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Q99707

- METH_HUMAN

UniProt

Q99707 - METH_HUMAN

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

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.

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 – 2601Zinc By similarity
Metal bindingi323 – 3231Zinc By similarity
Metal bindingi324 – 3241Zinc By similarity
Metal bindingi785 – 7851Cobalt (cobalamin axial ligand) By similarity
Binding sitei830 – 8301Cobalamin By similarity
Binding sitei974 – 9741S-adenosyl-L-methionine By similarity
Binding sitei1172 – 11721S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding sitei1176 – 11761Cobalamin; via carbonyl oxygen By similarity

GO - Molecular functioni

  1. S-adenosylmethionine-homocysteine S-methyltransferase activity Source: InterPro
  2. cobalamin binding Source: UniProtKB-KW
  3. methionine synthase activity Source: UniProtKB-EC
  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
Complete GO annotation...

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti919 – 9191D → G May be associated with susceptibility to FS-NTD. 4 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 synthase
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiQ99707.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 338320Hcy-binding
Add
BLAST
Domaini371 – 632262Pterin-binding
Add
BLAST
Domaini662 – 75998B12-binding N-terminal
Add
BLAST
Domaini772 – 907136B12-binding
Add
BLAST
Domaini923 – 1265343AdoMet activation
Add
BLAST

Region

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

Sequence similaritiesi

Contains 1 B12-binding domain.
Contains 1 Hcy-binding domain.

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. 4 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 150 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

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