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Protein

Methionine synthase reductase

Gene

MTRR

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

Protein has several cofactor binding sites:
  • FAD1 Publication
  • FMN1 Publication

Kineticsi

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

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei318NADP1 Publication1
    Binding sitei686NADP1 Publication1
    Binding sitei724FAD1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi120 – 151FMNPROSITE-ProRule annotationAdd BLAST32
    Nucleotide bindingi478 – 481FAD1 Publication4
    Nucleotide bindingi514 – 517FAD1 Publication4
    Nucleotide bindingi637 – 638NADP1 Publication2
    Nucleotide bindingi651 – 653NADP1 Publication3

    GO - Molecular functioni

    • [methionine synthase] reductase activity Source: UniProtKB
    • aquacobalamin reductase (NADPH) activity Source: CACAO
    • FAD binding Source: BHF-UCL
    • flavin adenine dinucleotide binding Source: UniProtKB
    • FMN binding Source: UniProtKB
    • NADP binding Source: UniProtKB
    • NADPH binding Source: BHF-UCL
    • NADPH-hemoprotein reductase activity Source: BHF-UCL
    • oxidoreductase activity, oxidizing metal ions, NAD or NADP as acceptor Source: UniProtKB

    GO - Biological processi

    • cobalamin metabolic process Source: Reactome
    • DNA methylation Source: UniProtKB
    • folic acid metabolic process Source: UniProtKB
    • homocysteine catabolic process Source: BHF-UCL
    • methionine biosynthetic process Source: BHF-UCL
    • methionine metabolic process Source: UniProtKB
    • methylation Source: Reactome
    • negative regulation of cystathionine beta-synthase activity Source: BHF-UCL
    • oxidation-reduction process Source: UniProtKB
    • S-adenosylmethionine cycle Source: BHF-UCL
    • sulfur amino acid 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.
    ZFISH:HS04756-MONOMER.
    BRENDAi1.16.1.8. 2681.
    ReactomeiR-HSA-156581. Methylation.
    R-HSA-1614635. Sulfur amino acid metabolism.
    R-HSA-196741. Cobalamin (Cbl, vitamin B12) transport and metabolism.
    R-HSA-3359467. Defective MTRR causes methylmalonic aciduria and homocystinuria type cblE.
    R-HSA-3359469. Defective MTR causes methylmalonic aciduria and homocystinuria type cblG.
    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
    Proteomesi
    • UP000005640 Componenti: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:7473. MTRR.

    Subcellular locationi

    Isoform A :

    GO - Cellular componenti

    • cytoplasm Source: HPA
    • cytosol Source: UniProtKB
    • intermediate filament cytoskeleton Source: HPA
    • nucleoplasm Source: HPA
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Homocystinuria-megaloblastic anemia, cblE complementation type (HMAE)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. 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.
    See also OMIM:236270
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_01283781Missing in HMAE. 1 Publication1
    Natural variantiVAR_01283883V → M in HMAE. 1 PublicationCorresponds to variant rs761061866dbSNPEnsembl.1
    Natural variantiVAR_012839156A → T in HMAE. 1 Publication1
    Natural variantiVAR_012841432C → R in HMAE. 1 Publication1
    Natural variantiVAR_012842514G → R in HMAE. 1 PublicationCorresponds to variant rs137853061dbSNPEnsembl.1
    Natural variantiVAR_015731581G → R in HMAE. 1 Publication1
    Natural variantiVAR_012843603Missing in HMAE. 1 Publication1
    Neural tube defects, folate-sensitive (NTDFS)2 Publications
    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

    DisGeNETi4552.
    MalaCardsiMTRR.
    MIMi236270. phenotype.
    601634. phenotype.
    OpenTargetsiENSG00000124275.
    Orphaneti2169. Methylcobalamin deficiency type cblE.
    PharmGKBiPA31277.

    Chemistry databases

    DrugBankiDB00115. Cyanocobalamin.
    DB00200. Hydroxocobalamin.
    DB00134. L-Methionine.

    Polymorphism and mutation databases

    BioMutaiMTRR.
    DMDMi296439300.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000217851 – 725Methionine synthase reductaseAdd BLAST725

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei198PhosphoserineCombined sources1
    Modified residuei216PhosphoserineCombined sources1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    EPDiQ9UBK8.
    MaxQBiQ9UBK8.
    PaxDbiQ9UBK8.
    PeptideAtlasiQ9UBK8.
    PRIDEiQ9UBK8.

    PTM databases

    iPTMnetiQ9UBK8.
    PhosphoSitePlusiQ9UBK8.
    SwissPalmiQ9UBK8.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    BgeeiENSG00000124275.
    CleanExiHS_MTRR.
    ExpressionAtlasiQ9UBK8. baseline and differential.
    GenevisibleiQ9UBK8. HS.

    Organism-specific databases

    HPAiHPA038113.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FLJ13057Q53SE73EBI-10319161,EBI-10172181

    Protein-protein interaction databases

    BioGridi110645. 14 interactors.
    DIPiDIP-61183N.
    IntActiQ9UBK8. 8 interactors.
    STRINGi9606.ENSP00000264668.

    Structurei

    Secondary structure

    1725
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi262 – 264Combined sources3
    Beta strandi277 – 282Combined sources6
    Beta strandi301 – 310Combined sources10
    Beta strandi320 – 326Combined sources7
    Beta strandi339 – 343Combined sources5
    Helixi348 – 357Combined sources10
    Helixi361 – 363Combined sources3
    Beta strandi366 – 372Combined sources7
    Helixi393 – 399Combined sources7
    Helixi409 – 416Combined sources8
    Helixi422 – 432Combined sources11
    Helixi437 – 443Combined sources7
    Turni444 – 448Combined sources5
    Helixi451 – 457Combined sources7
    Helixi465 – 471Combined sources7
    Beta strandi478 – 481Combined sources4
    Turni486 – 488Combined sources3
    Beta strandi492 – 498Combined sources7
    Beta strandi501 – 503Combined sources3
    Beta strandi510 – 513Combined sources4
    Helixi515 – 523Combined sources9
    Turni524 – 527Combined sources4
    Beta strandi546 – 551Combined sources6
    Beta strandi567 – 570Combined sources4
    Helixi573 – 576Combined sources4
    Helixi577 – 592Combined sources16
    Beta strandi601 – 608Combined sources8
    Turni610 – 612Combined sources3
    Helixi617 – 625Combined sources9
    Beta strandi631 – 639Combined sources9
    Helixi652 – 658Combined sources7
    Helixi660 – 669Combined sources10
    Beta strandi673 – 679Combined sources7
    Helixi681 – 699Combined sources19
    Helixi703 – 715Combined sources13
    Beta strandi718 – 723Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2QTLX-ray1.90A192-725[»]
    2QTZX-ray1.90A192-725[»]
    ProteinModelPortaliQ9UBK8.
    SMRiQ9UBK8.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UBK8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini32 – 174Flavodoxin-likePROSITE-ProRule annotationAdd BLAST143
    Domaini298 – 560FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST263

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni193 – 274HingeAdd BLAST82

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiKOG1158. Eukaryota.
    COG0369. LUCA.
    GeneTreeiENSGT00840000129757.
    HOGENOMiHOG000007485.
    HOVERGENiHBG108376.
    InParanoidiQ9UBK8.
    KOiK00597.
    OMAiFSVICPN.
    OrthoDBiEOG091G045Q.
    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-like.
    IPR008254. Flavodoxin/NO_synth.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR029039. Flavoprotein-like_dom.
    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. AlignAdd to basket

    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

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_01283649I → M Polymorphism; may increase risk for spina bifida. 3 PublicationsCorresponds to variant rs1801394dbSNPEnsembl.1
    Natural variantiVAR_01283781Missing in HMAE. 1 Publication1
    Natural variantiVAR_01283883V → M in HMAE. 1 PublicationCorresponds to variant rs761061866dbSNPEnsembl.1
    Natural variantiVAR_012839156A → T in HMAE. 1 Publication1
    Natural variantiVAR_034595202S → L.Combined sources3 PublicationsCorresponds to variant rs1532268dbSNPEnsembl.1
    Natural variantiVAR_034596284S → T.Corresponds to variant rs2303080dbSNPEnsembl.1
    Natural variantiVAR_012840360L → V.1 PublicationCorresponds to variant rs10064631dbSNPEnsembl.1
    Natural variantiVAR_034597377K → R.1 PublicationCorresponds to variant rs162036dbSNPEnsembl.1
    Natural variantiVAR_012841432C → R in HMAE. 1 Publication1
    Natural variantiVAR_034598442R → C.Corresponds to variant rs2287780dbSNPEnsembl.1
    Natural variantiVAR_034599477P → R.Corresponds to variant rs16879334dbSNPEnsembl.1
    Natural variantiVAR_012842514G → R in HMAE. 1 PublicationCorresponds to variant rs137853061dbSNPEnsembl.1
    Natural variantiVAR_056947542A → V.Corresponds to variant rs16879355dbSNPEnsembl.1
    Natural variantiVAR_015731581G → R in HMAE. 1 Publication1
    Natural variantiVAR_012843603Missing in HMAE. 1 Publication1
    Natural variantiVAR_014944622H → Y.Corresponds to variant rs10380dbSNPEnsembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0039101 – 27Missing in isoform B and isoform C. 3 PublicationsAdd BLAST27
    Alternative sequenceiVSP_00391171 – 85YDLKT…VVVVS → VSVIQNTPTFAMGGR in isoform C. 2 PublicationsAdd BLAST15
    Alternative sequenceiVSP_00391286 – 725Missing in isoform C. 2 PublicationsAdd BLAST640

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.4. human. [Q9UBK8-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    The hidden things - Issue 166 of December 2014

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2QTLX-ray1.90A192-725[»]
    2QTZX-ray1.90A192-725[»]
    ProteinModelPortaliQ9UBK8.
    SMRiQ9UBK8.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi110645. 14 interactors.
    DIPiDIP-61183N.
    IntActiQ9UBK8. 8 interactors.
    STRINGi9606.ENSP00000264668.

    Chemistry databases

    DrugBankiDB00115. Cyanocobalamin.
    DB00200. Hydroxocobalamin.
    DB00134. L-Methionine.

    PTM databases

    iPTMnetiQ9UBK8.
    PhosphoSitePlusiQ9UBK8.
    SwissPalmiQ9UBK8.

    Polymorphism and mutation databases

    BioMutaiMTRR.
    DMDMi296439300.

    Proteomic databases

    EPDiQ9UBK8.
    MaxQBiQ9UBK8.
    PaxDbiQ9UBK8.
    PeptideAtlasiQ9UBK8.
    PRIDEiQ9UBK8.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    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.4. human. [Q9UBK8-1]

    Organism-specific databases

    CTDi4552.
    DisGeNETi4552.
    GeneCardsiMTRR.
    GeneReviewsiMTRR.
    H-InvDBHIX0031952.
    HGNCiHGNC:7473. MTRR.
    HPAiHPA038113.
    MalaCardsiMTRR.
    MIMi236270. phenotype.
    601634. phenotype.
    602568. gene.
    neXtProtiNX_Q9UBK8.
    OpenTargetsiENSG00000124275.
    Orphaneti2169. Methylcobalamin deficiency type cblE.
    PharmGKBiPA31277.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG1158. Eukaryota.
    COG0369. LUCA.
    GeneTreeiENSGT00840000129757.
    HOGENOMiHOG000007485.
    HOVERGENiHBG108376.
    InParanoidiQ9UBK8.
    KOiK00597.
    OMAiFSVICPN.
    OrthoDBiEOG091G045Q.
    PhylomeDBiQ9UBK8.
    TreeFamiTF105716.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04756-MONOMER.
    ZFISH:HS04756-MONOMER.
    BRENDAi1.16.1.8. 2681.
    ReactomeiR-HSA-156581. Methylation.
    R-HSA-1614635. Sulfur amino acid metabolism.
    R-HSA-196741. Cobalamin (Cbl, vitamin B12) transport and metabolism.
    R-HSA-3359467. Defective MTRR causes methylmalonic aciduria and homocystinuria type cblE.
    R-HSA-3359469. Defective MTR causes methylmalonic aciduria and homocystinuria type cblG.
    SABIO-RKQ9UBK8.

    Miscellaneous databases

    EvolutionaryTraceiQ9UBK8.
    GeneWikiiMTRR_(gene).
    GenomeRNAii4552.
    PROiQ9UBK8.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000124275.
    CleanExiHS_MTRR.
    ExpressionAtlasiQ9UBK8. baseline and differential.
    GenevisibleiQ9UBK8. HS.

    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-like.
    IPR008254. Flavodoxin/NO_synth.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR029039. Flavoprotein-like_dom.
    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]
    ProtoNetiSearch...

    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: November 2, 2016
    This is version 166 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. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    7. SIMILARITY comments
      Index of protein domains and families

    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 one 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.