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Protein
Submitted name:

Methionine synthase

Gene

MTR

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Cofactori

Note: Cobalamin.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi339 – 3391Cobalt (cobalamin axial ligand)UniRule annotation
Binding sitei528 – 5281S-adenosyl-L-methionineUniRule annotation
Binding sitei726 – 7261S-adenosyl-L-methionine; via carbonyl oxygenUniRule annotation
Binding sitei730 – 7301Cobalamin; via carbonyl oxygenUniRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. pteridine-containing compound metabolic process Source: InterPro
Complete GO annotation...

Keywords - Ligandi

CobalaminUniRule annotation, Cobalt, Metal-bindingUniRule annotation, S-adenosyl-L-methionineUniRule annotation

Names & Taxonomyi

Protein namesi
Submitted name:
Methionine synthaseImported
Gene namesi
Name:MTRImported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:7468. MTR.

Subcellular locationi

GO - Cellular componenti

  1. intracellular Source: InterPro
Complete GO annotation...

PTM / Processingi

Proteomic databases

PRIDEiB1ANE3.

Expressioni

Gene expression databases

BgeeiB1ANE3.
ExpressionAtlasiB1ANE3. baseline and differential.

Structurei

3D structure databases

ProteinModelPortaliB1ANE3.
SMRiB1ANE3. Positions 2-819.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni414 – 4152Cobalamin-bindingUniRule annotation
Regioni781 – 7822S-adenosyl-L-methionine bindingUniRule annotation

Phylogenomic databases

GeneTreeiENSGT00420000029824.
HOGENOMiHOG000251409.
HOVERGENiHBG006347.

Family and domain databases

Gene3Di1.10.1240.10. 1 hit.
3.10.196.10. 1 hit.
3.20.20.20. 2 hits.
3.40.50.280. 1 hit.
InterProiIPR003759. Cbl-bd_cap.
IPR006158. Cobalamin-bd.
IPR011005. Dihydropteroate_synth-like.
IPR011822. MetH.
IPR000489. Pterin-binding.
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. 2 hits.
[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.
TIGRFAMsiTIGR02082. metH. 1 hit.
PROSITEiPS50974. ADOMET_ACTIVATION. 1 hit.
PS51332. B12_BINDING. 1 hit.
PS51337. B12_BINDING_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

B1ANE3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
GMLDGPSAMT RFCNLIASEP DIAKVPLCID SSNFAVIEAG LKCCQGKCIV
60 70 80 90 100
NSISLKEGEA TETDTKIRVC TRAYHLLVKK LGFNPNDIIF DPNILTIGTG
110 120 130 140 150
MEEHNLYAIN FIHATKVIKE TLPGARISGG LSNLSFSFRG MEAIREAMHG
160 170 180 190 200
VFLYHAIKSG MDMGIVNAGN LPVYDDIHKE LLQLCEDLIW NKDPEATEKL
210 220 230 240 250
LRYAQTQGTG GKKVIQTDEW RNGPVEERLE YALVKGIEKH IIEDTEEARL
260 270 280 290 300
NQKKYPRPLN IIEGPLMNGM KIVGDLFGAG KMFLPQVIKS ARVMKKAVGH
310 320 330 340 350
LIPFMEKERE ETRVLNGTVE EEDPYQGTIV LATVKGDVHD IGKNIVGVVL
360 370 380 390 400
GCNNFRVIDL GVMTPCDKIL KAALDHKADI IGLSGLITPS LDEMIFVAKE
410 420 430 440 450
MERLAIRIPL LIGGATTSKT HTAVKIAPRY SAPVIHVLDA SKSVVVCSQL
460 470 480 490 500
LDENLKDEYF EEIMEEYEDI RQDHYESLKE RRYLPLSQAR KSGFQMDWLS
510 520 530 540 550
EPHPVKPTFI GTQVFEDYDL QKLVDYIDWK PFFDVWQLRG KYPNRGFPKI
560 570 580 590 600
FNDKTVGGEA RKVYDDAHNM LNTLISQKKL RARGVVGFWP AQSIQDDIHL
610 620 630 640 650
YAEAAVPQAA EPIATFYGLR QQAEKDSAST EPYYCLSDFI APLHSGIRDY
660 670 680 690 700
LGLFAVACFG VEELSKAYED DGDDYSSIMV KALGDRLAEA FAEELHERVR
710 720 730 740 750
RELWAYCGSE QLDVADLRRL RYKGIRPAPG YPSQPDHTEK LTMWRLADIE
760 770 780 790 800
QSTGIRLTES LAMAPASAVS GLYFSNLKSK YFAVGKISKD QVEDYALRKN
810
ISVAEVEKWL GPILGYDTD
Length:819
Mass (Da):91,780
Last modified:April 8, 2008 - v1
Checksum:i412970EB2FA276A1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL359185 Genomic DNA. No translation available.
AL359259 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENST00000366576; ENSP00000355535; ENSG00000116984.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL359185 Genomic DNA. No translation available.
AL359259 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortaliB1ANE3.
SMRiB1ANE3. Positions 2-819.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiB1ANE3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366576; ENSP00000355535; ENSG00000116984.

Organism-specific databases

HGNCiHGNC:7468. MTR.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00420000029824.
HOGENOMiHOG000251409.
HOVERGENiHBG006347.

Miscellaneous databases

ChiTaRSiMTR. human.
NextBioi35466814.

Gene expression databases

BgeeiB1ANE3.
ExpressionAtlasiB1ANE3. baseline and differential.

Family and domain databases

Gene3Di1.10.1240.10. 1 hit.
3.10.196.10. 1 hit.
3.20.20.20. 2 hits.
3.40.50.280. 1 hit.
InterProiIPR003759. Cbl-bd_cap.
IPR006158. Cobalamin-bd.
IPR011005. Dihydropteroate_synth-like.
IPR011822. MetH.
IPR000489. Pterin-binding.
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. 2 hits.
[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.
TIGRFAMsiTIGR02082. metH. 1 hit.
PROSITEiPS50974. ADOMET_ACTIVATION. 1 hit.
PS51332. B12_BINDING. 1 hit.
PS51337. B12_BINDING_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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., 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., 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., 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., 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., McLaren S., Milne S., Mistry S., Moore M.J., 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., 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., Banerjee R., Bryant S.P., Burford D.C., Burrill W.D., Clegg S.M., Dhami P., Dovey O., Faulkner L.M., Gribble S.M., Langford C.F., Pandian R.D., Porter K.M., Prigmore E.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiB1ANE3_HUMAN
AccessioniPrimary (citable) accession number: B1ANE3
Entry historyi
Integrated into UniProtKB/TrEMBL: April 8, 2008
Last sequence update: April 8, 2008
Last modified: April 29, 2015
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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.