Reviewed,
UniProtKB/Swiss-Prot O60942 (MCE1_HUMAN)
Last modified
November 25, 2008.
Version 87.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
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Names and origin
| Protein names | Recommended name: mRNA-capping enzyme Alternative name(s): HCE HCAP1 Including the following 2 domains: 1- Recommended name: Polynucleotide 5'-triphosphatase EC=3.1.3.33 Alternative name(s): mRNA 5'-triphosphatase Short name=TPase 2- Recommended name: mRNA guanylyltransferase EC=2.7.7.50 Alternative name(s): GTP--RNA guanylyltransferase Short name=GTase | ||||
| Gene names |
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| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 597 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Bifunctional mRNA-capping enzyme exhibiting RNA 5'-triphosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the gmp moiety of GTP to the 5'-diphosphate terminus. |
| Catalytic activity | A 5'-phosphopolynucleotide + H(2)O = a polynucleotide + phosphate. GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA. |
| Subunit structure | Interacts with SUPT5H and RNMT. Interacts with HIV-1 Tat. |
| Subcellular location | NucleusBy similarity. |
| Tissue specificity | Isoform 1 and isoform 4 (at a lesser extent) are expressed in cerebrum, cerebellum, thyroid, lung, heart, liver, kidney, spleen, large intestine, testis, skin and muscle. |
| Miscellaneous | Isoform 2 to isoform 4 lack mRNA 5'-guanylyltransferase activity due to disruptions of the GTase domain. |
| Sequence similarities | In the N-terminal section; belongs to the non-receptor class of the protein-tyrosine phosphatase family. In the C-terminal section; belongs to the eukaryotic GTase family. |
Ontologies
Alternative products
| This entry describes 4 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: O60942-1) Also known as: HCE1; HCAP1A; 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. | ||||||
| Isoform 2 (identifier: O60942-2) Also known as: HCE1A; The sequence of this isoform differs from the canonical sequence as follows: 424-446: Missing. | ||||||
| Isoform 3 (identifier: O60942-3) Also known as: HCE1B; The sequence of this isoform differs from the canonical sequence as follows: 424-446: Missing. 481-597: Missing. | ||||||
| Isoform 4 (identifier: O60942-4) Also known as: HCAP1B; The sequence of this isoform differs from the canonical sequence as follows: 504-597: TKELKQYDNK...PPPKRPRPLT → CLFIFSVLFL...KISCSSTLGG |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 597 | 597 | mRNA-capping enzyme | PRO_0000210108 | ||||||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||||||
| Region | 1 – 212 | 212 | TPase | |||||||||||||||||||||||||||||||||||
| Region | 229 – 597 | 369 | GTase | |||||||||||||||||||||||||||||||||||
| Compositional bias | 195 – 205 | 11 | Asp/Glu-rich | |||||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||||
| Active site | 126 | 1 | For RNA 5'-triphosphatase activity By similarity | |||||||||||||||||||||||||||||||||||
| Active site | 294 | 1 | N6-GMP-lysine intermediate | |||||||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||||||||
| Modified residue | 210 | 1 | Phosphoserine | |||||||||||||||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 424 – 446 | 23 | Missing in isoform 2 and isoform 3. | VSP_003202 | ||||||||||||||||||||||||||||||||||
| Alternative sequence | 481 – 597 | 117 | Missing in isoform 3. | VSP_003203 | ||||||||||||||||||||||||||||||||||
| Alternative sequence | 504 – 597 | 94 | TKELK…PRPLT → CLFIFSVLFLDVLLSGIHQN LANNNQHIKISCSSTLGG in isoform 4. | VSP_003204 | ||||||||||||||||||||||||||||||||||
| Natural variant | 594 | 1 | R → H: dbSNP rs17856595. | VAR_046481 | ||||||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 294 | 1 | K → A: Loss of GTase activity | |||||||||||||||||||||||||||||||||||
| Mutagenesis | 299 | 1 | R → A: Loss of GTase activity | |||||||||||||||||||||||||||||||||||
| Mutagenesis | 345 | 1 | E → A: Loss of GTase activity | |||||||||||||||||||||||||||||||||||
| Mutagenesis | 458 | 1 | K → A: Loss of GTase activity | |||||||||||||||||||||||||||||||||||
| Mutagenesis | 460 | 1 | K → A: Loss of GTase activity | |||||||||||||||||||||||||||||||||||
| Sequence conflict | 30 | 1 | M → I in AAB91559. Ref.1 | |||||||||||||||||||||||||||||||||||
| Sequence conflict | 212 | 1 | P → T in AAH19954. Ref.6 | |||||||||||||||||||||||||||||||||||
| Sequence conflict | 484 | 1 | Q → P in AAB91559. Ref.1 | |||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||
| Turn | 21 – 23 | 3 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 24 – 27 | 4 | ||||||||||||||||||||||||||||||||||||
| Helix | 33 – 38 | 6 | ||||||||||||||||||||||||||||||||||||
| Helix | 41 – 43 | 3 | ||||||||||||||||||||||||||||||||||||
| Helix | 47 – 57 | 11 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 60 – 66 | 7 | ||||||||||||||||||||||||||||||||||||
| Helix | 77 – 80 | 4 | ||||||||||||||||||||||||||||||||||||
| Turn | 81 – 83 | 3 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 85 – 88 | 4 | ||||||||||||||||||||||||||||||||||||
| Helix | 100 – 110 | 11 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 120 – 125 | 6 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 127 – 130 | 4 | ||||||||||||||||||||||||||||||||||||
| Helix | 131 – 143 | 13 | ||||||||||||||||||||||||||||||||||||
| Helix | 149 – 159 | 11 | ||||||||||||||||||||||||||||||||||||
| Helix | 167 – 177 | 11 | ||||||||||||||||||||||||||||||||||||
| Helix | 180 – 182 | 3 | ||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II." Yue Z., Maldonado E., Pillutla R., Cho H., Reinberg D., Shatkin A.J. Proc. Natl. Acad. Sci. U.S.A. 94:12898-12903(1997) [PubMed: 9371772] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). |
| [2] | "Isolation and characterization of a human cDNA for mRNA 5'-capping enzyme." Yamada-Okabe T., Doi R., Shimmi O., Arisawa M., Yamada-Okabe H. Nucleic Acids Res. 26:1700-1706(1998) [PubMed: 9512541] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), MUTAGENESIS. |
| [3] | "Cloning and characterization of two human cDNAs encoding the mRNA capping enzyme." Tsukamoto T., Shibagaki Y., Murakoshi T., Suzuki M., Nakamura A., Gotoh H., Mizumoto K. Biochem. Biophys. Res. Commun. 243:101-108(1998) [PubMed: 9473487] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4). Tissue: Colon adenocarcinoma. |
| [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. Beck S.Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [5] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-594. Tissue: Skin. |
| [7] | "Recombinant human mRNA cap methyltransferase binds capping enzyme/RNA polymerase IIo complexes." Pillutla R.C., Yue Z., Maldonado E., Shatkin A.J. J. Biol. Chem. 273:21443-21446(1998) [PubMed: 9705270] [Abstract] Cited for: INTERACTION WITH RNMT. |
| [8] | "Transcription elongation factor hSPT5 stimulates mRNA capping." Wen Y., Shatkin A.J. Genes Dev. 13:1774-1779(1999) [PubMed: 10421630] [Abstract] Cited for: INTERACTION WITH SUPT5H. |
| [9] | "HIV-1 Tat protein interacts with mammalian capping enzyme and stimulates capping of TAR RNA." Chiu Y.-L., Coronel E., Ho C.K., Shuman S., Rana T.M. J. Biol. Chem. 276:12959-12966(2001) [PubMed: 11278368] [Abstract] Cited for: INTERACTION WITH HIV-1 TAT. |
| [10] | "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, MASS SPECTROMETRY. Tissue: Epithelium. |
Cross-references
Sequence databases | |
|---|---|
| AF025654 mRNA. Translation: AAB91559.1. AB009022 mRNA. Translation: BAA25894.1. AB009023 mRNA. Translation: BAA25895.1. AB009024 mRNA. Translation: BAA25896.1. AB012142 mRNA. Translation: BAA25198.1. AB012143 mRNA. Translation: BAA25199.1. AL079342 AL445530 Genomic DNA. Translation: CAI22537.1. AL096868 AL445530 Genomic DNA. Translation: CAI21547.1. AL133408 ![]() | |

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