UniProt Accession

 MCE1_HUMAN; O60942; E1P513; E1P514; O43483; O60257; O60351; Q5TCW8; Q8WUM8 

Genbank Protein ID

 AF025654; AB009022; AB009023; AB009024; AB012142; AB012143; AL079342; AL096868; AL133408; AL445530; AL096868; AL079342; AL133408; AL445530; AL133408; AL079342; AL096868; AL445530; AL445530; AL079342; AL096868; AL133408; CH471051; CH471051; CH471051; CH471051; BC019954 

Genbank Nucleotide ID

 AAB91559.1; BAA25894.1; BAA25895.1; BAA25896.1; BAA25198.1; BAA25199.1; CAI22537.1; CAI22537.1; CAI22537.1; CAI22537.1; CAI21547.1; CAI21547.1; CAI21547.1; CAI21547.1; CAI21542.1; CAI21542.1; CAI21542.1; CAI21542.1; CAI22048.1; CAI22048.1; CAI22048.1; CAI22048.1; EAW48566.1; EAW48567.1; EAW48569.1; EAW48570.1; AAH19954.1 

Protein Name

 mRNA-capping enzyme 

Protein Synonyms/Alias

 HCAP1; HCE; Polynucleotide 5'-triphosphatase; mRNA 5'-triphosphatase; TPase; mRNA guanylyltransferase; GTP--RNA guanylyltransferase; GTase 

Gene Name

 RNGTT 

Gene Synonyms/Alias

 CAP1A 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
28	AGRFLPLKTMLGPRY	ubiquitination	[1, 2, 3, 4]
81	YDRNDIEKEGIKYIK	ubiquitination	[3]
85	DIEKEGIKYIKLQCK	ubiquitination	[3]
92	KYIKLQCKGHGECPT	ubiquitination	[3]
171	IYKGDYLKELFRRYG	ubiquitination	[1, 3, 4, 5]
249	TQVTTQPKLGEVQQK	ubiquitination	[3]
287	NIKLLDLKPYKVSWK	ubiquitination	[3]
290	LLDLKPYKVSWKADG	ubiquitination	[3]
294	KPYKVSWKADGTRYM	ubiquitination	[3]
395	IISPRHEKMKTGLID	acetylation	[6]
397	SPRHEKMKTGLIDKT	acetylation	[6]
397	SPRHEKMKTGLIDKT	ubiquitination	[3]
403	MKTGLIDKTQEPFSV	ubiquitination	[3, 5]
413	EPFSVRNKPFFDICT	ubiquitination	[3]
423	FDICTSRKLLEGNFA	ubiquitination	[3]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 

Functional Description

 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. 

Sequence Annotation

 REGION 1 212 TPase.
 REGION 229 597 GTase.
 ACT_SITE 126 126 For RNA 5'-triphosphatase activity (By
 ACT_SITE 294 294 N6-GMP-lysine intermediate.  

Keyword

 3D-structure; Alternative splicing; Complete proteome; GTP-binding; Host-virus interaction; Hydrolase; mRNA capping; mRNA processing; Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase; Nucleus; Polymorphism; Reference proteome; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 597 AA 

Protein Sequence

Gene Ontology

 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0004484; F:mRNA guanylyltransferase activity; TAS:ProtInc.
 GO:0004651; F:polynucleotide 5'-phosphatase activity; IEA:EC.
 GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
 GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
 GO:0006370; P:7-methylguanosine mRNA capping; TAS:Reactome.
 GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC.
 GO:0006366; P:transcription from RNA polymerase II promoter; TAS:Reactome.
 GO:0022415; P:viral reproductive process; TAS:Reactome.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 

Interpro

 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.
 IPR000387; Tyr/Dual-sp_Pase.
 IPR016130; Tyr_Pase_AS. 

Pfam

 PF00782; DSPc
 PF03919; mRNA_cap_C
 PF01331; mRNA_cap_enzyme 

SMART

  

PROSITE

 PS00383; TYR_PHOSPHATASE_1
 PS50056; TYR_PHOSPHATASE_2 

PRINTS