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Q00266

- METK1_HUMAN

UniProt

Q00266 - METK1_HUMAN

Protein

S-adenosylmethionine synthase isoform type-1

Gene

MAT1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 2 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    Catalyzes the formation of S-adenosylmethionine from methionine and ATP.

    Catalytic activityi

    ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine.

    Cofactori

    Binds 2 divalent ions per subunit. Magnesium or cobalt By similarity.By similarity
    Binds 1 potassium ion per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei29 – 291Substrate1 Publication
    Metal bindingi31 – 311MagnesiumBy similarity
    Metal bindingi57 – 571PotassiumBy similarity
    Binding sitei159 – 1591ATPSequence Analysis
    Binding sitei179 – 1791Substrate1 Publication
    Binding sitei247 – 2471Substrate1 Publication
    Binding sitei249 – 2491Substrate; via carbonyl oxygen1 Publication
    Binding sitei258 – 2581Substrate1 Publication
    Metal bindingi283 – 2831PotassiumBy similarity
    Metal bindingi291 – 2911MagnesiumBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi131 – 1366ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. methionine adenosyltransferase activity Source: ProtInc

    GO - Biological processi

    1. cellular amino acid metabolic process Source: ProtInc
    2. cellular nitrogen compound metabolic process Source: Reactome
    3. methylation Source: Reactome
    4. one-carbon metabolic process Source: UniProtKB-KW
    5. S-adenosylmethionine biosynthetic process Source: UniProtKB-UniPathway
    6. small molecule metabolic process Source: Reactome
    7. sulfur amino acid metabolic process Source: Reactome
    8. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    One-carbon metabolism

    Keywords - Ligandi

    ATP-binding, Cobalt, Magnesium, Metal-binding, Nucleotide-binding, Potassium

    Enzyme and pathway databases

    ReactomeiREACT_115639. Sulfur amino acid metabolism.
    REACT_6946. Methylation.
    UniPathwayiUPA00315; UER00080.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    S-adenosylmethionine synthase isoform type-1 (EC:2.5.1.6)
    Short name:
    AdoMet synthase 1
    Alternative name(s):
    Methionine adenosyltransferase 1
    Short name:
    MAT 1
    Methionine adenosyltransferase I/III
    Short name:
    MAT-I/III
    Gene namesi
    Name:MAT1A
    Synonyms:AMS1, MATA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:6903. MAT1A.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Involvement in diseasei

    Methionine adenosyltransferase deficiency (MATD) [MIM:250850]: An inborn error of metabolism resulting in isolated hypermethioninemia. Most patients have no clinical abnormalities, although some neurologic symptoms may be present in rare cases with severe loss of methionine adenosyltransferase activity.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti38 – 381S → N in MATD; abolishes enzyme activity. 1 Publication
    VAR_031242
    Natural varianti55 – 551A → D in MATD. 1 Publication
    VAR_006935
    Natural varianti199 – 1991R → C in MATD; retains 11% of wild-type activity. 1 Publication
    VAR_006936
    Natural varianti264 – 2641R → C in MATD; has virtually no enzymatic activity. 1 Publication
    VAR_031243
    Natural varianti264 – 2641R → H in MATD; dominant mutation. 2 Publications
    VAR_006937
    Natural varianti305 – 3051L → P in MATD. 1 Publication
    VAR_006938
    Natural varianti322 – 3221I → M in MATD; diminishes but do not completely abolishes enzyme activity; 46% of the level of the wild-type enzyme. 2 Publications
    VAR_006939
    Natural varianti336 – 3361G → R in MATD; retains significant enzymatic activity; 23% of the level of the wild-type enzyme. 1 Publication
    VAR_031244
    Natural varianti344 – 3441E → A in MATD; diminishes but do not completely abolishes enzyme activity; 12% of the level of the wild-type enzyme. 1 Publication
    VAR_031245
    Natural varianti356 – 3561R → Q in MATD. 1 Publication
    Corresponds to variant rs138742870 [ dbSNP | Ensembl ].
    VAR_006940
    Natural varianti357 – 3571P → L in MATD. 1 Publication
    VAR_006941
    Natural varianti378 – 3781G → S in MATD. 1 Publication
    VAR_006942

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi250850. phenotype.
    Orphaneti168598. Brain demyelination due to methionine adenosyltransferase deficiency.
    PharmGKBiPA30646.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 395395S-adenosylmethionine synthase isoform type-1PRO_0000174432Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi34 ↔ 60By similarity
    Modified residuei120 – 1201S-nitrosocysteineBy similarity

    Post-translational modificationi

    S-nitrosylation of Cys-120 inactivates the enzyme.By similarity

    Keywords - PTMi

    Disulfide bond, S-nitrosylation

    Proteomic databases

    MaxQBiQ00266.
    PaxDbiQ00266.
    PRIDEiQ00266.

    PTM databases

    PhosphoSiteiQ00266.

    Expressioni

    Tissue specificityi

    Expressed in liver.

    Gene expression databases

    ArrayExpressiQ00266.
    BgeeiQ00266.
    CleanExiHS_MAT1A.
    GenevestigatoriQ00266.

    Organism-specific databases

    HPAiHPA048627.

    Interactioni

    Subunit structurei

    Homotetramer (MAT-I) or homodimer (MAT-III).1 Publication

    Protein-protein interaction databases

    BioGridi110313. 4 interactions.
    STRINGi9606.ENSP00000361287.

    Structurei

    Secondary structure

    1
    395
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi18 – 258
    Helixi30 – 4819
    Beta strandi53 – 619
    Beta strandi64 – 729
    Helixi79 – 9012
    Helixi95 – 973
    Turni101 – 1033
    Beta strandi105 – 1117
    Helixi115 – 1217
    Turni122 – 1243
    Helixi127 – 1293
    Beta strandi132 – 1343
    Beta strandi136 – 1438
    Helixi152 – 17019
    Beta strandi171 – 1733
    Beta strandi176 – 19116
    Beta strandi194 – 20916
    Beta strandi211 – 2133
    Helixi215 – 22410
    Helixi227 – 2304
    Helixi233 – 2353
    Beta strandi241 – 2455
    Helixi254 – 2563
    Turni266 – 2738
    Helixi290 – 30718
    Beta strandi312 – 3209
    Beta strandi328 – 3336
    Helixi342 – 35211
    Helixi357 – 3637
    Turni364 – 3674
    Helixi371 – 3744
    Beta strandi375 – 3773
    Beta strandi379 – 3813
    Helixi386 – 3883

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2OBVX-ray2.05A16-395[»]
    ProteinModelPortaliQ00266.
    SMRiQ00266. Positions 14-395.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ00266.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AdoMet synthase family.Curated

    Phylogenomic databases

    eggNOGiCOG0192.
    HOGENOMiHOG000245710.
    HOVERGENiHBG001562.
    InParanoidiQ00266.
    KOiK00789.
    OMAiHEAVREQ.
    OrthoDBiEOG7TF79H.
    PhylomeDBiQ00266.
    TreeFamiTF300511.

    Family and domain databases

    HAMAPiMF_00086. S_AdoMet_synth1.
    InterProiIPR022631. ADOMET_SYNTHASE_CS.
    IPR022630. S-AdoMet_synt_C.
    IPR022629. S-AdoMet_synt_central.
    IPR022628. S-AdoMet_synt_N.
    IPR002133. S-AdoMet_synthetase.
    IPR022636. S-AdoMet_synthetase_sfam.
    [Graphical view]
    PANTHERiPTHR11964. PTHR11964. 1 hit.
    PfamiPF02773. S-AdoMet_synt_C. 1 hit.
    PF02772. S-AdoMet_synt_M. 1 hit.
    PF00438. S-AdoMet_synt_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000497. MAT. 1 hit.
    SUPFAMiSSF55973. SSF55973. 3 hits.
    TIGRFAMsiTIGR01034. metK. 1 hit.
    PROSITEiPS00376. ADOMET_SYNTHASE_1. 1 hit.
    PS00377. ADOMET_SYNTHASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q00266-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNGPVDGLCD HSLSEGVFMF TSESVGEGHP DKICDQISDA VLDAHLKQDP    50
    NAKVACETVC KTGMVLLCGE ITSMAMVDYQ RVVRDTIKHI GYDDSAKGFD 100
    FKTCNVLVAL EQQSPDIAQC VHLDRNEEDV GAGDQGLMFG YATDETEECM 150
    PLTIILAHKL NARMADLRRS GLLPWLRPDS KTQVTVQYMQ DNGAVIPVRI 200
    HTIVISVQHN EDITLEEMRR ALKEQVIRAV VPAKYLDEDT VYHLQPSGRF 250
    VIGGPQGDAG VTGRKIIVDT YGGWGAHGGG AFSGKDYTKV DRSAAYAARW 300
    VAKSLVKAGL CRRVLVQVSY AIGVAEPLSI SIFTYGTSQK TERELLDVVH 350
    KNFDLRPGVI VRDLDLKKPI YQKTACYGHF GRSEFPWEVP RKLVF 395
    Length:395
    Mass (Da):43,648
    Last modified:October 1, 1993 - v2
    Checksum:iB3462A5670A5B0D4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti272 – 2732GG → AA in BAA08355. (PubMed:1772450)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti38 – 381S → N in MATD; abolishes enzyme activity. 1 Publication
    VAR_031242
    Natural varianti55 – 551A → D in MATD. 1 Publication
    VAR_006935
    Natural varianti119 – 1191Q → H.
    Corresponds to variant rs1143693 [ dbSNP | Ensembl ].
    VAR_028944
    Natural varianti199 – 1991R → C in MATD; retains 11% of wild-type activity. 1 Publication
    VAR_006936
    Natural varianti264 – 2641R → C in MATD; has virtually no enzymatic activity. 1 Publication
    VAR_031243
    Natural varianti264 – 2641R → H in MATD; dominant mutation. 2 Publications
    VAR_006937
    Natural varianti305 – 3051L → P in MATD. 1 Publication
    VAR_006938
    Natural varianti322 – 3221I → M in MATD; diminishes but do not completely abolishes enzyme activity; 46% of the level of the wild-type enzyme. 2 Publications
    VAR_006939
    Natural varianti336 – 3361G → R in MATD; retains significant enzymatic activity; 23% of the level of the wild-type enzyme. 1 Publication
    VAR_031244
    Natural varianti344 – 3441E → A in MATD; diminishes but do not completely abolishes enzyme activity; 12% of the level of the wild-type enzyme. 1 Publication
    VAR_031245
    Natural varianti356 – 3561R → Q in MATD. 1 Publication
    Corresponds to variant rs138742870 [ dbSNP | Ensembl ].
    VAR_006940
    Natural varianti357 – 3571P → L in MATD. 1 Publication
    VAR_006941
    Natural varianti378 – 3781G → S in MATD. 1 Publication
    VAR_006942

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D49357 mRNA. Translation: BAA08355.1.
    X69078 mRNA. Translation: CAA48822.1.
    AL359195 Genomic DNA. Translation: CAI13695.1.
    CH471142 Genomic DNA. Translation: EAW80396.1.
    CH471142 Genomic DNA. Translation: EAW80397.1.
    BC018359 mRNA. Translation: AAH18359.1.
    CCDSiCCDS7365.1.
    PIRiS27363.
    RefSeqiNP_000420.1. NM_000429.2.
    XP_005269899.1. XM_005269842.2.
    UniGeneiHs.282670.

    Genome annotation databases

    EnsembliENST00000372213; ENSP00000361287; ENSG00000151224.
    GeneIDi4143.
    KEGGihsa:4143.
    UCSCiuc001kbw.3. human.

    Polymorphism databases

    DMDMi417297.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D49357 mRNA. Translation: BAA08355.1 .
    X69078 mRNA. Translation: CAA48822.1 .
    AL359195 Genomic DNA. Translation: CAI13695.1 .
    CH471142 Genomic DNA. Translation: EAW80396.1 .
    CH471142 Genomic DNA. Translation: EAW80397.1 .
    BC018359 mRNA. Translation: AAH18359.1 .
    CCDSi CCDS7365.1.
    PIRi S27363.
    RefSeqi NP_000420.1. NM_000429.2.
    XP_005269899.1. XM_005269842.2.
    UniGenei Hs.282670.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2OBV X-ray 2.05 A 16-395 [» ]
    ProteinModelPortali Q00266.
    SMRi Q00266. Positions 14-395.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110313. 4 interactions.
    STRINGi 9606.ENSP00000361287.

    Chemistry

    DrugBanki DB00134. L-Methionine.
    DB00118. S-Adenosylmethionine.

    PTM databases

    PhosphoSitei Q00266.

    Polymorphism databases

    DMDMi 417297.

    Proteomic databases

    MaxQBi Q00266.
    PaxDbi Q00266.
    PRIDEi Q00266.

    Protocols and materials databases

    DNASUi 4143.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000372213 ; ENSP00000361287 ; ENSG00000151224 .
    GeneIDi 4143.
    KEGGi hsa:4143.
    UCSCi uc001kbw.3. human.

    Organism-specific databases

    CTDi 4143.
    GeneCardsi GC10M082021.
    HGNCi HGNC:6903. MAT1A.
    HPAi HPA048627.
    MIMi 250850. phenotype.
    610550. gene.
    neXtProti NX_Q00266.
    Orphaneti 168598. Brain demyelination due to methionine adenosyltransferase deficiency.
    PharmGKBi PA30646.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0192.
    HOGENOMi HOG000245710.
    HOVERGENi HBG001562.
    InParanoidi Q00266.
    KOi K00789.
    OMAi HEAVREQ.
    OrthoDBi EOG7TF79H.
    PhylomeDBi Q00266.
    TreeFami TF300511.

    Enzyme and pathway databases

    UniPathwayi UPA00315 ; UER00080 .
    Reactomei REACT_115639. Sulfur amino acid metabolism.
    REACT_6946. Methylation.

    Miscellaneous databases

    EvolutionaryTracei Q00266.
    GenomeRNAii 4143.
    NextBioi 16272.
    PROi Q00266.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q00266.
    Bgeei Q00266.
    CleanExi HS_MAT1A.
    Genevestigatori Q00266.

    Family and domain databases

    HAMAPi MF_00086. S_AdoMet_synth1.
    InterProi IPR022631. ADOMET_SYNTHASE_CS.
    IPR022630. S-AdoMet_synt_C.
    IPR022629. S-AdoMet_synt_central.
    IPR022628. S-AdoMet_synt_N.
    IPR002133. S-AdoMet_synthetase.
    IPR022636. S-AdoMet_synthetase_sfam.
    [Graphical view ]
    PANTHERi PTHR11964. PTHR11964. 1 hit.
    Pfami PF02773. S-AdoMet_synt_C. 1 hit.
    PF02772. S-AdoMet_synt_M. 1 hit.
    PF00438. S-AdoMet_synt_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000497. MAT. 1 hit.
    SUPFAMi SSF55973. SSF55973. 3 hits.
    TIGRFAMsi TIGR01034. metK. 1 hit.
    PROSITEi PS00376. ADOMET_SYNTHASE_1. 1 hit.
    PS00377. ADOMET_SYNTHASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of a full-length cDNA encoding human liver S-adenosylmethionine synthetase: tissue-specific gene expression and mRNA levels in hepatopathies."
      Alvarez L., Corrales F., Mato J.M.
      Biochem. J. 293:481-486(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Molecular cloning and nucleotide sequence of cDNA encoding the human liver S-adenosylmethionine synthetase."
      Horikawa S., Tsukada K.
      Biochem. Int. 25:81-90(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    3. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [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].
      Tissue: Lymph.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Crystal structure of the human s-adenosylmethionine synthetase 1 in complex with the product."
      Structural genomics consortium (SGC)
      Submitted (JUL-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 14-395 IN COMPLEX WITH SUBSTRATE.
    8. "Molecular mechanisms of an inborn error of methionine pathway. Methionine adenosyltransferase deficiency."
      Ubagai T., Lei K.-J., Huang S., Mudd S.H., Levy H.L., Chou J.Y.
      J. Clin. Invest. 96:1943-1947(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MATD ASP-55; PRO-305; MET-322 AND LEU-357.
    9. "Demyelination of the brain is associated with methionine adenosyltransferase I/III deficiency."
      Chamberlin M.E., Ubagai T., Mudd S.H., Wilson W.G., Leonard J.V., Chou J.Y.
      J. Clin. Invest. 98:1021-1027(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MATD CYS-199; GLN-356 AND SER-378.
    10. "Dominant inheritance of isolated hypermethioninemia is associated with a mutation in the human methionine adenosyltransferase 1A gene."
      Chamberlin M.E., Ubagai T., Mudd S.H., Levy H.L., Chou J.Y.
      Am. J. Hum. Genet. 60:540-546(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MATD HIS-264.
    11. "Methionine adenosyltransferase I/III deficiency: novel mutations and clinical variations."
      Chamberlin M.E., Ubagai T., Mudd S.H., Thomas J., Pao V.Y., Nguyen T.K., Levy H.L., Greene C., Freehauf C., Chou J.Y.
      Am. J. Hum. Genet. 66:347-355(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MATD ASN-38; CYS-264; HIS-264; MET-322; ARG-336 AND ALA-344, CHARACTERIZATION OF VARIANTS MATD ASN-38; CYS-264; HIS-264; MET-322; ARG-336 AND ALA-344.

    Entry informationi

    Entry nameiMETK1_HUMAN
    AccessioniPrimary (citable) accession number: Q00266
    Secondary accession number(s): D3DWD5, Q5QP09
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 160 of the entry and version 2 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 10
      Human chromosome 10: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3