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Protein

Monofunctional C1-tetrahydrofolate synthase, mitochondrial

Gene

MTHFD1L

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

Functioni

May provide the missing metabolic reaction required to link the mitochondria and the cytoplasm in the mammalian model of one-carbon folate metabolism in embryonic an transformed cells complementing thus the enzymatic activities of MTHFD2.By similarity

Catalytic activityi

ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate.

Kineticsi

  1. KM=500 µM for THF monoglutamate1 Publication
  2. KM=16 µM for THF triglutamate1 Publication
  3. KM=3.6 µM for THF pentaglutamate1 Publication

    Pathway: tetrahydrofolate interconversion

    This protein is involved in the pathway tetrahydrofolate interconversion, which is part of One-carbon metabolism.
    View all proteins of this organism that are known to be involved in the pathway tetrahydrofolate interconversion and in One-carbon metabolism.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi423 – 4308ATPBy similarity

    GO - Molecular functioni

    • ATP binding Source: BHF-UCL
    • formate-tetrahydrofolate ligase activity Source: BHF-UCL
    • protein homodimerization activity Source: BHF-UCL

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    One-carbon metabolism

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi6.3.4.3. 2681.
    UniPathwayiUPA00193.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Monofunctional C1-tetrahydrofolate synthase, mitochondrial (EC:6.3.4.3)
    Alternative name(s):
    Formyltetrahydrofolate synthetase
    Gene namesi
    Name:MTHFD1L
    Synonyms:FTHFSDC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:21055. MTHFD1L.

    Subcellular locationi

    • Mitochondrion 1 Publication

    GO - Cellular componenti

    • membrane Source: UniProtKB
    • mitochondrion Source: BHF-UCL
    Complete GO annotation...

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134927803.

    Polymorphism and mutation databases

    BioMutaiMTHFD1L.
    DMDMi74749360.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3131Mitochondrion1 PublicationAdd
    BLAST
    Chaini32 – 978947Monofunctional C1-tetrahydrofolate synthase, mitochondrialPRO_0000343177Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei189 – 1891N6-acetyllysine; alternate1 Publication
    Modified residuei189 – 1891N6-succinyllysine; alternateBy similarity
    Modified residuei596 – 5961N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ6UB35.
    PaxDbiQ6UB35.
    PRIDEiQ6UB35.

    PTM databases

    PhosphoSiteiQ6UB35.

    Expressioni

    Tissue specificityi

    Detected in most tissues, highest expression found in placenta, thymus and brain. Low expression is found in liver and skeletal muscle. Up-regulated in colon adenocarcinoma.2 Publications

    Gene expression databases

    BgeeiQ6UB35.
    CleanExiHS_MTHFD1L.
    ExpressionAtlasiQ6UB35. baseline and differential.
    GenevisibleiQ6UB35. HS.

    Organism-specific databases

    HPAiHPA015006.
    HPA029040.
    HPA029041.
    HPA050052.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CASP4P496621EBI-1046835,EBI-1057327
    MAGED1Q9Y5V31EBI-1046835,EBI-716006
    WDR8Q9P2S51EBI-1046835,EBI-1054904

    Protein-protein interaction databases

    BioGridi117409. 13 interactions.
    IntActiQ6UB35. 2 interactions.
    STRINGi9606.ENSP00000356290.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6UB35.
    SMRiQ6UB35. Positions 83-295, 359-978.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni31 – 348318Methylenetetrahydrofolate dehydrogenase and cyclohydrolaseAdd
    BLAST
    Regioni349 – 978630Formyltetrahydrofolate synthetaseAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi34 – 429Poly-Gly

    Domaini

    This monofunctional enzyme consists of two major domains: an N-terminal inactive methylene-THF dehydrogenase and cyclohydrolase domain and an active larger formyl-THF synthetase C-terminal domain.

    Sequence similaritiesi

    In the N-terminal section; belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.Curated
    In the C-terminal section; belongs to the formate--tetrahydrofolate ligase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0190.
    GeneTreeiENSGT00790000123036.
    HOVERGENiHBG004916.
    InParanoidiQ6UB35.
    KOiK13402.
    OMAiLHENTQT.
    OrthoDBiEOG76T9QN.
    PhylomeDBiQ6UB35.
    TreeFamiTF300623.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    3.40.50.720. 2 hits.
    HAMAPiMF_01543. FTHFS.
    InterProiIPR000559. Formate_THF_ligase.
    IPR020628. Formate_THF_ligase_CS.
    IPR016040. NAD(P)-bd_dom.
    IPR027417. P-loop_NTPase.
    IPR000672. THF_DH/CycHdrlase.
    IPR020630. THF_DH/CycHdrlase_cat_dom.
    IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
    [Graphical view]
    PfamiPF01268. FTHFS. 1 hit.
    PF00763. THF_DHG_CYH. 1 hit.
    PF02882. THF_DHG_CYH_C. 1 hit.
    [Graphical view]
    PRINTSiPR00085. THFDHDRGNASE.
    SUPFAMiSSF52540. SSF52540. 2 hits.
    PROSITEiPS00721. FTHFS_1. 1 hit.
    PS00722. FTHFS_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

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

    Isoform 1 (identifier: Q6UB35-1) [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
    MGTRLPLVLR QLRRPPQPPG PPRRLRVPCR ASSGGGGGGG GGREGLLGQR
    60 70 80 90 100
    RPQDGQARSS CSPGGRTPAA RDSIVREVIQ NSKEVLSLLQ EKNPAFKPVL
    110 120 130 140 150
    AIIQAGDDNL MQEINQNLAE EAGLNITHIC LPPDSSEAEI IDEILKINED
    160 170 180 190 200
    TRVHGLALQI SENLFSNKVL NALKPEKDVD GVTDINLGKL VRGDAHECFV
    210 220 230 240 250
    SPVAKAVIEL LEKSGVNLDG KKILVVGAHG SLEAALQCLF QRKGSMTMSI
    260 270 280 290 300
    QWKTRQLQSK LHEADIVVLG SPKPEEIPLT WIQPGTTVLN CSHDFLSGKV
    310 320 330 340 350
    GCGSPRIHFG GLIEEDDVIL LAAALRIQNM VSSGRRWLRE QQHRRWRLHC
    360 370 380 390 400
    LKLQPLSPVP SDIEISRGQT PKAVDVLAKE IGLLADEIEI YGKSKAKVRL
    410 420 430 440 450
    SVLERLKDQA DGKYVLVAGI TPTPLGEGKS TVTIGLVQAL TAHLNVNSFA
    460 470 480 490 500
    CLRQPSQGPT FGVKGGAAGG GYAQVIPMEE FNLHLTGDIH AITAANNLLA
    510 520 530 540 550
    AAIDTRILHE NTQTDKALYN RLVPLVNGVR EFSEIQLARL KKLGINKTDP
    560 570 580 590 600
    STLTEEEVSK FARLDIDPST ITWQRVLDTN DRFLRKITIG QGNTEKGHYR
    610 620 630 640 650
    QAQFDIAVAS EIMAVLALTD SLADMKARLG RMVVASDKSG QPVTADDLGV
    660 670 680 690 700
    TGALTVLMKD AIKPNLMQTL EGTPVFVHAG PFANIAHGNS SVLADKIALK
    710 720 730 740 750
    LVGEEGFVVT EAGFGADIGM EKFFNIKCRA SGLVPNVVVL VATVRALKMH
    760 770 780 790 800
    GGGPSVTAGV PLKKEYTEEN IQLVADGCCN LQKQIQITQL FGVPVVVALN
    810 820 830 840 850
    VFKTDTRAEI DLVCELAKRA GAFDAVPCYH WSVGGKGSVD LARAVREAAS
    860 870 880 890 900
    KRSRFQFLYD VQVPIVDKIR TIAQAVYGAK DIELSPEAQA KIDRYTQQGF
    910 920 930 940 950
    GNLPICMAKT HLSLSHQPDK KGVPRDFILP ISDVRASIGA GFIYPLVGTM
    960 970
    STMPGLPTRP CFYDIDLDTE TEQVKGLF
    Length:978
    Mass (Da):105,790
    Last modified:July 5, 2004 - v1
    Checksum:i7D655CD8D2503378
    GO
    Isoform 2 (identifier: Q6UB35-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         261-275: LHEADIVVLGSPKPE → TESRSVTRLECRRVI
         276-978: Missing.

    Show »
    Length:275
    Mass (Da):29,804
    Checksum:iAA044C3A5C698249
    GO

    Sequence cautioni

    The sequence AAH08629.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence BAB15009.1 differs from that shown. Reason: Erroneous initiation. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti79 – 791I → V in AAI10320 (PubMed:15489334).Curated
    Sequence conflicti870 – 8701R → M in BAB15009 (PubMed:14702039).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti444 – 4441L → R in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_044346

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei261 – 27515LHEAD…SPKPE → TESRSVTRLECRRVI in isoform 2. 1 PublicationVSP_034565Add
    BLAST
    Alternative sequencei276 – 978703Missing in isoform 2. 1 PublicationVSP_034566Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY374130 mRNA. Translation: AAQ82696.1.
    AY374131 mRNA. Translation: AAQ82697.1.
    AB127387 mRNA. Translation: BAD93193.1.
    CH471051 Genomic DNA. Translation: EAW47762.1.
    AL035086, AL049694, AL133260 Genomic DNA. Translation: CAI42794.1.
    AL133260, AL035086, AL049694 Genomic DNA. Translation: CAI95678.1.
    AL049694, AL035086, AL133260 Genomic DNA. Translation: CAI95774.1.
    AL117452 mRNA. Translation: CAB55934.1.
    BC008629 mRNA. Translation: AAH08629.1. Different initiation.
    BC017477 mRNA. Translation: AAH17477.2.
    BC110319 mRNA. Translation: AAI10320.1.
    AK024798 mRNA. Translation: BAB15009.1. Different initiation.
    CCDSiCCDS5228.1. [Q6UB35-1]
    CCDS56457.1. [Q6UB35-2]
    PIRiT17244.
    RefSeqiNP_001229696.1. NM_001242767.1.
    NP_001229697.1. NM_001242768.1.
    NP_001229698.1. NM_001242769.1. [Q6UB35-2]
    NP_056255.2. NM_015440.4. [Q6UB35-1]
    UniGeneiHs.591343.

    Genome annotation databases

    EnsembliENST00000367307; ENSP00000356276; ENSG00000120254. [Q6UB35-2]
    ENST00000367321; ENSP00000356290; ENSG00000120254. [Q6UB35-1]
    GeneIDi25902.
    KEGGihsa:25902.
    UCSCiuc003qoa.2. human. [Q6UB35-2]
    uc003qob.3. human. [Q6UB35-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY374130 mRNA. Translation: AAQ82696.1.
    AY374131 mRNA. Translation: AAQ82697.1.
    AB127387 mRNA. Translation: BAD93193.1.
    CH471051 Genomic DNA. Translation: EAW47762.1.
    AL035086, AL049694, AL133260 Genomic DNA. Translation: CAI42794.1.
    AL133260, AL035086, AL049694 Genomic DNA. Translation: CAI95678.1.
    AL049694, AL035086, AL133260 Genomic DNA. Translation: CAI95774.1.
    AL117452 mRNA. Translation: CAB55934.1.
    BC008629 mRNA. Translation: AAH08629.1. Different initiation.
    BC017477 mRNA. Translation: AAH17477.2.
    BC110319 mRNA. Translation: AAI10320.1.
    AK024798 mRNA. Translation: BAB15009.1. Different initiation.
    CCDSiCCDS5228.1. [Q6UB35-1]
    CCDS56457.1. [Q6UB35-2]
    PIRiT17244.
    RefSeqiNP_001229696.1. NM_001242767.1.
    NP_001229697.1. NM_001242768.1.
    NP_001229698.1. NM_001242769.1. [Q6UB35-2]
    NP_056255.2. NM_015440.4. [Q6UB35-1]
    UniGeneiHs.591343.

    3D structure databases

    ProteinModelPortaliQ6UB35.
    SMRiQ6UB35. Positions 83-295, 359-978.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi117409. 13 interactions.
    IntActiQ6UB35. 2 interactions.
    STRINGi9606.ENSP00000356290.

    PTM databases

    PhosphoSiteiQ6UB35.

    Polymorphism and mutation databases

    BioMutaiMTHFD1L.
    DMDMi74749360.

    Proteomic databases

    MaxQBiQ6UB35.
    PaxDbiQ6UB35.
    PRIDEiQ6UB35.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000367307; ENSP00000356276; ENSG00000120254. [Q6UB35-2]
    ENST00000367321; ENSP00000356290; ENSG00000120254. [Q6UB35-1]
    GeneIDi25902.
    KEGGihsa:25902.
    UCSCiuc003qoa.2. human. [Q6UB35-2]
    uc003qob.3. human. [Q6UB35-1]

    Organism-specific databases

    CTDi25902.
    GeneCardsiGC06P151186.
    H-InvDBHIX0008064.
    HIX0023219.
    HIX0058616.
    HGNCiHGNC:21055. MTHFD1L.
    HPAiHPA015006.
    HPA029040.
    HPA029041.
    HPA050052.
    MIMi611427. gene.
    neXtProtiNX_Q6UB35.
    PharmGKBiPA134927803.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0190.
    GeneTreeiENSGT00790000123036.
    HOVERGENiHBG004916.
    InParanoidiQ6UB35.
    KOiK13402.
    OMAiLHENTQT.
    OrthoDBiEOG76T9QN.
    PhylomeDBiQ6UB35.
    TreeFamiTF300623.

    Enzyme and pathway databases

    UniPathwayiUPA00193.
    BRENDAi6.3.4.3. 2681.

    Miscellaneous databases

    ChiTaRSiMTHFD1L. human.
    GeneWikiiMTHFD1L.
    GenomeRNAii25902.
    NextBioi47370.
    PROiQ6UB35.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ6UB35.
    CleanExiHS_MTHFD1L.
    ExpressionAtlasiQ6UB35. baseline and differential.
    GenevisibleiQ6UB35. HS.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    3.40.50.720. 2 hits.
    HAMAPiMF_01543. FTHFS.
    InterProiIPR000559. Formate_THF_ligase.
    IPR020628. Formate_THF_ligase_CS.
    IPR016040. NAD(P)-bd_dom.
    IPR027417. P-loop_NTPase.
    IPR000672. THF_DH/CycHdrlase.
    IPR020630. THF_DH/CycHdrlase_cat_dom.
    IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
    [Graphical view]
    PfamiPF01268. FTHFS. 1 hit.
    PF00763. THF_DHG_CYH. 1 hit.
    PF02882. THF_DHG_CYH_C. 1 hit.
    [Graphical view]
    PRINTSiPR00085. THFDHDRGNASE.
    SUPFAMiSSF52540. SSF52540. 2 hits.
    PROSITEiPS00721. FTHFS_1. 1 hit.
    PS00722. FTHFS_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Human mitochondrial C1-tetrahydrofolate synthase: gene structure, tissue distribution of the mRNA, and immunolocalization in Chinese hamster ovary calls."
      Prasannan P., Pike S., Peng K., Shane B., Appling D.R.
      J. Biol. Chem. 278:43178-43187(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. "A novel mitochondrial C1-tetrahydrofolate synthetase is upregulated in human colon adenocarcinoma."
      Sugiura T., Nagano Y., Inoue T., Hirotani K.
      Biochem. Biophys. Res. Commun. 315:204-211(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Testis.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Enzymatic characterization of human mitochondrial C1-tetrahydrofolate synthase."
      Walkup A.S., Appling D.R.
      Arch. Biochem. Biophys. 442:196-205(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 32-66, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 62-978 (ISOFORM 1).
      Tissue: Uterus.
    7. "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] OF 79-978 (ISOFORM 1).
      Tissue: Cervix, Eye and Muscle.
    8. Bienvenut W.V., Matallanas D., Cooper W.N., Kolch W.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 522-530; 564-575 AND 926-935, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Mammary carcinoma.
    9. "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 591-978 (ISOFORM 1).
    10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-444.

    Entry informationi

    Entry nameiC1TM_HUMAN
    AccessioniPrimary (citable) accession number: Q6UB35
    Secondary accession number(s): Q2TBF3
    , Q8WVW0, Q96HG8, Q9H789, Q9UFU8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 2008
    Last sequence update: July 5, 2004
    Last modified: June 24, 2015
    This is version 109 of the entry and version 1 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

    May participate in the progression of colorectal cancer by conferring growth advantage. Could be a new molecular target for cancer therapy.

    Caution

    This enzyme lacks methylenetetrahydrofolate dehydrogenase (EC 1.5.1.5) and ethenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) activities. An enzyme performing these two complementary activities has not been found in adult mitochondrial tissues; MTHFD2, which performs these two activities, was found in developing tissues only.Curated
    Was originally thought to be a trifunctional enzyme but only a formyltetrahydrofolate synthetase activity was detected and not a dehydrogenase/cyclohydrogenase activity.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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. 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.