CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000979
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein arginine N-methyltransferase 3 
Protein Synonyms/Alias
 Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3 
Gene Name
 PRMT3 
Gene Synonyms/Alias
 HRMT1L3 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
81NIDSMVHKHGLEFYGmethylation[1]
187REDLQKMKQFAQDFVubiquitination[2]
Reference
 [1] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510]
 [2] 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] 
Functional Description
 Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins. 
Sequence Annotation
 ZN_FING 48 71 C2H2-type.
 ACT_SITE 329 329 By similarity.
 ACT_SITE 338 338 By similarity.
 BINDING 230 230 S-adenosyl-L-methionine (By similarity).
 BINDING 239 239 S-adenosyl-L-methionine.
 BINDING 263 263 S-adenosyl-L-methionine; via carbonyl
 BINDING 285 285 S-adenosyl-L-methionine.
 BINDING 314 314 S-adenosyl-L-methionine.
 MOD_RES 2 2 N-acetylcysteine.
 MOD_RES 25 25 Phosphoserine.
 MOD_RES 27 27 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Metal-binding; Methyltransferase; Phosphoprotein; Polymorphism; Reference proteome; S-adenosyl-L-methionine; Transferase; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 531 AA 
Protein Sequence
MCSLASGATG GRGAVENEED LPELSDSGDE AAWEDEDDAD LPHGKQQTPC LFCNRLFTSA 60
EETFSHCKSE HQFNIDSMVH KHGLEFYGYI KLINFIRLKN PTVEYMNSIY NPVPWEKEEY 120
LKPVLEDDLL LQFDVEDLYE PVSVPFSYPN GLSENTSVVE KLKHMEARAL SAEAALARAR 180
EDLQKMKQFA QDFVMHTDVR TCSSSTSVIA DLQEDEDGVY FSSYGHYGIH EEMLKDKIRT 240
ESYRDFIYQN PHIFKDKVVL DVGCGTGILS MFAAKAGAKK VLGVDQSEIL YQAMDIIRLN 300
KLEDTITLIK GKIEEVHLPV EKVDVIISEW MGYFLLFESM LDSVLYAKNK YLAKGGSVYP 360
DICTISLVAV SDVNKHADRI AFWDDVYGFK MSCMKKAVIP EAVVEVLDPK TLISEPCGIK 420
HIDCHTTSIS DLEFSSDFTL KITRTSMCTA IAGYFDIYFE KNCHNRVVFS TGPQSTKTHW 480
KQTVFLLEKP FSVKAGEALK GKVTVHKSKK DPRSLTVTLT LNNSTQTYGL Q 531 
Gene Ontology
 GO:0005737; C:cytoplasm; NAS:UniProtKB.
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005840; C:ribosome; IEA:Compara.
 GO:0016274; F:protein-arginine N-methyltransferase activity; NAS:UniProtKB.
 GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IEA:Compara.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR025799; Arg_MeTrfase.
 IPR010456; Ribosomal-L11_MeTrfase_PrmA.
 IPR007087; Znf_C2H2.
 IPR015880; Znf_C2H2-like. 
Pfam
 PF06325; PrmA 
SMART
 SM00355; ZnF_C2H2 
PROSITE
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS