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Q6UB35

- C1TM_HUMAN

UniProt

Q6UB35 - C1TM_HUMAN

Protein

Monofunctional C1-tetrahydrofolate synthase, mitochondrial

Gene

MTHFD1L

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    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

    Pathwayi

    Regions

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

    GO - Molecular functioni

    1. ATP binding Source: BHF-UCL
    2. formate-tetrahydrofolate ligase activity Source: BHF-UCL
    3. protein homodimerization activity Source: BHF-UCL

    GO - Biological processi

    1. folic acid-containing compound biosynthetic process Source: InterPro
    2. folic acid-containing compound metabolic process Source: BHF-UCL
    3. formate metabolic process Source: BHF-UCL
    4. one-carbon metabolic process Source: RefGenome
    5. oxidation-reduction process Source: InterPro
    6. tetrahydrofolate interconversion Source: UniProtKB-UniPathway
    7. tetrahydrofolate metabolic process Source: BHF-UCL

    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: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:21055. MTHFD1L.

    Subcellular locationi

    Mitochondrion 1 Publication

    GO - Cellular componenti

    1. membrane Source: UniProtKB
    2. mitochondrion Source: BHF-UCL

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134927803.

    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

    ArrayExpressiQ6UB35.
    BgeeiQ6UB35.
    CleanExiHS_MTHFD1L.
    GenevestigatoriQ6UB35.

    Organism-specific databases

    HPAiHPA015006.

    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. 12 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.
    HOVERGENiHBG004916.
    InParanoidiQ6UB35.
    KOiK13402.
    OMAiVNGVREF.
    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. Align

    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

    MGTRLPLVLR QLRRPPQPPG PPRRLRVPCR ASSGGGGGGG GGREGLLGQR    50
    RPQDGQARSS CSPGGRTPAA RDSIVREVIQ NSKEVLSLLQ EKNPAFKPVL 100
    AIIQAGDDNL MQEINQNLAE EAGLNITHIC LPPDSSEAEI IDEILKINED 150
    TRVHGLALQI SENLFSNKVL NALKPEKDVD GVTDINLGKL VRGDAHECFV 200
    SPVAKAVIEL LEKSGVNLDG KKILVVGAHG SLEAALQCLF QRKGSMTMSI 250
    QWKTRQLQSK LHEADIVVLG SPKPEEIPLT WIQPGTTVLN CSHDFLSGKV 300
    GCGSPRIHFG GLIEEDDVIL LAAALRIQNM VSSGRRWLRE QQHRRWRLHC 350
    LKLQPLSPVP SDIEISRGQT PKAVDVLAKE IGLLADEIEI YGKSKAKVRL 400
    SVLERLKDQA DGKYVLVAGI TPTPLGEGKS TVTIGLVQAL TAHLNVNSFA 450
    CLRQPSQGPT FGVKGGAAGG GYAQVIPMEE FNLHLTGDIH AITAANNLLA 500
    AAIDTRILHE NTQTDKALYN RLVPLVNGVR EFSEIQLARL KKLGINKTDP 550
    STLTEEEVSK FARLDIDPST ITWQRVLDTN DRFLRKITIG QGNTEKGHYR 600
    QAQFDIAVAS EIMAVLALTD SLADMKARLG RMVVASDKSG QPVTADDLGV 650
    TGALTVLMKD AIKPNLMQTL EGTPVFVHAG PFANIAHGNS SVLADKIALK 700
    LVGEEGFVVT EAGFGADIGM EKFFNIKCRA SGLVPNVVVL VATVRALKMH 750
    GGGPSVTAGV PLKKEYTEEN IQLVADGCCN LQKQIQITQL FGVPVVVALN 800
    VFKTDTRAEI DLVCELAKRA GAFDAVPCYH WSVGGKGSVD LARAVREAAS 850
    KRSRFQFLYD VQVPIVDKIR TIAQAVYGAK DIELSPEAQA KIDRYTQQGF 900
    GNLPICMAKT HLSLSHQPDK KGVPRDFILP ISDVRASIGA GFIYPLVGTM 950
    STMPGLPTRP CFYDIDLDTE TEQVKGLF 978
    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.
    The sequence BAB15009.1 differs from that shown. Reason: Erroneous initiation.

    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:
    EMBL
    GenBank
    DDBJ
    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]

    Polymorphism databases

    DMDMi74749360.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS5228.1. [Q6UB35-1 ]
    CCDS56457.1. [Q6UB35-2 ]
    PIRi T17244.
    RefSeqi NP_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 ]
    UniGenei Hs.591343.

    3D structure databases

    ProteinModelPortali Q6UB35.
    SMRi Q6UB35. Positions 83-295, 359-978.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117409. 12 interactions.
    IntActi Q6UB35. 2 interactions.
    STRINGi 9606.ENSP00000356290.

    PTM databases

    PhosphoSitei Q6UB35.

    Polymorphism databases

    DMDMi 74749360.

    Proteomic databases

    MaxQBi Q6UB35.
    PaxDbi Q6UB35.
    PRIDEi Q6UB35.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367307 ; ENSP00000356276 ; ENSG00000120254 . [Q6UB35-2 ]
    ENST00000367321 ; ENSP00000356290 ; ENSG00000120254 . [Q6UB35-1 ]
    GeneIDi 25902.
    KEGGi hsa:25902.
    UCSCi uc003qoa.2. human. [Q6UB35-2 ]
    uc003qob.3. human. [Q6UB35-1 ]

    Organism-specific databases

    CTDi 25902.
    GeneCardsi GC06P151186.
    H-InvDB HIX0008064.
    HIX0023219.
    HIX0058616.
    HGNCi HGNC:21055. MTHFD1L.
    HPAi HPA015006.
    MIMi 611427. gene.
    neXtProti NX_Q6UB35.
    PharmGKBi PA134927803.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0190.
    HOVERGENi HBG004916.
    InParanoidi Q6UB35.
    KOi K13402.
    OMAi VNGVREF.
    OrthoDBi EOG76T9QN.
    PhylomeDBi Q6UB35.
    TreeFami TF300623.

    Enzyme and pathway databases

    UniPathwayi UPA00193 .
    BRENDAi 6.3.4.3. 2681.

    Miscellaneous databases

    ChiTaRSi MTHFD1L. human.
    GeneWikii MTHFD1L.
    GenomeRNAii 25902.
    NextBioi 47370.
    PROi Q6UB35.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6UB35.
    Bgeei Q6UB35.
    CleanExi HS_MTHFD1L.
    Genevestigatori Q6UB35.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    3.40.50.720. 2 hits.
    HAMAPi MF_01543. FTHFS.
    InterProi IPR000559. 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 ]
    Pfami PF01268. FTHFS. 1 hit.
    PF00763. THF_DHG_CYH. 1 hit.
    PF02882. THF_DHG_CYH_C. 1 hit.
    [Graphical view ]
    PRINTSi PR00085. THFDHDRGNASE.
    SUPFAMi SSF52540. SSF52540. 2 hits.
    PROSITEi PS00721. FTHFS_1. 1 hit.
    PS00722. FTHFS_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 102 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