PRMT7

Protein arginine N-methyltransferase 7

720 amino acids

Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA).

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily.

80.504 kDa

MPSCCCLLGLGFPSPPSALRILRRRMASRAFQLRLNPLTGDSEWLVVEEEEEEDHHPTPPPKQLLATTSYLDMLNDSARNRAYRRAIEAAVTDPSSRVLDIGAGTGLLSMMAARALAAVGGETRGGSVSACESYLPMGKLMRRVLRANGMENRVKVFHKRSDELKVGDDLDSPADILVSEILDSELLGEGLIPTLQQAYDMLLAKNPKIVPYRATTYGQLVESTFLWKLHDLHNNEANAADGVWLTPGEMERIVSVKPQQHAMQCDALEDEIRLLSEPFKVFEFDFWKRPDSHREANIKIQTTRDGYVHAIISWWVLQLDSAGSIFYSTAPRWARQSSSEGPQRDMKDWCDHWKQCVWFMQGKGIPATEDQVLSLRARHNQTSISYQLNINDEACDRSSKGDHLTLLPERIALYGDKDWRSALINTIKNALTVKSSPTCVVADDSMFLALLISSMSPTSKVIAMYPGLRDKGAAYLRSVADANNFSIDQIQVIGKRASSITADDLKHKKVNLLVGEPFYLGSEGMLPWQNLRFWSVRTLLDSMLSEDAFIMPCKGILKLCAMSLPDLWRSRSSLKDVEGFDHSVVNETLGACGYLPGDQQGPCLPYYVWQCGYTKKLSKVYSLMDFNFSEPIHSCFGKTKIEFSHDGTCHGFAVWIDWVLDERKSVVLTTGPDNRYWKQGVQLFGKPVEVNPGKSVMHVEASFDPSTGEITFSSSSTTCS

PRMT7

Protein arginine N-methyltransferase 7

720 amino acids

Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA).

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily.

80.601 kDa

MPSCCCLLGLGFPSPPSALRILRRRMASRAFQLRLNPLTGDSEWLVVEEEEEEDHHPTPPPKQLLATTSYLDMLNDSARNRAYRRAIEAAVTDPSSRVLDIGAGTGLLSMMAARALAAVGGETRGGSVSACESYLPMGKLMRRVLRANGMENRVKVFHKRSDELKVRDDLDSPADILVSEILDSELLGEGLIPTLQQAYDMLLAKNPKIVPYRATTYGQLVESTFLWKLHDLHNNEANAADGVWLTPGEMERIVSVKPQQHAMQCDALEDEIRLLSEPFKVFEFDFWKRPDSHREANIKIRTTRDGYVHAIISWWVLQLDSAGSIFYSTAPRWARQSSSEGPQRDMKDWCDHWKQCVWFMQGKGIPATEDQVLSLRARHNQTSISYQLNINDEACDRSSKGDHLTLLPERIALYGDKDWRSALINTIKNALTVKSSPTCVVADDSMFLALLISSMSPTSKVIAMYPGLRDKGAAYLRSVADANNFSIDQIQVIGKRASSITADDLKHKKVNLLVGEPFYLGSEGMLPWQNLRFWSVRTLLDSMLSEDAFIMPCKGILKLCAMSLPDLWRSRSSLKDVEGFDHSVVNETLGACGCLPGDQQGPCLPYYVWQCGYTKKLSKVYSLMDFNFSEPIHSCFGKTKIEFSHDGTCHGFAVWIDWVLDERKSVVLTTGPDNRYWKQGVQLFSKPVEVNPGKSVMHVEASFDPSTGEITFSSSSTTCS

PRMT7

Protein arginine N-methyltransferase 7

695 amino acids

Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily.

78.654 kDa

MKVFCGRANPTTGSVEWLEEDEHYDYHQEIARSSYADMLHDKDRNMKYYQGIRAAVSRVKDRGQKALVLDIGTGTGLLSMMAVTAGADFCYAIEVFKPMADAAVKIVEKNGFSDKIKVINKHSTEVTVGPDGDMPCRANILITELFDTELIGEGALPSYEHAHRHLVQANCEAVPHRATVYAQLVESRRMWSWNKLFPIRVQTSRGERVIIPPLELERCPGAPSVCDIQLNQVSPADFTILSDVLPMFSVDFSKQVSSSAACHSRQFEPLVSGRAQVVLSWWDIEMDPEGKIKCTMAPSWAHSDPEELQWRDHWMQCVYFLPQEEPVVQGLALCLVAYHDDYCVWYSLQKTSPEKNGRVHPVRPVCDCQAHLLWNRPRFGEINDRNRTDQYIQALRTVLKPDSVCLCVSDGSLLSMLAYHLGVEQVFTIENSAVSHRLMKKIFKANHLEDKINIIEKRPELLTPADLEGKKVSLLLGEPFFTTSLLPWHNLYFWYVRTAVDQHLGPGAVVMPQAASLHVVVVEFRDLWRIRSPCGDCEGFDVHIMDDMIKRALDFRESKEAEPHPLWEYPCSSLSEPQQILTFDFRQPVPLQPIHAEGTIELRRCGRSHGAVLWMEYHLTADSTVSTGLLKSAEDEGDCCWNPHCKQAVYFFNTTLDPRAPPGSSQTVTYTVEFHPHTGDITMDFTLSDALDSGC

Prmt7

Protein arginine N-methyltransferase 7

693 amino acids

Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily.

78.346 kDa

MKVFCGRANPTTGSLEWLEEDEHYDYHQEIARSSYADMLHDKDRNIKYYQGIRAAVSRVKDKGQKALVLDIGTGTGLLSMMAVTAGADFCYAVEVFKPMAEAAVKIVEKNGFSDKIKVINKHSTEVTVGPDGDLPCRANILVTELFDTELIGEGALPSYEHAHKHLVQEDCEAVPHRATVYAQLVESKRMWSWNKLFPVRVQTGLGEQLIIPPSELERCPGAPSVYDIQLNQVSPADFTVLSDVLPMFSVDFSKQVSSSAACHSKQFVPLASGQAQVVLSWWDIEMDPEGKIKCTMAPFWAQTDPQELQWRDHWMQCVYFLPQEEPIMQGSPRCLAAHHDDYCVWYSLQRTSPDENNSAYQVRPVCDCQAHLLWNRPRFGEINDQDRTDHYARALRTMLMPGSICLCVSDGSLLSVLAHHLGAEQVFTVESSVASYRLMKRIFKVNHLEDKITVINKRPELLTSADLEGKKVSLLLGEPFFTTSLLPWHNLYFWYVRTSVDQHLAPGAVVMPQAASLHAVIVEFRDLWRIRSPCGDCEGFDVHIMDDMIKHSLDFRESREAEPQPLWEYPCRSLSEPRQILTFDFQQPIPQQPMQSRGVMELRRPGKSHGAVLWMEYQLTPDSTVSTGLMNPAEDKGDCCWNPHCKQAVYFLSATLDPSAPLDGPQSVSYAVEFHPLTGDITMEFRLADDTLN

Prmt7

Protein arginine N-methyltransferase 7

692 amino acids

Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily.

78.298 kDa

MKVFCGRANPTTGSLEWLEEDEHYDYHQEIARSSYADMLHDKDRNIKYYQGIRAAVSRVKDRGQKALVLDIGTGTGLLSMMAVTAGADFCYAIEVFKPMADAAVKIVEKNGFSDKIKVINKHSTEVTVGPDGDLPCRANILVTELFDTELIGEGALPSYEHAHRHLVQENCEAVPHKATVYAQLVESRRMWSWNKLFPVHVQTSLGEQVIVPPSELERCPGAPSVYDIQLNQVPSTDFTALSDVLPMFSVDFSKQVSSSAACHSKQFVPLASGQAQVVLSWWDIEMDPEGKITCTMAPFWAQTNPQELQWRDHWMQCVYFLPQEEPVVQGSPRCLVAHHDDYCVWYSLQRTSADENEEVYQVRPVCDCQAHLLWNRPRFGEINDQDRTDQYAQALRTVLMPGTICLCVSDGSLLSLLAHHLGAEQVFTVESSAASYRLMKRIFKANHLEDKVSIIKKRPELLTSADLEGKKVSLLLGEPFFATSLLPWHNLYFWYARTSVDQHLEPGAVVMPQAASLYAMIVEFRDLWRIRSPCGDCEGFDVHIMDDMIKHSLDFRESREAEPHPLWEYPCRSLSEPQQILTFDFQQPVPQKPVHAEGSMELRRPGKSHGAVLWMEYHLTPDSTVSTGLMNPLEDKGDCCWNPHCKQAVYFLSTTVDPRVPLDGPQSVSYAVEFHPLTGDITMEFRLADTLN

PRMT7

Protein arginine N-methyltransferase 7

692 amino acids

Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily.

78.459 kDa

MKIFCSRANPTTGSVEWLEEDEHYDYHQEIARSSYADMLHDKDRNVKYYQGIRAAVSRVKDRGQKALVLDIGTGTGLLSMMAVTAGADFCYAIEVFKPMADAAVKIVEKNGFSDKIKVINKHSTEVTVGPEGDMPCRANILVTELFDTELIGEGALPSYEHAHRHLVEENCEAVPHRATVYAQLVESGRMWSWNKLFPIHVQTSLGEQVIVPPVDVESCPGAPSVCDIQLNQVSPADFTVLSDVLPMFSIDFSKQVSSSAACHSRRFEPLTSGRAQVVLSWWDIEMDPEGKIKCTMAPFWAHSDPEEMQWRDHWMQCVYFLPQEEPVVQGSALYLVAHHDDYCVWYSLQRTSPEKNERVRQMRPVCDCQAHLLWNRPRFGEINDQDRTDRYVQALRTVLKPDSVCLCVSDGSLLSVLAHHLGVEQVFTVESSAASHKLLRKIFKANHLEDKINIIEKRPELLTNEDLQGRKVSLLLGEPFFTTSLLPWHNLYFWYVRTAVDQHLGPGAMVMPQAASLHAVVVEFRDLWRIRSPCGDCEGFDVHIMDDMIKRALDFRESREAEPHPLWEYPCRSLSEPWQILTFDFQQPVPLQPLCAEGTVELRRPGQSHAAVLWMEYHLTPECTLSTGLLEPADPEGGCCWNPHCKQAVYFFSPAPDPRALLGGPRTVSYAVEFHPDTGDIIMEFRHADTPD

Prmt7

Protein arginine N-methyltransferase 7

692 amino acids

Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo (By similarity).

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily.

78.301 kDa

MKVFCGRANPTTGSLEWLEEDEHYDYHQEIARSSYADMLHDKDRNIKYYQGIRAAVSRVKDRGQKALVLDIGTGTGLLSMMAVTAGADFCYAIEVFKPMAEAAVKIVERNGFSDKIKVINKHSTEVTVGPDGDLPCRANILITELFDTELIGEGALPSYEHAHKHLVQEDCEAVPHRATVYAQLVESRRMWSWNKLFPVRVRTSLGEQVIVPPSELERCPGAPSVCDIQLNQVSPADFTVLSDVLPMFSVDFSKQVSSSAACHSRQFVPLASGQAQVVLSWWDIEMDPEGKIKCTMAPFWAQTDPQELQWRDHWMQCVYFLPQEEPVVQGSPRCLVAHHDDYCVWYSLQRTSPDENDSAYQVRPVCDCQAHLLWNRPRFGEINDQDRTDHYAQALRTVLLPGSVCLCVSDGSLLSMLAHHLGAEQVFTVESSVASYRLMKRIFKVNHLEDKISVINKRPELLTAADLEGKKVSLLLGEPFFTTSLLPWHNLYFWYVRTSVDQHLAPGAVVMPQAASLHAVIVEFRDLWRIRSPCGDCEGFDVHIMDDMIKHSLDFRESREAEPHPLWEYPCRSLSKPQEILTFDFQQPIPQQPMQSKGTMELTRPGKSHGAVLWMEYQLTPDSTISTGLINPAEDKGDCCWNPHCKQAVYFLSTTLDLRVPLNGPRSVSYVVEFHPLTGDITMEFRLADTLS

PRMT7

Protein arginine N-methyltransferase 7

689 amino acids

Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily.

78.071 kDa

MKTFCGRANPTTGSLEWVEEDEDYDYHQEIARSRYADMLHDKDRNMKYYQGIRAAVSRVKGRGEKAIVLDIGTGTGLLSMMAASAGADFCYAVEVFKPMANAAVKIVEKNGFGDKIKVINKHSTEVTVGPDGDMQCRANILVTELFDTELIGEGALPTYEHAHKYLVQEGCEAVPHRATVYVQLVESKRMWSWNKLFPVHVEAEDGEKIIVSPSEMENCPGVPSVCDIQLNQMPSSDFTILSDVVTMFSVDFSKPVRSASTCYRAQLDPVKSGKAQIVLSWWDIDMDPSGTINCTMAPYWVKPMSAFQWRDHWMQCVYFLPKEEQVLQGEKVHLTACRDEYSVWYTLQKAREEDESKADARVESPVCRCQAHLLWNRPRFGELNDQNRTRQYIKSLMSVLRTDSVCLCISDGSLLPVLAHYLGAEQVFTLENSAVSCSVMKKFFKANHLEDKIKIVEARPELLTSSHLEEKKISVLVGEPFFTTSLLPWHNLYFWYARTAVTEHLASDVTVLPQSAALHMMIVEFQDLWRIRSPCGTCEGFDVQTMDDMIKNSLNFRESKEAEPHPLWEYPCKSLSNPQEVLLFDFRKTVPQHCLSTEGSVNLLRKGKSHGAVLWMEYHLTADISVSTGLMQISNEKGNCEWNPHCKQAVYFFSSVIESETLADVPTAVTYAIKFDTKTGEIAMDFKLL

prmt7

Protein arginine N-methyltransferase 7

685 amino acids

Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily.

77.291 kDa

MKVFCGRVNPTTGAMDWVEEDEHYDYHQEIARSSYADMLHDKDRNEKYYQGICAAVRRVKQRGQEAVVLDIGTGTGLLSMMAVTAGADCCYAIEVFKPMSDAAVQIVKANGFSDKIKVINKHSTEVTVGPDGDMKTKANILITELFDTELIGEGALPSYEHAQHNLMQETWEAVPHRATVFAQLVESTRLWSWNKLFPLNLETGDIKPHPELETCPGAPSVCDIQLSQLNPRDFKILSEVLCVFRVDFSCQVSSAPTSHPVHFTSLASGAAQVVLSWWEIDMDPDGSITCTMQPSWMYETQQSVPWRDHWMQCVYFLPKECSVTQGEVCCLTAHQDDYCVWYSLNKSSAENDPVCRERPTCHCGAHITWNRARFGELNDRHRTQQYFEALKKVVTPSSTCLCVSDGSLLPVLAHSLGAKQIYTLESSSIAQHLMKKLFQVNHLGEKIQVLHKSADSLITADFEDRKISTLIGEPFFTTNLLPWHNLYFWYSRTALSTNLAKDCTVLPLSASLHVVAVEFKDLWRIRSPCGMCEGFDVSIMDKMIKNSLNFRESQEAEPHPLWEYPCRALSEPIQVMTFNFTEPVPTEEIRASGSLNLVRSGQCHGAVLWMVYELTKEITVSTGLIGISEEMGECQWYPHRKQGVYFFSSILNPQTIPAQSPSSVSYSVTFIPKEGDIRMCFEPDF

prmt7

Protein arginine N-methyltransferase 7

683 amino acids

Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily.

76.547 kDa

MKTFCGRANPTTGALDWVEESEEYDYHQEIARSCYADMLHDKDRNEKYYEGIRAAVRRVKARGERPVVLDIGTGTGLLSMMAVTAGADFCYAIEVFKPMAQAASCIVERNGFSDKIKIINKHSTEVTVGPDGDMQERANILVTELFDTELIGEGALPSYEHAHMHLVQTGCEAVPHRATIYAQLVESDMLWKWAQMRPIDVDGHRLMPPGAVQECAGAPSVCDIQLSQVPTDAFTAISPVCTMFSVDFSKPVSSAAQSYTVRFKSQTGGRAQVVLSWWDIDMDPEGNIVCTMAPSWSYADPHAYPWRDHWMQSVYFLPAEENVSEGEELMLMVSHDDYSLWYSLTHSEQNDVRVAPFRPCCTCQAHLVWTRPRFGELNDEQRTESYVSALRSILKPDSVCLSVSDGSLLPVFAHLLGSKKVFSLESSGMAKQVIEQVLHTNSLKDGVQLLGIRAEQLSLADLDGNQISVLMGEPYFSTSLLPWHSLFFWYCRTAVAQLLQPDATILPRAATLYAVAVEFQDLWRIRFPCGTCEGFDVSPMDEMIQRSLDFRESWEAEPHPLWEYPCRALTKPCPVMTFDFTQCVPEQPISSDGAVPFTGRGRCHGVALWMEYQLTDDISVSMGLTKAVSQEGACEWNPHRKQGVFFFRSAKETSGDGREDLSYSLTFEPHSGDIKMDFSITES

PRMT7

Protein arginine N-methyltransferase 7

390 amino acids

Arginine methyltransferase that specifically catalyzes the formation of omega-N monomethylarginine (MMA). Has activity toward multiple substrates in vitro. Able to mediate the arginine methylation of histones and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily.

44.026 kDa

MPPKQHRHQKKDKNDNALQNTIGFVPPGATLASVSGYRPPDAFVNRIDRNIPVPARLRHTPVSLIEAVNDFHYAMMNDEERNNFYYEVLKKHVTPETGVLEIGAGSGLLSLMAAKLGAKWVVAVEGSEELAKLARENIRANNMEHQVKVLHMMSTELKSKHLPEPPDVLLSEIFGTMMLGESALDYVVDVRNRLLKPTTKIIPQFGTQYAVPIECDALHRISSVSGWRDLDLKHMMTLQDTVSIVFAKHYGIRMNSVNFRRLSDPIELFRVDFSSSNRNDIPRRKHFDVVAKESGTAHAMLFYWKVTDDEFVMSTDPEDTVNNFPRDMQWGQALQLLDASNGPLPTPVVFTEGKNYNFECNFSGDRVILHMQLCPESGNGEMTECEGKTT