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Protein

Mitochondrial enolase superfamily member 1

Gene

ENOSF1

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

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

Mg2+1 PublicationNote: Binds 1 Mg2+ ion 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
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial enolase superfamily member 1 (EC:4.2.1.681 Publication)
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 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:30365. ENOSF1.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
Complete GO annotation...

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

BgeeiQ7L5Y1.
CleanExiHS_ENOSF1.
ExpressionAtlasiQ7L5Y1. baseline and differential.
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 – 1511Combined sources
Helixi18 – 203Combined sources
Beta strandi35 – 4511Combined sources
Beta strandi51 – 577Combined sources
Helixi62 – 7211Combined sources
Helixi73 – 753Combined sources
Turni76 – 783Combined sources
Helixi81 – 855Combined sources
Helixi88 – 969Combined sources
Helixi101 – 1044Combined sources
Beta strandi106 – 1083Combined sources
Helixi109 – 13022Combined sources
Helixi134 – 1407Combined sources
Helixi143 – 1475Combined sources
Turni153 – 1586Combined sources
Helixi161 – 17010Combined sources
Turni171 – 1744Combined sources
Helixi175 – 18511Combined sources
Beta strandi187 – 1915Combined sources
Helixi201 – 21313Combined sources
Beta strandi218 – 2225Combined sources
Helixi227 – 24115Combined sources
Beta strandi245 – 2506Combined sources
Helixi257 – 26711Combined sources
Helixi268 – 2703Combined sources
Beta strandi273 – 2764Combined sources
Helixi284 – 29411Combined sources
Helixi295 – 2973Combined sources
Beta strandi300 – 3034Combined sources
Helixi310 – 3189Combined sources
Beta strandi323 – 3253Combined sources
Turni329 – 3313Combined sources
Helixi334 – 34714Combined sources
Turni358 – 3603Combined sources
Helixi361 – 37515Combined sources
Beta strandi385 – 3873Combined sources
Helixi392 – 3943Combined sources
Beta strandi395 – 3973Combined sources
Beta strandi400 – 4078Combined sources
Beta strandi411 – 4133Combined sources
Helixi420 – 4267Combined sources
Turni428 – 4303Combined sources
Helixi432 – 4376Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000014290.
HOGENOMiHOG000113757.
HOVERGENiHBG053904.
InParanoidiQ7L5Y1.
KOiK18334.
OMAiSAAYCIL.
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_dom.
IPR001354. MR/MLE/MAL.
[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. AlignAdd to basket

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

        10         20         30         40         50
MVRGRISRLS VRDVRFPTSL GGHGADAMHT DPDYSAAYVV IETDAEDGIK
60 70 80 90 100
GCGITFTLGK GTEVVVCAVN ALAHHVLNKD LKDIVGDFRG FYRQLTSDGQ
110 120 130 140 150
LRWIGPEKGV VHLATAAVLN AVWDLWAKQE GKPVWKLLVD MDPRMLVSCI
160 170 180 190 200
DFRYITDVLT EEDALEILQK GQIGKKEREK QMLAQGYPAY TTSCAWLGYS
210 220 230 240 250
DDTLKQLCAQ ALKDGWTRFK VKVGADLQDD MRRCQIIRDM IGPEKTLMMD
260 270 280 290 300
ANQRWDVPEA VEWMSKLAKF KPLWIEEPTS PDDILGHATI SKALVPLGIG
310 320 330 340 350
IATGEQCHNR VIFKQLLQAK ALQFLQIDSC RLGSVNENLS VLLMAKKFEI
360 370 380 390 400
PVCPHAGGVG LCELVQHLII FDYISVSASL ENRVCEYVDH LHEHFKYPVM
410 420 430 440
IQRASYMPPK DPGYSTEMKE ESVKKHQYPD GEVWKKLLPA QEN
Length:443
Mass (Da):49,786
Last modified:May 23, 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.Curated
The sequence CAA47471.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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:
EMBLi
GenBanki
DDBJi
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. [Q7L5Y1-6]
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:
EMBLi
GenBanki
DDBJi
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. [Q7L5Y1-6]
UniGeneiHs.658550.
Hs.731510.
Hs.732707.

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiQ7L5Y1.

Polymorphism databases

DMDMi74739173.

Proteomic databases

MaxQBiQ7L5Y1.
PaxDbiQ7L5Y1.
PRIDEiQ7L5Y1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi55556.
GeneCardsiGC18M000664.
HGNCiHGNC:30365. ENOSF1.
HPAiHPA047829.
MIMi607427. gene.
neXtProtiNX_Q7L5Y1.
PharmGKBiPA134897613.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG4948.
GeneTreeiENSGT00390000014290.
HOGENOMiHOG000113757.
HOVERGENiHBG053904.
InParanoidiQ7L5Y1.
KOiK18334.
OMAiSAAYCIL.
OrthoDBiEOG77DJ5S.
PhylomeDBiQ7L5Y1.
TreeFamiTF300529.

Miscellaneous databases

ChiTaRSiENOSF1. human.
GenomeRNAii55556.
NextBioi13632971.
PROiQ7L5Y1.
SOURCEiSearch...

Gene expression databases

BgeeiQ7L5Y1.
CleanExiHS_ENOSF1.
ExpressionAtlasiQ7L5Y1. baseline and differential.
GenevestigatoriQ7L5Y1.

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_dom.
IPR001354. MR/MLE/MAL.
[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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a naturally occurring antisense RNA to human thymidylate synthase mRNA."
    Dolnick B.J.
    Nucleic Acids Res. 21:1747-1752(1992) [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(1995) [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(2003) [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(2003) [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(1995) [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(2001) [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(2004) [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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-148, SUMOYLATION.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "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(2013) [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 28, 2008
Last sequence update: May 23, 2005
Last modified: March 31, 2015
This is version 87 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

Caution

Was originally (PubMed:8493092) identified as a gene coding for an antisense RNA to thymidylate synthase, and was proposed to down-regulate TYMS activity (PubMed:8869746), possibly by promoting the degradation of TYMS mRNA via an antisense RNA-based mechanism (PubMed:12084460).3 Publications

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.