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P55200

- KMT2A_MOUSE

UniProt

P55200 - KMT2A_MOUSE

Protein

Histone-lysine N-methyltransferase 2A

Gene

Kmt2a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

    S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei2662 – 26632Cleavage; by TASP1, site 1By similarity
    Sitei2714 – 27152Cleavage; by TASP1, site 2By similarity
    Sitei3762 – 37621Important for WDR5-recognition and bindingBy similarity
    Binding sitei3836 – 38361S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei3838 – 38381S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei3880 – 38801S-adenosyl-L-methioninePROSITE-ProRule annotation
    Metal bindingi3906 – 39061ZincBy similarity
    Metal bindingi3954 – 39541ZincBy similarity
    Binding sitei3955 – 39551S-adenosyl-L-methioninePROSITE-ProRule annotation
    Metal bindingi3956 – 39561ZincBy similarity
    Metal bindingi3961 – 39611ZincBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi167 – 17812A.T hook 1Add
    BLAST
    DNA bindingi215 – 22511A.T hook 2Add
    BLAST
    DNA bindingi299 – 3079A.T hook 3
    Zinc fingeri1144 – 119249CXXC-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1430 – 148152PHD-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1478 – 153255PHD-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1565 – 162965PHD-type 3PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: MGI
    2. histone methyltransferase activity (H3-K4 specific) Source: UniProtKB
    3. lysine-acetylated histone binding Source: UniProtKB
    4. protein binding Source: MGI
    5. transcription regulatory region DNA binding Source: Ensembl
    6. unmethylated CpG binding Source: UniProtKB
    7. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. anterior/posterior pattern specification Source: MGI
    2. DNA methylation Source: MGI
    3. embryonic hemopoiesis Source: MGI
    4. histone H3-K4 methylation Source: UniProtKB
    5. histone H3-K4 trimethylation Source: Ensembl
    6. histone H4-K16 acetylation Source: UniProtKB
    7. negative regulation of cell proliferation Source: MGI
    8. positive regulation of cellular response to drug Source: Ensembl
    9. positive regulation of transcription, DNA-templated Source: UniProtKB
    10. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    11. positive regulation of transporter activity Source: Ensembl
    12. protein complex assembly Source: Ensembl
    13. regulation of histone H3-K4 methylation Source: MGI
    14. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Methyltransferase, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, S-adenosyl-L-methionine, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone-lysine N-methyltransferase 2A (EC:2.1.1.43)
    Short name:
    Lysine N-methyltransferase 2A
    Alternative name(s):
    ALL-1
    Myeloid/lymphoid or mixed-lineage leukemia
    Myeloid/lymphoid or mixed-lineage leukemia protein 1
    Zinc finger protein HRX
    Cleaved into the following 2 chains:
    Alternative name(s):
    N-terminal cleavage product of 320 kDa
    Short name:
    p320
    Alternative name(s):
    C-terminal cleavage product of 180 kDa
    Short name:
    p180
    Gene namesi
    Name:Kmt2a
    Synonyms:All1, Hrx, Mll, Mll1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:96995. Kmt2a.

    Subcellular locationi

    Nucleus By similarity
    Chain MLL cleavage product C180 : Nucleus By similarity
    Note: Localizes to a diffuse nuclear pattern when not associated with MLL cleavage product N320.

    GO - Cellular componenti

    1. histone methyltransferase complex Source: UniProtKB
    2. MLL1 complex Source: UniProtKB
    3. nucleus Source: MGI

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 39663966Histone-lysine N-methyltransferase 2APRO_0000124877Add
    BLAST
    Chaini1 – 27142714MLL cleavage product N320By similarityPRO_0000390951Add
    BLAST
    Chaini2715 – 39661252MLL cleavage product C180By similarityPRO_0000390952Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei151 – 1511PhosphoserineBy similarity
    Modified residuei195 – 1951PhosphoserineBy similarity
    Cross-linki214 – 214Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki218 – 218Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki219 – 219Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei237 – 2371N6-acetyllysine1 Publication
    Modified residuei371 – 3711N6-acetyllysine1 Publication
    Modified residuei516 – 5161PhosphoserineBy similarity
    Modified residuei634 – 6341N6-acetyllysineBy similarity
    Modified residuei678 – 6781PhosphoserineBy similarity
    Modified residuei837 – 8371PhosphothreonineBy similarity
    Modified residuei923 – 9231PhosphoserineBy similarity
    Modified residuei1053 – 10531PhosphoserineBy similarity
    Modified residuei1127 – 11271N6-acetyllysineBy similarity
    Modified residuei1232 – 12321N6-acetyllysineBy similarity
    Modified residuei1847 – 18471PhosphothreonineBy similarity
    Modified residuei1860 – 18601PhosphoserineBy similarity
    Modified residuei2100 – 21001PhosphoserineBy similarity
    Modified residuei2148 – 21481PhosphothreonineBy similarity
    Modified residuei2152 – 21521PhosphoserineBy similarity
    Modified residuei2202 – 22021PhosphoserineBy similarity
    Modified residuei2951 – 29511PhosphoserineBy similarity
    Modified residuei2954 – 29541N6-acetyllysine1 Publication
    Modified residuei3032 – 30321PhosphoserineBy similarity
    Modified residuei3369 – 33691PhosphothreonineBy similarity
    Modified residuei3459 – 34591N6-acetyllysine1 Publication
    Modified residuei3510 – 35101PhosphoserineBy similarity

    Post-translational modificationi

    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 By similarity.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP55200.
    PRIDEiP55200.

    PTM databases

    PhosphoSiteiP55200.

    Expressioni

    Gene expression databases

    ArrayExpressiP55200.
    BgeeiP55200.
    CleanExiMM_MLL1.
    GenevestigatoriP55200.

    Interactioni

    Subunit structurei

    MLL cleavage product N320 heterodimerizes with MLL cleavage product C180 (via SET and FYRC domains). Interacts with WDR5; the interaction is direct. Interacts with KAT8/MOF; the interaction is direct. Interacts with SBF1 and PPP1R15A By similarity. Interacts with ZNF335 By similarity. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCF1/HCF1, HCFC2, WDR5, DPY30 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10.By similarity1 Publication

    Protein-protein interaction databases

    DIPiDIP-58597N.
    IntActiP55200. 1 interaction.
    MINTiMINT-4084570.

    Structurei

    3D structure databases

    ProteinModelPortaliP55200.
    SMRiP55200. Positions 6-39, 101-133, 1144-1200, 1563-1781, 2836-2865, 3787-3966.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1705 – 175046Bromo; divergentPROSITE-ProRule annotationAdd
    BLAST
    Domaini2020 – 207657FYR N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini3663 – 374482FYR C-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini3826 – 3942117SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini3950 – 396617Post-SETPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni3903 – 39042S-adenosyl-L-methionine bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi14 – 150137Gly-richAdd
    BLAST
    Compositional biasi17 – 10084Ala/Gly/Ser-richAdd
    BLAST
    Compositional biasi80 – 9920Ser-richAdd
    BLAST
    Compositional biasi135 – 1417Poly-Gly
    Compositional biasi199 – 28789Lys-richAdd
    BLAST
    Compositional biasi443 – 49149Ser-richAdd
    BLAST
    Compositional biasi559 – 60143Pro-richAdd
    BLAST
    Compositional biasi559 – 5624Poly-Pro
    Compositional biasi566 – 5694Poly-Pro
    Compositional biasi703 – 807105Ser-richAdd
    BLAST
    Compositional biasi1234 – 1366133Pro-richAdd
    BLAST
    Compositional biasi1819 – 186749Pro-richAdd
    BLAST
    Compositional biasi2185 – 2320136Ser-richAdd
    BLAST

    Domaini

    The SET domain structure is atypical and is not in an optimal position to have methyltransferase activity. It requires other components of the MLL1/MLL complex, such as ASH2L or RBBP5, to order the active site and obtain optimal histone methyltransferase activity By similarity.By similarity
    The CXXC-type zinc finger binds bind to nonmethyl-CpG dinucleotides.By similarity

    Sequence similaritiesi

    Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. TRX/MLL subfamily.PROSITE-ProRule annotation
    Contains 3 A.T hook DNA-binding domains.Curated
    Contains 1 bromo domain.PROSITE-ProRule annotation
    Contains 1 CXXC-type zinc finger.PROSITE-ProRule annotation
    Contains 1 FYR C-terminal domain.PROSITE-ProRule annotation
    Contains 1 FYR N-terminal domain.PROSITE-ProRule annotation
    Contains 3 PHD-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 post-SET domain.PROSITE-ProRule annotation
    Contains 1 SET domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1144 – 119249CXXC-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1430 – 148152PHD-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1478 – 153255PHD-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1565 – 162965PHD-type 3PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Bromodomain, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG2940.
    GeneTreeiENSGT00740000115089.
    HOGENOMiHOG000112954.
    HOVERGENiHBG051927.
    InParanoidiP55200.
    KOiK09186.
    OMAiRIMSPMR.
    OrthoDBiEOG7XH6NX.
    TreeFamiTF319820.

    Family and domain databases

    Gene3Di3.30.40.10. 2 hits.
    InterProiIPR017956. 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.
    [Graphical view]
    PfamiPF05965. FYRC. 1 hit.
    PF05964. FYRN. 1 hit.
    PF00628. PHD. 2 hits.
    PF00856. SET. 1 hit.
    PF02008. zf-CXXC. 1 hit.
    [Graphical view]
    PIRSFiPIRSF010354. Methyltransferase_trithorax. 1 hit.
    SMARTiSM00384. AT_hook. 3 hits.
    SM00297. BROMO. 1 hit.
    SM00542. FYRC. 1 hit.
    SM00541. FYRN. 1 hit.
    SM00249. PHD. 4 hits.
    SM00508. PostSET. 1 hit.
    SM00317. SET. 1 hit.
    [Graphical view]
    SUPFAMiSSF47370. SSF47370. 1 hit.
    SSF57903. SSF57903. 2 hits.
    PROSITEiPS50014. BROMODOMAIN_2. 1 hit.
    PS51543. FYRC. 1 hit.
    PS51542. FYRN. 1 hit.
    PS50868. POST_SET. 1 hit.
    PS50280. SET. 1 hit.
    PS51058. ZF_CXXC. 1 hit.
    PS01359. ZF_PHD_1. 3 hits.
    PS50016. ZF_PHD_2. 3 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P55200-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRVPALLL PPGPQAGGGG     50
    PGAPPSPPAV AAAAAGSSGA GVPGGAAAAS AASSSSASSS SSSSSSASSG 100
    PALLRVGPGF DAALQVSAAI GTNLRRFRAV FGESGGGGGS GEDEQFLGFG 150
    SDEEVRVRSP TRSPSVKASP RKPRGRPRSG SDRNPAILSD PSVFSPLNKS 200
    ETKSADKIKK KDSKSIEKKR GRPPTFPGVK IKITHGKDIA ELTQGSKEDS 250
    LKKVKRTPSA MFQQATKIKK LRAGKLSPLK SKFKTGKLQI GRKGVQIVRR 300
    RGRPPSTERI KTPSGLLINS ELEKPQKVRK DKEGTPPLTK EDKTVVRQSP 350
    RRIKPVRIIP SCKRTDATIA KQLLQRAKKG AQKKIEKEAA QLQGRKVKTQ 400
    VKNIRQFIMP VVSAISSRII KTPRRFIEDE DYDPPMKIAR LESTPNSRFS 450
    ATSCGSSEKS SAASQHSSQM SSDSSRSSSP SIDTTSDSQA SEEIQALPEE 500
    RSNTPEVHTP LPISQSPENE SNDRRSRRYS MSERSFGSRA TKKLPTLQSA 550
    PQQQTSSSPP PPLLTPPPPL QPASGISDHT PWLMPPTIPL ASPFLPASAA 600
    PMQGKRKSIL REPTFRWTSL KHSRSEPQYF SSAKYAKEGL IRKPIFDNFR 650
    PPPLTPEDVG FASGFSASGT AASARLFSPL HSGTRFDIHK RSPILRAPRF 700
    TPSEAHSRIF ESVTLPSNRT SSGASSSGVS NRKRKRKVFS PIRSEPRSPS 750
    HSMRTRSGRL STSELSPLTP PSSVSSSLSI PVSPLAASAL NPTFTFPSHS 800
    LTQSGESTEK NQRARKQTSA LAEPFSSNSP ALFPWFTPGS QTEKGRKKDT 850
    APEELSKDRD ADKSVEKDKS RERDREREKE NKRESRKEKR KKGSDIQSSS 900
    ALYPVGRVSK EKVAGEDVGT SSSAKKATGR KKSSSLDSGA DVAPVTLGDT 950
    TAVKAKILIK KGRGNLEKNN LDLGPAAPSL EKERTPCLSA PSSSTVKHST 1000
    SSIGSMLAQA DKLPMTDKRV ASLLKKAKAQ LCKIEKSKSL KQTDQPKAQG 1050
    QESDSSETSV RGPRIKHVCR RAAVALGRKR AVFPDDMPTL SALPWEEREK 1100
    ILSSMGNDDK SSVAGSEDAE PLAPPIKPIK PVTRNKAPQE PPVKKGRRSR 1150
    RCGQCPGCQV PEDCGICTNC LDKPKFGGRN IKKQCCKMRK CQNLQWMPSK 1200
    ASLQKQTKAV KKKEKKSKTT EKKESKESTA VKSPLEPAQK AAPPPREEPA 1250
    PKKSSSEPPP RKPVEEKSEE GGAPAPAPAP EPKQVSAPAS RKSSKQVSQP 1300
    AAVVPPQPPS TAPQKKEAPK AVPSEPKKKQ PPPPEPGPEQ SKQKKVAPRP 1350
    SIPVKQKPKD KEKPPPVSKQ ENAGTLNILN PLSNGISSKQ KIPADGVHRI 1400
    RVDFKEDCEA ENVWEMGGLG ILTSVPITPR VVCFLCASSG HVEFVYCQVC 1450
    CEPFHKFCLE ENERPLEDQL ENWCCRRCKF CHVCGRQHQA TKQLLECNKC 1500
    RNSYHPECLG PNYPTKPTKK KKVWICTKCV RCKSCGSTTP GKGWDAQWSH 1550
    DFSLCHDCAK LFAKGNFCPL CDKCYDDDDY ESKMMQCGKC DRWVHSKCES 1600
    LSGTEDEMYE ILSNLPESVA YTCVNCTERH PAEWRLALEK ELQASLKQVL 1650
    TALLNSRTTS HLLRYRQAAK PPDLNPETEE SIPSRSSPEG PDPPVLTEVS 1700
    KQDEQQPLDL EGVKKRMDQG SYVSVLEFSD DIVKIIQAAI NSDGGQPEIK 1750
    KANSMVKSFF IRQMERVFPW FSVKKSRFWE PNKVSNNSGM LPNAVLPPSL 1800
    DHNYAQWQER EESSHTEQPP LMKKIIPAPK PKGPGEPDSP TPLHPPTPPI 1850
    LSTDRSREDS PELNPPPGID DNRQCALCLM YGDDSANDAG RLLYIGQNEW 1900
    THVNCALWSA EVFEDDDGSL KNVHMAVIRG KQLRCEFCQK PGATVGCCLT 1950
    SCTSNYHFMC SRAKNCVFLD DKKVYCQRHR DLIKGEVVPE NGFEVFRRVF 2000
    VDFEGISLRR KFLNGLEPEN IHMMIGSMTI DCLGILNDLS DCEDKLFPIG 2050
    YQCSRVYWST TDARKRCVYT CKIMECRPPV VEPDINSTVE HDDNRTIAHS 2100
    PSSFIDASCK DSQSTAAILS PPSPDRPHSQ TSGSCYYHVI SKVPRIRTPS 2150
    YSPTQRSPGC RPLPSAGSPT PTTHEIVTVG DPLLSSGLRS IGSRRHSTSS 2200
    LSPLRSKLRI MSPVRTGSAY SRSSVSSVPS LGTATDPEAS AKASDRGGLL 2250
    SSSANLGHSA PPSSSSQRTV GGSKTSHLDG SSPSEVKRCS ASDLVPKGSL 2300
    VKGEKNRTSS SKSTDGSAHS TAYPGIPKLT PQVHNATPGE LNISKIGSFA 2350
    EPSTVPFSSK DTVSYPQLHL RGQRSDRDQH MDPSQSVKPS PNEDGEIKTL 2400
    KLPGMGHRPS ILHEHIGSSS RDRRQKGKKS SKETCKEKHS SKSYLEPGQV 2450
    TTGEEGNLKP EFADEVLTPG FLGQRPCNNV SSEKIGDKVL PLSGVPKGQS 2500
    TQVEGSSKEL QAPRKCSVKV TPLKMEGENQ SKNTQKESGP GSPAHIESVC 2550
    PAEPVSASRS PGAGPGVQPS PNNTLSQDPQ SNNYQNLPEQ DRNLMIPDGP 2600
    KPQEDGSFKR RYPRRSARAR SNMFFGLTPL YGVRSYGEED IPFYSNSTGK 2650
    KRGKRSAEGQ VDGADDLSTS DEDDLYYYNF TRTVISSGGE ERLASHNLFR 2700
    EEEQCDLPKI SQLDGVDDGT ESDTSVTATS RKSSQIPKRN GKENGTENLK 2750
    IDRPEDAGEK EHVIKSAVGH KNEPKLDNCH SVSRVKAQGQ DSLEAQLSSL 2800
    ESSRRVHTST PSDKNLLDTY NAELLKSDSD NNNSDDCGNI LPSDIMDFVL 2850
    KNTPSMQALG ESPESSSSEL LTLGEGLGLD SNREKDIGLF EVFSQQLPAT 2900
    EPVDSSVSSS ISAEEQFELP LELPSDLSVL TTRSPTVPSQ NPSRLAVISD 2950
    SGEKRVTITE KSVASSEGDP ALLSPGVDPA PEGHMTPDHF IQGHMDADHI 3000
    SSPPCGSVEQ GHGNSQDLTR NSGTPGLQVP VSPTVPVQNQ KYVPSSTDSP 3050
    GPSQISNAAV QTTPPHLKPA TEKLIVVNQN MQPLYVLQTL PNGVTQKIQL 3100
    TSPVSSTPSV METNTSVLGP MGSGLTLTTG LNPSLPPSPS LFPPASKGLL 3150
    SVPHHQHLHS FPAAAQSSFP PNISSPPSGL LIGVQPPPDP QLLGSEANQR 3200
    TDLTTTVATP SSGLKKRPIS RLHTRKNKKL APSSAPSNIA PSDVVSNMTL 3250
    INFTPSQLSN HPSLLDLGSL NPSSHRTVPN IIKRSKSGIM YFEQAPLLPP 3300
    QSVGGTAATA AGSSTISQDT SHLTSGPVSA LASGSSVLNV VSMQTTAAPT 3350
    SSTSVPGHVT LANQRLLGTP DIGSISHLLI KASHQSLGIQ DQPVALPPSS 3400
    GMFPQLGTSQ TPSAAAMTAA SSICVLPSSQ TAGMTAASPP GEAEEHYKLQ 3450
    RGNQLLAGKT GTLTSQRDRD PDSAPGTQPS NFTQTAEAPN GVRLEQNKTL 3500
    PSAKPASSAS PGSSPSSGQQ SGSSSVPGPT KPKPKAKRIQ LPLDKGSGKK 3550
    HKVSHLRTSS EAHIPHRDTD PAPQPSVTRT PRANREQQDA AGVEQPSQKE 3600
    CGQPAGPVAA LPEVQATQNP ANEQENAEPK AMEEEESGFS SPLMLWLQQE 3650
    QKRKESITER KPKKGLVFEI SSDDGFQICA ESIEDAWKSL TDKVQEARSN 3700
    ARLKQLSFAG VNGLRMLGIL HDAVVFLIEQ LAGAKHCRNY KFRFHKPEEA 3750
    NEPPLNPHGS ARAEVHLRQS AFDMFNFLAS KHRQPPEYNP NDEEEEEVQL 3800
    KSARRATSMD LPMPMRFRHL KKTSKEAVGV YRSPIHGRGL FCKRNIDAGE 3850
    MVIEYAGNVI RSIQTDKREK YYDSKGIGCY MFRIDDSEVV DATMHGNAAR 3900
    FINHSCEPNC YSRVINIDGQ KHIVIFAMRK IYRGEELTYD YKFPIEDASN 3950
    KLPCNCGAKK CRKFLN 3966
    Length:3,966
    Mass (Da):429,649
    Last modified:July 27, 2011 - v3
    Checksum:iEA9CB2A467AB3545
    GO
    Isoform 2 (identifier: P55200-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1603-1605: Missing.

    Show »
    Length:3,963
    Mass (Da):429,362
    Checksum:i5E5106EB6EF1B932
    GO

    Sequence cautioni

    The sequence BAE24386.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti372 – 3721Q → E in BAE28820. (PubMed:16141072)Curated
    Sequence conflicti554 – 5541Q → K in AAA62593. (PubMed:8327517)Curated
    Sequence conflicti564 – 5641L → F in AAA62593. (PubMed:8327517)Curated
    Sequence conflicti797 – 7971P → S in BAE28820. (PubMed:16141072)Curated
    Sequence conflicti806 – 8061E → D in AAA62593. (PubMed:8327517)Curated
    Sequence conflicti806 – 8061E → D in BAE28820. (PubMed:16141072)Curated
    Sequence conflicti821 – 8211L → P in AAA62593. (PubMed:8327517)Curated
    Sequence conflicti821 – 8211L → P in BAE28820. (PubMed:16141072)Curated
    Sequence conflicti1069 – 10691C → Y in AAA62593. (PubMed:8327517)Curated
    Sequence conflicti1230 – 12301A → S in AAA62593. (PubMed:8327517)Curated
    Sequence conflicti1349 – 13491R → L in AAA62593. (PubMed:8327517)Curated
    Sequence conflicti1437 – 14371A → S in AAA62593. (PubMed:8327517)Curated
    Sequence conflicti1440 – 14401G → E in AAA62593. (PubMed:8327517)Curated
    Sequence conflicti1632 – 16321A → P in AAA62593. (PubMed:8327517)Curated
    Sequence conflicti2292 – 22921S → L in AAA62593. (PubMed:8327517)Curated
    Sequence conflicti3481 – 34811N → I in AAA62593. (PubMed:8327517)Curated
    Sequence conflicti3493 – 34931R → S in AAA62593. (PubMed:8327517)Curated
    Sequence conflicti3548 – 35481G → V in AAA62593. (PubMed:8327517)Curated
    Sequence conflicti3769 – 37691Q → K in AAA62593. (PubMed:8327517)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1597 – 15971K → T.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1603 – 16053Missing in isoform 2. 1 PublicationVSP_006667

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC061963 Genomic DNA. No translation available.
    AC142113 Genomic DNA. No translation available.
    L17069 mRNA. Translation: AAA62593.1.
    AK140439 mRNA. Translation: BAE24386.1. Different initiation.
    AK149341 mRNA. Translation: BAE28820.1.
    CCDSiCCDS40603.1. [P55200-2]
    RefSeqiNP_001074518.1. NM_001081049.1. [P55200-2]
    UniGeneiMm.2389.

    Genome annotation databases

    EnsembliENSMUST00000002095; ENSMUSP00000002095; ENSMUSG00000002028. [P55200-2]
    ENSMUST00000114689; ENSMUSP00000110337; ENSMUSG00000002028. [P55200-1]
    GeneIDi214162.
    KEGGimmu:214162.
    UCSCiuc009pep.1. mouse. [P55200-2]
    uc009peq.1. mouse. [P55200-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC061963 Genomic DNA. No translation available.
    AC142113 Genomic DNA. No translation available.
    L17069 mRNA. Translation: AAA62593.1 .
    AK140439 mRNA. Translation: BAE24386.1 . Different initiation.
    AK149341 mRNA. Translation: BAE28820.1 .
    CCDSi CCDS40603.1. [P55200-2 ]
    RefSeqi NP_001074518.1. NM_001081049.1. [P55200-2 ]
    UniGenei Mm.2389.

    3D structure databases

    ProteinModelPortali P55200.
    SMRi P55200. Positions 6-39, 101-133, 1144-1200, 1563-1781, 2836-2865, 3787-3966.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-58597N.
    IntActi P55200. 1 interaction.
    MINTi MINT-4084570.

    PTM databases

    PhosphoSitei P55200.

    Proteomic databases

    PaxDbi P55200.
    PRIDEi P55200.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000002095 ; ENSMUSP00000002095 ; ENSMUSG00000002028 . [P55200-2 ]
    ENSMUST00000114689 ; ENSMUSP00000110337 ; ENSMUSG00000002028 . [P55200-1 ]
    GeneIDi 214162.
    KEGGi mmu:214162.
    UCSCi uc009pep.1. mouse. [P55200-2 ]
    uc009peq.1. mouse. [P55200-1 ]

    Organism-specific databases

    CTDi 4297.
    MGIi MGI:96995. Kmt2a.

    Phylogenomic databases

    eggNOGi COG2940.
    GeneTreei ENSGT00740000115089.
    HOGENOMi HOG000112954.
    HOVERGENi HBG051927.
    InParanoidi P55200.
    KOi K09186.
    OMAi RIMSPMR.
    OrthoDBi EOG7XH6NX.
    TreeFami TF319820.

    Miscellaneous databases

    NextBioi 374214.
    PROi P55200.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P55200.
    Bgeei P55200.
    CleanExi MM_MLL1.
    Genevestigatori P55200.

    Family and domain databases

    Gene3Di 3.30.40.10. 2 hits.
    InterProi 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.
    [Graphical view ]
    Pfami PF05965. FYRC. 1 hit.
    PF05964. FYRN. 1 hit.
    PF00628. PHD. 2 hits.
    PF00856. SET. 1 hit.
    PF02008. zf-CXXC. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF010354. Methyltransferase_trithorax. 1 hit.
    SMARTi SM00384. AT_hook. 3 hits.
    SM00297. BROMO. 1 hit.
    SM00542. FYRC. 1 hit.
    SM00541. FYRN. 1 hit.
    SM00249. PHD. 4 hits.
    SM00508. PostSET. 1 hit.
    SM00317. SET. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47370. SSF47370. 1 hit.
    SSF57903. SSF57903. 2 hits.
    PROSITEi PS50014. BROMODOMAIN_2. 1 hit.
    PS51543. FYRC. 1 hit.
    PS51542. FYRN. 1 hit.
    PS50868. POST_SET. 1 hit.
    PS50280. SET. 1 hit.
    PS51058. ZF_CXXC. 1 hit.
    PS01359. ZF_PHD_1. 3 hits.
    PS50016. ZF_PHD_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    2. "Analysis of the murine All-1 gene reveals conserved domains with human ALL-1 and identifies a motif shared with DNA methyltransferases."
      Ma Q., Alder H., Nelson K.K., Chatterjee D., Gu Y., Nakamura T., Canaani E., Croce C.M., Siracusa L.D., Buchberg A.M.
      Proc. Natl. Acad. Sci. U.S.A. 90:6350-6354(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 101-3966 (ISOFORMS 1 AND 2).
      Strain: C57BL/6 X CBA and C57BL/6J.
      Tissue: Lung and Spleen.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 372-1517 (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Medulla oblongata and Retina.
    4. "Role for Dpy-30 in ES cell-fate specification by regulation of H3K4 methylation within bivalent domains."
      Jiang H., Shukla A., Wang X., Chen W.Y., Bernstein B.E., Roeder R.G.
      Cell 144:513-525(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN MLL COMPLEX, INTERACTION WITH ASH2L; DPY30; KMT2D; RRBP5 AND WDR5.
    5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-237; LYS-371; LYS-2954 AND LYS-3459, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiKMT2A_MOUSE
    AccessioniPrimary (citable) accession number: P55200
    Secondary accession number(s): E9QNE7, Q3UEU1, Q3USE7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 135 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3