UniProt Accession

 MTR1_HUMAN; Q8N1G2; A8K949; Q14670; Q96FJ9 

Genbank Protein ID

 D43949; AK292564; AL353597; BC010731; BC031890 

Genbank Nucleotide ID

 BAA07893.2; BAF85253.1; CAI19603.1; AAH10731.2; AAH31890.1 

Protein Name

 Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 

Protein Synonyms/Alias

 Cap1 2'O-ribose methyltransferase 1; MTr1; hMTr1; FtsJ methyltransferase domain-containing protein 2; Interferon-stimulated gene 95 kDa protein; ISG95 

Gene Name

 FTSJD2 

Gene Synonyms/Alias

 KIAA0082; MTR1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
93	MYNSVSQKLMAKMGF	ubiquitination	[1]
97	VSQKLMAKMGFREGE	acetylation	[2]
97	VSQKLMAKMGFREGE	ubiquitination	[1]
108	REGEGLGKYSQGRKD	acetylation	[3]
108	REGEGLGKYSQGRKD	ubiquitination	[1]
114	GKYSQGRKDIVEASS	ubiquitination	[1]
123	IVEASSQKGRRGLGL	ubiquitination	[1]
239	FLNRAAMKMANMDFV	ubiquitination	[1]
260	NPRDSYGKPLVKDRE	ubiquitination	[1]
447	SERYVVCKGLKVGID	ubiquitination	[1, 4]
450	YVVCKGLKVGIDDVR	ubiquitination	[1]
487	VVPLEVIKGDHEFTD	ubiquitination	[1]
509	SHCSLQIKALAKIHA	ubiquitination	[1]
513	LQIKALAKIHAFVQD	ubiquitination	[1]
584	LTSKTLEKIRPVFDY	acetylation	[5]
584	LTSKTLEKIRPVFDY	ubiquitination	[1]
608	KFLIGLGKSQIYTWD	ubiquitination	[1, 4]
624	RQSDRWIKLDLKTEL	ubiquitination	[1]
685	QRIQLAEKFVKAVSK	ubiquitination	[1]
692	KFVKAVSKPSRPDMN	ubiquitination	[1]
704	DMNPIRVKEVYRLEE	ubiquitination	[1]
714	YRLEEMEKIFVRLEM	ubiquitination	[1]
722	IFVRLEMKIIKGSSG	ubiquitination	[1]
732	KGSSGTPKLSYTGRD	ubiquitination	[1]
764	PWTMGFSKSFKKKFF	ubiquitination	[1]
767	MGFSKSFKKKFFYNK	ubiquitination	[1]
774	KKKFFYNKKTKDSTF	ubiquitination	[1]
777	FFYNKKTKDSTFDLP	ubiquitination	[1]
823	QDQDKLSKEDVLSFI	ubiquitination	[6, 7, 8]

Reference

 [1] 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]
 [2] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [3] 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]
 [4] 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]
 [5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [6] 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]
 [7] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [8] 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] 

Functional Description

 S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA to produce m(7)GpppNmp (cap1). Cap1 modification is linked to higher levels of translation. May be involved in the interferon response pathway. 

Sequence Annotation

 DOMAIN 87 133 G-patch.
 DOMAIN 752 786 WW.
 REGION 727 835 Interaction with POLR2A.
 ACT_SITE 404 404 Proton acceptor (By similarity).
 BINDING 281 281 S-adenosyl-L-methionine; via amide
 BINDING 311 311 S-adenosyl-L-methionine (By similarity).
 BINDING 364 364 S-adenosyl-L-methionine (By similarity).
 MOD_RES 28 28 Phosphoserine (By similarity).
 MOD_RES 31 31 Phosphoserine (By similarity).
 MOD_RES 108 108 N6-acetyllysine.  

Keyword

 Acetylation; Complete proteome; Methyltransferase; mRNA capping; mRNA processing; Nucleus; Phosphoprotein; Reference proteome; S-adenosyl-L-methionine; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 835 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IDA:UniProtKB.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0006370; P:7-methylguanosine mRNA capping; IMP:UniProtKB. 

Interpro

 IPR025816; Cap_mRNA_MeTrfase_1.
 IPR000467; G_patch_dom.
 IPR002877; rRNA_MeTrfase_FtsJ_dom.
 IPR001202; WW_dom. 

Pfam

 PF01728; FtsJ
 PF01585; G-patch 

SMART

 SM00443; G_patch
 SM00456; WW 

PROSITE

 PS50174; G_PATCH
 PS01159; WW_DOMAIN_1
 PS50020; WW_DOMAIN_2 

PRINTS