971. MDH2.
HPAi HPA019714.
HPA019716.
HPA019848.
HPA026720.
MIMi 154100. gene.
neXtProti NX_P40926.
PharmGKBi PA30716.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0039.
HOGENOMi HOG000213792.
HOVERGENi HBG001662.
InParanoidi P40926.
KOi K00026.
OMAi MVAEAMS.
OrthoDBi EOG74R1R7.
PhylomeDBi P40926.
TreeFami TF300834.

Enzyme and pathway databases

BioCyci MetaCyc:HS07366-MONOMER.
Reactomei REACT_1520. Gluconeogenesis.
REACT_1785. Citric acid cycle (TCA cycle).

Miscellaneous databases

ChiTaRSi Mdh2. human.
EvolutionaryTracei P40926.
GeneWikii Malate_dehydrogenase_2.
GenomeRNAii 4191.
NextBioi 16514.
PROi P40926.
SOURCEi Search...

Gene expression databases

ArrayExpressi P40926.
Bgeei P40926.
CleanExi HS_MDH2.
Genevestigatori P40926.

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. "Human homolog of mouse and pig MDH mRNA."
    Hu G.
    Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-9.
  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: Kidney and Tongue.
  3. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [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), VARIANT VAL-9.
    Tissue: Lung.
  6. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "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-165; LYS-185; LYS-301; LYS-314; LYS-329 AND LYS-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: ACETYLATION AT LYS-185; LYS-301; LYS-307 AND LYS-314, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF LYS-185; LYS-301; LYS-307 AND LYS-314.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: MALONYLATION AT LYS-307.
  12. "Crystal structure of human malate dehydrogenase type 2."
    Structural genomics consortium (SGC)
    Submitted (MAR-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 20-338 IN COMPLEX WITH NAD AND SUBSTRATE, SUBUNIT.

Entry informationi

Entry nameiMDHM_HUMAN
AccessioniPrimary (citable) accession number: P40926
Secondary accession number(s): A8K414
, B2RE78, B4DE44, E9PDB2, O43682
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 25, 2008
Last modified: September 3, 2014
This is version 155 of the entry and version 3 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 7
    Human chromosome 7: 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

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