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Q7L5Y1

- ENOF1_HUMAN

UniProt

Q7L5Y1 - ENOF1_HUMAN

Protein

Mitochondrial enolase superfamily member 1

Gene

ENOSF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (24 May 2005)
      Previous versions | rss
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    Functioni

    Plays a role in the catabolism of L-fucose, a sugar that is part of the carbohydrates that are attached to cellular glycoproteins. Catalyzes the dehydration of L-fuconate to 2-keto-3-deoxy-L-fuconate by the abstraction of the 2-proton to generate an enediolate intermediate that is stabilized by the magnesium ion (PubMed:24697329).1 Publication

    Catalytic activityi

    L-fuconate = 2-dehydro-3-deoxy-L-fuconate + H2O.1 Publication

    Cofactori

    Binds 1 Mg2+ per subunit.1 Publication

    Kineticsi

    kcat is 0.5 sec(-1) for L-fuconate. kcat is 0.3 sec(-1) for L-galactonate. kcat is 0.3 sec(-1) for L-arabinonate. kcat is 0.04 sec(-1) for D-arabinonate. kcat is 0.002 sec(-1) for D-ribonate.

    1. KM=0.2 mM for L-fuconate1 Publication
    2. KM=3.0 mM for L-galactonate1 Publication
    3. KM=2.0 mM for D-arabinonate1 Publication
    4. KM=4.0 mM for L-arabinonate1 Publication
    5. KM=0.4 mM for D-ribonate1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei34 – 341SubstrateBy similarity
    Binding sitei220 – 2201SubstrateBy similarity
    Active sitei222 – 2221Proton donor/acceptorBy similarity
    Metal bindingi250 – 2501Magnesium1 Publication
    Binding sitei252 – 2521SubstrateBy similarity
    Metal bindingi276 – 2761Magnesium1 Publication
    Binding sitei276 – 2761SubstrateBy similarity
    Metal bindingi305 – 3051Magnesium1 Publication
    Binding sitei305 – 3051SubstrateBy similarity
    Active sitei355 – 3551Sequence Analysis
    Binding sitei386 – 3861SubstrateBy similarity

    GO - Molecular functioni

    1. isomerase activity Source: UniProtKB-KW
    2. L-fuconate dehydratase activity Source: UniProtKB
    3. magnesium ion binding Source: UniProtKB

    GO - Biological processi

    1. cellular amino acid catabolic process Source: InterPro
    2. cellular carbohydrate catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Isomerase, Lyase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitochondrial enolase superfamily member 1 (EC:4.2.1.68)
    Alternative name(s):
    Antisense RNA to thymidylate synthase
    Short name:
    rTS
    L-fuconate dehydratase
    Gene namesi
    Name:ENOSF1
    Synonyms:RTS, TYMSAS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:30365. ENOSF1.

    Subcellular locationi

    Mitochondrion 1 Publication

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1 – 2727Missing: Impairs protein solubility. Abolishes catalytic activity. 1 PublicationAdd
    BLAST

    Organism-specific databases

    PharmGKBiPA134897613.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 443443Mitochondrial enolase superfamily member 1PRO_0000331652Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei148 – 1481Phosphoserine1 Publication

    Post-translational modificationi

    Could be sumoylated.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ7L5Y1.
    PaxDbiQ7L5Y1.
    PRIDEiQ7L5Y1.

    PTM databases

    PhosphoSiteiQ7L5Y1.

    Expressioni

    Gene expression databases

    ArrayExpressiQ7L5Y1.
    BgeeiQ7L5Y1.
    CleanExiHS_ENOSF1.
    GenevestigatoriQ7L5Y1.

    Organism-specific databases

    HPAiHPA047829.

    Interactioni

    Protein-protein interaction databases

    BioGridi120716. 1 interaction.
    IntActiQ7L5Y1. 1 interaction.
    STRINGi9606.ENSP00000345974.

    Structurei

    Secondary structure

    1
    443
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 1511
    Helixi18 – 203
    Beta strandi35 – 4511
    Beta strandi51 – 577
    Helixi62 – 7211
    Helixi73 – 753
    Turni76 – 783
    Helixi81 – 855
    Helixi88 – 969
    Helixi101 – 1044
    Beta strandi106 – 1083
    Helixi109 – 13022
    Helixi134 – 1407
    Helixi143 – 1475
    Turni153 – 1586
    Helixi161 – 17010
    Turni171 – 1744
    Helixi175 – 18511
    Beta strandi187 – 1915
    Helixi201 – 21313
    Beta strandi218 – 2225
    Helixi227 – 24115
    Beta strandi245 – 2506
    Helixi257 – 26711
    Helixi268 – 2703
    Beta strandi273 – 2764
    Helixi284 – 29411
    Helixi295 – 2973
    Beta strandi300 – 3034
    Helixi310 – 3189
    Beta strandi323 – 3253
    Turni329 – 3313
    Helixi334 – 34714
    Turni358 – 3603
    Helixi361 – 37515
    Beta strandi385 – 3873
    Helixi392 – 3943
    Beta strandi395 – 3973
    Beta strandi400 – 4078
    Beta strandi411 – 4133
    Helixi420 – 4267
    Turni428 – 4303
    Helixi432 – 4376

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4A35X-ray1.74A1-440[»]
    ProteinModelPortaliQ7L5Y1.
    SMRiQ7L5Y1. Positions 1-440.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni24 – 263Substrate bindingBy similarity
    Regioni355 – 3573Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG4948.
    HOVERGENiHBG053904.
    OMAiHEHFLYP.
    OrthoDBiEOG77DJ5S.
    PhylomeDBiQ7L5Y1.
    TreeFamiTF300529.

    Family and domain databases

    Gene3Di3.20.20.120. 1 hit.
    3.30.390.10. 1 hit.
    InterProiIPR029065. Enolase_C-like.
    IPR029017. Enolase_N_like.
    IPR018110. Mandel_Rmase/mucon_lact_enz_CS.
    IPR013342. Mandelate_racemase_C.
    IPR013341. Mandelate_racemase_N.
    IPR001354. MR_MLE.
    [Graphical view]
    PANTHERiPTHR13794. PTHR13794. 1 hit.
    PfamiPF01188. MR_MLE. 1 hit.
    PF02746. MR_MLE_N. 1 hit.
    [Graphical view]
    SMARTiSM00922. MR_MLE. 1 hit.
    [Graphical view]
    SUPFAMiSSF51604. SSF51604. 1 hit.
    SSF54826. SSF54826. 1 hit.
    PROSITEiPS00909. MR_MLE_2. 1 hit.
    [Graphical view]

    Sequences (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q7L5Y1-1) [UniParc]FASTAAdd to Basket

    Also known as: rTSgamma

    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

    MVRGRISRLS VRDVRFPTSL GGHGADAMHT DPDYSAAYVV IETDAEDGIK    50
    GCGITFTLGK GTEVVVCAVN ALAHHVLNKD LKDIVGDFRG FYRQLTSDGQ 100
    LRWIGPEKGV VHLATAAVLN AVWDLWAKQE GKPVWKLLVD MDPRMLVSCI 150
    DFRYITDVLT EEDALEILQK GQIGKKEREK QMLAQGYPAY TTSCAWLGYS 200
    DDTLKQLCAQ ALKDGWTRFK VKVGADLQDD MRRCQIIRDM IGPEKTLMMD 250
    ANQRWDVPEA VEWMSKLAKF KPLWIEEPTS PDDILGHATI SKALVPLGIG 300
    IATGEQCHNR VIFKQLLQAK ALQFLQIDSC RLGSVNENLS VLLMAKKFEI 350
    PVCPHAGGVG LCELVQHLII FDYISVSASL ENRVCEYVDH LHEHFKYPVM 400
    IQRASYMPPK DPGYSTEMKE ESVKKHQYPD GEVWKKLLPA QEN 443
    Length:443
    Mass (Da):49,786
    Last modified:May 24, 2005 - v1
    Checksum:i82BEDAC229D1A729
    GO
    Isoform 2 (identifier: Q7L5Y1-2) [UniParc]FASTAAdd to Basket

    Also known as: rTSalpha

    The sequence of this isoform differs from the canonical sequence as follows:
         1-102: Missing.
         103-103: W → MQKMESRGVELPSLWEKALKL

    Show »
    Length:361
    Mass (Da):41,024
    Checksum:i73B469F1C9C7E144
    GO
    Isoform 3 (identifier: Q7L5Y1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         65-117: VVCAVNALAH...KGVVHLATAA → DWSRKGRGAP...GILHRFQVHH
         118-443: Missing.

    Show »
    Length:117
    Mass (Da):12,286
    Checksum:iB277BFA534E7DAF2
    GO
    Isoform 4 (identifier: Q7L5Y1-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-24: MVRGRISRLSVRDVRFPTSLGGHG → MVSADAMVSADAMVSADAMVSADAMVSADAMVSADAMVSADAMVS
         293-306: Missing.

    Note: Gene prediction based on EST data.

    Show »
    Length:450
    Mass (Da):50,170
    Checksum:i7D6BD13DF0F12AD0
    GO
    Isoform 5 (identifier: Q7L5Y1-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-24: MVRGRISRLSVRDVRFPTSLGGHG → MVSADAMVSA...AMVSADAMVS
         293-306: Missing.

    Show »
    Length:474
    Mass (Da):52,468
    Checksum:i97FA6018CAADF8CB
    GO
    Isoform 6 (identifier: Q7L5Y1-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-181: Missing.

    Show »
    Length:262
    Mass (Da):29,710
    Checksum:i5296CB2DCA806273
    GO
    Isoform 7 (identifier: Q7L5Y1-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-230: Missing.

    Show »
    Length:213
    Mass (Da):24,284
    Checksum:iF2CF0580E05E10BA
    GO

    Sequence cautioni

    The sequence AAG29537.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAA47471.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti31 – 311D → E.
    Corresponds to variant rs34724061 [ dbSNP | Ensembl ].
    VAR_042933
    Natural varianti145 – 1451M → T.4 Publications
    Corresponds to variant rs2612086 [ dbSNP | Ensembl ].
    VAR_042934
    Natural varianti428 – 4281Y → S.
    Corresponds to variant rs2847620 [ dbSNP | Ensembl ].
    VAR_042935

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 230230Missing in isoform 7. 1 PublicationVSP_055241Add
    BLAST
    Alternative sequencei1 – 181181Missing in isoform 6. 1 PublicationVSP_055242Add
    BLAST
    Alternative sequencei1 – 102102Missing in isoform 2. 1 PublicationVSP_033311Add
    BLAST
    Alternative sequencei1 – 2424MVRGR…LGGHG → MVSADAMVSADAMVSADAMV SADAMVSADAMVSADAMVSA DAMVS in isoform 4. CuratedVSP_047153Add
    BLAST
    Alternative sequencei1 – 2424MVRGR…LGGHG → MVSADAMVSADAMVSADAMV SADAMVSADAMVSADAMVSA DAMVSADAMVSADAMVSADA MVSADAMVS in isoform 5. 1 PublicationVSP_055243Add
    BLAST
    Alternative sequencei65 – 11753VVCAV…LATAA → DWSRKGRGAPGDSGRPKRGV GLVGQAGGKACLEVTCGHGS QDAGILHRFQVHH in isoform 3. 1 PublicationVSP_033312Add
    BLAST
    Alternative sequencei103 – 1031W → MQKMESRGVELPSLWEKALK L in isoform 2. 1 PublicationVSP_033313
    Alternative sequencei118 – 443326Missing in isoform 3. 1 PublicationVSP_033314Add
    BLAST
    Alternative sequencei293 – 30614Missing in isoform 4 and isoform 5. 1 PublicationVSP_047154Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF305057 Genomic DNA. Translation: AAG29536.1.
    X67098 mRNA. Translation: CAA47472.1.
    AF305057 Genomic DNA. Translation: AAG29537.1. Different initiation.
    X67098 mRNA. Translation: CAA47471.1. Different initiation.
    X89602 mRNA. Translation: CAA61761.1.
    AK127818 mRNA. Translation: BAC87148.1.
    AK093873 mRNA. Translation: BAG52778.1.
    AK127219 mRNA. Translation: BAG54456.1.
    AK292780 mRNA. Translation: BAF85469.1.
    AP001178 Genomic DNA. No translation available.
    CH471113 Genomic DNA. Translation: EAX01713.1.
    CH471113 Genomic DNA. Translation: EAX01714.1.
    CH471113 Genomic DNA. Translation: EAX01715.1.
    BC001285 mRNA. Translation: AAH01285.2.
    CCDSiCCDS11822.1. [Q7L5Y1-1]
    CCDS11823.1. [Q7L5Y1-4]
    CCDS45821.1. [Q7L5Y1-2]
    RefSeqiNP_001119595.1. NM_001126123.3. [Q7L5Y1-2]
    NP_059982.2. NM_017512.5. [Q7L5Y1-1]
    NP_974487.1. NM_202758.3. [Q7L5Y1-4]
    XP_005258175.1. XM_005258118.2.
    UniGeneiHs.658550.
    Hs.731510.
    Hs.732707.

    Genome annotation databases

    EnsembliENST00000251101; ENSP00000251101; ENSG00000132199. [Q7L5Y1-1]
    ENST00000340116; ENSP00000345974; ENSG00000132199. [Q7L5Y1-4]
    ENST00000383578; ENSP00000373072; ENSG00000132199. [Q7L5Y1-2]
    GeneIDi55556.
    KEGGihsa:55556.
    UCSCiuc002kkt.4. human. [Q7L5Y1-2]
    uc002kku.4. human. [Q7L5Y1-1]

    Polymorphism databases

    DMDMi74739173.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF305057 Genomic DNA. Translation: AAG29536.1 .
    X67098 mRNA. Translation: CAA47472.1 .
    AF305057 Genomic DNA. Translation: AAG29537.1 . Different initiation.
    X67098 mRNA. Translation: CAA47471.1 . Different initiation.
    X89602 mRNA. Translation: CAA61761.1 .
    AK127818 mRNA. Translation: BAC87148.1 .
    AK093873 mRNA. Translation: BAG52778.1 .
    AK127219 mRNA. Translation: BAG54456.1 .
    AK292780 mRNA. Translation: BAF85469.1 .
    AP001178 Genomic DNA. No translation available.
    CH471113 Genomic DNA. Translation: EAX01713.1 .
    CH471113 Genomic DNA. Translation: EAX01714.1 .
    CH471113 Genomic DNA. Translation: EAX01715.1 .
    BC001285 mRNA. Translation: AAH01285.2 .
    CCDSi CCDS11822.1. [Q7L5Y1-1 ]
    CCDS11823.1. [Q7L5Y1-4 ]
    CCDS45821.1. [Q7L5Y1-2 ]
    RefSeqi NP_001119595.1. NM_001126123.3. [Q7L5Y1-2 ]
    NP_059982.2. NM_017512.5. [Q7L5Y1-1 ]
    NP_974487.1. NM_202758.3. [Q7L5Y1-4 ]
    XP_005258175.1. XM_005258118.2.
    UniGenei Hs.658550.
    Hs.731510.
    Hs.732707.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4A35 X-ray 1.74 A 1-440 [» ]
    ProteinModelPortali Q7L5Y1.
    SMRi Q7L5Y1. Positions 1-440.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120716. 1 interaction.
    IntActi Q7L5Y1. 1 interaction.
    STRINGi 9606.ENSP00000345974.

    PTM databases

    PhosphoSitei Q7L5Y1.

    Polymorphism databases

    DMDMi 74739173.

    Proteomic databases

    MaxQBi Q7L5Y1.
    PaxDbi Q7L5Y1.
    PRIDEi Q7L5Y1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000251101 ; ENSP00000251101 ; ENSG00000132199 . [Q7L5Y1-1 ]
    ENST00000340116 ; ENSP00000345974 ; ENSG00000132199 . [Q7L5Y1-4 ]
    ENST00000383578 ; ENSP00000373072 ; ENSG00000132199 . [Q7L5Y1-2 ]
    GeneIDi 55556.
    KEGGi hsa:55556.
    UCSCi uc002kkt.4. human. [Q7L5Y1-2 ]
    uc002kku.4. human. [Q7L5Y1-1 ]

    Organism-specific databases

    CTDi 55556.
    GeneCardsi GC18M000664.
    HGNCi HGNC:30365. ENOSF1.
    HPAi HPA047829.
    MIMi 607427. gene.
    neXtProti NX_Q7L5Y1.
    PharmGKBi PA134897613.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4948.
    HOVERGENi HBG053904.
    OMAi HEHFLYP.
    OrthoDBi EOG77DJ5S.
    PhylomeDBi Q7L5Y1.
    TreeFami TF300529.

    Miscellaneous databases

    ChiTaRSi ENOSF1. human.
    GenomeRNAii 55556.
    NextBioi 13632971.
    PROi Q7L5Y1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7L5Y1.
    Bgeei Q7L5Y1.
    CleanExi HS_ENOSF1.
    Genevestigatori Q7L5Y1.

    Family and domain databases

    Gene3Di 3.20.20.120. 1 hit.
    3.30.390.10. 1 hit.
    InterProi IPR029065. Enolase_C-like.
    IPR029017. Enolase_N_like.
    IPR018110. Mandel_Rmase/mucon_lact_enz_CS.
    IPR013342. Mandelate_racemase_C.
    IPR013341. Mandelate_racemase_N.
    IPR001354. MR_MLE.
    [Graphical view ]
    PANTHERi PTHR13794. PTHR13794. 1 hit.
    Pfami PF01188. MR_MLE. 1 hit.
    PF02746. MR_MLE_N. 1 hit.
    [Graphical view ]
    SMARTi SM00922. MR_MLE. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51604. SSF51604. 1 hit.
    SSF54826. SSF54826. 1 hit.
    PROSITEi PS00909. MR_MLE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a naturally occurring antisense RNA to human thymidylate synthase mRNA."
      Dolnick B.J.
      Nucleic Acids Res. 21:1747-1752(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), VARIANT THR-145.
      Tissue: Cervix carcinoma.
    2. "Alternate splicing of the rTS gene product and its overexpression in a 5-fluorouracil-resistant cell line."
      Dolnick B.J., Black A.R.
      Cancer Res. 56:3207-3210(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 23-443 (ISOFORM 3), VARIANT THR-145.
      Tissue: Cervix carcinoma.
    3. "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] (ISOFORMS 1; 5; 6 AND 7), VARIANT THR-145.
      Tissue: Trachea.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-145.
    6. "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] (ISOFORM 1).
      Tissue: Placenta.
    7. "rTS gene expression is associated with altered cell sensitivity to thymidylate synthase inhibitors."
      Dolnick B.J., Black A.R., Winkler P.M., Schindler K., Hsueh C.-T.
      Adv. Enzyme Regul. 36:165-180(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: ORIGINALLY PROPOSED FUNCTION.
    8. "Natural antisense (rTSalpha) RNA induces site-specific cleavage of thymidylate synthase mRNA."
      Chu J., Dolnick B.J.
      Biochim. Biophys. Acta 1587:183-193(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ORIGINALLY PROPOSED FUNCTION.
    9. "Comparative genomic analysis reveals a novel mitochondrial isoform of human rTS protein and unusual phylogenetic distribution of the rTS gene."
      Liang P., Nair J.R., Song L., McGuire J.J., Dolnick B.J.
      BMC Genomics 6:125-125(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    10. "Enhancement of 5-fluorouracil sensitivity by an rTS signaling mimic in H630 colon cancer cells."
      Dolnick R., Wu Q., Angelino N.J., Stephanie L.V., Chow K.-C., Sufrin J.R., Dolnick B.J.
      Cancer Res. 65:5917-5924(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-148, SUMOYLATION.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Enzymatic and structural characterization of rTSgamma provides insights into the function of rTSbeta."
      Wichelecki D.J., Froese D.S., Kopec J., Muniz J.R., Yue W.W., Gerlt J.A.
      Biochemistry 53:2732-2738(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 1-440 IN COMPLEX WITH MAGNESIUM, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF 1-MET--HIS-27.

    Entry informationi

    Entry nameiENOF1_HUMAN
    AccessioniPrimary (citable) accession number: Q7L5Y1
    Secondary accession number(s): A6NMP3
    , A8K9R5, B3KSL6, B3KXE4, D3DUH0, Q15407, Q15594, Q15595, Q6ZS08, Q9HAS5, Q9HAS6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 29, 2008
    Last sequence update: May 24, 2005
    Last modified: October 1, 2014
    This is version 81 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3