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O60942

- MCE1_HUMAN

UniProt

O60942 - MCE1_HUMAN

Protein

mRNA-capping enzyme

Gene

RNGTT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    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.3 Publications

    Catalytic activityi

    A 5'-phosphopolynucleotide + H2O = a polynucleotide + phosphate.
    GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei126 – 1261For RNA 5'-triphosphatase activityBy similarity
    Active sitei294 – 2941N6-GMP-lysine intermediate1 Publication
    Binding sitei299 – 2991GTPBy similarity
    Binding sitei315 – 3151GTPSequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi343 – 3453GTPSequence Analysis
    Nucleotide bindingi458 – 4603GTPSequence Analysis
    Nucleotide bindingi528 – 5336GTPSequence Analysis

    GO - Molecular functioni

    1. GTP binding Source: UniProtKB-KW
    2. mRNA guanylyltransferase activity Source: UniProtKB
    3. polynucleotide 5'-phosphatase activity Source: UniProtKB-EC
    4. protein tyrosine/serine/threonine phosphatase activity Source: InterPro
    5. protein tyrosine phosphatase activity Source: InterPro
    6. RNA guanylyltransferase activity Source: UniProtKB
    7. triphosphatase activity Source: UniProtKB

    GO - Biological processi

    1. 7-methylguanosine mRNA capping Source: UniProtKB
    2. gene expression Source: Reactome
    3. RNA processing Source: UniProtKB
    4. transcription from RNA polymerase II promoter Source: Reactome
    5. viral process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Host-virus interaction, mRNA capping, mRNA processing

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03479-MONOMER.
    BRENDAi2.7.7.50. 2681.
    ReactomeiREACT_1470. mRNA Capping.
    REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
    REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    mRNA-capping enzyme
    Alternative name(s):
    HCAP1
    HCE
    Including the following 2 domains:
    Polynucleotide 5'-triphosphatase (EC:3.1.3.33)
    Alternative name(s):
    mRNA 5'-triphosphatase
    Short name:
    TPase
    mRNA guanylyltransferase (EC:2.7.7.50)
    Alternative name(s):
    GTP--RNA guanylyltransferase
    Short name:
    GTase
    Gene namesi
    Name:RNGTT
    Synonyms:CAP1A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:10073. RNGTT.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. nucleus Source: ProtInc

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi234 – 2341E → A: No effect on GTase activity. 1 Publication
    Mutagenesisi294 – 2941K → A: Loss of GTase activity. 1 Publication
    Mutagenesisi299 – 2991R → A: Loss of GTase activity. 1 Publication
    Mutagenesisi345 – 3451E → A: Loss of GTase activity. 1 Publication
    Mutagenesisi458 – 4581K → A: Loss of GTase activity. 2 Publications
    Mutagenesisi460 – 4601K → A: Loss of GTase activity. 2 Publications
    Mutagenesisi528 – 5281R → A: Strongly reduced GTase activity. 1 Publication
    Mutagenesisi530 – 5301R → A: Loss of GTase activity. 1 Publication
    Mutagenesisi532 – 5321D → A: Loss of GTase activity. 1 Publication
    Mutagenesisi533 – 5331K → A: Loss of GTase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA34446.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 597597mRNA-capping enzymePRO_0000210108Add
    BLAST

    Proteomic databases

    MaxQBiO60942.
    PaxDbiO60942.
    PRIDEiO60942.

    PTM databases

    PhosphoSiteiO60942.

    Expressioni

    Tissue specificityi

    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.

    Gene expression databases

    ArrayExpressiO60942.
    BgeeiO60942.
    CleanExiHS_RNGTT.
    GenevestigatoriO60942.

    Organism-specific databases

    HPAiHPA003750.

    Interactioni

    Subunit structurei

    Interacts with POLR2A (via C-terminus); this enhances guanylyltransferase activity. Binds (via GTase domain) to the elongating phosphorylated form of RNA polymerase II; can form direct interactions with the phosphorylated POLR2A C-terminal domain and indirect interactions via bound RNA By similarity. Interacts with SUPT5H and RNMT. Interacts with HIV-1 Tat.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi114270. 8 interactions.
    IntActiO60942. 1 interaction.
    STRINGi9606.ENSP00000358497.

    Structurei

    Secondary structure

    1
    597
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni21 – 233
    Beta strandi24 – 274
    Helixi33 – 386
    Helixi41 – 433
    Helixi47 – 5711
    Beta strandi60 – 667
    Helixi77 – 804
    Turni81 – 833
    Beta strandi85 – 884
    Helixi100 – 11011
    Beta strandi120 – 1256
    Beta strandi127 – 1304
    Helixi131 – 14313
    Helixi149 – 15911
    Helixi167 – 17711
    Helixi180 – 1823
    Beta strandi232 – 2354
    Beta strandi241 – 2433
    Helixi247 – 26115
    Beta strandi265 – 2673
    Beta strandi270 – 2756
    Turni278 – 2803
    Helixi281 – 2855
    Beta strandi289 – 2957
    Beta strandi298 – 3047
    Beta strandi306 – 3083
    Beta strandi310 – 3145
    Beta strandi319 – 3246
    Beta strandi339 – 35113
    Beta strandi354 – 36714
    Helixi372 – 3743
    Helixi377 – 38711
    Helixi389 – 3946
    Turni395 – 3973
    Beta strandi398 – 4014
    Turni403 – 4053
    Beta strandi406 – 4127
    Helixi418 – 4247
    Beta strandi437 – 44610
    Beta strandi451 – 4599
    Helixi462 – 4643
    Beta strandi466 – 47611
    Beta strandi484 – 4907
    Beta strandi498 – 5014
    Helixi507 – 5093
    Beta strandi512 – 5209
    Beta strandi523 – 5297
    Helixi539 – 55012
    Helixi555 – 5639

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2C46X-ray1.60A/B/C/D1-219[»]
    3S24X-ray3.01A/B/C/D/E/F/G229-567[»]
    ProteinModelPortaliO60942.
    SMRiO60942. Positions 4-199, 229-565.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO60942.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 212212TPaseAdd
    BLAST
    Regioni229 – 597369GTaseAdd
    BLAST
    Regioni330 – 38657Interaction with POLR2ABy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi195 – 20511Asp/Glu-richAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the non-receptor class of the protein-tyrosine phosphatase family.Curated
    In the C-terminal section; belongs to the eukaryotic GTase family.Curated

    Phylogenomic databases

    eggNOGiCOG5226.
    HOVERGENiHBG006332.
    InParanoidiO60942.
    KOiK13917.
    OMAiRFNERSP.
    OrthoDBiEOG7HB592.
    PhylomeDBiO60942.
    TreeFamiTF314914.

    Family and domain databases

    Gene3Di2.40.50.140. 1 hit.
    3.90.190.10. 1 hit.
    InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
    IPR017074. mRNA_cap_enz_bifunc.
    IPR001339. mRNA_cap_enzyme.
    IPR013846. mRNA_cap_enzyme_C.
    IPR012340. NA-bd_OB-fold.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view]
    PfamiPF00782. DSPc. 1 hit.
    PF03919. mRNA_cap_C. 1 hit.
    PF01331. mRNA_cap_enzyme. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036958. mRNA_capping_HCE. 1 hit.
    SUPFAMiSSF50249. SSF50249. 1 hit.
    SSF52799. SSF52799. 1 hit.
    PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O60942-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAHNKIPPRW LNCPRRGQPV AGRFLPLKTM LGPRYDSQVA EENRFHPSML    50
    SNYLKSLKVK MGLLVDLTNT SRFYDRNDIE KEGIKYIKLQ CKGHGECPTT 100
    ENTETFIRLC ERFNERNPPE LIGVHCTHGF NRTGFLICAF LVEKMDWSIE 150
    AAVATFAQAR PPGIYKGDYL KELFRRYGDI EEAPPPPLLP DWCFEDDEDE 200
    DEDEDGKKES EPGSSASFGK RRKERLKLGA IFLEGVTVKG VTQVTTQPKL 250
    GEVQQKCHQF CGWEGSGFPG AQPVSMDKQN IKLLDLKPYK VSWKADGTRY 300
    MMLIDGTNEV FMIDRDNSVF HVSNLEFPFR KDLRMHLSNT LLDGEMIIDR 350
    VNGQAVPRYL IYDIIKFNSQ PVGDCDFNVR LQCIEREIIS PRHEKMKTGL 400
    IDKTQEPFSV RNKPFFDICT SRKLLEGNFA KEVSHEMDGL IFQPTGKYKP 450
    GRCDDILKWK PPSLNSVDFR LKITRMGGEG LLPQNVGLLY VGGYERPFAQ 500
    IKVTKELKQY DNKIIECKFE NNSWVFMRQR TDKSFPNAYN TAMAVCNSIS 550
    NPVTKEMLFE FIDRCTAASQ GQKRKHHLDP DTELMPPPPP KRPRPLT 597
    Length:597
    Mass (Da):68,557
    Last modified:August 1, 1998 - v1
    Checksum:i51CEEC1B190603DE
    GO
    Isoform 2 (identifier: O60942-2) [UniParc]FASTAAdd to Basket

    Also known as: HCE1A

    The sequence of this isoform differs from the canonical sequence as follows:
         424-446: Missing.

    Show »
    Length:574
    Mass (Da):66,042
    Checksum:iCFE64E51F6F88232
    GO
    Isoform 3 (identifier: O60942-3) [UniParc]FASTAAdd to Basket

    Also known as: HCE1B

    The sequence of this isoform differs from the canonical sequence as follows:
         424-446: Missing.
         481-597: Missing.

    Show »
    Length:457
    Mass (Da):52,533
    Checksum:i4F3B52CA4F6CC56B
    GO
    Isoform 4 (identifier: O60942-4) [UniParc]FASTAAdd to Basket

    Also known as: HCAP1B

    The sequence of this isoform differs from the canonical sequence as follows:
         504-597: TKELKQYDNK...PPPKRPRPLT → CLFIFSVLFL...KISCSSTLGG

    Show »
    Length:541
    Mass (Da):61,705
    Checksum:iDF795898785EC2D4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti30 – 301M → I in AAB91559. (PubMed:9371772)Curated
    Sequence conflicti212 – 2121P → T in AAH19954. (PubMed:15489334)Curated
    Sequence conflicti484 – 4841Q → P in AAB91559. (PubMed:9371772)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti594 – 5941R → H.1 Publication
    Corresponds to variant rs17856595 [ dbSNP | Ensembl ].
    VAR_046481

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei424 – 44623Missing in isoform 2 and isoform 3. 1 PublicationVSP_003202Add
    BLAST
    Alternative sequencei481 – 597117Missing in isoform 3. 1 PublicationVSP_003203Add
    BLAST
    Alternative sequencei504 – 59794TKELK…PRPLT → CLFIFSVLFLDVLLSGIHQN LANNNQHIKISCSSTLGG in isoform 4. 1 PublicationVSP_003204Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , AL096868, AL133408, AL445530 Genomic DNA. Translation: CAI22537.1.
    AL096868
    , AL079342, AL133408, AL445530 Genomic DNA. Translation: CAI21547.1.
    AL133408
    , AL079342, AL096868, AL445530 Genomic DNA. Translation: CAI21542.1.
    AL445530
    , AL079342, AL096868, AL133408 Genomic DNA. Translation: CAI22048.1.
    CH471051 Genomic DNA. Translation: EAW48566.1.
    CH471051 Genomic DNA. Translation: EAW48567.1.
    CH471051 Genomic DNA. Translation: EAW48569.1.
    CH471051 Genomic DNA. Translation: EAW48570.1.
    BC019954 mRNA. Translation: AAH19954.1.
    CCDSiCCDS5017.1. [O60942-1]
    CCDS69153.1. [O60942-2]
    PIRiJC5936.
    JC5937.
    RefSeqiNP_001273355.1. NM_001286426.1. [O60942-2]
    NP_001273357.1. NM_001286428.1.
    NP_003791.3. NM_003800.4. [O60942-1]
    UniGeneiHs.567378.
    Hs.627135.

    Genome annotation databases

    EnsembliENST00000369485; ENSP00000358497; ENSG00000111880. [O60942-1]
    GeneIDi8732.
    KEGGihsa:8732.
    UCSCiuc003pmr.2. human. [O60942-1]
    uc003pms.2. human. [O60942-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , AL096868 , AL133408 , AL445530 Genomic DNA. Translation: CAI22537.1 .
    AL096868
    , AL079342 , AL133408 , AL445530 Genomic DNA. Translation: CAI21547.1 .
    AL133408
    , AL079342 , AL096868 , AL445530 Genomic DNA. Translation: CAI21542.1 .
    AL445530
    , AL079342 , AL096868 , AL133408 Genomic DNA. Translation: CAI22048.1 .
    CH471051 Genomic DNA. Translation: EAW48566.1 .
    CH471051 Genomic DNA. Translation: EAW48567.1 .
    CH471051 Genomic DNA. Translation: EAW48569.1 .
    CH471051 Genomic DNA. Translation: EAW48570.1 .
    BC019954 mRNA. Translation: AAH19954.1 .
    CCDSi CCDS5017.1. [O60942-1 ]
    CCDS69153.1. [O60942-2 ]
    PIRi JC5936.
    JC5937.
    RefSeqi NP_001273355.1. NM_001286426.1. [O60942-2 ]
    NP_001273357.1. NM_001286428.1.
    NP_003791.3. NM_003800.4. [O60942-1 ]
    UniGenei Hs.567378.
    Hs.627135.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2C46 X-ray 1.60 A/B/C/D 1-219 [» ]
    3S24 X-ray 3.01 A/B/C/D/E/F/G 229-567 [» ]
    ProteinModelPortali O60942.
    SMRi O60942. Positions 4-199, 229-565.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114270. 8 interactions.
    IntActi O60942. 1 interaction.
    STRINGi 9606.ENSP00000358497.

    PTM databases

    PhosphoSitei O60942.

    Proteomic databases

    MaxQBi O60942.
    PaxDbi O60942.
    PRIDEi O60942.

    Protocols and materials databases

    DNASUi 8732.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369485 ; ENSP00000358497 ; ENSG00000111880 . [O60942-1 ]
    GeneIDi 8732.
    KEGGi hsa:8732.
    UCSCi uc003pmr.2. human. [O60942-1 ]
    uc003pms.2. human. [O60942-2 ]

    Organism-specific databases

    CTDi 8732.
    GeneCardsi GC06M089376.
    HGNCi HGNC:10073. RNGTT.
    HPAi HPA003750.
    MIMi 603512. gene.
    neXtProti NX_O60942.
    PharmGKBi PA34446.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5226.
    HOVERGENi HBG006332.
    InParanoidi O60942.
    KOi K13917.
    OMAi RFNERSP.
    OrthoDBi EOG7HB592.
    PhylomeDBi O60942.
    TreeFami TF314914.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS03479-MONOMER.
    BRENDAi 2.7.7.50. 2681.
    Reactomei REACT_1470. mRNA Capping.
    REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
    REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.

    Miscellaneous databases

    ChiTaRSi RNGTT. human.
    EvolutionaryTracei O60942.
    GeneWikii RNGTT.
    GenomeRNAii 8732.
    NextBioi 32757.
    PROi O60942.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60942.
    Bgeei O60942.
    CleanExi HS_RNGTT.
    Genevestigatori O60942.

    Family and domain databases

    Gene3Di 2.40.50.140. 1 hit.
    3.90.190.10. 1 hit.
    InterProi IPR000340. Dual-sp_phosphatase_cat-dom.
    IPR017074. mRNA_cap_enz_bifunc.
    IPR001339. mRNA_cap_enzyme.
    IPR013846. mRNA_cap_enzyme_C.
    IPR012340. NA-bd_OB-fold.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view ]
    Pfami PF00782. DSPc. 1 hit.
    PF03919. mRNA_cap_C. 1 hit.
    PF01331. mRNA_cap_enzyme. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036958. mRNA_capping_HCE. 1 hit.
    SUPFAMi SSF50249. SSF50249. 1 hit.
    SSF52799. SSF52799. 1 hit.
    PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), MUTAGENESIS OF LYS-294; ARG-299; GLU-345; LYS-458 AND LYS-460, FUNCTION.
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), FUNCTION, CATALYTIC ACTIVITY.
      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.
      , 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.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 TAT.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 229-567, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF GLU-234; LYS-458; LYS-460; ARG-528; ARG-530; ASP-532 AND LYS-533, ACTIVE SITE.

    Entry informationi

    Entry nameiMCE1_HUMAN
    AccessioniPrimary (citable) accession number: O60942
    Secondary accession number(s): E1P513
    , E1P514, O43483, O60257, O60351, Q5TCW8, Q8WUM8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 143 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

    Miscellaneous

    Isoform 2 to isoform 4 lack mRNA 5'-guanylyltransferase activity due to disruptions of the GTase domain.

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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