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Q9UBK8

- MTRR_HUMAN

UniProt

Q9UBK8 - MTRR_HUMAN

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Protein

Methionine synthase reductase

Gene

MTRR

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

Functioni

Involved in the reductive regeneration of cob(I)alamin (vitamin B12) cofactor required for the maintenance of methionine synthase in a functional state. Necessary for utilization of methylgroups from the folate cycle, thereby affecting transgenerational epigenetic inheritance. Folate pathway donates methyl groups necessary for cellular methylation and affects different pathways such as DNA methylation, possibly explaining the transgenerational epigenetic inheritance effects.1 Publication

Catalytic activityi

2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+ = 2 [methionine synthase]-cob(II)alamin + NADPH + 2 S-adenosyl-L-methionine.1 Publication

Cofactori

FAD.1 Publication
FMN.1 Publication

Kineticsi

  1. KM=2.89 µM for NADPH1 Publication
  2. KM=3540 µM for NADH1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei318 – 3181NADP1 Publication
Binding sitei686 – 6861NADP1 Publication
Binding sitei724 – 7241FAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi120 – 15132FMNPROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi478 – 4814FAD1 Publication
Nucleotide bindingi514 – 5174FAD1 Publication
Nucleotide bindingi637 – 6382NADP1 Publication
Nucleotide bindingi651 – 6533NADP1 Publication

GO - Molecular functioni

  1. [methionine synthase] reductase activity Source: UniProtKB
  2. flavin adenine dinucleotide binding Source: UniProtKB
  3. FMN binding Source: UniProtKB
  4. iron ion binding Source: InterPro
  5. NADP binding Source: UniProtKB
  6. oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen Source: RefGenome
  7. oxidoreductase activity, oxidizing metal ions, NAD or NADP as acceptor Source: UniProtKB

GO - Biological processi

  1. cellular nitrogen compound metabolic process Source: Reactome
  2. cobalamin metabolic process Source: Reactome
  3. DNA methylation Source: UniProtKB
  4. folic acid metabolic process Source: UniProtKB
  5. methionine biosynthetic process Source: UniProtKB-KW
  6. methionine metabolic process Source: UniProtKB
  7. methylation Source: Reactome
  8. oxidation-reduction process Source: UniProtKB
  9. small molecule metabolic process Source: Reactome
  10. sulfur amino acid metabolic process Source: Reactome
  11. vitamin metabolic process Source: Reactome
  12. water-soluble vitamin metabolic process Source: Reactome
  13. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Keywords - Ligandi

FAD, Flavoprotein, FMN, NADP, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:HS04756-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.
SABIO-RKQ9UBK8.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine synthase reductase (EC:1.16.1.8)
Short name:
MSR
Gene namesi
Name:MTRR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:7473. MTRR.

Subcellular locationi

Isoform A : Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: UniProtKB
  3. intermediate filament cytoskeleton Source: HPA
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Homocystinuria-megaloblastic anemia, cblE complementation type (HMAE) [MIM:236270]: 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. Cells from patients with HMAE fail to incorporate methyltetrahydrofolate into methionine in whole cells, but cell extracts show normal methionine synthase activity in the presence of a reducing agent.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti81 – 811Missing in HMAE. 1 Publication
VAR_012837
Natural varianti83 – 831V → M in HMAE. 1 Publication
VAR_012838
Natural varianti156 – 1561A → T in HMAE. 1 Publication
VAR_012839
Natural varianti432 – 4321C → R in HMAE. 1 Publication
VAR_012841
Natural varianti514 – 5141G → R in HMAE. 1 Publication
VAR_012842
Natural varianti581 – 5811G → R in HMAE. 1 Publication
VAR_015731
Natural varianti603 – 6031Missing in HMAE. 1 Publication
VAR_012843
Folate-sensitive neural tube defects (FS-NTD) [MIM:601634]: The most common NTDs are open spina bifida (myelomeningocele) and anencephaly.2 Publications
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi236270. phenotype.
601634. phenotype.
Orphaneti2169. Methylcobalamin deficiency type cblE.
PharmGKBiPA31277.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 725725Methionine synthase reductasePRO_0000021785Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei198 – 1981Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UBK8.
PaxDbiQ9UBK8.
PRIDEiQ9UBK8.

PTM databases

PhosphoSiteiQ9UBK8.

Expressioni

Tissue specificityi

Found in all tissues tested, particularly abundant in skeletal muscle.

Gene expression databases

BgeeiQ9UBK8.
CleanExiHS_MTRR.
ExpressionAtlasiQ9UBK8. baseline and differential.
GenevestigatoriQ9UBK8.

Organism-specific databases

HPAiHPA038113.

Interactioni

Protein-protein interaction databases

BioGridi110645. 5 interactions.
STRINGi9606.ENSP00000264668.

Structurei

Secondary structure

1
725
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi262 – 2643Combined sources
Beta strandi277 – 2826Combined sources
Beta strandi301 – 31010Combined sources
Beta strandi320 – 3267Combined sources
Beta strandi339 – 3435Combined sources
Helixi348 – 35710Combined sources
Helixi361 – 3633Combined sources
Beta strandi366 – 3727Combined sources
Helixi393 – 3997Combined sources
Helixi409 – 4168Combined sources
Helixi422 – 43211Combined sources
Helixi437 – 4437Combined sources
Turni444 – 4485Combined sources
Helixi451 – 4577Combined sources
Helixi465 – 4717Combined sources
Beta strandi478 – 4814Combined sources
Turni486 – 4883Combined sources
Beta strandi492 – 4987Combined sources
Beta strandi501 – 5033Combined sources
Beta strandi510 – 5134Combined sources
Helixi515 – 5239Combined sources
Turni524 – 5274Combined sources
Beta strandi546 – 5516Combined sources
Beta strandi567 – 5704Combined sources
Helixi573 – 5764Combined sources
Helixi577 – 59216Combined sources
Beta strandi601 – 6088Combined sources
Turni610 – 6123Combined sources
Helixi617 – 6259Combined sources
Beta strandi631 – 6399Combined sources
Helixi652 – 6587Combined sources
Helixi660 – 66910Combined sources
Beta strandi673 – 6797Combined sources
Helixi681 – 69919Combined sources
Helixi703 – 71513Combined sources
Beta strandi718 – 7236Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QTLX-ray1.90A192-725[»]
2QTZX-ray1.90A192-725[»]
ProteinModelPortaliQ9UBK8.
SMRiQ9UBK8. Positions 19-725.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UBK8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 174143Flavodoxin-likePROSITE-ProRule annotationAdd
BLAST
Domaini298 – 560263FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni193 – 27482HingeAdd
BLAST

Sequence similaritiesi

Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
Contains 1 flavodoxin-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0369.
GeneTreeiENSGT00620000087711.
HOGENOMiHOG000007485.
HOVERGENiHBG108376.
InParanoidiQ9UBK8.
KOiK00597.
OMAiLAFPSCQ.
OrthoDBiEOG7NCV31.
PhylomeDBiQ9UBK8.
TreeFamiTF105716.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
InterProiIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform A (identifier: Q9UBK8-1) [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
MGAASVRAGA RLVEVALCSF TVTCLEVMRR FLLLYATQQG QAKAIAEEIC
60 70 80 90 100
EQAVVHGFSA DLHCISESDK YDLKTETAPL VVVVSTTGTG DPPDTARKFV
110 120 130 140 150
KEIQNQTLPV DFFAHLRYGL LGLGDSEYTY FCNGGKIIDK RLQELGARHF
160 170 180 190 200
YDTGHADDCV GLELVVEPWI AGLWPALRKH FRSSRGQEEI SGALPVASPA
210 220 230 240 250
SSRTDLVKSE LLHIESQVEL LRFDDSGRKD SEVLKQNAVN SNQSNVVIED
260 270 280 290 300
FESSLTRSVP PLSQASLNIP GLPPEYLQVH LQESLGQEES QVSVTSADPV
310 320 330 340 350
FQVPISKAVQ LTTNDAIKTT LLVELDISNT DFSYQPGDAF SVICPNSDSE
360 370 380 390 400
VQSLLQRLQL EDKREHCVLL KIKADTKKKG ATLPQHIPAG CSLQFIFTWC
410 420 430 440 450
LEIRAIPKKA FLRALVDYTS DSAEKRRLQE LCSKQGAADY SRFVRDACAC
460 470 480 490 500
LLDLLLAFPS CQPPLSLLLE HLPKLQPRPY SCASSSLFHP GKLHFVFNIV
510 520 530 540 550
EFLSTATTEV LRKGVCTGWL ALLVASVLQP NIHASHEDSG KALAPKISIS
560 570 580 590 600
PRTTNSFHLP DDPSIPIIMV GPGTGIAPFI GFLQHREKLQ EQHPDGNFGA
610 620 630 640 650
MWLFFGCRHK DRDYLFRKEL RHFLKHGILT HLKVSFSRDA PVGEEEAPAK
660 670 680 690 700
YVQDNIQLHG QQVARILLQE NGHIYVCGDA KNMAKDVHDA LVQIISKEVG
710 720
VEKLEAMKTL ATLKEEKRYL QDIWS
Length:725
Mass (Da):80,410
Last modified:May 18, 2010 - v3
Checksum:iC3EF82DAC388BAF1
GO
Isoform B (identifier: Q9UBK8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-27: Missing.

Show »
Length:698
Mass (Da):77,674
Checksum:iD4B394F0B24A07E5
GO
Isoform C (identifier: Q9UBK8-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-27: Missing.
     71-85: YDLKTETAPLVVVVS → VSVIQNTPTFAMGGR
     86-725: Missing.

Show »
Length:58
Mass (Da):6,368
Checksum:i5FDB3101DE6A9453
GO

Polymorphismi

Variant Met-49 has been associated with an increased risk for spina bifida and may be associated with chromosomal non-disjunction and Down syndrome.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti49 – 491I → M May be associated with susceptibility to folate-sensitive NTD.
Corresponds to variant rs1801394 [ dbSNP | Ensembl ].
VAR_012836
Natural varianti81 – 811Missing in HMAE. 1 Publication
VAR_012837
Natural varianti83 – 831V → M in HMAE. 1 Publication
VAR_012838
Natural varianti156 – 1561A → T in HMAE. 1 Publication
VAR_012839
Natural varianti202 – 2021S → L.2 Publications
Corresponds to variant rs1532268 [ dbSNP | Ensembl ].
VAR_034595
Natural varianti284 – 2841S → T.
Corresponds to variant rs2303080 [ dbSNP | Ensembl ].
VAR_034596
Natural varianti360 – 3601L → V.1 Publication
Corresponds to variant rs10064631 [ dbSNP | Ensembl ].
VAR_012840
Natural varianti377 – 3771K → R.
Corresponds to variant rs162036 [ dbSNP | Ensembl ].
VAR_034597
Natural varianti432 – 4321C → R in HMAE. 1 Publication
VAR_012841
Natural varianti442 – 4421R → C.
Corresponds to variant rs2287780 [ dbSNP | Ensembl ].
VAR_034598
Natural varianti477 – 4771P → R.
Corresponds to variant rs16879334 [ dbSNP | Ensembl ].
VAR_034599
Natural varianti514 – 5141G → R in HMAE. 1 Publication
VAR_012842
Natural varianti542 – 5421A → V.
Corresponds to variant rs16879355 [ dbSNP | Ensembl ].
VAR_056947
Natural varianti581 – 5811G → R in HMAE. 1 Publication
VAR_015731
Natural varianti603 – 6031Missing in HMAE. 1 Publication
VAR_012843
Natural varianti622 – 6221H → Y.
Corresponds to variant rs10380 [ dbSNP | Ensembl ].
VAR_014944

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2727Missing in isoform B and isoform C. 3 PublicationsVSP_003910Add
BLAST
Alternative sequencei71 – 8515YDLKT…VVVVS → VSVIQNTPTFAMGGR in isoform C. 2 PublicationsVSP_003911Add
BLAST
Alternative sequencei86 – 725640Missing in isoform C. 2 PublicationsVSP_003912Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF121213
, AF121202, AF121203, AF121204, AF121205, AF121206, AF121207, AF121208, AF121209, AF121210, AF121211, AF121212 Genomic DNA. Translation: AAF17303.1.
AF121214 mRNA. Translation: AAF16876.1.
AF121213
, AF121202, AF121203, AF121204, AF121205, AF121206, AF121207, AF121208, AF121209, AF121210, AF121211, AF121212 Genomic DNA. Translation: AAF17304.1.
AF025794 mRNA. Translation: AAC39667.1.
AC010346 Genomic DNA. No translation available.
AC025174 Genomic DNA. No translation available.
BC054816 mRNA. Translation: AAH54816.2.
BC109216 mRNA. Translation: AAI09217.1.
CCDSiCCDS3874.1. [Q9UBK8-1]
CCDS47190.1. [Q9UBK8-2]
RefSeqiNP_002445.2. NM_002454.2. [Q9UBK8-2]
NP_076915.2. NM_024010.2. [Q9UBK8-1]
UniGeneiHs.481551.

Genome annotation databases

EnsembliENST00000264668; ENSP00000264668; ENSG00000124275. [Q9UBK8-1]
ENST00000440940; ENSP00000402510; ENSG00000124275. [Q9UBK8-2]
ENST00000510279; ENSP00000427200; ENSG00000124275. [Q9UBK8-3]
ENST00000514369; ENSP00000426132; ENSG00000124275. [Q9UBK8-3]
GeneIDi4552.
KEGGihsa:4552.
UCSCiuc003jed.3. human. [Q9UBK8-1]

Polymorphism databases

DMDMi296439300.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF121213
, AF121202 , AF121203 , AF121204 , AF121205 , AF121206 , AF121207 , AF121208 , AF121209 , AF121210 , AF121211 , AF121212 Genomic DNA. Translation: AAF17303.1 .
AF121214 mRNA. Translation: AAF16876.1 .
AF121213
, AF121202 , AF121203 , AF121204 , AF121205 , AF121206 , AF121207 , AF121208 , AF121209 , AF121210 , AF121211 , AF121212 Genomic DNA. Translation: AAF17304.1 .
AF025794 mRNA. Translation: AAC39667.1 .
AC010346 Genomic DNA. No translation available.
AC025174 Genomic DNA. No translation available.
BC054816 mRNA. Translation: AAH54816.2 .
BC109216 mRNA. Translation: AAI09217.1 .
CCDSi CCDS3874.1. [Q9UBK8-1 ]
CCDS47190.1. [Q9UBK8-2 ]
RefSeqi NP_002445.2. NM_002454.2. [Q9UBK8-2 ]
NP_076915.2. NM_024010.2. [Q9UBK8-1 ]
UniGenei Hs.481551.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2QTL X-ray 1.90 A 192-725 [» ]
2QTZ X-ray 1.90 A 192-725 [» ]
ProteinModelPortali Q9UBK8.
SMRi Q9UBK8. Positions 19-725.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110645. 5 interactions.
STRINGi 9606.ENSP00000264668.

Chemistry

DrugBanki DB00115. Cyanocobalamin.
DB00200. Hydroxocobalamin.
DB00134. L-Methionine.

PTM databases

PhosphoSitei Q9UBK8.

Polymorphism databases

DMDMi 296439300.

Proteomic databases

MaxQBi Q9UBK8.
PaxDbi Q9UBK8.
PRIDEi Q9UBK8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264668 ; ENSP00000264668 ; ENSG00000124275 . [Q9UBK8-1 ]
ENST00000440940 ; ENSP00000402510 ; ENSG00000124275 . [Q9UBK8-2 ]
ENST00000510279 ; ENSP00000427200 ; ENSG00000124275 . [Q9UBK8-3 ]
ENST00000514369 ; ENSP00000426132 ; ENSG00000124275 . [Q9UBK8-3 ]
GeneIDi 4552.
KEGGi hsa:4552.
UCSCi uc003jed.3. human. [Q9UBK8-1 ]

Organism-specific databases

CTDi 4552.
GeneCardsi GC05P007851.
GeneReviewsi MTRR.
H-InvDB HIX0031952.
HGNCi HGNC:7473. MTRR.
HPAi HPA038113.
MIMi 236270. phenotype.
601634. phenotype.
602568. gene.
neXtProti NX_Q9UBK8.
Orphaneti 2169. Methylcobalamin deficiency type cblE.
PharmGKBi PA31277.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0369.
GeneTreei ENSGT00620000087711.
HOGENOMi HOG000007485.
HOVERGENi HBG108376.
InParanoidi Q9UBK8.
KOi K00597.
OMAi LAFPSCQ.
OrthoDBi EOG7NCV31.
PhylomeDBi Q9UBK8.
TreeFami TF105716.

Enzyme and pathway databases

BioCyci MetaCyc:HS04756-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.
SABIO-RK Q9UBK8.

Miscellaneous databases

EvolutionaryTracei Q9UBK8.
GeneWikii MTRR_(gene).
GenomeRNAii 4552.
NextBioi 17541.
PROi Q9UBK8.
SOURCEi Search...

Gene expression databases

Bgeei Q9UBK8.
CleanExi HS_MTRR.
ExpressionAtlasi Q9UBK8. baseline and differential.
Genevestigatori Q9UBK8.

Family and domain databases

Gene3Di 1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
InterProi IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view ]
Pfami PF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view ]
PRINTSi PR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMi SSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEi PS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, expression and physical mapping of the human methionine synthase reductase gene."
    Leclerc D., Odievre M.-H., Wu Q., Wilson A., Huizenga J., Rozen R., Scherer S.W., Gravel R.A.
    Gene 240:75-88(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A; B AND C), VARIANT LEU-202.
  2. "Cloning and mapping of a cDNA for methionine synthase reductase, a flavoprotein defective in patients with homocystinuria."
    Leclerc D., Wilson A., Dumas R., Gafuik C., Song D., Watkins D., Heng H.H.Q., Rommens J.M., Scherer S.W., Rosenblatt D.S., Gravel R.A.
    Proc. Natl. Acad. Sci. U.S.A. 95:3059-3064(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C), VARIANT LEU-202, VARIANT HMAE LEU-603 DEL.
  3. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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 A AND B).
    Tissue: Lung.
  5. "Restricted role for methionine synthase reductase defined by subcellular localization."
    Froese D.S., Wu X., Zhang J., Dumas R., Schoel W.M., Amrein M., Gravel R.A.
    Mol. Genet. Metab. 94:68-77(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION (ISOFORM A).
  6. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Mechanism of coenzyme binding to human methionine synthase reductase revealed through the crystal structure of the FNR-like module and isothermal titration calorimetry."
    Wolthers K.R., Lou X., Toogood H.S., Leys D., Scrutton N.S.
    Biochemistry 46:11833-11844(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 192-725 IN COMPLEX WITH FAD AND NADP, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, FUNCTION.
  9. "Molecular basis for methionine synthase reductase deficiency in patients belonging to the cblE complementation group of disorders in folate/cobalamin metabolism."
    Wilson A., Leclerc D., Rosenblatt D.S., Gravel R.A.
    Hum. Mol. Genet. 8:2009-2016(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HMAE VAL-81 DEL; MET-83; THR-156; ARG-432; ARG-514 AND ARG-581, VARIANT VAL-360.
  10. "A common variant in methionine synthase reductase combined with low cobalamin (vitamin B12) increases risk for spina bifida."
    Wilson A., Platt R., Wu Q., Leclerc D., Christensen B., Yang H., Gravel R.A., Rozen R.
    Mol. Genet. Metab. 67:317-323(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION OF VARIANT MET-49 WITH SUSCEPTIBILITY TO FS-NTD.
  11. "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 MET-49 WITH SUSCEPTIBILITY TO FS-NTD.
  12. "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 VARIANTS MET-49; LEU-202 AND ARG-377 WITH SUSCEPTIBILITY TO FS-NTD.

Entry informationi

Entry nameiMTRR_HUMAN
AccessioniPrimary (citable) accession number: Q9UBK8
Secondary accession number(s): O60471, Q32MA9, Q7Z4M8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: May 18, 2010
Last modified: October 29, 2014
This is version 143 of the entry and version 3 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3