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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).By similarity

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

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
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.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

BgeeiQ99707.
CleanExiHS_MTR.
ExpressionAtlasiQ99707. baseline and differential.
GenevestigatoriQ99707.

Organism-specific databases

HPAiHPA044474.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
MMACHCQ9Y4U13EBI-1045782,EBI-9775184

Protein-protein interaction databases

BioGridi110642. 17 interactions.
IntActiQ99707. 3 interactions.
STRINGi9606.ENSP00000355536.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00420000029824.
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

        10         20         30         40         50
MSPALQDLSQ PEGLKKTLRD EINAILQKRI MVLDGGMGTM IQREKLNEEH
60 70 80 90 100
FRGQEFKDHA RPLKGNNDIL SITQPDVIYQ IHKEYLLAGA DIIETNTFSS
110 120 130 140 150
TSIAQADYGL EHLAYRMNMC SAGVARKAAE EVTLQTGIKR FVAGALGPTN
160 170 180 190 200
KTLSVSPSVE RPDYRNITFD ELVEAYQEQA KGLLDGGVDI LLIETIFDTA
210 220 230 240 250
NAKAALFALQ NLFEEKYAPR PIFISGTIVD KSGRTLSGQT GEGFVISVSH
260 270 280 290 300
GEPLCIGLNC ALGAAEMRPF IEIIGKCTTA YVLCYPNAGL PNTFGDYDET
310 320 330 340 350
PSMMAKHLKD FAMDGLVNIV GGCCGSTPDH IREIAEAVKN CKPRVPPATA
360 370 380 390 400
FEGHMLLSGL EPFRIGPYTN FVNIGERCNV AGSRKFAKLI MAGNYEEALC
410 420 430 440 450
VAKVQVEMGA QVLDVNMDDG MLDGPSAMTR FCNLIASEPD IAKVPLCIDS
460 470 480 490 500
SNFAVIEAGL KCCQGKCIVN SISLKEGEDD FLEKARKIKK YGAAMVVMAF
510 520 530 540 550
DEEGQATETD TKIRVCTRAY HLLVKKLGFN PNDIIFDPNI LTIGTGMEEH
560 570 580 590 600
NLYAINFIHA TKVIKETLPG ARISGGLSNL SFSFRGMEAI REAMHGVFLY
610 620 630 640 650
HAIKSGMDMG IVNAGNLPVY DDIHKELLQL CEDLIWNKDP EATEKLLRYA
660 670 680 690 700
QTQGTGGKKV IQTDEWRNGP VEERLEYALV KGIEKHIIED TEEARLNQKK
710 720 730 740 750
YPRPLNIIEG PLMNGMKIVG DLFGAGKMFL PQVIKSARVM KKAVGHLIPF
760 770 780 790 800
MEKEREETRV LNGTVEEEDP YQGTIVLATV KGDVHDIGKN IVGVVLGCNN
810 820 830 840 850
FRVIDLGVMT PCDKILKAAL DHKADIIGLS GLITPSLDEM IFVAKEMERL
860 870 880 890 900
AIRIPLLIGG ATTSKTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN
910 920 930 940 950
LKDEYFEEIM EEYEDIRQDH YESLKERRYL PLSQARKSGF QMDWLSEPHP
960 970 980 990 1000
VKPTFIGTQV FEDYDLQKLV DYIDWKPFFD VWQLRGKYPN RGFPKIFNDK
1010 1020 1030 1040 1050
TVGGEARKVY DDAHNMLNTL ISQKKLRARG VVGFWPAQSI QDDIHLYAEA
1060 1070 1080 1090 1100
AVPQAAEPIA TFYGLRQQAE KDSASTEPYY CLSDFIAPLH SGIRDYLGLF
1110 1120 1130 1140 1150
AVACFGVEEL SKAYEDDGDD YSSIMVKALG DRLAEAFAEE LHERVRRELW
1160 1170 1180 1190 1200
AYCGSEQLDV ADLRRLRYKG IRPAPGYPSQ PDHTEKLTMW RLADIEQSTG
1210 1220 1230 1240 1250
IRLTESLAMA PASAVSGLYF SNLKSKYFAV GKISKDQVED YALRKNISVA
1260
EVEKWLGPIL GYDTD
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 17 interactions.
IntActi Q99707. 3 interactions.
STRINGi 9606.ENSP00000355536.

Chemistry

BindingDBi Q99707.
ChEMBLi CHEMBL2150844.
DrugBanki DB00115. Cyanocobalamin.
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.
GeneTreei ENSGT00420000029824.
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

Bgeei Q99707.
CleanExi HS_MTR.
ExpressionAtlasi Q99707. baseline and differential.
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: November 26, 2014
This is version 153 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