CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008961
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone-lysine N-methyltransferase 2A 
Protein Synonyms/Alias
 Lysine N-methyltransferase 2A; ALL-1; Myeloid/lymphoid or mixed-lineage leukemia; Myeloid/lymphoid or mixed-lineage leukemia protein 1; Zinc finger protein HRX; MLL cleavage product N320; N-terminal cleavage product of 320 kDa; p320; MLL cleavage product C180; C-terminal cleavage product of 180 kDa; p180 
Gene Name
 Kmt2a 
Gene Synonyms/Alias
 All1; Hrx; Mll; Mll1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
2771IKSAVGHKNEPKLDNacetylation[1]
2814HTSTPSDKNLLDTYNacetylation[1]
2954VISDSGEKRVTITEKacetylation[1]
3459GNQLLAGKTGTLTSQacetylation[1]
3693AWKSLTDKVQEARSNubiquitination[2]
3781MFNFLASKHRQPPEYacetylation[3]
Reference
 [1] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [2] 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]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441] 
Functional Description
 Histone methyltransferase that plays an essential role in early development and hematopoiesis. 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). In the MLL1/MLL complex, it specifically mediates H3K4me, a specific tag for epigenetic transcriptional activation. Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity. 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'. Required for transcriptional activation of HOXA9. Promotes PPP1R15A-induced apoptosis (By similarity). 
Sequence Annotation
 DOMAIN 1705 1750 Bromo; divergent.
 DOMAIN 2020 2076 FYR N-terminal.
 DOMAIN 3663 3744 FYR C-terminal.
 DOMAIN 3826 3942 SET.
 DOMAIN 3950 3966 Post-SET.
 DNA_BIND 167 178 A.T hook 1.
 DNA_BIND 215 225 A.T hook 2.
 DNA_BIND 299 307 A.T hook 3.
 ZN_FING 1144 1192 CXXC-type.
 ZN_FING 1430 1481 PHD-type 1.
 ZN_FING 1478 1532 PHD-type 2.
 ZN_FING 1565 1629 PHD-type 3.
 REGION 3903 3904 S-adenosyl-L-methionine binding (By
 METAL 3906 3906 Zinc (By similarity).
 METAL 3954 3954 Zinc (By similarity).
 METAL 3956 3956 Zinc (By similarity).
 METAL 3961 3961 Zinc (By similarity).
 BINDING 3836 3836 S-adenosyl-L-methionine (By similarity).
 BINDING 3838 3838 S-adenosyl-L-methionine (By similarity).
 BINDING 3880 3880 S-adenosyl-L-methionine (By similarity).
 BINDING 3955 3955 S-adenosyl-L-methionine (By similarity).
 MOD_RES 151 151 Phosphoserine (By similarity).
 MOD_RES 195 195 Phosphoserine (By similarity).
 MOD_RES 516 516 Phosphoserine (By similarity).
 MOD_RES 634 634 N6-acetyllysine (By similarity).
 MOD_RES 678 678 Phosphoserine (By similarity).
 MOD_RES 837 837 Phosphothreonine (By similarity).
 MOD_RES 923 923 Phosphoserine (By similarity).
 MOD_RES 1053 1053 Phosphoserine (By similarity).
 MOD_RES 1127 1127 N6-acetyllysine (By similarity).
 MOD_RES 1232 1232 N6-acetyllysine (By similarity).
 MOD_RES 1847 1847 Phosphothreonine (By similarity).
 MOD_RES 1860 1860 Phosphoserine (By similarity).
 MOD_RES 2100 2100 Phosphoserine (By similarity).
 MOD_RES 2148 2148 Phosphothreonine (By similarity).
 MOD_RES 2152 2152 Phosphoserine (By similarity).
 MOD_RES 2202 2202 Phosphoserine (By similarity).
 MOD_RES 2951 2951 Phosphoserine (By similarity).
 MOD_RES 3032 3032 Phosphoserine (By similarity).
 MOD_RES 3369 3369 Phosphothreonine (By similarity).
 MOD_RES 3510 3510 Phosphoserine (By similarity).
 CROSSLNK 214 214 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 218 218 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 219 219 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Acetylation; Alternative splicing; Bromodomain; Chromatin regulator; Complete proteome; DNA-binding; Isopeptide bond; Metal-binding; Methyltransferase; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; S-adenosyl-L-methionine; Transcription; Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3966 AA 
Protein Sequence
MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRVPALLL PPGPQAGGGG PGAPPSPPAV 60
AAAAAGSSGA GVPGGAAAAS AASSSSASSS SSSSSSASSG PALLRVGPGF DAALQVSAAI 120
GTNLRRFRAV FGESGGGGGS GEDEQFLGFG SDEEVRVRSP TRSPSVKASP RKPRGRPRSG 180
SDRNPAILSD PSVFSPLNKS ETKSADKIKK KDSKSIEKKR GRPPTFPGVK IKITHGKDIA 240
ELTQGSKEDS LKKVKRTPSA MFQQATKIKK LRAGKLSPLK SKFKTGKLQI GRKGVQIVRR 300
RGRPPSTERI KTPSGLLINS ELEKPQKVRK DKEGTPPLTK EDKTVVRQSP RRIKPVRIIP 360
SCKRTDATIA KQLLQRAKKG AQKKIEKEAA QLQGRKVKTQ VKNIRQFIMP VVSAISSRII 420
KTPRRFIEDE DYDPPMKIAR LESTPNSRFS ATSCGSSEKS SAASQHSSQM SSDSSRSSSP 480
SIDTTSDSQA SEEIQALPEE RSNTPEVHTP LPISQSPENE SNDRRSRRYS MSERSFGSRA 540
TKKLPTLQSA PQQQTSSSPP PPLLTPPPPL QPASGISDHT PWLMPPTIPL ASPFLPASAA 600
PMQGKRKSIL REPTFRWTSL KHSRSEPQYF SSAKYAKEGL IRKPIFDNFR PPPLTPEDVG 660
FASGFSASGT AASARLFSPL HSGTRFDIHK RSPILRAPRF TPSEAHSRIF ESVTLPSNRT 720
SSGASSSGVS NRKRKRKVFS PIRSEPRSPS HSMRTRSGRL STSELSPLTP PSSVSSSLSI 780
PVSPLAASAL NPTFTFPSHS LTQSGESTEK NQRARKQTSA LAEPFSSNSP ALFPWFTPGS 840
QTEKGRKKDT APEELSKDRD ADKSVEKDKS RERDREREKE NKRESRKEKR KKGSDIQSSS 900
ALYPVGRVSK EKVAGEDVGT SSSAKKATGR KKSSSLDSGA DVAPVTLGDT TAVKAKILIK 960
KGRGNLEKNN LDLGPAAPSL EKERTPCLSA PSSSTVKHST SSIGSMLAQA DKLPMTDKRV 1020
ASLLKKAKAQ LCKIEKSKSL KQTDQPKAQG QESDSSETSV RGPRIKHVCR RAAVALGRKR 1080
AVFPDDMPTL SALPWEEREK ILSSMGNDDK SSVAGSEDAE PLAPPIKPIK PVTRNKAPQE 1140
PPVKKGRRSR RCGQCPGCQV PEDCGICTNC LDKPKFGGRN IKKQCCKMRK CQNLQWMPSK 1200
ASLQKQTKAV KKKEKKSKTT EKKESKESTA VKSPLEPAQK AAPPPREEPA PKKSSSEPPP 1260
RKPVEEKSEE GGAPAPAPAP EPKQVSAPAS RKSSKQVSQP AAVVPPQPPS TAPQKKEAPK 1320
AVPSEPKKKQ PPPPEPGPEQ SKQKKVAPRP SIPVKQKPKD KEKPPPVSKQ ENAGTLNILN 1380
PLSNGISSKQ KIPADGVHRI RVDFKEDCEA ENVWEMGGLG ILTSVPITPR VVCFLCASSG 1440
HVEFVYCQVC CEPFHKFCLE ENERPLEDQL ENWCCRRCKF CHVCGRQHQA TKQLLECNKC 1500
RNSYHPECLG PNYPTKPTKK KKVWICTKCV RCKSCGSTTP GKGWDAQWSH DFSLCHDCAK 1560
LFAKGNFCPL CDKCYDDDDY ESKMMQCGKC DRWVHSKCES LSGTEDEMYE ILSNLPESVA 1620
YTCVNCTERH PAEWRLALEK ELQASLKQVL TALLNSRTTS HLLRYRQAAK PPDLNPETEE 1680
SIPSRSSPEG PDPPVLTEVS KQDEQQPLDL EGVKKRMDQG SYVSVLEFSD DIVKIIQAAI 1740
NSDGGQPEIK KANSMVKSFF IRQMERVFPW FSVKKSRFWE PNKVSNNSGM LPNAVLPPSL 1800
DHNYAQWQER EESSHTEQPP LMKKIIPAPK PKGPGEPDSP TPLHPPTPPI LSTDRSREDS 1860
PELNPPPGID DNRQCALCLM YGDDSANDAG RLLYIGQNEW THVNCALWSA EVFEDDDGSL 1920
KNVHMAVIRG KQLRCEFCQK PGATVGCCLT SCTSNYHFMC SRAKNCVFLD DKKVYCQRHR 1980
DLIKGEVVPE NGFEVFRRVF VDFEGISLRR KFLNGLEPEN IHMMIGSMTI DCLGILNDLS 2040
DCEDKLFPIG YQCSRVYWST TDARKRCVYT CKIMECRPPV VEPDINSTVE HDDNRTIAHS 2100
PSSFIDASCK DSQSTAAILS PPSPDRPHSQ TSGSCYYHVI SKVPRIRTPS YSPTQRSPGC 2160
RPLPSAGSPT PTTHEIVTVG DPLLSSGLRS IGSRRHSTSS LSPLRSKLRI MSPVRTGSAY 2220
SRSSVSSVPS LGTATDPEAS AKASDRGGLL SSSANLGHSA PPSSSSQRTV GGSKTSHLDG 2280
SSPSEVKRCS ASDLVPKGSL VKGEKNRTSS SKSTDGSAHS TAYPGIPKLT PQVHNATPGE 2340
LNISKIGSFA EPSTVPFSSK DTVSYPQLHL RGQRSDRDQH MDPSQSVKPS PNEDGEIKTL 2400
KLPGMGHRPS ILHEHIGSSS RDRRQKGKKS SKETCKEKHS SKSYLEPGQV TTGEEGNLKP 2460
EFADEVLTPG FLGQRPCNNV SSEKIGDKVL PLSGVPKGQS TQVEGSSKEL QAPRKCSVKV 2520
TPLKMEGENQ SKNTQKESGP GSPAHIESVC PAEPVSASRS PGAGPGVQPS PNNTLSQDPQ 2580
SNNYQNLPEQ DRNLMIPDGP KPQEDGSFKR RYPRRSARAR SNMFFGLTPL YGVRSYGEED 2640
IPFYSNSTGK KRGKRSAEGQ VDGADDLSTS DEDDLYYYNF TRTVISSGGE ERLASHNLFR 2700
EEEQCDLPKI SQLDGVDDGT ESDTSVTATS RKSSQIPKRN GKENGTENLK IDRPEDAGEK 2760
EHVIKSAVGH KNEPKLDNCH SVSRVKAQGQ DSLEAQLSSL ESSRRVHTST PSDKNLLDTY 2820
NAELLKSDSD NNNSDDCGNI LPSDIMDFVL KNTPSMQALG ESPESSSSEL LTLGEGLGLD 2880
SNREKDIGLF EVFSQQLPAT EPVDSSVSSS ISAEEQFELP LELPSDLSVL TTRSPTVPSQ 2940
NPSRLAVISD SGEKRVTITE KSVASSEGDP ALLSPGVDPA PEGHMTPDHF IQGHMDADHI 3000
SSPPCGSVEQ GHGNSQDLTR NSGTPGLQVP VSPTVPVQNQ KYVPSSTDSP GPSQISNAAV 3060
QTTPPHLKPA TEKLIVVNQN MQPLYVLQTL PNGVTQKIQL TSPVSSTPSV METNTSVLGP 3120
MGSGLTLTTG LNPSLPPSPS LFPPASKGLL SVPHHQHLHS FPAAAQSSFP PNISSPPSGL 3180
LIGVQPPPDP QLLGSEANQR TDLTTTVATP SSGLKKRPIS RLHTRKNKKL APSSAPSNIA 3240
PSDVVSNMTL INFTPSQLSN HPSLLDLGSL NPSSHRTVPN IIKRSKSGIM YFEQAPLLPP 3300
QSVGGTAATA AGSSTISQDT SHLTSGPVSA LASGSSVLNV VSMQTTAAPT SSTSVPGHVT 3360
LANQRLLGTP DIGSISHLLI KASHQSLGIQ DQPVALPPSS GMFPQLGTSQ TPSAAAMTAA 3420
SSICVLPSSQ TAGMTAASPP GEAEEHYKLQ RGNQLLAGKT GTLTSQRDRD PDSAPGTQPS 3480
NFTQTAEAPN GVRLEQNKTL PSAKPASSAS PGSSPSSGQQ SGSSSVPGPT KPKPKAKRIQ 3540
LPLDKGSGKK HKVSHLRTSS EAHIPHRDTD PAPQPSVTRT PRANREQQDA AGVEQPSQKE 3600
CGQPAGPVAA LPEVQATQNP ANEQENAEPK AMEEEESGFS SPLMLWLQQE QKRKESITER 3660
KPKKGLVFEI SSDDGFQICA ESIEDAWKSL TDKVQEARSN ARLKQLSFAG VNGLRMLGIL 3720
HDAVVFLIEQ LAGAKHCRNY KFRFHKPEEA NEPPLNPHGS ARAEVHLRQS AFDMFNFLAS 3780
KHRQPPEYNP NDEEEEEVQL KSARRATSMD LPMPMRFRHL KKTSKEAVGV YRSPIHGRGL 3840
FCKRNIDAGE MVIEYAGNVI RSIQTDKREK YYDSKGIGCY MFRIDDSEVV DATMHGNAAR 3900
FINHSCEPNC YSRVINIDGQ KHIVIFAMRK IYRGEELTYD YKFPIEDASN KLPCNCGAKK 3960
CRKFLN 3966 
Gene Ontology
 GO:0071339; C:MLL1 complex; ISS:UniProtKB.
 GO:0003682; F:chromatin binding; IDA:MGI.
 GO:0070577; F:histone acetyl-lysine binding; ISS:UniProtKB.
 GO:0042800; F:histone methyltransferase activity (H3-K4 specific); ISS:UniProtKB.
 GO:0045322; F:unmethylated CpG binding; ISS:UniProtKB.
 GO:0008270; F:zinc ion binding; ISS:UniProtKB.
 GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
 GO:0006306; P:DNA methylation; IMP:MGI.
 GO:0035162; P:embryonic hemopoiesis; IMP:MGI.
 GO:0043984; P:histone H4-K16 acetylation; ISS:UniProtKB.
 GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
 GO:0051569; P:regulation of histone H3-K4 methylation; IMP:MGI.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR017956; AT_hook_DNA-bd_motif.
 IPR001487; Bromodomain.
 IPR003889; FYrich_C.
 IPR003888; FYrich_N.
 IPR016569; MeTrfase_trithorax.
 IPR003616; Post-SET_dom.
 IPR001214; SET_dom.
 IPR002857; Znf_CXXC.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF05965; FYRC
 PF05964; FYRN
 PF00628; PHD
 PF00856; SET
 PF02008; zf-CXXC 
SMART
 SM00384; AT_hook
 SM00297; BROMO
 SM00542; FYRC
 SM00541; FYRN
 SM00249; PHD
 SM00508; PostSET
 SM00317; SET 
PROSITE
 PS00633; BROMODOMAIN_1
 PS50014; BROMODOMAIN_2
 PS51543; FYRC
 PS51542; FYRN
 PS50868; POST_SET
 PS50280; SET
 PS51058; ZF_CXXC
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS