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O60942

- MCE1_HUMAN

UniProt

O60942 - MCE1_HUMAN

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Protein
mRNA-capping enzyme
Gene
RNGTT, CAP1A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.2 Publications
GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei126 – 1261For RNA 5'-triphosphatase activity By similarity
Active sitei294 – 2941N6-GMP-lysine intermediate1 Publication
Binding sitei299 – 2991GTP By similarity
Binding sitei315 – 3151GTP Reviewed prediction

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi343 – 3453GTP Reviewed prediction
Nucleotide bindingi458 – 4603GTP Reviewed prediction
Nucleotide bindingi528 – 5336GTP Reviewed prediction

GO - Molecular functioni

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

GO - Biological processi

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

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
Complete GO annotation...

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 enzyme
PRO_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.3 Publications

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiO60942.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 212212TPase
Add
BLAST
Regioni229 – 597369GTase
Add
BLAST
Regioni330 – 38657Interaction with POLR2A By similarity
Add
BLAST

Compositional bias

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

Sequence similaritiesi

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.

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

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.
VSP_003202Add
BLAST
Alternative sequencei481 – 597117Missing in isoform 3.
VSP_003203Add
BLAST
Alternative sequencei504 – 59794TKELK…PRPLT → CLFIFSVLFLDVLLSGIHQN LANNNQHIKISCSSTLGG in isoform 4.
VSP_003204Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301M → I in AAB91559. 1 Publication
Sequence conflicti212 – 2121P → T in AAH19954. 1 Publication
Sequence conflicti484 – 4841Q → P in AAB91559. 1 Publication

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

EnsembliENST00000265607; ENSP00000265607; ENSG00000111880. [O60942-2]
ENST00000369485; 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...

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 ENST00000265607 ; ENSP00000265607 ; ENSG00000111880 . [O60942-2 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 142 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

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