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Q96DP5

- FMT_HUMAN

UniProt

Q96DP5 - FMT_HUMAN

Protein

Methionyl-tRNA formyltransferase, mitochondrial

Gene

MTFMT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (27 Jan 2003)
      Previous versions | rss
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    Functioni

    Formylates methionyl-tRNA in mitochondria. A single tRNA(Met) gene gives rise to both an initiator and an elongator species via an unknown mechanism By similarity.By similarity

    Catalytic activityi

    10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet).

    GO - Molecular functioni

    1. methionyl-tRNA formyltransferase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Protein biosynthesis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionyl-tRNA formyltransferase, mitochondrial (EC:2.1.2.9)
    Short name:
    MtFMT
    Gene namesi
    Name:MTFMT
    Synonyms:FMT, FMT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:29666. MTFMT.

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Combined oxidative phosphorylation deficiency 15 (COXPD15) [MIM:614947]: An autosomal recessive, mitochondrial, neurologic disorder characterized by features of Leigh syndrome and combined oxidative phosphorylation deficiency. Clinical features include mild global developmental delay, white matter abnormalities, ataxia, incoordination, speech and reading difficulties, T2-weighted hyperintensities in the basal ganglia, corpus callosum, and brainstem.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti125 – 1251S → L in COXPD15. 1 Publication
    VAR_069303
    Natural varianti209 – 2091S → L in COXPD15; also found in Leigh syndrome. 2 Publications
    VAR_069304
    Leigh syndrome (LS) [MIM:256000]: An early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Disease mutation, Leigh syndrome

    Organism-specific databases

    MIMi256000. phenotype.
    614947. phenotype.
    Orphaneti319524. Combined oxidative phosphorylation defect type 15.
    2609. Isolated NADH-CoQ reductase deficiency.
    PharmGKBiPA142671304.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 389Methionyl-tRNA formyltransferase, mitochondrialPRO_0000010093
    Transit peptidei1 – ?MitochondrionSequence Analysis

    Proteomic databases

    MaxQBiQ96DP5.
    PaxDbiQ96DP5.
    PRIDEiQ96DP5.

    PTM databases

    PhosphoSiteiQ96DP5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ96DP5.
    BgeeiQ96DP5.
    CleanExiHS_MTFMT.
    GenevestigatoriQ96DP5.

    Organism-specific databases

    HPAiHPA040710.

    Interactioni

    Protein-protein interaction databases

    BioGridi125820. 3 interactions.
    STRINGi9606.ENSP00000220058.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96DP5.
    SMRiQ96DP5. Positions 49-347.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    Composed of an N- and a C-terminal domain. The N-terminal domain carries the tetrahydrofolate (THF)-binding site and the C-terminal domain is presumably involved in positioning the Met-tRNA substrate for the formylation reaction.

    Sequence similaritiesi

    Belongs to the Fmt family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0223.
    HOGENOMiHOG000261177.
    HOVERGENiHBG031552.
    InParanoidiQ96DP5.
    KOiK00604.
    OMAiKAQAQNE.
    OrthoDBiEOG7CZK68.
    PhylomeDBiQ96DP5.
    TreeFamiTF323405.

    Family and domain databases

    Gene3Di3.40.50.170. 1 hit.
    InterProiIPR005794. Fmt.
    IPR005793. Formyl_trans_C.
    IPR002376. Formyl_transf_N.
    IPR011034. Formyl_transferase_C-like.
    IPR015518. Met_tRNA_Form_TA-like.
    [Graphical view]
    PANTHERiPTHR11138. PTHR11138. 1 hit.
    PfamiPF02911. Formyl_trans_C. 1 hit.
    PF00551. Formyl_trans_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50486. SSF50486. 1 hit.
    SSF53328. SSF53328. 1 hit.
    TIGRFAMsiTIGR00460. fmt. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q96DP5-1 [UniParc]FASTAAdd to Basket

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    MRVLVRRCWG PPLAHGARRG RPSPQWRALA RLGWEDCRDS RVREKPPWRV    50
    LFFGTDQFAR EALRALHAAR ENKEEELIDK LEVVTMPSPS PKGLPVKQYA 100
    VQSQLPVYEW PDVGSGEYDV GVVASFGRLL NEALILKFPY GILNVHPSCL 150
    PRWRGPAPVI HTVLHGDTVT GVTIMQIRPK RFDVGPILKQ ETVPVPPKST 200
    AKELEAVLSR LGANMLISVL KNLPESLSNG RQQPMEGATY APKISAGTSC 250
    IKWEEQTSEQ IFRLYRAIGN IIPLQTLWMA NTIKLLDLVE VNSSVLADPK 300
    LTGQALIPGS VIYHKQSQIL LVYCKDGWIG VRSVMLKKSL TATDFYNGYL 350
    HPWYQKNSQA QPSQCRFQTL RLPTKKKQKK TVAMQQCIE 389
    Length:389
    Mass (Da):43,832
    Last modified:January 27, 2003 - v2
    Checksum:iEBBE92142AB954E0
    GO

    Sequence cautioni

    The sequence AAH16630.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAH33687.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAB70984.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti5 – 51V → A.
    Corresponds to variant rs2946655 [ dbSNP | Ensembl ].
    VAR_059289
    Natural varianti125 – 1251S → L in COXPD15. 1 Publication
    VAR_069303
    Natural varianti209 – 2091S → L in COXPD15; also found in Leigh syndrome. 2 Publications
    VAR_069304

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC016630 mRNA. Translation: AAH16630.2. Different initiation.
    BC033687 mRNA. Translation: AAH33687.1. Different initiation.
    AK055688 mRNA. Translation: BAB70984.1. Different initiation.
    CCDSiCCDS45280.1.
    RefSeqiNP_640335.2. NM_139242.3.
    XP_005254215.1. XM_005254158.2.
    UniGeneiHs.531615.

    Genome annotation databases

    EnsembliENST00000220058; ENSP00000220058; ENSG00000103707.
    ENST00000558460; ENSP00000452646; ENSG00000103707.
    GeneIDi123263.
    KEGGihsa:123263.
    UCSCiuc002aof.4. human.

    Polymorphism databases

    DMDMi27923776.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC016630 mRNA. Translation: AAH16630.2 . Different initiation.
    BC033687 mRNA. Translation: AAH33687.1 . Different initiation.
    AK055688 mRNA. Translation: BAB70984.1 . Different initiation.
    CCDSi CCDS45280.1.
    RefSeqi NP_640335.2. NM_139242.3.
    XP_005254215.1. XM_005254158.2.
    UniGenei Hs.531615.

    3D structure databases

    ProteinModelPortali Q96DP5.
    SMRi Q96DP5. Positions 49-347.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125820. 3 interactions.
    STRINGi 9606.ENSP00000220058.

    Chemistry

    DrugBanki DB00116. Tetrahydrofolic acid.

    PTM databases

    PhosphoSitei Q96DP5.

    Polymorphism databases

    DMDMi 27923776.

    Proteomic databases

    MaxQBi Q96DP5.
    PaxDbi Q96DP5.
    PRIDEi Q96DP5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000220058 ; ENSP00000220058 ; ENSG00000103707 .
    ENST00000558460 ; ENSP00000452646 ; ENSG00000103707 .
    GeneIDi 123263.
    KEGGi hsa:123263.
    UCSCi uc002aof.4. human.

    Organism-specific databases

    CTDi 123263.
    GeneCardsi GC15M065293.
    HGNCi HGNC:29666. MTFMT.
    HPAi HPA040710.
    MIMi 256000. phenotype.
    611766. gene.
    614947. phenotype.
    neXtProti NX_Q96DP5.
    Orphaneti 319524. Combined oxidative phosphorylation defect type 15.
    2609. Isolated NADH-CoQ reductase deficiency.
    PharmGKBi PA142671304.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0223.
    HOGENOMi HOG000261177.
    HOVERGENi HBG031552.
    InParanoidi Q96DP5.
    KOi K00604.
    OMAi KAQAQNE.
    OrthoDBi EOG7CZK68.
    PhylomeDBi Q96DP5.
    TreeFami TF323405.

    Miscellaneous databases

    GeneWikii MTFMT.
    GenomeRNAii 123263.
    NextBioi 81093.
    PROi Q96DP5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96DP5.
    Bgeei Q96DP5.
    CleanExi HS_MTFMT.
    Genevestigatori Q96DP5.

    Family and domain databases

    Gene3Di 3.40.50.170. 1 hit.
    InterProi IPR005794. Fmt.
    IPR005793. Formyl_trans_C.
    IPR002376. Formyl_transf_N.
    IPR011034. Formyl_transferase_C-like.
    IPR015518. Met_tRNA_Form_TA-like.
    [Graphical view ]
    PANTHERi PTHR11138. PTHR11138. 1 hit.
    Pfami PF02911. Formyl_trans_C. 1 hit.
    PF00551. Formyl_trans_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50486. SSF50486. 1 hit.
    SSF53328. SSF53328. 1 hit.
    TIGRFAMsi TIGR00460. fmt. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "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].
      Tissue: Brain and Mammary gland.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-389.
      Tissue: Neuroblastoma.
    3. Cited for: VARIANTS COXPD15 LEU-125 AND LEU-209.
    4. Cited for: VARIANT LS LEU-209.

    Entry informationi

    Entry nameiFMT_HUMAN
    AccessioniPrimary (citable) accession number: Q96DP5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 27, 2003
    Last sequence update: January 27, 2003
    Last modified: October 1, 2014
    This is version 116 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3