KMT2A
entrez
4297
canonical
uniprot
Q03164
canonical
ensembl
ENSG00000118058
resolver
ensp
ENSP00000374157
resolver
ensp
ENSP00000432391
resolver
ensp
ENSP00000436786
resolver
ensp
ENSP00000518343
resolver
ensp
ENSP00000596449
resolver
enst
ENST00000531904
resolver
enst
ENST00000710560
resolver
genesymbol
KMT2A
resolver
genesymbol_syn
ALL1
resolver
genesymbol_syn
CXXC7
resolver
genesymbol_syn
HRX
resolver
genesymbol_syn
HTRX
resolver
genesymbol_syn
MLL
resolver
genesymbol_syn
MLL1
resolver
genesymbol_syn
TRX1
resolver
hgnc
HGNC:7132
resolver
uniprot
A0AA34QVI8
resolver
uniprot
E9PQG7
resolver
uniprot
E9PR05
resolver
uniprot
Q13743
resolver
uniprot
Q13744
resolver
uniprot
Q14845
resolver
uniprot
Q16364
resolver
uniprot
Q59FF2
resolver
uniprot
Q6UBD1
resolver
uniprot
Q9HBJ3
resolver
uniprot
Q9UD94
resolver
uniprot
Q9UMA3
resolver
uniprot_entry
A0AA34QVI8_HUMAN
resolver
uniprot_entry
E9PR05_HUMAN
resolver
uniprot_entry
KMT2A_HUMAN
resolver
uniprot_sec
E9PQG7
resolver
uniprot_sec
Q13743
resolver
uniprot_sec
Q13744
resolver
uniprot_sec
Q14845
resolver
uniprot_sec
Q16364
resolver
uniprot_sec
Q59FF2
resolver
uniprot_sec
Q6UBD1
resolver
uniprot_sec
Q9HBJ3
resolver
uniprot_sec
Q9UD94
resolver
uniprot_sec
Q9UMA3
resolver
amino_acid_sequence
MAHSCRWRFPARPGTTGGGGGGGRRGLGGAPRQRVPALLLPPGPPVGGGGPGAPPSPPAVAAAAAAAGSSGAGVPGGAAAASAASSSSASSSSSSSSSASSGPALLRVGPGFDAALQVSAAIGTNLRRFRAVFGESGGGGGSGEDEQFLGFGSDEEVRVRSPTRSPSVKTSPRKPRGRPRSGSDRNSAILSDPSVFSPLNKSETKSGDKIKKKDSKSIEKKRGRPPTFPGVKIKITHGKDISELPKGNKEDSLKKIKRTPSATFQQATKIKKLRAGKLSPLKSKFKTGKLQIGRKGVQIVRRRGRPPSTERIKTPSGLLINSELEKPQKVRKDKEGTPPLTKEDKTVVRQSPRRIKPVRIIPSSKRTDATIAKQLLQRAKKGAQKKIEKEAAQLQGRKVKTQVKNIRQFIMPVVSAISSRIIKTPRRFIEDEDYDPPIKIARLESTPNSRFSAPSCGSSEKSSAASQHSSQMSSDSSRSSSPSVDTSTDSQASEEIQVLPEERSDTPEVHPPLPISQSPENESNDRRSRRYSVSERSFGSRTTKKLSTLQSAPQQQTSSSPPPPLLTPPPPLQPASSISDHTPWLMPPTIPLASPFLPASTAPMQGKRKSILREPTFRWTSLKHSRSEPQYFSSAKYAKEGLIRKPIFDNFRPPPLTPEDVGFASGFSASGTAASARLFSPLHSGTRFDMHKRSPLLRAPRFTPSEAHSRIFESVTLPSNRTSAGTSSSGVSNRKRKRKVFSPIRSEPRSPSHSMRTRSGRLSSSELSPLTPPSSVSSSLSISVSPLATSALNPTFTFPSHSLTQSGESAEKNQRPRKQTSAPAEPFSSSSPTPLFPWFTPGSQTERGRNKDKAPEELSKDRDADKSVEKDKSRERDREREKENKRESRKEKRKKGSEIQSSSALYPVGRVSKEKVVGEDVATSSSAKKATGRKKSSSHDSGTDITSVTLGDTTAVKTKILIKKGRGNLEKTNLDLGPTAPSLEKEKTLCLSTPSSSTVKHSTSSIGSMLAQADKLPMTDKRVASLLKKAKAQLCKIEKSKSLKQTDQPKAQGQESDSSETSVRGPRIKHVCRRAAVALGRKRAVFPDDMPTLSALPWEEREKILSSMGNDDKSSIAGSEDAEPLAPPIKPIKPVTRNKAPQEPPVKKGRRSRRCGQCPGCQVPEDCGVCTNCLDKPKFGGRNIKKQCCKMRKCQNLQWMPSKAYLQKQAKAVKKKEKKSKTSEKKDSKESSVVKNVVDSSQKPTPSAREDPAPKKSSSEPPPRKPVEEKSEEGNVSAPGPESKQATTPASRKSSKQVSQPALVIPPQPPTTGPPRKEVPKTTPSEPKKKQPPPPESGPEQSKQKKVAPRPSIPVKQKPKEKEKPPPVNKQENAGTLNILSTLSNGNSSKQKIPADGVHRIRVDFKEDCEAENVWEMGGLGILTSVPITPRVVCFLCASSGHVEFVYCQVCCEPFHKFCLEENERPLEDQLENWCCRRCKFCHVCGRQHQATKQLLECNKCRNSYHPECLGPNYPTKPTKKKKVWICTKCVRCKSCGSTTPGKGWDAQWSHDFSLCHDCAKLFAKGNFCPLCDKCYDDDDYESKMMQCGKCDRWVHSKCENLSDEMYEILSNLPESVAYTCVNCTERHPAEWRLALEKELQISLKQVLTALLNSRTTSHLLRYRQAAKPPDLNPETEESIPSRSSPEGPDPPVLTEVSKQDDQQPLDLEGVKRKMDQGNYTSVLEFSDDIVKIIQAAINSDGGQPEIKKANSMVKSFFIRQMERVFPWFSVKKSRFWEPNKVSSNSGMLPNAVLPPSLDHNYAQWQEREENSHTEQPPLMKKIIPAPKPKGPGEPDSPTPLHPPTPPILSTDRSREDSPELNPPPGIEDNRQCALCLTYGDDSANDAGRLLYIGQNEWTHVNCALWSAEVFEDDDGSLKNVHMAVIRGKQLRCEFCQKPGATVGCCLTSCTSNYHFMCSRAKNCVFLDDKKVYCQRHRDLIKGEVVPENGFEVFRRVFVDFEGISLRRKFLNGLEPENIHMMIGSMTIDCLGILNDLSDCEDKLFPIGYQCSRVYWSTTDARKRCVYTCKIVECRPPVVEPDINSTVEHDENRTIAHSPTSFTESSSKESQNTAEIISPPSPDRPPHSQTSGSCYYHVISKVPRIRTPSYSPTQRSPGCRPLPSAGSPTPTTHEIVTVGDPLLSSGLRSIGSRRHSTSSLSPQRSKLRIMSPMRTGNTYSRNNVSSVSTTGTATDLESSAKVVDHVLGPLNSSTSLGQNTSTSSNLQRTVVTVGNKNSHLDGSSSSEMKQSSASDLVSKSSSLKGEKTKVLSSKSSEGSAHNVAYPGIPKLAPQVHNTTSRELNVSKIGSFAEPSSVSFSSKEALSFPHLHLRGQRNDRDQHTDSTQSANSSPDEDTEVKTLKLSGMSNRSSIINEHMGSSSRDRRQKGKKSCKETFKEKHSSKSFLEPGQVTTGEEGNLKPEFMDEVLTPEYMGQRPCNNVSSDKIGDKGLSMPGVPKAPPMQVEGSAKELQAPRKRTVKVTLTPLKMENESQSKNALKESSPASPLQIESTSPTEPISASENPGDGPVAQPSPNNTSCQDSQSNNYQNLPVQDRNLMLPDGPKPQEDGSFKRRYPRRSARARSNMFFGLTPLYGVRSYGEEDIPFYSSSTGKKRGKRSAEGQVDGADDLSTSDEDDLYYYNFTRTVISSGGEERLASHNLFREEEQCDLPKISQLDGVDDGTESDTSVTATTRKSSQIPKRNGKENGTENLKIDRPEDAGEKEHVTKSSVGHKNEPKMDNCHSVSRVKTQGQDSLEAQLSSLESSRRVHTSTPSDKNLLDTYNTELLKSDSDNNNSDDCGNILPSDIMDFVLKNTPSMQALGESPESSSSELLNLGEGLGLDSNREKDMGLFEVFSQQLPTTEPVDSSVSSSISAEEQFELPLELPSDLSVLTTRSPTVPSQNPSRLAVISDSGEKRVTITEKSVASSESDPALLSPGVDPTPEGHMTPDHFIQGHMDADHISSPPCGSVEQGHGNNQDLTRNSSTPGLQVPVSPTVPIQNQKYVPNSTDSPGPSQISNAAVQTTPPHLKPATEKLIVVNQNMQPLYVLQTLPNGVTQKIQLTSSVSSTPSVMETNTSVLGPMGGGLTLTTGLNPSLPTSQSLFPSASKGLLPMSHHQHLHSFPAATQSSFPPNISNPPSGLLIGVQPPPDPQLLVSESSQRTDLSTTVATPSSGLKKRPISRLQTRKNKKLAPSSTPSNIAPSDVVSNMTLINFTPSQLPNHPSLLDLGSLNTSSHRTVPNIIKRSKSSIMYFEPAPLLPQSVGGTAATAAGTSTISQDTSHLTSGSVSGLASSSSVLNVVSMQTTTTPTSSASVPGHVTLTNPRLLGTPDIGSISNLLIKASQQSLGIQDQPVALPPSSGMFPQLGTSQTPSTAAITAASSICVLPSTQTTGITAASPSGEADEHYQLQHVNQLLASKTGIHSSQRDLDSASGPQVSNFTQTVDAPNSMGLEQNKALSSAVQASPTSPGGSPSSPSSGQRSASPSVPGPTKPKPKTKRFQLPLDKGNGKKHKVSHLRTSSSEAHIPDQETTSLTSGTGTPGAEAEQQDTASVEQSSQKECGQPAGQVAVLPEVQVTQNPANEQESAEPKTVEEEESNFSSPLMLWLQQEQKRKESITEKKPKKGLVFEISSDDGFQICAESIEDAWKSLTDKVQEARSNARLKQLSFAGVNGLRMLGILHDAVVFLIEQLSGAKHCRNYKFRFHKPEEANEPPLNPHGSARAEVHLRKSAFDMFNFLASKHRQPPEYNPNDEEEEEVQLKSARRATSMDLPMPMRFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGNVIRSIQTDKREKYYDSKGIGCYMFRIDDSEVVDATMHGNAARFINHSCEPNCYSRVINIDGQKHIVIFAMRKIYRGEELTYDYKFPIEDASNKLPCNCGAKKCRKFLN
uniprot
proteins
disease_involvement
DISEASE: Wiedemann-Steiner syndrome (WDSTS) [MIM:605130]: A syndrome characterized by hairy elbows (hypertrichosis cubiti), intellectual disability, a distinctive facial appearance, and short stature. Facial characteristics include long eyelashes, thick or arched eyebrows with a lateral flare, and downslanting and vertically narrow palpebral fissures. {ECO:0000269|PubMed:22795537}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=Chromosomal aberrations involving KMT2A are a cause of acute leukemias. Translocation t(1;11)(q21;q23) with MLLT11/AF1Q; translocation t(3;11)(p21;q23) with NCKIPSD/AF3p21; translocation t(3,11)(q25,q23) with GMPS; translocation t(4;11)(q21;q23) with AFF1/MLLT2/AF4; insertion ins(5;11)(q31;q13q23) with AFF4/AF5Q31; translocation t(5;11)(q12;q23) with AF5-alpha/CENPK; translocation t(6;11)(q27;q23) with AFDN; translocation t(9;11)(p22;q23) with MLLT3/AF9; translocation t(10;11)(p11.2;q23) with ABI1; translocation t(10;11)(p12;q23) with MLLT10/AF10; t(11;15)(q23;q14) with KNL1 and ZFYVE19; translocation t(11;17)(q23;q21) with MLLT6/AF17; translocation t(11;19)(q23;p13.3) with ELL; translocation t(11;19)(q23;p13.3) with MLLT1/ENL; translocation t(11;19)(q23;p23) with GAS7; translocation t(X;11)(q13;q23) with FOXO4/AFX1. Translocation t(3;11)(q28;q23) with LPP. Translocation t(10;11)(q22;q23) with TET1. Translocation t(9;11)(q34;q23) with DAB2IP. Translocation t(4;11)(p12;q23) with FRYL. Fusion proteins KMT2A-MLLT1, KMT2A-MLLT3 and KMT2A-ELL interact with PPP1R15A and, on the contrary to unfused KMT2A, inhibit PPP1R15A-induced apoptosis. Fusion protein KMT2A-MLLT3 interacts with MEN1 and PSIP1 (PubMed:22936661, PubMed:25305204). {ECO:0000269|PubMed:10490642, ECO:0000269|PubMed:22936661, ECO:0000269|PubMed:25305204}.; DISEASE: Note=A chromosomal aberration involving KMT2A may be a cause of chronic neutrophilic leukemia. Translocation t(4;11)(q21;q23) with SEPT11. {ECO:0000269|PubMed:10490642}.
uniprot
proteins
ec_number
2.1.1.-
uniprot
proteins
ec_number
2.1.1.364
uniprot
proteins
function
FUNCTION: Histone methyltransferase that plays an essential role in early development and hematopoiesis (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:26886794). Catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac) (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:24235145, PubMed:26886794). Catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism. Part of chromatin remodeling machinery predominantly forms H3K4me1 and H3K4me2 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:25561738, PubMed:26886794). Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity (PubMed:19187761, PubMed:26886794). Has no activity toward histone H3 phosphorylated on 'Thr-3', less activity toward H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher activity toward H3 acetylated on 'Lys-9' (PubMed:19187761). Binds to unmethylated CpG elements in the promoter of target genes and helps maintain them in the nonmethylated state (PubMed:20010842). Required for transcriptional activation of HOXA9 (PubMed:12453419, PubMed:20010842, PubMed:20677832). Promotes PPP1R15A-induced apoptosis (PubMed:10490642). Plays a critical role in the control of circadian gene expression and is essential for the transcriptional activation mediated by the CLOCK-BMAL1 heterodimer (By similarity). Establishes a permissive chromatin state for circadian transcription by mediating a rhythmic methylation of 'Lys-4' of histone H3 (H3K4me) and this histone modification directs the circadian acetylation at H3K9 and H3K14 allowing the recruitment of CLOCK-BMAL1 to chromatin (By similarity). Also has auto-methylation activity on Cys-3882 in absence of histone H3 substrate (PubMed:24235145). {ECO:0000250|UniProtKB:P55200, ECO:0000269|PubMed:10490642, ECO:0000269|PubMed:12453419, ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:19187761, ECO:0000269|PubMed:19556245, ECO:0000269|PubMed:20010842, ECO:0000269|PubMed:21220120, ECO:0000269|PubMed:24235145, ECO:0000269|PubMed:26886794, ECO:0000305|PubMed:20677832}.
uniprot
proteins
mass_dalton
431764
uniprot
proteins
mutagenesis
MUTAGEN 6; /note="R->A: Reduced interaction with MEN1."; /evidence="ECO:0000269|PubMed:22327296"; MUTAGEN 7; /note="W->A: Reduced interaction with MEN1."; /evidence="ECO:0000269|PubMed:22327296"; MUTAGEN 8; /note="R->A: Reduced interaction with MEN1."; /evidence="ECO:0000269|PubMed:22327296"; MUTAGEN 9; /note="F->A: Loss of interaction with MEN1."; /evidence="ECO:0000269|PubMed:22327296"; MUTAGEN 9; /note="F->H,Y: Reduced interaction with MEN1."; /evidence="ECO:0000269|PubMed:22327296"; MUTAGEN 10; /note="P->A: Reduced interaction with MEN1."; /evidence="ECO:0000269|PubMed:22327296"; MUTAGEN 11; /note="A->R: Reduced interaction with MEN1."; /evidence="ECO:0000269|PubMed:22327296"; MUTAGEN 12; /note="R->A: Reduced interaction with MEN1."; /evidence="ECO:0000269|PubMed:22327296"; MUTAGEN 13; /note="P->A: Reduced interaction with MEN1."; /evidence="ECO:0000269|PubMed:22327296"; MUTAGEN 24; /note="R->E: Reduced interaction with MEN1; when associated with E-25."; /evidence="ECO:0000269|PubMed:22327296"; MUTAGEN 25; /note="R->E: Reduced interaction with MEN1; when associated with E-24."; /evidence="ECO:0000269|PubMed:22327296"; MUTAGEN 129; /note="F->A: Weakly affects interaction with PSIP1 whereas significantly decreases interaction of KMT2A-MEN1 complex with PSIP1. Reduced interaction with PSIP1; when associated with A-133."; /evidence="ECO:0000269|PubMed:25082813, ECO:0000269|PubMed:25305204"; MUTAGEN 132; /note="V->A: Reduced interaction with PSIP1; when associated with A-133."; /evidence="ECO:0000269|PubMed:29997176"; MUTAGEN 133; /note="F->A: Reduced interaction with PSIP1; when associated with A-129 or A-132."; /evidence="ECO:0000269|PubMed:25082813, ECO:0000269|PubMed:29997176"; MUTAGEN 136; /note="S->D: Phosphomimetic mutant. Significant increase in interaction with PSIP1; when associated with D-142."; /evidence="ECO:0000269|PubMed:29997176"; MUTAGEN 142; /note="S->D: Phosphomimetic mutant. Significant increase in interaction with PSIP1; when associated with D-136."; /evidence="ECO:0000269|PubMed:29997176"; MUTAGEN 144; /note="E->Q: Loss of interaction with PSIP1; when associated with Q-146 and A-148."; /evidence="ECO:0000269|PubMed:25082813"; MUTAGEN 146; /note="E->Q: Loss of interaction with PSIP1; when associated with Q-144 and A-148."; /evidence="ECO:0000269|PubMed:25082813"; MUTAGEN 148; /note="F->A: Reduced interaction with PSIP1. Loss of interaction with PSIP1; when associated with A-149 or Q-144 and Q-146."; /evidence="ECO:0000269|PubMed:25082813, ECO:0000269|PubMed:25305204"; MUTAGEN 149; /note="L->A: Loss of interaction with PSIP1; when associated with A-148."; /evidence="ECO:0000269|PubMed:25305204"; MUTAGEN 151; /note="F->A: Reduced interaction with PSIP1."; /evidence="ECO:0000269|PubMed:25082813"; MUTAGEN 1150; /note="R->A: Impairs DNA-binding."; /evidence="ECO:0000269|PubMed:20010842"; MUTAGEN 1151; /note="R->A: Impairs DNA-binding."; /evidence="ECO:0000269|PubMed:16990798"; MUTAGEN 1153; /note="R->A: No effect on stability or DNA-binding."; /evidence="ECO:0000269|PubMed:16990798"; MUTAGEN 1154; /note="R->A: Impairs DNA-binding."; /evidence="ECO:0000269|PubMed:16990798, ECO:0000269|PubMed:20010842"; MUTAGEN 1155; /note="C->A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding."; /evidence="ECO:0000269|PubMed:16990798"; MUTAGEN 1158; /note="C->A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding."; /evidence="ECO:0000269|PubMed:16990798"; MUTAGEN 1161; /note="C->A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding."; /evidence="ECO:0000269|PubMed:16990798"; MUTAGEN 1162; /note="Q->A: No effect on stability or DNA-binding."; /evidence="ECO:0000269|PubMed:16990798"; MUTAGEN 1166; /note="D->A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding."; /evidence="ECO:0000269|PubMed:16990798"; MUTAGEN 1167; /note="C->A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding."; /evidence="ECO:0000269|PubMed:16990798"; MUTAGEN 1170; /note="C->A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding."; /evidence="ECO:0000269|PubMed:16990798"; MUTAGEN 1172; /note="N->A: No effect on stability or DNA-binding."; /evidence="ECO:0000269|PubMed:16990798"; MUTAGEN 1173; /note="C->A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding."; /evidence="ECO:0000269|PubMed:16990798"; MUTAGEN 1175; /note="D->A: Impairs DNA-binding."; /evidence="ECO:0000269|PubMed:16990798"; MUTAGEN 1176; /note="K->A: Impairs DNA-binding."; /evidence="ECO:0000269|PubMed:16990798"; MUTAGEN 1178..1181; /note="KFGG->AAAA: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding."; /evidence="ECO:0000269|PubMed:16990798"; MUTAGEN 1178; /note="K->A: Impairs DNA-binding."; /evidence="ECO:0000269|PubMed:16990798"; MUTAGEN 1179; /note="F->A: Impairs DNA-binding."; /evidence="ECO:0000269|PubMed:16990798"; MUTAGEN 1183; /note="N->A: Impairs DNA-binding."; /evidence="ECO:0000269|PubMed:16990798"; MUTAGEN 1185; /note="K->A: Impairs DNA-binding."; /evidence="ECO:0000269|PubMed:16990798, ECO:0000269|PubMed:20010842"; MUTAGEN 1186; /note="K->A: Impairs DNA-binding."; /evidence="ECO:0000269|PubMed:16990798"; MUTAGEN 1187; /note="Q->A: Impairs DNA-binding."; /evidence="ECO:0000269|PubMed:16990798, ECO:0000269|PubMed:20010842"; MUTAGEN 1188; /note="C->A: No effect on stability or DNA-binding."; /evidence="ECO:0000269|PubMed:16990798, ECO:0000269|PubMed:20010842"; MUTAGEN 1188; /note="C->D: Abolishes DNA-binding and increases CpG methylation of the HOXA9 promoter region. Does not lead to the development of leukemia when overexpressed in mice as gene fusion with MLLT3."; /evidence="ECO:0000269|PubMed:20010842"; MUTAGEN 1189; /note="C->A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding."; /evidence="ECO:0000269|PubMed:16990798"; MUTAGEN 1192; /note="R->A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding."; /evidence="ECO:0000269|PubMed:16990798"; MUTAGEN 1193; /note="K->A: Impairs DNA-binding."; /evidence="ECO:0000269|PubMed:16990798, ECO:0000269|PubMed:20010842"; MUTAGEN 1194; /note="C->A: Impairs zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding."; /evidence="ECO:0000269|PubMed:16990798"; MUTAGEN 1195; /note="Q->A: No effect on stability or DNA-binding."; /evidence="ECO:0000269|PubMed:16990798"; MUTAGEN 1196; /note="N->A: No effect on stability or DNA-binding."; /evidence="ECO:0000269|PubMed:16990798"; MUTAGEN 1197; /note="L->A: Mildly decreases DNA-binding."; /evidence="ECO:0000269|PubMed:20010842"; MUTAGEN 1200; /note="M->A: No effect on DNA-binding."; /evidence="ECO:0000269|PubMed:20010842"; MUTAGEN 1581; /note="Y->A: Decreases affinity for histone H3K4me3."; /evidence="ECO:0000269|PubMed:20541251"; MUTAGEN 1587; /note="Q->A: Decreases affinity for histone H3K4me3."; /evidence="ECO:0000269|PubMed:20541251"; MUTAGEN 1594; /note="W->A: Abolishes interaction with histone H3K4me3."; /evidence="ECO:0000269|PubMed:20677832"; MUTAGEN 1594; /note="W->E: Decreases affinity for histone H3K4me3."; /evidence="ECO:0000269|PubMed:20541251"; MUTAGEN 1617; /note="V->A: Decreases binding affinity for PPIE."; /evidence="ECO:0000269|PubMed:20677832"; MUTAGEN 1619; /note="Y->A: May perturb protein folding and thereby decrease binding affinity for PPIE."; /evidence="ECO:0000269|PubMed:20677832"; MUTAGEN 2666..2667; /note="DG->AA: Reduces cleavage without abolishing it. Abolishes cleavage by TASP1; when associated with 2718-A--A-2720."; /evidence="ECO:0000269|PubMed:14636557"; MUTAGEN 2718..2720; /note="DGV->AAA: Abolishes cleavage by TASP1; when associated with 2666-A-A-2667."; /evidence="ECO:0000269|PubMed:12482972, ECO:0000269|PubMed:14636557"; MUTAGEN 3763; /note="S->A: Increased interaction with WDR5."; /evidence="ECO:0000269|PubMed:22665483"; MUTAGEN 3765; /note="R->A: Loss of interaction with the WRAD complex and WDR5."; /evidence="ECO:0000269|PubMed:18840606, ECO:0000269|PubMed:22665483"; MUTAGEN 3769; /note="H->A,F: Slight decrease in interaction with WDR5."; /evidence="ECO:0000269|PubMed:18840606"; MUTAGEN 3769; /note="H->Y: Increased interaction with WDR5."; /evidence="ECO:0000269|PubMed:22665483"; MUTAGEN 3858; /note="Y->A: Impairs methyltransferase activity toward unmodified or monomethylated H3K4me."; /evidence="ECO:0000269|PubMed:19187761"; MUTAGEN 3858; /note="Y->F: Slightly affects methyltransferase activity toward unmodified or monomethylated H3K4me."; /evidence="ECO:0000269|PubMed:19187761"; MUTAGEN 3861; /note="N->I: Leads to stable interaction with ASH2L and RBBP5 in the absence of WDR5; when associated with L-3867."; /evidence="ECO:0000269|PubMed:26886794"; MUTAGEN 3861; /note="N->T: Leads to stable interaction with ASH2L and RBBP5 in the absence of WDR5; when associated with V-3867."; /evidence="ECO:0000269|PubMed:26886794"; MUTAGEN 3864; /note="R->A: Disrupts interaction with ASH2L and RBBP5 and nearly abolishes histone methyltransferase activity."; /evidence="ECO:0000269|PubMed:26886794"; MUTAGEN 3867; /note="Q->A: Slightly affects methyltransferase activity of the enzyme alone, while it impairs methyltransferase activity in complex; when associated with A-3871."; /evidence="ECO:0000269|PubMed:19187761"; MUTAGEN 3867; /note="Q->L: Leads to stable interaction with ASH2L and RBBP5 in the absence of WDR5; when associated with I-3861."; /evidence="ECO:0000269|PubMed:26886794"; MUTAGEN 3867; /note="Q->V: Leads to stable interaction with ASH2L and RBBP5 in the absence of WDR5; when associated with T-3861."; /evidence="ECO:0000269|PubMed:26886794"; MUTAGEN 3869; /note="D->A: Does not affect methyltransferase activity of the enzyme alone or in complex; when associated with A-3872."; /evidence="ECO:0000269|PubMed:19187761"; MUTAGEN 3871; /note="R->A: Slightly affects methyltransferase activity of the enzyme alone, while it impairs methyltransferase activity in complex; when associated with A-3867."; /evidence="ECO:0000269|PubMed:19187761"; MUTAGEN 3872; /note="E->A: Does not affect methyltransferase activity of the enzyme alone or in complex; when associated with A-3869."; /evidence="ECO:0000269|PubMed:19187761"; MUTAGEN 3874; /note="Y->A: Affects methyltransferase activity of the enzyme alone, while it does not affect methyltransferase activity in complex; when associated with A-3878."; /evidence="ECO:0000269|PubMed:19187761"; MUTAGEN 3878; /note="K->A: Affects methyltransferase activity of the enzyme alone, while it does not affect methyltransferase activity in complex; when associated with A-3874."; /evidence="ECO:0000269|PubMed:19187761"; MUTAGEN 3882; /note="C->A,S: Abolished auto-methylation."; /evidence="ECO:0000269|PubMed:24235145"; MUTAGEN 3906; /note="N->A: Loss of the histone H3 methyltransferase activity. Abolishes interaction with S-adenosyl-L-methionine."; /evidence="ECO:0000269|PubMed:19556245, ECO:0000269|PubMed:25561738"; MUTAGEN 3942; /note="Y->A,F: Impairs methyltransferase activity toward unmodified or monomethylated H3K4me."; /evidence="ECO:0000269|PubMed:19187761, ECO:0000269|PubMed:19556245"; MUTAGEN 3942; /note="Y->F: Shifts from a specific monomethyltransferase to a di- and trimethyltransferase activity."; /evidence="ECO:0000269|PubMed:19187761, ECO:0000269|PubMed:19556245
uniprot
proteins
post_translational_modification
PTM: Proteolytic cleavage by TASP1 generates MLL cleavage product N320 and MLL cleavage product C180, which reassemble through a non-covalent association. 2 cleavage sites exist, cleavage site 1 (CS1) and cleavage site 2 (CS2), to generate MLL cleavage products N320 and C180. CS2 is the major site. {ECO:0000269|PubMed:12482972, ECO:0000269|PubMed:14636557}.; PTM: Phosphorylation increases its interaction with PSIP1. {ECO:0000269|PubMed:29997176}.; PTM: Auto-methylated at Cys-3882: auto-methylation is inhibited by the WRAD complex and unmodified histone H3. {ECO:0000269|PubMed:24235145}.
uniprot
proteins
protein_family
Class V-like SAM-binding methyltransferase superfamily
uniprot
proteins
protein_family
Histone-lysine methyltransferase family
uniprot
proteins
protein_family
TRX/MLL subfamily
uniprot
proteins
pubmed
10490642
uniprot
proteins
pubmed
10588740
uniprot
proteins
pubmed
10648423
uniprot
proteins
pubmed
10706619
uniprot
proteins
pubmed
11110714
uniprot
proteins
pubmed
11433529
uniprot
proteins
pubmed
12124344
uniprot
proteins
pubmed
12453419
uniprot
proteins
pubmed
12482972
uniprot
proteins
pubmed
12618766
uniprot
proteins
pubmed
12618768
uniprot
proteins
pubmed
1303259
uniprot
proteins
pubmed
1423624
uniprot
proteins
pubmed
1423625
uniprot
proteins
pubmed
14636557
uniprot
proteins
pubmed
14978793
uniprot
proteins
pubmed
14999297
uniprot
proteins
pubmed
15199122
uniprot
proteins
pubmed
15960975
uniprot
proteins
pubmed
16061630
uniprot
proteins
pubmed
16253272
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
16990798
uniprot
proteins
pubmed
17467953
uniprot
proteins
pubmed
17500065
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18829459
uniprot
proteins
pubmed
18840606
uniprot
proteins
pubmed
19187761
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19556245
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20010842
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20541251
uniprot
proteins
pubmed
20677832
uniprot
proteins
pubmed
21220120
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22327296
uniprot
proteins
pubmed
22665483
uniprot
proteins
pubmed
22795537
uniprot
proteins
pubmed
22936661
uniprot
proteins
pubmed
23178126
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23508102
uniprot
proteins
pubmed
23651431
uniprot
proteins
pubmed
24235145
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25082813
uniprot
proteins
pubmed
25305204
uniprot
proteins
pubmed
25561738
uniprot
proteins
pubmed
25593309
uniprot
proteins
pubmed
26886794
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
29276034
uniprot
proteins
pubmed
29997176
uniprot
proteins
pubmed
34850113
uniprot
proteins
pubmed
7598802
uniprot
proteins
pubmed
7794749
uniprot
proteins
pubmed
8162575
uniprot
proteins
pubmed
8378076
uniprot
proteins
pubmed
8401594
uniprot
proteins
pubmed
8414518
uniprot
proteins
pubmed
8703835
uniprot
proteins
pubmed
8950979
uniprot
proteins
pubmed
9537414
uniprot
proteins
pubmed
9694699
uniprot
proteins
sequence_length
3969
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12482972, ECO:0000269|PubMed:25593309, ECO:0000269|PubMed:34850113}.; SUBCELLULAR LOCATION: [MLL cleavage product N320]: Nucleus.; SUBCELLULAR LOCATION: [MLL cleavage product C180]: Nucleus. Note=Localizes to a diffuse nuclear pattern when not associated with MLL cleavage product N320.
uniprot
proteins