Full text data of ENOSF1
ENOSF1
(RTS, TYMSAS)
[Confidence: low (only semi-automatic identification from reviews)]
Mitochondrial enolase superfamily member 1; 5.-.-.- (Antisense RNA to thymidylate synthase; rTS)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Mitochondrial enolase superfamily member 1; 5.-.-.- (Antisense RNA to thymidylate synthase; rTS)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q7L5Y1
ID ENOF1_HUMAN Reviewed; 443 AA.
AC Q7L5Y1; A6NMP3; A8K9R5; D3DUH0; Q15407; Q15594; Q15595; Q9HAS5;
read moreAC Q9HAS6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 22-JAN-2014, entry version 73.
DE RecName: Full=Mitochondrial enolase superfamily member 1;
DE EC=5.-.-.-;
DE AltName: Full=Antisense RNA to thymidylate synthase;
DE Short=rTS;
GN Name=ENOSF1; Synonyms=RTS, TYMSAS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), AND VARIANT
RP THR-145.
RC TISSUE=Cervix carcinoma;
RX PubMed=8493092; DOI=10.1093/nar/21.8.1747;
RA Dolnick B.J.;
RT "Cloning and characterization of a naturally occurring antisense RNA
RT to human thymidylate synthase mRNA.";
RL Nucleic Acids Res. 21:1747-1752(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), NUCLEOTIDE
RP SEQUENCE [MRNA] OF 23-443 (ISOFORM 3), AND VARIANT THR-145.
RC TISSUE=Cervix carcinoma;
RX PubMed=8764108;
RA Dolnick B.J., Black A.R.;
RT "Alternate splicing of the rTS gene product and its overexpression in
RT a 5-fluorouracil-resistant cell line.";
RL Cancer Res. 56:3207-3210(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP THR-145.
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
RA Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
RA Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
RA Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
RA Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
RA Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
RA O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-145.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION.
RX PubMed=8869746; DOI=10.1016/0065-2571(95)00009-7;
RA Dolnick B.J., Black A.R., Winkler P.M., Schindler K., Hsueh C.-T.;
RT "rTS gene expression is associated with altered cell sensitivity to
RT thymidylate synthase inhibitors.";
RL Adv. Enzyme Regul. 36:165-180(1996).
RN [8]
RP FUNCTION.
RX PubMed=14508106;
RA Dolnick B.J., Angelino N.J., Dolnick R., Sufrin J.R.;
RT "A novel function for the rTS gene.";
RL Cancer Biol. Ther. 2:364-369(2003).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=16162288; DOI=10.1186/1471-2164-6-125;
RA Liang P., Nair J.R., Song L., McGuire J.J., Dolnick B.J.;
RT "Comparative genomic analysis reveals a novel mitochondrial isoform of
RT human rTS protein and unusual phylogenetic distribution of the rTS
RT gene.";
RL BMC Genomics 6:125-125(2005).
RN [10]
RP PHOSPHORYLATION AT SER-148, AND SUMOYLATION.
RX PubMed=15994970; DOI=10.1158/0008-5472.CAN-05-0431;
RA Dolnick R., Wu Q., Angelino N.J., Stephanie L.V., Chow K.-C.,
RA Sufrin J.R., Dolnick B.J.;
RT "Enhancement of 5-fluorouracil sensitivity by an rTS signaling mimic
RT in H630 colon cancer cells.";
RL Cancer Res. 65:5917-5924(2005).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May regulate thymidylate synthase activity.
CC -!- COFACTOR: Divalent metal ions. Magnesium seems to be the preferred
CC ion (By similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrion (Probable).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=rTSgamma;
CC IsoId=Q7L5Y1-1; Sequence=Displayed;
CC Name=2; Synonyms=rTSalpha;
CC IsoId=Q7L5Y1-2; Sequence=VSP_033311, VSP_033313;
CC Name=3;
CC IsoId=Q7L5Y1-3; Sequence=VSP_033312, VSP_033314;
CC Name=4;
CC IsoId=Q7L5Y1-4; Sequence=VSP_047153, VSP_047154;
CC Note=Gene prediction based on EST data;
CC -!- PTM: Could be sumoylated.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. ENOSF1 subfamily.
CC -!- CAUTION: Was originally (PubMed:8493092) identified as a gene
CC coding for an antisense RNA to thymidylate synthase.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG29537.1; Type=Erroneous initiation;
CC Sequence=CAA47471.1; Type=Erroneous initiation;
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DR EMBL; AF305057; AAG29536.1; -; Genomic_DNA.
DR EMBL; X67098; CAA47472.1; -; mRNA.
DR EMBL; AF305057; AAG29537.1; ALT_INIT; Genomic_DNA.
DR EMBL; X67098; CAA47471.1; ALT_INIT; mRNA.
DR EMBL; X89602; CAA61761.1; -; mRNA.
DR EMBL; AK292780; BAF85469.1; -; mRNA.
DR EMBL; AP001178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471113; EAX01713.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01714.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01715.1; -; Genomic_DNA.
DR EMBL; BC001285; AAH01285.2; -; mRNA.
DR RefSeq; NP_001119595.1; NM_001126123.3.
DR RefSeq; NP_059982.2; NM_017512.5.
DR RefSeq; NP_974487.1; NM_202758.3.
DR RefSeq; XP_005258169.1; XM_005258112.1.
DR RefSeq; XP_005258172.1; XM_005258115.1.
DR RefSeq; XP_005258173.1; XM_005258116.1.
DR UniGene; Hs.658550; -.
DR UniGene; Hs.731510; -.
DR UniGene; Hs.732707; -.
DR PDB; 4A35; X-ray; 1.74 A; A=1-440.
DR PDBsum; 4A35; -.
DR ProteinModelPortal; Q7L5Y1; -.
DR SMR; Q7L5Y1; 1-440.
DR IntAct; Q7L5Y1; 1.
DR STRING; 9606.ENSP00000345974; -.
DR PhosphoSite; Q7L5Y1; -.
DR DMDM; 74739173; -.
DR PaxDb; Q7L5Y1; -.
DR PRIDE; Q7L5Y1; -.
DR Ensembl; ENST00000251101; ENSP00000251101; ENSG00000132199.
DR Ensembl; ENST00000340116; ENSP00000345974; ENSG00000132199.
DR Ensembl; ENST00000383578; ENSP00000373072; ENSG00000132199.
DR GeneID; 55556; -.
DR KEGG; hsa:55556; -.
DR UCSC; uc010dkf.3; human.
DR CTD; 55556; -.
DR GeneCards; GC18M000664; -.
DR HGNC; HGNC:30365; ENOSF1.
DR HPA; HPA047829; -.
DR MIM; 607427; gene.
DR neXtProt; NX_Q7L5Y1; -.
DR PharmGKB; PA134897613; -.
DR eggNOG; COG4948; -.
DR HOVERGEN; HBG053904; -.
DR OMA; MKVGRDL; -.
DR OrthoDB; EOG77DJ5S; -.
DR ChiTaRS; ENOSF1; human.
DR GenomeRNAi; 55556; -.
DR NextBio; 60026; -.
DR PRO; PR:Q7L5Y1; -.
DR ArrayExpress; Q7L5Y1; -.
DR Bgee; Q7L5Y1; -.
DR CleanEx; HS_ENOSF1; -.
DR Genevestigator; Q7L5Y1; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009063; P:cellular amino acid catabolic process; IEA:InterPro.
DR InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR013341; Mandelate_racemase_N.
DR InterPro; IPR001354; MR_MLE.
DR PANTHER; PTHR13794; PTHR13794; 1.
DR Pfam; PF01188; MR_MLE; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SMART; SM00922; MR_MLE; 1.
DR PROSITE; PS00908; MR_MLE_1; FALSE_NEG.
DR PROSITE; PS00909; MR_MLE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Isomerase;
KW Magnesium; Metal-binding; Mitochondrion; Phosphoprotein; Polymorphism;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1 443 Mitochondrial enolase superfamily member
FT 1.
FT /FTId=PRO_0000331652.
FT ACT_SITE 222 222 By similarity.
FT ACT_SITE 355 355 By similarity.
FT METAL 250 250 Magnesium (By similarity).
FT METAL 276 276 Magnesium (By similarity).
FT METAL 305 305 Magnesium (By similarity).
FT MOD_RES 148 148 Phosphoserine.
FT VAR_SEQ 1 102 Missing (in isoform 2).
FT /FTId=VSP_033311.
FT VAR_SEQ 1 24 MVRGRISRLSVRDVRFPTSLGGHG -> MVSADAMVSADAM
FT VSADAMVSADAMVSADAMVSADAMVSADAMVS (in
FT isoform 4).
FT /FTId=VSP_047153.
FT VAR_SEQ 65 117 VVCAVNALAHHVLNKDLKDIVGDFRGFYRQLTSDGQLRWIG
FT PEKGVVHLATAA -> DWSRKGRGAPGDSGRPKRGVGLVGQ
FT AGGKACLEVTCGHGSQDAGILHRFQVHH (in isoform
FT 3).
FT /FTId=VSP_033312.
FT VAR_SEQ 103 103 W -> MQKMESRGVELPSLWEKALKL (in isoform
FT 2).
FT /FTId=VSP_033313.
FT VAR_SEQ 118 443 Missing (in isoform 3).
FT /FTId=VSP_033314.
FT VAR_SEQ 293 306 Missing (in isoform 4).
FT /FTId=VSP_047154.
FT VARIANT 31 31 D -> E (in dbSNP:rs34724061).
FT /FTId=VAR_042933.
FT VARIANT 145 145 M -> T (in dbSNP:rs2612086).
FT /FTId=VAR_042934.
FT VARIANT 428 428 Y -> S (in dbSNP:rs2847620).
FT /FTId=VAR_042935.
FT STRAND 5 15
FT HELIX 18 20
FT STRAND 35 45
FT STRAND 51 57
FT HELIX 62 72
FT HELIX 73 75
FT TURN 76 78
FT HELIX 81 85
FT HELIX 88 96
FT HELIX 101 104
FT STRAND 106 108
FT HELIX 109 130
FT HELIX 134 140
FT HELIX 143 147
FT TURN 153 158
FT HELIX 161 170
FT TURN 171 174
FT HELIX 175 185
FT STRAND 187 191
FT HELIX 201 213
FT STRAND 218 222
FT HELIX 227 241
FT STRAND 245 250
FT HELIX 257 267
FT HELIX 268 270
FT STRAND 273 276
FT HELIX 284 294
FT HELIX 295 297
FT STRAND 300 303
FT HELIX 310 318
FT STRAND 323 325
FT TURN 329 331
FT HELIX 334 347
FT TURN 358 360
FT HELIX 361 375
FT STRAND 385 387
FT HELIX 392 394
FT STRAND 395 397
FT STRAND 400 407
FT STRAND 411 413
FT HELIX 420 426
FT TURN 428 430
FT HELIX 432 437
SQ SEQUENCE 443 AA; 49786 MW; 82BEDAC229D1A729 CRC64;
MVRGRISRLS VRDVRFPTSL GGHGADAMHT DPDYSAAYVV IETDAEDGIK GCGITFTLGK
GTEVVVCAVN ALAHHVLNKD LKDIVGDFRG FYRQLTSDGQ LRWIGPEKGV VHLATAAVLN
AVWDLWAKQE GKPVWKLLVD MDPRMLVSCI DFRYITDVLT EEDALEILQK GQIGKKEREK
QMLAQGYPAY TTSCAWLGYS DDTLKQLCAQ ALKDGWTRFK VKVGADLQDD MRRCQIIRDM
IGPEKTLMMD ANQRWDVPEA VEWMSKLAKF KPLWIEEPTS PDDILGHATI SKALVPLGIG
IATGEQCHNR VIFKQLLQAK ALQFLQIDSC RLGSVNENLS VLLMAKKFEI PVCPHAGGVG
LCELVQHLII FDYISVSASL ENRVCEYVDH LHEHFKYPVM IQRASYMPPK DPGYSTEMKE
ESVKKHQYPD GEVWKKLLPA QEN
//
ID ENOF1_HUMAN Reviewed; 443 AA.
AC Q7L5Y1; A6NMP3; A8K9R5; D3DUH0; Q15407; Q15594; Q15595; Q9HAS5;
read moreAC Q9HAS6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 22-JAN-2014, entry version 73.
DE RecName: Full=Mitochondrial enolase superfamily member 1;
DE EC=5.-.-.-;
DE AltName: Full=Antisense RNA to thymidylate synthase;
DE Short=rTS;
GN Name=ENOSF1; Synonyms=RTS, TYMSAS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), AND VARIANT
RP THR-145.
RC TISSUE=Cervix carcinoma;
RX PubMed=8493092; DOI=10.1093/nar/21.8.1747;
RA Dolnick B.J.;
RT "Cloning and characterization of a naturally occurring antisense RNA
RT to human thymidylate synthase mRNA.";
RL Nucleic Acids Res. 21:1747-1752(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), NUCLEOTIDE
RP SEQUENCE [MRNA] OF 23-443 (ISOFORM 3), AND VARIANT THR-145.
RC TISSUE=Cervix carcinoma;
RX PubMed=8764108;
RA Dolnick B.J., Black A.R.;
RT "Alternate splicing of the rTS gene product and its overexpression in
RT a 5-fluorouracil-resistant cell line.";
RL Cancer Res. 56:3207-3210(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP THR-145.
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
RA Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
RA Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
RA Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
RA Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
RA Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
RA O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-145.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION.
RX PubMed=8869746; DOI=10.1016/0065-2571(95)00009-7;
RA Dolnick B.J., Black A.R., Winkler P.M., Schindler K., Hsueh C.-T.;
RT "rTS gene expression is associated with altered cell sensitivity to
RT thymidylate synthase inhibitors.";
RL Adv. Enzyme Regul. 36:165-180(1996).
RN [8]
RP FUNCTION.
RX PubMed=14508106;
RA Dolnick B.J., Angelino N.J., Dolnick R., Sufrin J.R.;
RT "A novel function for the rTS gene.";
RL Cancer Biol. Ther. 2:364-369(2003).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=16162288; DOI=10.1186/1471-2164-6-125;
RA Liang P., Nair J.R., Song L., McGuire J.J., Dolnick B.J.;
RT "Comparative genomic analysis reveals a novel mitochondrial isoform of
RT human rTS protein and unusual phylogenetic distribution of the rTS
RT gene.";
RL BMC Genomics 6:125-125(2005).
RN [10]
RP PHOSPHORYLATION AT SER-148, AND SUMOYLATION.
RX PubMed=15994970; DOI=10.1158/0008-5472.CAN-05-0431;
RA Dolnick R., Wu Q., Angelino N.J., Stephanie L.V., Chow K.-C.,
RA Sufrin J.R., Dolnick B.J.;
RT "Enhancement of 5-fluorouracil sensitivity by an rTS signaling mimic
RT in H630 colon cancer cells.";
RL Cancer Res. 65:5917-5924(2005).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May regulate thymidylate synthase activity.
CC -!- COFACTOR: Divalent metal ions. Magnesium seems to be the preferred
CC ion (By similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrion (Probable).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=rTSgamma;
CC IsoId=Q7L5Y1-1; Sequence=Displayed;
CC Name=2; Synonyms=rTSalpha;
CC IsoId=Q7L5Y1-2; Sequence=VSP_033311, VSP_033313;
CC Name=3;
CC IsoId=Q7L5Y1-3; Sequence=VSP_033312, VSP_033314;
CC Name=4;
CC IsoId=Q7L5Y1-4; Sequence=VSP_047153, VSP_047154;
CC Note=Gene prediction based on EST data;
CC -!- PTM: Could be sumoylated.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. ENOSF1 subfamily.
CC -!- CAUTION: Was originally (PubMed:8493092) identified as a gene
CC coding for an antisense RNA to thymidylate synthase.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG29537.1; Type=Erroneous initiation;
CC Sequence=CAA47471.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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DR EMBL; AF305057; AAG29536.1; -; Genomic_DNA.
DR EMBL; X67098; CAA47472.1; -; mRNA.
DR EMBL; AF305057; AAG29537.1; ALT_INIT; Genomic_DNA.
DR EMBL; X67098; CAA47471.1; ALT_INIT; mRNA.
DR EMBL; X89602; CAA61761.1; -; mRNA.
DR EMBL; AK292780; BAF85469.1; -; mRNA.
DR EMBL; AP001178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471113; EAX01713.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01714.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01715.1; -; Genomic_DNA.
DR EMBL; BC001285; AAH01285.2; -; mRNA.
DR RefSeq; NP_001119595.1; NM_001126123.3.
DR RefSeq; NP_059982.2; NM_017512.5.
DR RefSeq; NP_974487.1; NM_202758.3.
DR RefSeq; XP_005258169.1; XM_005258112.1.
DR RefSeq; XP_005258172.1; XM_005258115.1.
DR RefSeq; XP_005258173.1; XM_005258116.1.
DR UniGene; Hs.658550; -.
DR UniGene; Hs.731510; -.
DR UniGene; Hs.732707; -.
DR PDB; 4A35; X-ray; 1.74 A; A=1-440.
DR PDBsum; 4A35; -.
DR ProteinModelPortal; Q7L5Y1; -.
DR SMR; Q7L5Y1; 1-440.
DR IntAct; Q7L5Y1; 1.
DR STRING; 9606.ENSP00000345974; -.
DR PhosphoSite; Q7L5Y1; -.
DR DMDM; 74739173; -.
DR PaxDb; Q7L5Y1; -.
DR PRIDE; Q7L5Y1; -.
DR Ensembl; ENST00000251101; ENSP00000251101; ENSG00000132199.
DR Ensembl; ENST00000340116; ENSP00000345974; ENSG00000132199.
DR Ensembl; ENST00000383578; ENSP00000373072; ENSG00000132199.
DR GeneID; 55556; -.
DR KEGG; hsa:55556; -.
DR UCSC; uc010dkf.3; human.
DR CTD; 55556; -.
DR GeneCards; GC18M000664; -.
DR HGNC; HGNC:30365; ENOSF1.
DR HPA; HPA047829; -.
DR MIM; 607427; gene.
DR neXtProt; NX_Q7L5Y1; -.
DR PharmGKB; PA134897613; -.
DR eggNOG; COG4948; -.
DR HOVERGEN; HBG053904; -.
DR OMA; MKVGRDL; -.
DR OrthoDB; EOG77DJ5S; -.
DR ChiTaRS; ENOSF1; human.
DR GenomeRNAi; 55556; -.
DR NextBio; 60026; -.
DR PRO; PR:Q7L5Y1; -.
DR ArrayExpress; Q7L5Y1; -.
DR Bgee; Q7L5Y1; -.
DR CleanEx; HS_ENOSF1; -.
DR Genevestigator; Q7L5Y1; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009063; P:cellular amino acid catabolic process; IEA:InterPro.
DR InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR013341; Mandelate_racemase_N.
DR InterPro; IPR001354; MR_MLE.
DR PANTHER; PTHR13794; PTHR13794; 1.
DR Pfam; PF01188; MR_MLE; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SMART; SM00922; MR_MLE; 1.
DR PROSITE; PS00908; MR_MLE_1; FALSE_NEG.
DR PROSITE; PS00909; MR_MLE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Isomerase;
KW Magnesium; Metal-binding; Mitochondrion; Phosphoprotein; Polymorphism;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1 443 Mitochondrial enolase superfamily member
FT 1.
FT /FTId=PRO_0000331652.
FT ACT_SITE 222 222 By similarity.
FT ACT_SITE 355 355 By similarity.
FT METAL 250 250 Magnesium (By similarity).
FT METAL 276 276 Magnesium (By similarity).
FT METAL 305 305 Magnesium (By similarity).
FT MOD_RES 148 148 Phosphoserine.
FT VAR_SEQ 1 102 Missing (in isoform 2).
FT /FTId=VSP_033311.
FT VAR_SEQ 1 24 MVRGRISRLSVRDVRFPTSLGGHG -> MVSADAMVSADAM
FT VSADAMVSADAMVSADAMVSADAMVSADAMVS (in
FT isoform 4).
FT /FTId=VSP_047153.
FT VAR_SEQ 65 117 VVCAVNALAHHVLNKDLKDIVGDFRGFYRQLTSDGQLRWIG
FT PEKGVVHLATAA -> DWSRKGRGAPGDSGRPKRGVGLVGQ
FT AGGKACLEVTCGHGSQDAGILHRFQVHH (in isoform
FT 3).
FT /FTId=VSP_033312.
FT VAR_SEQ 103 103 W -> MQKMESRGVELPSLWEKALKL (in isoform
FT 2).
FT /FTId=VSP_033313.
FT VAR_SEQ 118 443 Missing (in isoform 3).
FT /FTId=VSP_033314.
FT VAR_SEQ 293 306 Missing (in isoform 4).
FT /FTId=VSP_047154.
FT VARIANT 31 31 D -> E (in dbSNP:rs34724061).
FT /FTId=VAR_042933.
FT VARIANT 145 145 M -> T (in dbSNP:rs2612086).
FT /FTId=VAR_042934.
FT VARIANT 428 428 Y -> S (in dbSNP:rs2847620).
FT /FTId=VAR_042935.
FT STRAND 5 15
FT HELIX 18 20
FT STRAND 35 45
FT STRAND 51 57
FT HELIX 62 72
FT HELIX 73 75
FT TURN 76 78
FT HELIX 81 85
FT HELIX 88 96
FT HELIX 101 104
FT STRAND 106 108
FT HELIX 109 130
FT HELIX 134 140
FT HELIX 143 147
FT TURN 153 158
FT HELIX 161 170
FT TURN 171 174
FT HELIX 175 185
FT STRAND 187 191
FT HELIX 201 213
FT STRAND 218 222
FT HELIX 227 241
FT STRAND 245 250
FT HELIX 257 267
FT HELIX 268 270
FT STRAND 273 276
FT HELIX 284 294
FT HELIX 295 297
FT STRAND 300 303
FT HELIX 310 318
FT STRAND 323 325
FT TURN 329 331
FT HELIX 334 347
FT TURN 358 360
FT HELIX 361 375
FT STRAND 385 387
FT HELIX 392 394
FT STRAND 395 397
FT STRAND 400 407
FT STRAND 411 413
FT HELIX 420 426
FT TURN 428 430
FT HELIX 432 437
SQ SEQUENCE 443 AA; 49786 MW; 82BEDAC229D1A729 CRC64;
MVRGRISRLS VRDVRFPTSL GGHGADAMHT DPDYSAAYVV IETDAEDGIK GCGITFTLGK
GTEVVVCAVN ALAHHVLNKD LKDIVGDFRG FYRQLTSDGQ LRWIGPEKGV VHLATAAVLN
AVWDLWAKQE GKPVWKLLVD MDPRMLVSCI DFRYITDVLT EEDALEILQK GQIGKKEREK
QMLAQGYPAY TTSCAWLGYS DDTLKQLCAQ ALKDGWTRFK VKVGADLQDD MRRCQIIRDM
IGPEKTLMMD ANQRWDVPEA VEWMSKLAKF KPLWIEEPTS PDDILGHATI SKALVPLGIG
IATGEQCHNR VIFKQLLQAK ALQFLQIDSC RLGSVNENLS VLLMAKKFEI PVCPHAGGVG
LCELVQHLII FDYISVSASL ENRVCEYVDH LHEHFKYPVM IQRASYMPPK DPGYSTEMKE
ESVKKHQYPD GEVWKKLLPA QEN
//
MIM
607427
*RECORD*
*FIELD* NO
607427
*FIELD* TI
*607427 ENOLASE SUPERFAMILY MEMBER 1; ENOSF1
;;THYMIDYLATE SYNTHASE, ANTISENSE; RTS
read more*FIELD* TX
CLONING
By RT-PCR of KB cells (a human oral epidermoid carcinoma cell line),
Dolnick (1993) cloned a cDNA, which he designated 3-prime rTS, that is
antisense to thymidylate synthase (TS, or TYMS; 188350) mRNA. He cloned
the full-length cDNA by 5-prime RACE of a squamous cell carcinoma cell
line. The mRNA contains 4 possible open reading frames. Dolnick (1993)
determined that the 3-prime end of rTS shares 99.5% identity with the
antisense strand of the 3-prime untranslated region of TS and contains 2
discontinuities. All of TS exon 7 and part of intron 6 are overlapped by
3-prime rTS. Northern blot analysis of fractionated KB cells and other
carcinoma cell lines revealed rTS transcripts of 1.8 and 6.3 kb, as well
as several larger mRNA species. The presence and relative abundance of
the larger transcripts varied between cell lines, and in vitro
translation generated multiple translation products.
By screening a KB cell cDNA library for homology with rTS, Dolnick and
Black (1996) identified an alternatively spliced transcript, which they
called rTS-beta. The rTS-beta transcript has an insertion of 116
nucleotides in its 5-prime region and an altered 3-prime noncoding
region that is not complementary to TS mRNA. Dolnick and Black (1996)
determined that the original rTS transcript, which they renamed
rTS-alpha, encodes a protein with an apparent molecular mass of 41 kD
that shares homology with a superfamily of proteins that includes
mandelate racemase and muconate-lactonizing enzyme from Pseudomonas
putida. The rTS-beta protein was expressed by KB cells and by a colon
tumor cell line at an apparent molecular mass of 48 kD.
GENE FUNCTION
Dolnick and Black (1996) stated that rTS-alpha was overexpressed at both
the RNA and protein level in a leukemic cell line selected for
methotrexate resistance and that the overexpressing cell line lost its
ability to downregulate TS. Selection for 5-fluorouracil resistance in a
colon tumor cell line increased the expression of rTS-alpha and
rTS-beta, with highest expression of rTS-beta.
Chu and Dolnick (2002) found that rTS-alpha RNA and TS mRNA levels
varied inversely when the growth of HEp2 cells progressed from a
late-log phase to plateau phase. Transfection and expression of the
antisense region of rTS-alpha alone was sufficient to downregulate TS
mRNA. Downregulation was also associated with increased site-specific
cleavage of TS mRNA.
GENE STRUCTURE
Dolnick and Black (1996) determined that the ENOSF1 gene contains at
least 8 exons.
MAPPING
Dolnick (1993) identified the ENOSF1 gene on the complementary strand of
the TYMS gene, which maps to chromosome 18p11.32.
*FIELD* RF
1. Chu, J.; Dolnick, B. J.: Natural antisense (rTS-alpha) RNA induces
site-specific cleavage of thymidylate synthase mRNA. Biochim. Biophys.
Acta 1587: 183-193, 2002.
2. Dolnick, B. J.: Cloning and characterization of a naturally occurring
antisense RNA to human thymidylate synthase mRNA. Nucleic Acids Res. 21:
1747-1752, 1993.
3. Dolnick, B. J.; Black, A. R.: Alternate splicing of the rTS gene
product and its overexpression in a 5-fluorouracil-resistant cell
line. Cancer Res. 56: 3207-3210, 1996.
*FIELD* CD
Patricia A. Hartz: 12/17/2002
*FIELD* ED
alopez: 07/21/2010
mgross: 12/17/2002
*RECORD*
*FIELD* NO
607427
*FIELD* TI
*607427 ENOLASE SUPERFAMILY MEMBER 1; ENOSF1
;;THYMIDYLATE SYNTHASE, ANTISENSE; RTS
read more*FIELD* TX
CLONING
By RT-PCR of KB cells (a human oral epidermoid carcinoma cell line),
Dolnick (1993) cloned a cDNA, which he designated 3-prime rTS, that is
antisense to thymidylate synthase (TS, or TYMS; 188350) mRNA. He cloned
the full-length cDNA by 5-prime RACE of a squamous cell carcinoma cell
line. The mRNA contains 4 possible open reading frames. Dolnick (1993)
determined that the 3-prime end of rTS shares 99.5% identity with the
antisense strand of the 3-prime untranslated region of TS and contains 2
discontinuities. All of TS exon 7 and part of intron 6 are overlapped by
3-prime rTS. Northern blot analysis of fractionated KB cells and other
carcinoma cell lines revealed rTS transcripts of 1.8 and 6.3 kb, as well
as several larger mRNA species. The presence and relative abundance of
the larger transcripts varied between cell lines, and in vitro
translation generated multiple translation products.
By screening a KB cell cDNA library for homology with rTS, Dolnick and
Black (1996) identified an alternatively spliced transcript, which they
called rTS-beta. The rTS-beta transcript has an insertion of 116
nucleotides in its 5-prime region and an altered 3-prime noncoding
region that is not complementary to TS mRNA. Dolnick and Black (1996)
determined that the original rTS transcript, which they renamed
rTS-alpha, encodes a protein with an apparent molecular mass of 41 kD
that shares homology with a superfamily of proteins that includes
mandelate racemase and muconate-lactonizing enzyme from Pseudomonas
putida. The rTS-beta protein was expressed by KB cells and by a colon
tumor cell line at an apparent molecular mass of 48 kD.
GENE FUNCTION
Dolnick and Black (1996) stated that rTS-alpha was overexpressed at both
the RNA and protein level in a leukemic cell line selected for
methotrexate resistance and that the overexpressing cell line lost its
ability to downregulate TS. Selection for 5-fluorouracil resistance in a
colon tumor cell line increased the expression of rTS-alpha and
rTS-beta, with highest expression of rTS-beta.
Chu and Dolnick (2002) found that rTS-alpha RNA and TS mRNA levels
varied inversely when the growth of HEp2 cells progressed from a
late-log phase to plateau phase. Transfection and expression of the
antisense region of rTS-alpha alone was sufficient to downregulate TS
mRNA. Downregulation was also associated with increased site-specific
cleavage of TS mRNA.
GENE STRUCTURE
Dolnick and Black (1996) determined that the ENOSF1 gene contains at
least 8 exons.
MAPPING
Dolnick (1993) identified the ENOSF1 gene on the complementary strand of
the TYMS gene, which maps to chromosome 18p11.32.
*FIELD* RF
1. Chu, J.; Dolnick, B. J.: Natural antisense (rTS-alpha) RNA induces
site-specific cleavage of thymidylate synthase mRNA. Biochim. Biophys.
Acta 1587: 183-193, 2002.
2. Dolnick, B. J.: Cloning and characterization of a naturally occurring
antisense RNA to human thymidylate synthase mRNA. Nucleic Acids Res. 21:
1747-1752, 1993.
3. Dolnick, B. J.; Black, A. R.: Alternate splicing of the rTS gene
product and its overexpression in a 5-fluorouracil-resistant cell
line. Cancer Res. 56: 3207-3210, 1996.
*FIELD* CD
Patricia A. Hartz: 12/17/2002
*FIELD* ED
alopez: 07/21/2010
mgross: 12/17/2002