CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021634
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 RNA methyltransferase-like protein 1 
Protein Synonyms/Alias
  
Gene Name
 RNMTL1 
Gene Synonyms/Alias
 HC90 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
237AAGAGCSKVLLTKGCubiquitination[1]
242CSKVLLTKGCVDAWEubiquitination[1]
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
Functional Description
 Probable RNA methyltransferase (By similarity). 
Sequence Annotation
 BINDING 356 356 S-adenosyl-L-methionine; via carbonyl
 BINDING 380 380 S-adenosyl-L-methionine; via amide
 BINDING 389 389 S-adenosyl-L-methionine; via amide  
Keyword
 Complete proteome; Methyltransferase; Polymorphism; Reference proteome; S-adenosyl-L-methionine; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 420 AA 
Protein Sequence
MAALVRPARF VVRPLLQVVQ AWDLDARRWV RALRRSPVKV VFPSGEVVEQ KRAPGKQPRK 60
APSEASAQEQ REKQPLEESA SRAPSTWEES GLRYDKAYPG DRRLSSVMTI VKSRPFREKQ 120
GKILLEGRRL ISDALKAGAV PKMFFFSRLE YLKELPVDKL KGVSLIKVKF EDIKDWSDLV 180
TPQGIMGIFA KPDHVKMTYP KTQLQHSLPL LLICDNLRDP GNLGTILRSA AGAGCSKVLL 240
TKGCVDAWEP KVLRAGMGAH FRMPIINNLE WETVPNYLPP DTRVYVADNC GLYAQAEMSN 300
KASDHGWVCD QRVMKFHKYE EEEDVETGAS QDWLPHVEVQ SYDSDWTEAP AAVVIGGETY 360
GVSLESLQLA ESTGGKRLLI PVVPGVDSLN SAMAASILLF EGKRQLRGRA EDLSRDRSYH 420 
Gene Ontology
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0003723; F:RNA binding; IEA:InterPro.
 GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
 GO:0001510; P:RNA methylation; IEA:GOC.
 GO:0006396; P:RNA processing; IEA:InterPro. 
Interpro
 IPR001537; SpoU_MeTrfase.
 IPR013123; SpoU_subst-bd. 
Pfam
 PF00588; SpoU_methylase
 PF08032; SpoU_sub_bind 
SMART
 SM00967; SpoU_sub_bind 
PROSITE
  
PRINTS