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Q6UB35

- C1TM_HUMAN

UniProt

Q6UB35 - C1TM_HUMAN

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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

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
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: 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
Complete GO annotation...

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

BgeeiQ6UB35.
CleanExiHS_MTHFD1L.
ExpressionAtlasiQ6UB35. baseline and differential.
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. 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.
GeneTreeiENSGT00750000117401.
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

        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.
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. 13 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.
GeneTreei ENSGT00750000117401.
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

Bgeei Q6UB35.
CleanExi HS_MTHFD1L.
ExpressionAtlasi Q6UB35. baseline and differential.
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

« 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: October 29, 2014
This is version 103 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