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UniProtKB/Swiss-Prot entry O60942


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MCE1_HUMAN
Primary accession number O60942
Secondary accession numbers O43483 O60257 O60351 Q5TCW8 Q8WUM8
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on August 1, 1998 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 88)
Name and origin of the protein
Protein name mRNA-capping enzyme
Synonyms HCE
HCAP1
Includes Polynucleotide 5'-triphosphatase
     (EC 3.1.3.33)
     (mRNA 5'-triphosphatase)
     (TPase)
mRNA guanylyltransferase
     (EC 2.7.7.50)
     (GTP--RNA guanylyltransferase)
     (GTase)
Gene name
Name: RNGTT
Synonyms: CAP1A
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
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).
[2]
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).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
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., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-594.
TISSUE=Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
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).
[8]
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).
[9]
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).
[10]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF025654; AAB91559.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB009022; BAA25894.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB009023; BAA25895.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB009024; BAA25896.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB012142; BAA25198.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB012143; BAA25199.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL079342; CAI22537.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL096868; CAI22537.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133408; CAI22537.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL445530; CAI22537.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL096868; CAI21547.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL079342; CAI21547.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133408; CAI21547.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL445530; CAI21547.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133408; CAI21542.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL079342; CAI21542.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL096868; CAI21542.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL445530; CAI21542.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL445530; CAI22048.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL079342; CAI22048.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL096868; CAI22048.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133408; CAI22048.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471051; EAW48566.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC019954; AAH19954.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JC5936; JC5936.
JC5937; JC5937.
RefSeq NP_003791.3; -.
UniGene Hs.705569
3D structure databases
PDB
2C46; X-ray; 1.60 A; A/B/C/D=1-219.[ExPASy / RCSB / EBI]
PDBsum 2C46; -.
ModBase O60942.
PTM databases
PhosphoSite O60942; -.
Enzyme and pathway databases
Reactome REACT_1675; mRNA Processing.
REACT_1788; Transcription.
REACT_6185; HIV Infection.
REACT_71; Gene Expression.
Organism-specific databases
GeneCards GC06M089376; -.
H-InvDB HIX0006059; -.
HGNC HGNC:10073; RNGTT.
GenAtlas RNGTT.
HPA HPA003750; -.
MIM 603512; gene. [NCBI / EBI]
PharmGKB PA34446; -.
GeneCards O60942.
Gene expression databases
ArrayExpress O60942; -.
CleanEx HS_RNGTT; -.
GermOnline ENSG00000111880; Homo sapiens.
Ontologies
GO
GO:0005654; Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0004484; Molecular function: mRNA guanylyltransferase activity (traceable author statement from ProtInc).
GO:0004651; Molecular function: polynucleotide 5'-phosphatase activity (inferred from electronic annotation from EC).
GO:0004725; Molecular function: protein tyrosine phosphatase activity (inferred from electronic annotation from InterPro).
GO:0008138; Molecular function: protein tyrosine/serine/threonine phosphatase activity (inferred from electronic annotation from InterPro).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0006370; Biological process: mRNA capping (traceable author statement from ProtInc).
GO:0006470; Biological process: protein amino acid dephosphorylation (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR017074; mRNA_cap_enz_bifunc.
IPR001339; mRNA_cap_enzyme.
IPR013846; mRNA_cap_enzyme_C.
IPR000387; Tyr_Pase.
IPR016130; Tyr_Pase_AS.
IPR000340; Tyr_Pase_dual_specific.
Graphical view of domain structure.
Pfam PF00782; DSPc; 1.
PF03919; mRNA_cap_C; 1.
PF01331; mRNA_cap_enzyme; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF036958; mRNA_capping_HCE; 1.
PROSITE PS00383; TYR_PHOSPHATASE_1; 1.
PS50056; TYR_PHOSPHATASE_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomics databases
PRIDE O60942; -.
Genome annotation databases
Ensembl ENSG00000111880; Homo sapiens. [Contig view]
GeneID 8732; -.
KEGG hsa:8732; -.
Phylogenomic databases
HOGENOM O60942; -.
HOVERGEN O60942; -.
Other
LinkHub O60942; -.
NextBio 32757; -.
SOURCE RNGTT; Homo sapiens.
ProtoNet O60942.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Host-virus interaction; Hydrolase; mRNA capping; mRNA processing; Multifunctional enzyme; Nucleotidyltransferase; Nucleus; Phosphoprotein; Polymorphism; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   597  597     mRNA-capping enzyme. PRO_0000210108
REGION   1   212  212     TPase. 
REGION   229   597  369     GTase. 
COMPBIAS   195   205  11     Asp/Glu-rich. 
ACT_SITE   126   126        For RNA 5'-triphosphatase activity (By similarity). 
ACT_SITE   294   294        N6-GMP-lysine intermediate. 
MOD_RES   210   210        Phosphoserine. 
VAR_SEQ   424   446        Missing (in isoform 2 and isoform 3). VSP_003202
VAR_SEQ   481   597        Missing (in isoform 3). VSP_003203
VAR_SEQ   504   597        TKELKQYDNKIIECKFENNSWVFMRQRTDKSFPNAYNTAM AVCNSISNPVTKEMLFEFIDRCTAASQGQKRKHHLDPDTE LMPPPPPKRPRPLT -> CLFIFSVLFLDVLLSGIHQNLANNNQHIKISCSSTLGG (in isoform 4). VSP_003204
VARIANT   594   594  1     R -> H (in dbSNP:rs17856595 [NCBI]). VAR_046481 
MUTAGEN   294   294        K->A: Loss of GTase activity. 
MUTAGEN   299   299        R->A: Loss of GTase activity. 
MUTAGEN   345   345        E->A: Loss of GTase activity. 
MUTAGEN   458   458        K->A: Loss of GTase activity. 
MUTAGEN   460   460        K->A: Loss of GTase activity. 
CONFLICT   30    30        M -> I (in Ref. 1; AAB91559). 
CONFLICT   212   212        P -> T (in Ref. 6; AAH19954). 
CONFLICT   484   484        Q -> P (in Ref. 1; AAB91559). 
TURN   21    23  3      
STRAND   24    27  4      
HELIX   33    38  6      
HELIX   41    43  3      
HELIX   47    57  11      
STRAND   60    66  7      
HELIX   77    80  4      
TURN   81    83  3      
STRAND   85    88  4      
HELIX   100   110  11      
STRAND   120   125  6      
STRAND   127   130  4      
HELIX   131   143  13      
HELIX   149   159  11      
HELIX   167   177  11      
HELIX   180   182  3      
Sequence information
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]
        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 

O60942 in FASTA format

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