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[1]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
DOI=10.1073/pnas.94.24.12898; PubMed=9371772 [NCBI, ExPASy, EBI, Israel, Japan]
Yue Z.,
Maldonado E.,
Pillutla R.,
Cho H.,
Reinberg D.,
Shatkin A.J.;
"Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II.";
Proc. Natl. Acad. Sci. U.S.A. 94:12898-12903(1997).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND MUTAGENESIS.
DOI=10.1093/nar/26.7.1700; PubMed=9512541 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada-Okabe T.,
Doi R.,
Shimmi O.,
Arisawa M.,
Yamada-Okabe H.;
"Isolation and characterization of a human cDNA for mRNA 5'-capping enzyme.";
Nucleic Acids Res. 26:1700-1706(1998).
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[3]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4).
TISSUE=Colon adenocarcinoma;
DOI=10.1006/bbrc.1997.8038; PubMed=9473487 [NCBI, ExPASy, EBI, Israel, Japan]
Tsukamoto T.,
Shibagaki Y.,
Murakoshi T.,
Suzuki M.,
Nakamura A.,
Gotoh H.,
Mizumoto K.;
"Cloning and characterization of two human cDNAs encoding the mRNA capping enzyme.";
Biochem. Biophys. Res. Commun. 243:101-108(1998).
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[4]
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INTERACTION WITH RNMT.
DOI=10.1074/jbc.273.34.21443; PubMed=9705270 [NCBI, ExPASy, EBI, Israel, Japan]
Pillutla R.C.,
Yue Z.,
Maldonado E.,
Shatkin A.J.;
"Recombinant human mRNA cap methyltransferase binds capping enzyme/RNA polymerase IIo complexes.";
J. Biol. Chem. 273:21443-21446(1998).
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[5]
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INTERACTION WITH SUPT5H.
PubMed=10421630 [NCBI, ExPASy, EBI, Israel, Japan]
Wen Y.,
Shatkin A.J.;
"Transcription elongation factor hSPT5 stimulates mRNA capping.";
Genes Dev. 13:1774-1779(1999).
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[6]
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INTERACTION WITH HIV-1 TAT.
DOI=10.1074/jbc.M007901200; PubMed=11278368 [NCBI, ExPASy, EBI, Israel, Japan]
Chiu Y.-L.,
Coronel E.,
Ho C.K.,
Shuman S.,
Rana T.M.;
"HIV-1 Tat protein interacts with mammalian capping enzyme and stimulates capping of TAR RNA.";
J. Biol. Chem. 276:12959-12966(2001).
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[7]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V.,
Blagoev B.,
Gnad F.,
Macek B.,
Kumar C.,
Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
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- 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 + H2O = a polynucleotide + phosphate.
- CATALYTIC ACTIVITY: GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA.
- SUBUNIT: Interacts with SUPT5H and RNMT. Interacts with HIV-1 Tat.
- SUBCELLULAR LOCATION: Nucleus (By similarity).
- ALTERNATIVE PRODUCTS:
4 named isoforms [FASTA] produced by alternative splicing.
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| Name | 2 |
| Synonyms | HCE1A |
| Isoform ID | O60942-2 |
| Features which should be applied to build the isoform sequence: VSP_003202. |
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| Name | 4 |
| Synonyms | HCAP1B |
| Isoform ID | O60942-4 |
| Features which should be applied to build the isoform sequence: VSP_003204. |
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- 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.
- SIMILARITY: In the N-terminal section; belongs to the non-receptor class of the protein-tyrosine phosphatase family.
- SIMILARITY: In the C-terminal section; belongs to the eukaryotic GTase family.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 597 AA [This is the length of the unprocessed precursor] |
Molecular weight: 68557 Da [This is the MW of the unprocessed precursor] |
CRC64: 51CEEC1B190603DE [This is a checksum on the sequence] |
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10 20 30 40 50 60
MAHNKIPPRW LNCPRRGQPV AGRFLPLKTM LGPRYDSQVA EENRFHPSML SNYLKSLKVK
70 80 90 100 110 120
MGLLVDLTNT SRFYDRNDIE KEGIKYIKLQ CKGHGECPTT ENTETFIRLC ERFNERNPPE
130 140 150 160 170 180
LIGVHCTHGF NRTGFLICAF LVEKMDWSIE AAVATFAQAR PPGIYKGDYL KELFRRYGDI
190 200 210 220 230 240
EEAPPPPLLP DWCFEDDEDE DEDEDGKKES EPGSSASFGK RRKERLKLGA IFLEGVTVKG
250 260 270 280 290 300
VTQVTTQPKL GEVQQKCHQF CGWEGSGFPG AQPVSMDKQN IKLLDLKPYK VSWKADGTRY
310 320 330 340 350 360
MMLIDGTNEV FMIDRDNSVF HVSNLEFPFR KDLRMHLSNT LLDGEMIIDR VNGQAVPRYL
370 380 390 400 410 420
IYDIIKFNSQ PVGDCDFNVR LQCIEREIIS PRHEKMKTGL IDKTQEPFSV RNKPFFDICT
430 440 450 460 470 480
SRKLLEGNFA KEVSHEMDGL IFQPTGKYKP GRCDDILKWK PPSLNSVDFR LKITRMGGEG
490 500 510 520 530 540
LLPQNVGLLY VGGYERPFAQ IKVTKELKQY DNKIIECKFE NNSWVFMRQR TDKSFPNAYN
550 560 570 580 590
TAMAVCNSIS NPVTKEMLFE FIDRCTAASQ GQKRKHHLDP DTELMPPPPP KRPRPLT
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O60942 in FASTA format |
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