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Q99707

- METH_HUMAN

UniProt

Q99707 - METH_HUMAN

Protein

Methionine synthase

Gene

MTR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 2 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate By similarity.By similarity

    Catalytic activityi

    5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine.

    Cofactori

    Methylcobalamin (MeCBL).
    Binds 1 zinc ion per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi260 – 2601ZincPROSITE-ProRule annotation
    Metal bindingi323 – 3231ZincPROSITE-ProRule annotation
    Metal bindingi324 – 3241ZincPROSITE-ProRule annotation
    Metal bindingi785 – 7851Cobalt (cobalamin axial ligand)By similarity
    Binding sitei830 – 8301CobalaminBy similarity
    Binding sitei974 – 9741S-adenosyl-L-methionineBy similarity
    Binding sitei1172 – 11721S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
    Binding sitei1176 – 11761Cobalamin; via carbonyl oxygenBy similarity

    GO - Molecular functioni

    1. cobalamin binding Source: UniProtKB-KW
    2. methionine synthase activity Source: UniProtKB-EC
    3. S-adenosylmethionine-homocysteine S-methyltransferase activity Source: InterPro
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cellular nitrogen compound metabolic process Source: Reactome
    2. cobalamin metabolic process Source: Reactome
    3. methylation Source: Reactome
    4. nervous system development Source: ProtInc
    5. pteridine-containing compound metabolic process Source: InterPro
    6. small molecule metabolic process Source: Reactome
    7. sulfur amino acid metabolic process Source: Reactome
    8. vitamin metabolic process Source: Reactome
    9. water-soluble vitamin metabolic process Source: Reactome
    10. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Methionine biosynthesis

    Keywords - Ligandi

    Cobalamin, Cobalt, Metal-binding, S-adenosyl-L-methionine, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04076-MONOMER.
    ReactomeiREACT_115639. Sulfur amino acid metabolism.
    REACT_163862. Cobalamin (Cbl, vitamin B12) transport and metabolism.
    REACT_169149. Defective MTR causes methylmalonic aciduria and homocystinuria type cblG.
    REACT_169439. Defective MTRR causes methylmalonic aciduria and homocystinuria type cblE.
    REACT_6946. Methylation.
    UniPathwayiUPA00051; UER00081.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine synthase (EC:2.1.1.13)
    Alternative name(s):
    5-methyltetrahydrofolate--homocysteine methyltransferase
    Vitamin-B12 dependent methionine synthase
    Short name:
    MS
    Gene namesi
    Name:MTR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:7468. MTR.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Homocystinuria-megaloblastic anemia, cblG complementation type (HMAG) [MIM:250940]: An autosomal recessive inborn error of metabolism resulting from defects in the cobalamin-dependent pathway that converts homocysteine to methionine. It causes delayed psychomotor development, megaloblastic anemia, homocystinuria, and hypomethioninemia.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti881 – 8811Missing in HMAG. 2 Publications
    VAR_004328
    Natural varianti920 – 9201H → D in HMAG. 1 Publication
    Corresponds to variant rs28933097 [ dbSNP | Ensembl ].
    VAR_004330
    Natural varianti1173 – 11731P → L in HMAG. 1 Publication
    VAR_004331
    Folate-sensitive neural tube defects (FS-NTD) [MIM:601634]: The most common NTDs are open spina bifida (myelomeningocele) and anencephaly.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti919 – 9191D → G May be associated with susceptibility to FS-NTD. 2 Publications
    Corresponds to variant rs1805087 [ dbSNP | Ensembl ].
    VAR_004329

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi250940. phenotype.
    601634. phenotype.
    603174. phenotype.
    Orphaneti2170. Methylcobalamin deficiency type cblG.
    PharmGKBiPA31272.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12651265Methionine synthasePRO_0000204530Add
    BLAST

    Proteomic databases

    MaxQBiQ99707.
    PaxDbiQ99707.
    PRIDEiQ99707.

    PTM databases

    PhosphoSiteiQ99707.

    Expressioni

    Tissue specificityi

    Widely expressed. Expressed at the highest levels in pancreas, heart, brain, skeletal muscle and placenta. Expressed at lower levels in lung, liver and kidney.

    Gene expression databases

    ArrayExpressiQ99707.
    BgeeiQ99707.
    CleanExiHS_MTR.
    GenevestigatoriQ99707.

    Organism-specific databases

    HPAiHPA044474.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TSC22D1Q157141EBI-1045782,EBI-712609

    Protein-protein interaction databases

    BioGridi110642. 16 interactions.
    IntActiQ99707. 2 interactions.
    STRINGi9606.ENSP00000355536.

    Structurei

    Secondary structure

    1
    1265
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi18 – 2811
    Helixi37 – 448
    Helixi49 – 513
    Helixi67 – 693
    Helixi70 – 734
    Helixi75 – 8713
    Beta strandi92 – 943
    Helixi102 – 1054
    Helixi106 – 1083
    Helixi111 – 1133
    Helixi114 – 13623
    Beta strandi141 – 1466
    Beta strandi153 – 1553
    Beta strandi159 – 1613
    Helixi169 – 18517
    Beta strandi189 – 19810
    Helixi199 – 21315
    Turni214 – 2163
    Beta strandi222 – 2265
    Helixi241 – 2488
    Helixi249 – 2513
    Beta strandi254 – 26310
    Turni264 – 2674
    Helixi268 – 2758
    Beta strandi279 – 2879
    Beta strandi318 – 3203
    Helixi328 – 33811
    Turni348 – 3536
    Beta strandi355 – 36511
    Beta strandi372 – 3754
    Turni380 – 3823
    Helixi384 – 3918
    Helixi395 – 40713
    Beta strandi411 – 4166
    Helixi424 – 43714
    Helixi439 – 4424
    Beta strandi446 – 4494
    Helixi453 – 46210
    Beta strandi468 – 4725
    Helixi478 – 49114
    Beta strandi494 – 5018
    Helixi509 – 52719
    Helixi531 – 5333
    Beta strandi534 – 5374
    Helixi548 – 5525
    Helixi553 – 56715
    Helixi577 – 5848
    Helixi588 – 60518
    Beta strandi609 – 6124
    Helixi620 – 6223
    Helixi625 – 63511
    Helixi642 – 6487
    Helixi932 – 9376
    Helixi944 – 9463
    Beta strandi956 – 9627
    Helixi966 – 9705
    Helixi976 – 98712
    Helixi995 – 9984
    Helixi1005 – 102218
    Beta strandi1026 – 104015
    Beta strandi1043 – 10464
    Helixi1053 – 10553
    Beta strandi1059 – 10635
    Helixi1082 – 10854
    Helixi1089 – 10913
    Beta strandi1095 – 110612
    Helixi1107 – 111610
    Helixi1120 – 114728
    Turni1152 – 11554
    Helixi1160 – 11645
    Beta strandi1168 – 11714
    Helixi1185 – 11928
    Helixi1195 – 11995
    Beta strandi1209 – 122012
    Helixi1235 – 124511
    Helixi1249 – 12557
    Helixi1257 – 12593

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2O2KX-ray1.60A/B925-1265[»]
    4CCZX-ray2.70A16-657[»]
    ProteinModelPortaliQ99707.
    SMRiQ99707. Positions 17-651, 665-920, 926-1264.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99707.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini19 – 338320Hcy-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini371 – 632262Pterin-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini662 – 75998B12-binding N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini772 – 907136B12-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini923 – 1265343AdoMet activationPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni860 – 8612Cobalamin-bindingBy similarity
    Regioni1227 – 12282S-adenosyl-L-methionine bindingBy similarity

    Domaini

    Modular enzyme with four functionally distinct domains. The isolated Hcy-binding domain catalyzes methyl transfer from free methylcobalamin to homocysteine. The Hcy-binding domain in association with the pterin-binding domain catalyzes the methylation of cob(I)alamin by methyltetrahydrofolate and the methylation of homocysteine. The B12-binding domain binds the cofactor. The AdoMet activation domain binds S-adenosyl-L-methionine. Under aerobic conditions cob(I)alamin can be converted to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L-methionine and flavodoxin regenerates methylcobalamin By similarity.By similarity

    Sequence similaritiesi

    Contains 1 AdoMet activation domain.PROSITE-ProRule annotation
    Contains 1 B12-binding domain.PROSITE-ProRule annotation
    Contains 1 Hcy-binding domain.PROSITE-ProRule annotation
    Contains 1 pterin-binding domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG1410.
    HOGENOMiHOG000251409.
    HOVERGENiHBG006347.
    InParanoidiQ99707.
    KOiK00548.
    OMAiKAQPMVT.
    OrthoDBiEOG7TF786.
    PhylomeDBiQ99707.
    TreeFamiTF312829.

    Family and domain databases

    Gene3Di1.10.1240.10. 1 hit.
    3.10.196.10. 1 hit.
    3.20.20.20. 1 hit.
    3.20.20.330. 1 hit.
    3.40.50.280. 1 hit.
    InterProiIPR003759. Cbl-bd_cap.
    IPR006158. Cobalamin-bd.
    IPR011005. Dihydropteroate_synth-like.
    IPR011822. MetH.
    IPR000489. Pterin-binding.
    IPR003726. S_MeTrfase.
    IPR004223. VitB12-dep_Met_synth_activ_dom.
    [Graphical view]
    PfamiPF02310. B12-binding. 1 hit.
    PF02607. B12-binding_2. 1 hit.
    PF02965. Met_synt_B12. 1 hit.
    PF00809. Pterin_bind. 1 hit.
    PF02574. S-methyl_trans. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000381. MetH. 1 hit.
    SMARTiSM01018. B12-binding_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF47644. SSF47644. 1 hit.
    SSF51717. SSF51717. 1 hit.
    SSF52242. SSF52242. 1 hit.
    SSF56507. SSF56507. 1 hit.
    SSF82282. SSF82282. 1 hit.
    TIGRFAMsiTIGR02082. metH. 1 hit.
    PROSITEiPS50974. ADOMET_ACTIVATION. 1 hit.
    PS51332. B12_BINDING. 1 hit.
    PS51337. B12_BINDING_NTER. 1 hit.
    PS50970. HCY. 1 hit.
    PS50972. PTERIN_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q99707-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSPALQDLSQ PEGLKKTLRD EINAILQKRI MVLDGGMGTM IQREKLNEEH     50
    FRGQEFKDHA RPLKGNNDIL SITQPDVIYQ IHKEYLLAGA DIIETNTFSS 100
    TSIAQADYGL EHLAYRMNMC SAGVARKAAE EVTLQTGIKR FVAGALGPTN 150
    KTLSVSPSVE RPDYRNITFD ELVEAYQEQA KGLLDGGVDI LLIETIFDTA 200
    NAKAALFALQ NLFEEKYAPR PIFISGTIVD KSGRTLSGQT GEGFVISVSH 250
    GEPLCIGLNC ALGAAEMRPF IEIIGKCTTA YVLCYPNAGL PNTFGDYDET 300
    PSMMAKHLKD FAMDGLVNIV GGCCGSTPDH IREIAEAVKN CKPRVPPATA 350
    FEGHMLLSGL EPFRIGPYTN FVNIGERCNV AGSRKFAKLI MAGNYEEALC 400
    VAKVQVEMGA QVLDVNMDDG MLDGPSAMTR FCNLIASEPD IAKVPLCIDS 450
    SNFAVIEAGL KCCQGKCIVN SISLKEGEDD FLEKARKIKK YGAAMVVMAF 500
    DEEGQATETD TKIRVCTRAY HLLVKKLGFN PNDIIFDPNI LTIGTGMEEH 550
    NLYAINFIHA TKVIKETLPG ARISGGLSNL SFSFRGMEAI REAMHGVFLY 600
    HAIKSGMDMG IVNAGNLPVY DDIHKELLQL CEDLIWNKDP EATEKLLRYA 650
    QTQGTGGKKV IQTDEWRNGP VEERLEYALV KGIEKHIIED TEEARLNQKK 700
    YPRPLNIIEG PLMNGMKIVG DLFGAGKMFL PQVIKSARVM KKAVGHLIPF 750
    MEKEREETRV LNGTVEEEDP YQGTIVLATV KGDVHDIGKN IVGVVLGCNN 800
    FRVIDLGVMT PCDKILKAAL DHKADIIGLS GLITPSLDEM IFVAKEMERL 850
    AIRIPLLIGG ATTSKTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN 900
    LKDEYFEEIM EEYEDIRQDH YESLKERRYL PLSQARKSGF QMDWLSEPHP 950
    VKPTFIGTQV FEDYDLQKLV DYIDWKPFFD VWQLRGKYPN RGFPKIFNDK 1000
    TVGGEARKVY DDAHNMLNTL ISQKKLRARG VVGFWPAQSI QDDIHLYAEA 1050
    AVPQAAEPIA TFYGLRQQAE KDSASTEPYY CLSDFIAPLH SGIRDYLGLF 1100
    AVACFGVEEL SKAYEDDGDD YSSIMVKALG DRLAEAFAEE LHERVRRELW 1150
    AYCGSEQLDV ADLRRLRYKG IRPAPGYPSQ PDHTEKLTMW RLADIEQSTG 1200
    IRLTESLAMA PASAVSGLYF SNLKSKYFAV GKISKDQVED YALRKNISVA 1250
    EVEKWLGPIL GYDTD 1265
    Length:1,265
    Mass (Da):140,527
    Last modified:July 1, 1997 - v2
    Checksum:iB04C26BCBE9A57C2
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti52 – 521R → Q.
    Corresponds to variant rs12749581 [ dbSNP | Ensembl ].
    VAR_050033
    Natural varianti61 – 611R → K.1 Publication
    VAR_004326
    Natural varianti255 – 2551C → Y.1 Publication
    VAR_004327
    Natural varianti314 – 3141D → N.
    Corresponds to variant rs2229274 [ dbSNP | Ensembl ].
    VAR_061338
    Natural varianti881 – 8811Missing in HMAG. 2 Publications
    VAR_004328
    Natural varianti919 – 9191D → G May be associated with susceptibility to FS-NTD. 2 Publications
    Corresponds to variant rs1805087 [ dbSNP | Ensembl ].
    VAR_004329
    Natural varianti920 – 9201H → D in HMAG. 1 Publication
    Corresponds to variant rs28933097 [ dbSNP | Ensembl ].
    VAR_004330
    Natural varianti1173 – 11731P → L in HMAG. 1 Publication
    VAR_004331

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U71285 mRNA. Translation: AAC51188.1.
    U75743 mRNA. Translation: AAB58906.1.
    U73338 mRNA. Translation: AAB39704.1.
    AL359185, AL359259 Genomic DNA. Translation: CAH73198.1.
    AL359259, AL359185 Genomic DNA. Translation: CAH70983.1.
    CH471098 Genomic DNA. Translation: EAW70066.1.
    BC130616 mRNA. Translation: AAI30617.1.
    BC136440 mRNA. Translation: AAI36441.1.
    CCDSiCCDS1614.1.
    RefSeqiNP_000245.2. NM_000254.2.
    NP_001278869.1. NM_001291940.1.
    UniGeneiHs.498187.

    Genome annotation databases

    EnsembliENST00000366577; ENSP00000355536; ENSG00000116984.
    GeneIDi4548.
    KEGGihsa:4548.
    UCSCiuc001hyi.4. human.

    Polymorphism databases

    DMDMi2842762.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    5-methyltetrahydrofolate-homocysteine methyltransferase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U71285 mRNA. Translation: AAC51188.1 .
    U75743 mRNA. Translation: AAB58906.1 .
    U73338 mRNA. Translation: AAB39704.1 .
    AL359185 , AL359259 Genomic DNA. Translation: CAH73198.1 .
    AL359259 , AL359185 Genomic DNA. Translation: CAH70983.1 .
    CH471098 Genomic DNA. Translation: EAW70066.1 .
    BC130616 mRNA. Translation: AAI30617.1 .
    BC136440 mRNA. Translation: AAI36441.1 .
    CCDSi CCDS1614.1.
    RefSeqi NP_000245.2. NM_000254.2.
    NP_001278869.1. NM_001291940.1.
    UniGenei Hs.498187.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2O2K X-ray 1.60 A/B 925-1265 [» ]
    4CCZ X-ray 2.70 A 16-657 [» ]
    ProteinModelPortali Q99707.
    SMRi Q99707. Positions 17-651, 665-920, 926-1264.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110642. 16 interactions.
    IntActi Q99707. 2 interactions.
    STRINGi 9606.ENSP00000355536.

    Chemistry

    ChEMBLi CHEMBL2150844.
    DrugBanki DB00200. Hydroxocobalamin.
    DB00134. L-Methionine.
    DB00116. Tetrahydrofolic acid.

    PTM databases

    PhosphoSitei Q99707.

    Polymorphism databases

    DMDMi 2842762.

    Proteomic databases

    MaxQBi Q99707.
    PaxDbi Q99707.
    PRIDEi Q99707.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000366577 ; ENSP00000355536 ; ENSG00000116984 .
    GeneIDi 4548.
    KEGGi hsa:4548.
    UCSCi uc001hyi.4. human.

    Organism-specific databases

    CTDi 4548.
    GeneCardsi GC01P236958.
    GeneReviewsi MTR.
    HGNCi HGNC:7468. MTR.
    HPAi HPA044474.
    MIMi 156570. gene.
    250940. phenotype.
    601634. phenotype.
    603174. phenotype.
    neXtProti NX_Q99707.
    Orphaneti 2170. Methylcobalamin deficiency type cblG.
    PharmGKBi PA31272.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1410.
    HOGENOMi HOG000251409.
    HOVERGENi HBG006347.
    InParanoidi Q99707.
    KOi K00548.
    OMAi KAQPMVT.
    OrthoDBi EOG7TF786.
    PhylomeDBi Q99707.
    TreeFami TF312829.

    Enzyme and pathway databases

    UniPathwayi UPA00051 ; UER00081 .
    BioCyci MetaCyc:HS04076-MONOMER.
    Reactomei REACT_115639. Sulfur amino acid metabolism.
    REACT_163862. Cobalamin (Cbl, vitamin B12) transport and metabolism.
    REACT_169149. Defective MTR causes methylmalonic aciduria and homocystinuria type cblG.
    REACT_169439. Defective MTRR causes methylmalonic aciduria and homocystinuria type cblE.
    REACT_6946. Methylation.

    Miscellaneous databases

    ChiTaRSi MTR. human.
    EvolutionaryTracei Q99707.
    GeneWikii Methionine_synthase.
    GenomeRNAii 4548.
    NextBioi 17533.
    PROi Q99707.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99707.
    Bgeei Q99707.
    CleanExi HS_MTR.
    Genevestigatori Q99707.

    Family and domain databases

    Gene3Di 1.10.1240.10. 1 hit.
    3.10.196.10. 1 hit.
    3.20.20.20. 1 hit.
    3.20.20.330. 1 hit.
    3.40.50.280. 1 hit.
    InterProi IPR003759. Cbl-bd_cap.
    IPR006158. Cobalamin-bd.
    IPR011005. Dihydropteroate_synth-like.
    IPR011822. MetH.
    IPR000489. Pterin-binding.
    IPR003726. S_MeTrfase.
    IPR004223. VitB12-dep_Met_synth_activ_dom.
    [Graphical view ]
    Pfami PF02310. B12-binding. 1 hit.
    PF02607. B12-binding_2. 1 hit.
    PF02965. Met_synt_B12. 1 hit.
    PF00809. Pterin_bind. 1 hit.
    PF02574. S-methyl_trans. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000381. MetH. 1 hit.
    SMARTi SM01018. B12-binding_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47644. SSF47644. 1 hit.
    SSF51717. SSF51717. 1 hit.
    SSF52242. SSF52242. 1 hit.
    SSF56507. SSF56507. 1 hit.
    SSF82282. SSF82282. 1 hit.
    TIGRFAMsi TIGR02082. metH. 1 hit.
    PROSITEi PS50974. ADOMET_ACTIVATION. 1 hit.
    PS51332. B12_BINDING. 1 hit.
    PS51337. B12_BINDING_NTER. 1 hit.
    PS50970. HCY. 1 hit.
    PS50972. PTERIN_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human methionine synthase: cDNA cloning and identification of mutations in patients of the cblG complementation group of folate/cobalamin disorders."
      Leclerc D., Campeau E., Goyette P., Adjalla C.E., Christensen B., Ross M., Eydoux P., Rosenblatt D.S., Rozen R., Gravel R.A.
      Hum. Mol. Genet. 5:1867-1874(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS HMAG ILE-881 DEL AND ASP-920.
      Tissue: Fibroblast.
    2. "Cloning, mapping and RNA analysis of the human methionine synthase gene."
      Li Y.N., Gulati S., Baker P.J., Brody L.C., Banerjee R., Kruger W.D.
      Hum. Mol. Genet. 5:1851-1858(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    3. "Human methionine synthase. cDNA cloning, gene localization, and expression."
      Chen L.H., Liu M.-L., Hwang H.-Y., Chen L.-S., Korenberg J., Shane B.
      J. Biol. Chem. 272:3628-3634(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS TYR-255 AND GLY-919.
      Tissue: Fetal liver.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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], VARIANT GLY-919.
      Tissue: Testis.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: VARIANTS HMAG ILE-881 DEL AND LEU-1173, VARIANT LYS-61.
    9. "Maternal genetic effects, exerted by genes involved in homocysteine remethylation, influence the risk of spina bifida."
      Doolin M.-T., Barbaux S., McDonnell M., Hoess K., Whitehead A.S., Mitchell L.E.
      Am. J. Hum. Genet. 71:1222-1226(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION OF VARIANT GLY-919 WITH SUSCEPTIBILITY TO FS-NTD.
    10. "Analysis of methionine synthase reductase polymorphisms for neural tube defects risk association."
      O'Leary V.B., Mills J.L., Pangilinan F., Kirke P.N., Cox C., Conley M., Weiler A., Peng K., Shane B., Scott J.M., Parle-McDermott A., Molloy A.M., Brody L.C.
      Mol. Genet. Metab. 85:220-227(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NO ASSOCIATION OF VARIANT GLY-919 WITH SUSCEPTIBILITY TO FS-NTD.

    Entry informationi

    Entry nameiMETH_HUMAN
    AccessioniPrimary (citable) accession number: Q99707
    Secondary accession number(s): A1L4N8
    , A9Z1W4, B9EGF7, Q99713, Q99723
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 151 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

    Miscellaneous

    L-homocysteine is bound via the zinc atom.By similarity

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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