UniProt Accession

 NEP1_HUMAN; Q92979; O00675; O00726 

Genbank Protein ID

 U47924; U72514; BC055314 

Genbank Nucleotide ID

 AAB51325.1; AAC51641.1; AAH55314.1 

Protein Name

 Ribosomal RNA small subunit methyltransferase NEP1 

Protein Synonyms/Alias

 18S rRNA (pseudouridine-N1-)-methyltransferase NEP1; 18S rRNA Psi1248 methyltransferase; Nucleolar protein EMG1 homolog; Protein C2f; Ribosome biogenesis protein NEP1 

Gene Name

 EMG1 

Gene Synonyms/Alias

 C2F 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
9	AAPSDGFKPRERSGG	acetylation	[1, 2]
9	AAPSDGFKPRERSGG	ubiquitination	[2, 3, 4]
37	PRLGAGNKIGGRRLI	ubiquitination	[2, 4]
59	LETVKVGKTYELLNC	acetylation	[1, 2]
59	LETVKVGKTYELLNC	ubiquitination	[2, 4]
68	YELLNCDKHKSILLK	acetylation	[2]
75	KHKSILLKNGRDPGE	ubiquitination	[2, 5, 6]
154	RAADGPQKLLKVIKN	ubiquitination	[2]

Reference

 [1] 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]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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

 Involved in 40S ribosomal subunit biogenesis and 18S rRNA processing. Specifically catalyzes the N1-methylation of pseudouridine at position 1248 (Psi1248) in 18S rRNA. Thus, appears to be the methyltransferase involved in the biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) in position 1248 in 18S rRNA. Is not able to methylate uridine at this position. 

Sequence Annotation

 REGION 219 224 S-adenosyl-L-methionine binding (By
 BINDING 201 201 S-adenosyl-L-methionine; via amide
 BINDING 206 206 S-adenosyl-L-methionine; via carbonyl
 MOD_RES 2 2 N-acetylalanine.  

Keyword

 Acetylation; Complete proteome; Direct protein sequencing; Disease mutation; Methyltransferase; Nucleus; Polymorphism; Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing; rRNA-binding; S-adenosyl-L-methionine; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 244 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0005730; C:nucleolus; ISS:UniProtKB.
 GO:0003723; F:RNA binding; ISS:UniProtKB.
 GO:0070037; F:rRNA (pseudouridine) methyltransferase activity; IDA:UniProtKB.
 GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
 GO:0042274; P:ribosomal small subunit biogenesis; ISS:UniProtKB. 

Interpro

 IPR005304; Rbsml_bgen_MeTrfase_EMG1/NEP1. 

Pfam

 PF03587; EMG1 

SMART

  

PROSITE

  

PRINTS