Table 1.
Primary substrates, functions and disease relevance of PRMTs.
| PRMT | Substrate | Function | Disease relevance |
|---|---|---|---|
| PRMT1 | H4R3[188] hnRNP A1[189], BTG1[190], TIS2[190], IFNα/β[191], ILF3[192], SPT5[193], SAF-A[194], p53[195], MRE11[34], FMRP[196], Sam68[33], SLM[33], ERα[197], RUNX1[198], TAF15[199], BCR[200], CF Im59 and Im68[201], Ash2L[202], nuclear poly(A)-binding protein (PABP1)[203] | Transcriptional coactivator[134], signal transduction[197, 204], RNA splicing[205] and DNA repair[34] | Overexpressed or aberrant in breast, prostate, lung, colon, bladder cancer and leukemia.[2] Overexpressed or aberrant in pulmonary diseases: pulmonary fibrosis, pulmonary hypertension, chronic obstructive pulmonary disease (COPD) and asthma. [40, 47, 206] Play regulatory roles in cardiovascular disease[119, 207], diabetes[120, 121] and renal disease[44, 45, 122, 131]. |
| PRMT2 | H3R8[208] ERα[209], Glutathione transferase[210] | Transcriptional coactivator and androgen/estrogen receptor coactivator[211] | Overexpressed or aberrant in breast cancer [212, 213]. Overexpressed in pulmonary inflammation [206, 214]. |
| PRMT3 | FMRP[196], rpS2[128], PABP1[203] | Ribosomal homeostasis[129] | Enhanced activity in breast tumors [2]. Overexpressed in coronary heart disease [130] and chronic kidney disease [215]. |
| CARM1 | H3R2, H3R17, H3R26[216] PABP1[14]; SAP49 (CBP)/p300[217]; FMRP[196]; Sox9[218]; CA150, SmB, U1C and SF3b4[15] | Transcriptional coactivator[134], RNA splicing[219], cell proliferation[135], cell differentiation[136] | Overexpressed in breast, prostate and colorectal cancer [2]. Regulate human t-cell lymphotropic virus type 1 (HTLV1) [38]. |
| PRMT5 | H2AR3, H3R8, H4R3[138]; H3R2[220]; MBP (Myelin basic protein) [221]; LSm4, Sm D1 and Sm D3[31]; EBNA-2[222]; SPT5[193]; EBNA-1[223]; p53[200]; CBP-1[224]; CF Im68[201]; Ash2L[202]; PDCD4[225]; HoxA[41]; NFkB[226] | Transcriptional repressor[138], RNA splicing[139], signal transduction[140] and piRNA pathway[141] | Overexpression/increased activity in gastric, colorectal, lung cancer, lymphoma, and leukaemia [2]; mis-localized in prostate cancer cells [142]. Play regulatory roles in renal and cardiovascular disease [143], Huntington’s disease [144], Alzheimer’s disease [145] |
| PRMT6 | H2AR29[227], H3R2[148] PRMT6[228, 229]; HIV Tat[230]; HMGA1a[231], DNA polymerase β[149], PABP1[203] | Transcriptional repressor[150, 151] and activator[152] | Overexpressed in bladder and lung cancer [2] Suppress HIV-1 activity [39] Overexpressed or aberrant in pulmonary fibrosis, COPD and asthma [47] |
| PRMT7 | H4R3 and H2AR3[232], H3R2[220], Fibrillarin [233] | DNA damage[232], embryonic stem cell pluripotency[234], male germline gene imprinting[235, 236] | Involved in breast cancer metastasis [237] |
| PRMT8 | H2A, H4[238] MBP, PRMT8[238] EWS (Ewing sarcoma)[239] | Brain specific functions[240] | Somatic mutations were found in ovarian, skin and large intestine cancer [2] |
| PRMT9 | SAP145 (SF3B2)[9] | RNA splicing[5] | lymphoma, melanoma, testicular, and pancreatic cancers [241] |