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Protein

Methionine synthase

Gene

MTR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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:

Pathway: L-methionine biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes L-methionine from L-homocysteine (MetH route).
Proteins known to be involved in this subpathway in this organism are:
  1. Methionine synthase (MTR)
This subpathway is part of the pathway L-methionine biosynthesis via de novo pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-methionine from L-homocysteine (MetH route), the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis.

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

GO - Biological processi

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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:7468. MTR.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Homocystinuria-megaloblastic anemia, cblG complementation type (HMAG)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn 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.

See also OMIM:250940
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
Neural tube defects, folate-sensitive (NTDFS)1 Publication

Disease susceptibility is associated with variations affecting the gene represented in this entry.

Disease descriptionThe most common NTDs are open spina bifida (myelomeningocele) and anencephaly.

See also OMIM:601634

Keywords - Diseasei

Disease mutation

Organism-specific databases

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

Chemistry

DrugBankiDB00115. Cyanocobalamin.
DB00200. Hydroxocobalamin.
DB00134. L-Methionine.
DB00116. Tetrahydrofolic acid.

Polymorphism and mutation databases

BioMutaiMTR.
DMDMi2842762.

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.
GenevisibleiQ99707. HS.

Organism-specific databases

HPAiHPA044474.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi110642. 20 interactions.
DIPiDIP-40306N.
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, 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.
OMAiDYNSIMV.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99707-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        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
Isoform 2 (identifier: Q99707-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     682-732: Missing.

Note: No experimental confirmation available.
Show »
Length:1,214
Mass (Da):134,793
Checksum:i2E568CD852B22E8C
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.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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei682 – 73251Missing in isoform 2. 1 PublicationVSP_057283Add
BLAST

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.
BC144095 mRNA. Translation: AAI44096.1.
CCDSiCCDS1614.1. [Q99707-1]
CCDS73054.1. [Q99707-2]
RefSeqiNP_000245.2. NM_000254.2. [Q99707-1]
NP_001278868.1. NM_001291939.1. [Q99707-2]
NP_001278869.1. NM_001291940.1.
UniGeneiHs.498187.

Genome annotation databases

EnsembliENST00000366577; ENSP00000355536; ENSG00000116984. [Q99707-1]
ENST00000535889; ENSP00000441845; ENSG00000116984. [Q99707-2]
GeneIDi4548.
KEGGihsa:4548.
UCSCiuc001hyi.4. human. [Q99707-1]
uc010pxx.2. human.

Keywords - Coding sequence diversityi

Alternative splicing, 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.
BC144095 mRNA. Translation: AAI44096.1.
CCDSiCCDS1614.1. [Q99707-1]
CCDS73054.1. [Q99707-2]
RefSeqiNP_000245.2. NM_000254.2. [Q99707-1]
NP_001278868.1. NM_001291939.1. [Q99707-2]
NP_001278869.1. NM_001291940.1.
UniGeneiHs.498187.

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, 926-1264.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110642. 20 interactions.
DIPiDIP-40306N.
IntActiQ99707. 3 interactions.
STRINGi9606.ENSP00000355536.

Chemistry

BindingDBiQ99707.
ChEMBLiCHEMBL2150844.
DrugBankiDB00115. Cyanocobalamin.
DB00200. Hydroxocobalamin.
DB00134. L-Methionine.
DB00116. Tetrahydrofolic acid.

PTM databases

PhosphoSiteiQ99707.

Polymorphism and mutation databases

BioMutaiMTR.
DMDMi2842762.

Proteomic databases

MaxQBiQ99707.
PaxDbiQ99707.
PRIDEiQ99707.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366577; ENSP00000355536; ENSG00000116984. [Q99707-1]
ENST00000535889; ENSP00000441845; ENSG00000116984. [Q99707-2]
GeneIDi4548.
KEGGihsa:4548.
UCSCiuc001hyi.4. human. [Q99707-1]
uc010pxx.2. human.

Organism-specific databases

CTDi4548.
GeneCardsiGC01P236958.
GeneReviewsiMTR.
HGNCiHGNC:7468. MTR.
HPAiHPA044474.
MIMi156570. gene.
250940. phenotype.
601634. phenotype.
603174. phenotype.
neXtProtiNX_Q99707.
Orphaneti2170. Methylcobalamin deficiency type cblG.
PharmGKBiPA31272.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1410.
GeneTreeiENSGT00420000029824.
HOGENOMiHOG000251409.
HOVERGENiHBG006347.
InParanoidiQ99707.
KOiK00548.
OMAiDYNSIMV.
OrthoDBiEOG7TF786.
PhylomeDBiQ99707.
TreeFamiTF312829.

Enzyme and pathway databases

UniPathwayiUPA00051; UER00081.
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.

Miscellaneous databases

ChiTaRSiMTR. human.
EvolutionaryTraceiQ99707.
GeneWikiiMethionine_synthase.
GenomeRNAii4548.
NextBioi17533.
PROiQ99707.
SOURCEiSearch...

Gene expression databases

BgeeiQ99707.
CleanExiHS_MTR.
ExpressionAtlasiQ99707. baseline and differential.
GenevisibleiQ99707. HS.

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]
ProtoNetiSearch...

Publicationsi

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  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] (ISOFORM 1), 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] (ISOFORM 1).
    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] (ISOFORM 1), 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] (ISOFORMS 1 AND 2), 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: INVOLVEMENT IN SUSCEPTIBILITY TO NTDFS, VARIANT GLY-919.
  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: VARIANT GLY-919.

Entry informationi

Entry nameiMETH_HUMAN
AccessioniPrimary (citable) accession number: Q99707
Secondary accession number(s): A1L4N8
, A9Z1W4, B7ZLW7, B9EGF7, Q99713, Q99723
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: June 24, 2015
This is version 159 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.