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P40925

- MDHC_HUMAN

UniProt

P40925 - MDHC_HUMAN

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Protein
Malate dehydrogenase, cytoplasmic
Gene
MDH1, MDHA
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.1 Publication
3-(3,5-diiodo-4-hydroxyphenyl)lactate + NAD+ = 3-(3,5-diiodo-4-hydroxyphenyl)pyruvate + NADH.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei92 – 921Substrate By similarity
Binding sitei98 – 981Substrate By similarity
Binding sitei105 – 1051NAD By similarity
Binding sitei112 – 1121NAD By similarity
Binding sitei131 – 1311Substrate By similarity
Binding sitei162 – 1621Substrate
Active sitei187 – 1871Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 177NAD By similarity
Nucleotide bindingi129 – 1313NAD By similarity

GO - Molecular functioni

  1. L-malate dehydrogenase activity Source: Reactome
  2. NAD binding Source: Ensembl
  3. diiodophenylpyruvate reductase activity Source: UniProtKB-EC
  4. malic enzyme activity Source: ProtInc
Complete GO annotation...

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:HS00361-MONOMER.
ReactomeiREACT_1520. Gluconeogenesis.
SABIO-RKP40925.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase, cytoplasmic (EC:1.1.1.37)
Alternative name(s):
Cytosolic malate dehydrogenase
Diiodophenylpyruvate reductase (EC:1.1.1.96)
Gene namesi
Name:MDH1
Synonyms:MDHA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:6970. MDH1.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. centrosome Source: HPA
  2. cytoplasm Source: HPA
  3. cytosol Source: Reactome
  4. extracellular space Source: UniProt
  5. extracellular vesicular exosome Source: UniProt
  6. mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30714.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 334333Malate dehydrogenase, cytoplasmicUniRule annotation
PRO_0000113409Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei110 – 1101N6-succinyllysine By similarity
Modified residuei118 – 1181N6-acetyllysine2 Publications
Modified residuei121 – 1211N6-acetyllysine1 Publication
Modified residuei214 – 2141N6-succinyllysine By similarity
Modified residuei298 – 2981N6-acetyllysine; alternate2 Publications
Modified residuei298 – 2981N6-succinyllysine; alternate By similarity
Modified residuei318 – 3181N6-succinyllysine By similarity
Modified residuei333 – 3331Phosphoserine1 Publication

Post-translational modificationi

ISGylated.1 Publication
Acetylation at Lys-118 dramatically enhances enzymatic activity and promotes adipogenic differentiation.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP40925.
PaxDbiP40925.
PeptideAtlasiP40925.
PRIDEiP40925.

2D gel databases

REPRODUCTION-2DPAGEIPI00291005.
UCD-2DPAGEP40925.

PTM databases

PhosphoSiteiP40925.

Expressioni

Gene expression databases

ArrayExpressiP40925.
BgeeiP40925.
CleanExiHS_MDH1.
GenevestigatoriP40925.

Organism-specific databases

HPAiCAB047333.
HPA027296.
HPA054276.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi110355. 21 interactions.
IntActiP40925. 5 interactions.
MINTiMINT-4999585.
STRINGi9606.ENSP00000233114.

Structurei

3D structure databases

ProteinModelPortaliP40925.
SMRiP40925. Positions 2-334.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0039.
HOVERGENiHBG006340.
InParanoidiP40925.
KOiK00025.
OMAiNCLIASK.
OrthoDBiEOG78H3TM.
PhylomeDBiP40925.
TreeFamiTF105826.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_01517. Malate_dehydrog_2.
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.
IPR011274. Malate_DH_NAD-dep_euk.
IPR010945. Malate_DH_type2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR23382. PTHR23382. 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.
TIGRFAMsiTIGR01759. MalateDH-SF1. 1 hit.
TIGR01758. MDH_euk_cyt. 1 hit.
PROSITEiPS00068. MDH. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P40925-1) [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

MSEPIRVLVT GAAGQIAYSL LYSIGNGSVF GKDQPIILVL LDITPMMGVL    50
DGVLMELQDC ALPLLKDVIA TDKEDVAFKD LDVAILVGSM PRREGMERKD 100
LLKANVKIFK SQGAALDKYA KKSVKVIVVG NPANTNCLTA SKSAPSIPKE 150
NFSCLTRLDH NRAKAQIALK LGVTANDVKN VIIWGNHSST QYPDVNHAKV 200
KLQGKEVGVY EALKDDSWLK GEFVTTVQQR GAAVIKARKL SSAMSAAKAI 250
CDHVRDIWFG TPEGEFVSMG VISDGNSYGV PDDLLYSFPV VIKNKTWKFV 300
EGLPINDFSR EKMDLTAKEL TEEKESAFEF LSSA 334
Length:334
Mass (Da):36,426
Last modified:January 23, 2007 - v4
Checksum:i5F7ED9789CA1DB55
GO
Isoform 2 (identifier: P40925-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-89: Missing.

Show »
Length:245
Mass (Da):27,025
Checksum:iDEBC412374575BD9
GO
Isoform 3 (identifier: P40925-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRRCSYFPKDVTVFDKDDK

Note: No experimental confirmation available.

Show »
Length:352
Mass (Da):38,628
Checksum:i058B25735B30BBC2
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8989Missing in isoform 2.
VSP_042661Add
BLAST
Alternative sequencei1 – 11M → MRRCSYFPKDVTVFDKDDK in isoform 3.
VSP_045847

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151Q → R in BAH12223. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D55654 mRNA. Translation: BAA09513.1.
U20352 mRNA. Translation: AAC16436.1.
CR457405 mRNA. Translation: CAG33686.1.
AK295931 mRNA. Translation: BAH12223.1.
AK300719 mRNA. Translation: BAG62394.1.
AK312331 mRNA. Translation: BAG35252.1.
AC016734 Genomic DNA. Translation: AAY14893.1.
CH471053 Genomic DNA. Translation: EAW99959.1.
BC001484 mRNA. Translation: AAH01484.1.
CCDSiCCDS1874.1. [P40925-1]
CCDS56121.1. [P40925-3]
CCDS56122.1. [P40925-2]
PIRiG01650.
RefSeqiNP_001186040.1. NM_001199111.1. [P40925-3]
NP_001186041.1. NM_001199112.1. [P40925-2]
NP_005908.1. NM_005917.3. [P40925-1]
XP_005264377.1. XM_005264320.1. [P40925-2]
UniGeneiHs.526521.

Genome annotation databases

EnsembliENST00000233114; ENSP00000233114; ENSG00000014641. [P40925-1]
ENST00000394423; ENSP00000377945; ENSG00000014641. [P40925-1]
ENST00000539945; ENSP00000438144; ENSG00000014641. [P40925-3]
ENST00000544381; ENSP00000446395; ENSG00000014641. [P40925-2]
GeneIDi4190.
KEGGihsa:4190.
UCSCiuc002scj.2. human. [P40925-1]

Polymorphism databases

DMDMi1708967.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Wikipedia

Malate dehydrogenase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D55654 mRNA. Translation: BAA09513.1 .
U20352 mRNA. Translation: AAC16436.1 .
CR457405 mRNA. Translation: CAG33686.1 .
AK295931 mRNA. Translation: BAH12223.1 .
AK300719 mRNA. Translation: BAG62394.1 .
AK312331 mRNA. Translation: BAG35252.1 .
AC016734 Genomic DNA. Translation: AAY14893.1 .
CH471053 Genomic DNA. Translation: EAW99959.1 .
BC001484 mRNA. Translation: AAH01484.1 .
CCDSi CCDS1874.1. [P40925-1 ]
CCDS56121.1. [P40925-3 ]
CCDS56122.1. [P40925-2 ]
PIRi G01650.
RefSeqi NP_001186040.1. NM_001199111.1. [P40925-3 ]
NP_001186041.1. NM_001199112.1. [P40925-2 ]
NP_005908.1. NM_005917.3. [P40925-1 ]
XP_005264377.1. XM_005264320.1. [P40925-2 ]
UniGenei Hs.526521.

3D structure databases

ProteinModelPortali P40925.
SMRi P40925. Positions 2-334.
ModBasei Search...

Protein-protein interaction databases

BioGridi 110355. 21 interactions.
IntActi P40925. 5 interactions.
MINTi MINT-4999585.
STRINGi 9606.ENSP00000233114.

Chemistry

BindingDBi P40925.
ChEMBLi CHEMBL3560.
DrugBanki DB00157. NADH.

PTM databases

PhosphoSitei P40925.

Polymorphism databases

DMDMi 1708967.

2D gel databases

REPRODUCTION-2DPAGE IPI00291005.
UCD-2DPAGE P40925.

Proteomic databases

MaxQBi P40925.
PaxDbi P40925.
PeptideAtlasi P40925.
PRIDEi P40925.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000233114 ; ENSP00000233114 ; ENSG00000014641 . [P40925-1 ]
ENST00000394423 ; ENSP00000377945 ; ENSG00000014641 . [P40925-1 ]
ENST00000539945 ; ENSP00000438144 ; ENSG00000014641 . [P40925-3 ]
ENST00000544381 ; ENSP00000446395 ; ENSG00000014641 . [P40925-2 ]
GeneIDi 4190.
KEGGi hsa:4190.
UCSCi uc002scj.2. human. [P40925-1 ]

Organism-specific databases

CTDi 4190.
GeneCardsi GC02P063727.
HGNCi HGNC:6970. MDH1.
HPAi CAB047333.
HPA027296.
HPA054276.
MIMi 154200. gene.
neXtProti NX_P40925.
PharmGKBi PA30714.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0039.
HOVERGENi HBG006340.
InParanoidi P40925.
KOi K00025.
OMAi NCLIASK.
OrthoDBi EOG78H3TM.
PhylomeDBi P40925.
TreeFami TF105826.

Enzyme and pathway databases

BioCyci MetaCyc:HS00361-MONOMER.
Reactomei REACT_1520. Gluconeogenesis.
SABIO-RK P40925.

Miscellaneous databases

ChiTaRSi MDH1. human.
GenomeRNAii 4190.
NextBioi 16510.
PROi P40925.
SOURCEi Search...

Gene expression databases

ArrayExpressi P40925.
Bgeei P40925.
CleanExi HS_MDH1.
Genevestigatori P40925.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPi MF_01517. Malate_dehydrog_2.
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.
IPR011274. Malate_DH_NAD-dep_euk.
IPR010945. Malate_DH_type2.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PANTHERi PTHR23382. PTHR23382. 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 TIGR01759. MalateDH-SF1. 1 hit.
TIGR01758. MDH_euk_cyt. 1 hit.
PROSITEi PS00068. MDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and mapping of a human cDNA for cytosolic malate dehydrogenase (MDH1)."
    Tanaka T., Inazawa J., Nakamura Y.
    Genomics 32:128-130(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Heart.
  2. Lo A.S.Y., Waye M.M.Y.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Heart.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "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; 2 AND 3).
    Tissue: Cerebellum and Substantia nigra.
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Placenta.
  8. Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
    Submitted (MAY-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-18; 205-213 AND 324-334, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: T-cell.
  9. "The human myocardial two-dimensional gel protein database: update 1994."
    Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.
    Electrophoresis 15:1459-1465(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 168-181.
    Tissue: Heart.
  10. Lubec G., Vishwanath V.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 180-201 AND 299-310, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  11. "Biochemical and genetic identity of alpha-keto acid reductase and cytoplasmic malate dehydrogenase from human erythrocytes."
    Friedrich C.A., Ferrell R.E., Siciliano M.J., Kitto G.B.
    Ann. Hum. Genet. 52:25-37(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
  12. Cited for: ISGYLATION.
  13. "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-118 AND LYS-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Acetylation of malate dehydrogenase 1 promotes adipogenic differentiation via activating its enzymatic activity."
    Kim E.Y., Kim W.K., Kang H.J., Kim J.H., Chung S.J., Seo Y.S., Park S.G., Lee S.C., Bae K.H.
    J. Lipid Res. 53:1864-1876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-118; LYS-121 AND LYS-298.

Entry informationi

Entry nameiMDHC_HUMAN
AccessioniPrimary (citable) accession number: P40925
Secondary accession number(s): B2R5V5
, B4DUN2, B7Z3I7, F5H098, Q6I9V0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 153 of the entry and version 4 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi