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Q6PDK2

- KMT2D_MOUSE

UniProt

Q6PDK2 - KMT2D_MOUSE

Protein

Histone-lysine N-methyltransferase 2D

Gene

Kmt2d

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (30 Nov 2010)
      Previous versions | rss
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    Functioni

    Histone methyltransferase. Methylates 'Lys-4' of histone H3 (H3K4me). H3K4me represents a specific tag for epigenetic transcriptional activation. Acts as a coactivator for estrogen receptor by being recruited by ESR1, thereby activating transcription 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
    Binding sitei5502 – 55021S-adenosyl-L-methioninePROSITE-ProRule annotation
    Metal bindingi5528 – 55281ZincBy similarity
    Metal bindingi5576 – 55761ZincBy similarity
    Metal bindingi5578 – 55781ZincBy similarity
    Metal bindingi5583 – 55831ZincBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri226 – 27651PHD-type 1; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri229 – 27446RING-type 1; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri270 – 32354PHD-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri276 – 32146RING-type 2; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1071 – 112454PHD-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1121 – 117151PHD-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1198 – 125356PHD-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1201 – 125151RING-type 3; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4829 – 487446RING-type 4; degeneratePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. histone-lysine N-methyltransferase activity Source: UniProtKB-EC
    2. transcription regulatory region DNA binding Source: Ensembl
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. chromatin silencing Source: UniProtKB
    2. histone H3-K4 methylation Source: UniProtKB
    3. in utero embryonic development Source: MGI
    4. oocyte growth Source: UniProtKB
    5. oogenesis Source: UniProtKB
    6. positive regulation of cell proliferation Source: Ensembl
    7. positive regulation of intracellular estrogen receptor signaling pathway Source: Ensembl
    8. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    9. response to estrogen Source: Ensembl
    10. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Methyltransferase, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

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

    Enzyme and pathway databases

    ReactomeiREACT_216539. formation of the beta-catenin:TCF transactivating complex.
    REACT_219771. deactivation of the beta-catenin transactivating complex.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone-lysine N-methyltransferase 2D (EC:2.1.1.43)
    Short name:
    Lysine N-methyltransferase 2D
    Alternative name(s):
    ALL1-related protein
    Myeloid/lymphoid or mixed-lineage leukemia protein 2
    Gene namesi
    Name:Kmt2d
    Synonyms:Mll2, Mll4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:2682319. Kmt2d.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. histone methyltransferase complex Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 55885588Histone-lysine N-methyltransferase 2DPRO_0000401938Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1562 – 15621PhosphoserineBy similarity
    Modified residuei1627 – 16271Phosphoserine1 Publication
    Modified residuei2203 – 22031N6-acetyllysineBy similarity
    Modified residuei2231 – 22311PhosphoserineBy similarity
    Modified residuei2266 – 22661PhosphoserineBy similarity
    Modified residuei2268 – 22681PhosphoserineBy similarity
    Modified residuei3071 – 30711N6-acetyllysine1 Publication
    Modified residuei3122 – 31221PhosphoserineBy similarity
    Modified residuei3193 – 31931PhosphoserineBy similarity
    Modified residuei3430 – 34301N6-acetyllysineBy similarity
    Modified residuei4272 – 42721PhosphoserineBy similarity
    Modified residuei4410 – 44101PhosphoserineBy similarity
    Modified residuei4516 – 45161N6-acetyllysineBy similarity
    Modified residuei4789 – 47891Phosphoserine1 Publication
    Modified residuei4827 – 48271N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ6PDK2.
    PaxDbiQ6PDK2.
    PRIDEiQ6PDK2.

    PTM databases

    PhosphoSiteiQ6PDK2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ6PDK2.
    BgeeiQ6PDK2.
    GenevestigatoriQ6PDK2.

    Interactioni

    Subunit structurei

    Interacts with ESR1; interaction is direct By similarity. Component of the MLL2/3 complex (also named ASCOM complex), at least composed of KMT2D/MLL2 or KMT2C/MLL3, ASH2L, RBBP5, WDR5, NCOA6, DPY30, KDM6A, PAXIP1/PTIP, PAGR1 and alpha- and beta-tubulin.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi237747. 9 interactions.
    IntActiQ6PDK2. 2 interactions.
    STRINGi10090.ENSMUSP00000023741.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6PDK2.
    SMRiQ6PDK2. Positions 220-323, 1957-2034.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati442 – 44651
    Repeati460 – 46452
    Repeati469 – 47354
    Repeati477 – 48155
    Repeati520 – 52457
    Repeati529 – 53358
    Repeati538 – 54259
    Repeati547 – 551510
    Repeati574 – 578511
    Repeati583 – 587512
    Repeati592 – 596513
    Repeati610 – 614514
    Repeati637 – 641515
    Domaini5226 – 528661FYR N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini5287 – 537286FYR C-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini5448 – 5564117SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini5572 – 558817Post-SETPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni439 – 64220415 X 5 AA repeats of S/P-P-P-E/P-E/AAdd
    BLAST
    Regioni5525 – 55262S-adenosyl-L-methionine bindingBy similarity

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili2627 – 266539Sequence AnalysisAdd
    BLAST
    Coiled coili2768 – 281346Sequence AnalysisAdd
    BLAST
    Coiled coili3559 – 361355Sequence AnalysisAdd
    BLAST
    Coiled coili3712 – 374736Sequence AnalysisAdd
    BLAST
    Coiled coili3854 – 388330Sequence AnalysisAdd
    BLAST
    Coiled coili3912 – 4052141Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi2644 – 26485LXXLL motif 1
    Motifi3030 – 30345LXXLL motif 2
    Motifi4279 – 429315LXXLL motif 3Add
    BLAST
    Motifi4310 – 43145LXXLL motif 4
    Motifi4514 – 45185LXXLL motif 5
    Motifi5041 – 50455LXXLL motif 6

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1307 – 13115Poly-Glu
    Compositional biasi2064 – 2583520Pro-richAdd
    BLAST
    Compositional biasi2610 – 26134Poly-Ser
    Compositional biasi2769 – 281244Gln-richAdd
    BLAST
    Compositional biasi2813 – 28197Poly-Ala
    Compositional biasi3255 – 43321078Gln-richAdd
    BLAST
    Compositional biasi4841 – 48444Poly-Ala
    Compositional biasi4960 – 502869Pro-richAdd
    BLAST

    Domaini

    LXXLL motifs 5 and 6 are essential for the association with ESR1 nuclear receptor.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 1 FYR C-terminal domain.PROSITE-ProRule annotation
    Contains 1 FYR N-terminal domain.PROSITE-ProRule annotation
    Contains 5 PHD-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 post-SET domain.PROSITE-ProRule annotation
    Contains 4 RING-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 SET domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri226 – 27651PHD-type 1; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri229 – 27446RING-type 1; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri270 – 32354PHD-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri276 – 32146RING-type 2; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1071 – 112454PHD-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1121 – 117151PHD-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1198 – 125356PHD-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1201 – 125151RING-type 3; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4829 – 487446RING-type 4; degeneratePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG2940.
    GeneTreeiENSGT00740000115009.
    HOGENOMiHOG000168503.
    InParanoidiQ6PDK2.
    PhylomeDBiQ6PDK2.

    Family and domain databases

    Gene3Di3.30.40.10. 5 hits.
    InterProiIPR003889. FYrich_C.
    IPR003888. FYrich_N.
    IPR009071. HMG_box_dom.
    IPR003616. Post-SET_dom.
    IPR001214. SET_dom.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF05965. FYRC. 1 hit.
    PF05964. FYRN. 1 hit.
    PF00628. PHD. 3 hits.
    PF00856. SET. 1 hit.
    [Graphical view]
    SMARTiSM00542. FYRC. 1 hit.
    SM00541. FYRN. 1 hit.
    SM00398. HMG. 1 hit.
    SM00249. PHD. 7 hits.
    SM00508. PostSET. 1 hit.
    SM00184. RING. 6 hits.
    SM00317. SET. 1 hit.
    [Graphical view]
    SUPFAMiSSF47095. SSF47095. 1 hit.
    SSF57903. SSF57903. 5 hits.
    PROSITEiPS51543. FYRC. 1 hit.
    PS51542. FYRN. 1 hit.
    PS50868. POST_SET. 1 hit.
    PS50280. SET. 1 hit.
    PS01359. ZF_PHD_1. 5 hits.
    PS50016. ZF_PHD_2. 4 hits.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q6PDK2-1 [UniParc]FASTAAdd to Basket

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    MDSQKPPAED KDSDPAADGL AAPEKPGATE PDLPILCIGE VSVPGSGGSR     50
    PQKPPHDCSR GPARRCALCN CGEPGLHGQR ELQRFELPSD WPGFPVVPSG 100
    GNSGPCEAVL PKEDASQIGF PEGLTPAHLG EPGGHCWAHH WCAAWSAGVW 150
    GQEGPELCGV DKAIFSGISQ RCSHCARFGA SVPCRSPGCS RLYHFPCATA 200
    SGSFLSMKTL QLLCPEHSDG AAHLEEARCA VCEGPGQLCD LLFCTSCGHH 250
    YHGACLDTAL TARKRASWQC PECKVCQSCR KPGNDSKMLV CETCDKGYHT 300
    FCLKPPMEDL PAHSWKCKTC RLCRACGAGS AELNPNSEWF ENYSLCHRCH 350
    KAQGSQPVTS VAEQHPAVCS RLSPPEPGEI PIDAPDALYV ACQGQPKGGH 400
    VTSMQPKELA PLQCEAKPLG RAGTQLEAQL EAPLHEEMPL LPPPEESPLS 450
    PPPEESPTSP PPEASRLSPP TEESPLSPPP ESSPFSPLEG CPPSPALDTP 500
    LSPPPEASPL SPPFEESPLS PPPEELPSSP PPEASRLSPP PEESPMSPPP 550
    EESPMSPPPE ASRLFPPFEE SPLSPPPEDS PLSPPPEASR LSPPPEDSPM 600
    SPPPEDSPMS PPPEVSRFLP LPVLSHLSPL PEVSRLSPPP EESPLSPPPE 650
    DSPASPPPEA SRLSPPPEDS PASPPPEASR LSRPREDSPA SPPPEDSLVS 700
    LPMEESPLSP LPEELRLCPQ PEEPYLSPQP EEPRLCPQPE ELPLSPQSEE 750
    PCLSPVLVEP GPSSQPEEPH LSPVPQEPHL SPQPEEPHLS PQPQQLHLSP 800
    HSEEPCLSPM PEEPCLSPQP EELNGPPQPA EPPEEPSQSS APKELSLFSP 850
    SGEPPLPPML GEPALSEPGE PPLSPLPEEL PLSLSGEPVL SPQLMPPDPL 900
    PPPLSPIIPA AAPPALSPLG ELEYPFGAKG DSDPESPLAA PILETPISPP 950
    PEANCTDPEP VPPMILPPSP GSPLGPASPI LMERLPPPCS PLLPHSLPPP 1000
    TPPPSHCSPP ALPLSVPSPL SPVQKAVDVS DEAELHEMET DKGPEPECPA 1050
    LEPRATSPLP SPLGDLSCPA PSPAPALDDF SGLGEDTAPL DGTGQMSGSL 1100
    AGELKGSPVL LDPEELTPVT PMEVYGPECK QAGQGSPCEE QEEPGAPMAP 1150
    MPPTLIKSDI VNEISNLSQG DASASFPGSE PLLGSPDPEG GGSLSMELGV 1200
    STDVSPARDE GSLRLCTDSL PETDDSLLCD TGTATSGGKA EGDKGRRRSS 1250
    PARSRIKQGR SSSFPGRRRP RGGAAHGGRG RGRARLKSTT SSVETLVADI 1300
    DSSPSKEEEE EDDDTMQNTV VLFSNTDKFV LMQDMCVVCG SFGRGAEGHL 1350
    LACSQCSQCY HPYCVNSKIT KVMLLKGWRC VECIVCEVCG QASDPSRLLL 1400
    CDDCDISYHT YCLDPPLLTV PKGGWKCKWC VSCMQCGAAS PGFHCEWQNS 1450
    YTHCGPCASL VTCPVCHAPY VEEDLLIQCR HCERWMHAGC ESLFTEDEVE 1500
    QAADEGFDCV SCQPYVVKPV VPVAPPELVP VKVKEPEPQF FRFEGVWLTE 1550
    TGMAVLRNLT MSPLHKRRQR RGRLGLPGEA GLEGSEPSDA LGPDDKKDGD 1600
    LDTDDLLKGE GGVEQMECEI KLEGPASPDV ELGKEETEES KKRKRKPYRP 1650
    GIGGFMVRQR KSHTRVKRGP AAQAEVLSGD GQPDEVMPAD LPAEGSVEQS 1700
    LAEGDEKKKQ QRRARKKSKL EDMFPAYLQA AFFGKDLLDL SRKALFAVGV 1750
    GRPGFGLGAS KPRADGGSDR KELMTAMHKG DDGPDVADEE SHGPEGTADL 1800
    PGLEDGGVKA SPVPSDPEKP GTPGEGVLSS DLDRIPTEEL PKMESKDLQQ 1850
    LFKDVLGSER EQHLGCGTPG LEGGRTSLQR PFLQGGLALG SLPSSSPMDS 1900
    YPGLCQSPFL DSRERGGFFS PEPGEPDSPW TGSGGTTPST PTTPTTEGEG 1950
    DGLSYNQRSL QRWEKDEELG QLSTISPVLY ANINFPNLKQ DYPDWSSRCK 2000
    QIMKLWRKVP AADKAPYLQK AKDNRAAHRI SKVQKQAESQ ISKQAKMGDI 2050
    ARKTDRPALH LRIPSQPGAL GSPPPAAAPT IFLGSPTTPA GLSTSADGFL 2100
    KPPAGTVPGP DSPGELFLKL PPQVPAQVPS QDPFGLAPAY APEPRFSAAP 2150
    PTYPPYPSPT GAPAQPPMLG TTTRPGTGQP GEFHTTPPGT PRHQPSTPDP 2200
    FLKPRCPSLD NLAVPESPGV AGGKASEPLL SPPPFGESRK SLEVKKEELG 2250
    ASSPGYGPPN LGCVDSPSAG PHLGGLELKA PDVFKAPLTP RASQVEPQSP 2300
    GLGLRAQEPP PAQALAPSPP SHPDVFRSGP YPDPYAQPPL TPRPQPPPPE 2350
    SCCAPPPRSL PSDPFSRVPA SPQSQSSSQS PLTPRPLSAE AFCPSPVTPR 2400
    FQSPDPYSRP PSRPQSRDPF APLHKPPRPQ PPEVAFKAGP LAHTPLGAGG 2450
    FPAALPSGPA GELHAKVPSG QPTNFARSPG TGTFVGTPSP MRFTFPQGVG 2500
    EPSLKPPVPQ PGLPSPHGIN SHFGPGPTLG KPQSTNYAVA TGNFHPSGSP 2550
    LGPNSGPTGE GYGLSPLRPA SVLPPPAPDG SLPYLTHGAS QRVGITSPVE 2600
    KREDPGATMS SSSLATPELS SAQDAGISSL SQTELEKQRQ RQRLRELLIR 2650
    QQIQRNTLRQ EKETAAAAAG AVGPPGNWGA EPSSPAFEQL SRGQTPFTGS 2700
    QDRSSIVGLP ASKLGGPTLG PGAFSSDDRL ARPLPPATPS SMDMNSRQLV 2750
    GGSQAFYQRT PYPGSLPLQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQLWQ 2800
    QQQQQQQQQQ QQAAAAAAAT SMRLAMSARF PSTPGPELGR QALGSPLAGI 2850
    PTRLPGPAEP VPGPAGPAQF IELRHNVQKG LGPGVSPFPG QGPPQRPRFY 2900
    PVSEELHRLA PEGLRGLAVP GLPSQKPSAL PAPELNNSLH QTPHAKGPAL 2950
    ASGLELVSRP PSNTELSRPP LALEAGKLPC EDPELDDDFD AHKALEDDEE 3000
    LAHLGLGVDV AKGDDELGTL ENLETNDPHL DDLLNGDEFD LLAYTDPELD 3050
    TGDKKDIFNE HLRLVESANE KAEREALLRG VEPVSLGPEE RPPPAPDNSE 3100
    PRLTSVLPEV KPKVEEGGRH PSPCQFTINT PKVEPAPPAT SLSLGLKPGQ 3150
    TVMGTRDTRG GVGTGSFPSS GHTAEKGPFG ATGGTPAHLL NPSSLSGPAA 3200
    SSLLEKFELE SGALTLPSGH AAAGDELDKM ESSLVASELP LLIEDLLEHE 3250
    KKELQKKQQL SAQTVLPAQQ QQQQQQQQQQ QQQQHTLLPT PGPAQALPLP 3300
    HEPGPPQQLA LGIGSTRQPG LGQSMVPIQP PAHALQQRLA PSVAMVSNQG 3350
    HMLSGQQAGQ TGLVPQQSSQ PVLAQKPMSA MPASMCMKPQ QLAMQQQQLA 3400
    NSFFPDTDLD KFAAEDIIDP IAKAKMVALK GIKKVMAQGS IGVAPGMNRQ 3450
    QVSLLAQRLS GGSGSDLQNH VAPGSGQERN AGDPAQPRPN PPTFAQGVIN 3500
    EADQRQYEEW LFHTQQLLQM QLKVLEEQIG VHRKSRKALC AKQRTAKKAG 3550
    REFPEADAEK LKLVTEQQSK IQKQLDQVRK QQKEHTNLMA EYRNKQQQQQ 3600
    QQQQQQQQQQ HSAVLAVSPS QNPRVLTKLP GQLLPAHGLQ PPQAPPGGQA 3650
    GGLRLPPGGM VLPGQSGGPF LNTTLAQQQQ QQHSGVAGSL TGPPGSFFPG 3700
    NLALRSLGPD SRLLQERQLQ LQQQRMQLAQ KLQQQQQQQQ QQQQQQHLLG 3750
    QVAIQQQQGP GVQNQALGPK PQGLLPPSNH QGLLVQQLSP QQSQGSQGLL 3800
    GPAQVTVLQQ QQQQQQHSGA LGPQGPHRQV LMTQSRVLSS PQLAQQGHSL 3850
    MGHRLLTAQQ QQQQQQQQQQ QQQQQQQQQQ QQQGSMTGLS QLQQGMMSHG 3900
    GQPKMSAQAL GSLQQQQQQL QQQQMLQQQQ LQQQQQQLQQ QQQQQQLQQQ 3950
    QQQQLQLQQQ QQQQQQHLQH QQQQQQQLQQ QQQLQQQQQQ QLHLQQQLHQ 4000
    QQQLQLQQQQ MGLLNQNRTL LSPQQQQQQQ QQQQQQQQQQ QQQQQQQQQV 4050
    TLGPGLPVKP LQHFSSSGAL GPTLLLTGKE QNNAETALPS EVTEGPSTHQ 4100
    GGPPAVGTAP EPMSVEPGEV KPSISGDSQL LLVQSQAQSQ ATSVQLQPPL 4150
    RLPGQPQPQV NLLHTAGGGS HGQQLGSGSS SESPAVPHLL AQPSVSLGEQ 4200
    PGPMAQNLLG SQQPLGLDRP IQNNTGSQPP KSGPAPQSGQ GPPGAGVMPT 4250
    VGQLRAQLQG VLAKNPQLRH LSPQQQQQLQ ALLMQRQLQQ SQAVRQTPPF 4300
    QEPGTQPSPL QGLLGCQPQP GGFSVSQTGP LQELGAGSRP QGPPRLPVPQ 4350
    GALSTGPVLG PAHPTPPPSS PQEPKRPSQL PSPSAQLTPT HPGTPKPQGP 4400
    ALELPPGRVS PAAAQLADTF FGKGLGPWDP SDNLTEAQKP EQSSLVPGHL 4450
    DQVNGQVVHE PSQLSIKQEP REEPCALGAQ TVKREANGEP AGAPGTSNHL 4500
    LLAGSRSEAG HLLLQKLLRA KNVQLGAGRG PEGLRAEING HIDSKLSGLE 4550
    QKLQGTSSNK EDAATRKPLP AKPKRVQKTS DRLPSSRKKL RKEDGVRANE 4600
    ALLKQLKQEL SQLPLTEPTI TANFSLFAPF GSGCLVSGQS QLRGAFGSGA 4650
    LHTGPDYYSQ LLTKNNLSNP PTPPSSLPPT PPPSVQQKMV NGVTPSDELG 4700
    ERPKDTASAQ DSEGALRDAA EVKSLDLLAA LPTPPHNQTE DVRMESDEDS 4750
    DSPDSIVPAS SPESILGEEA PRFPQLGSGR WEQDNRALSP VIPIIPRTGI 4800
    PVFPDTKPYG VLDLEVPGKL PATAWEKGKG SEVSVMLTVS AAAAKNLNGV 4850
    MVAVAELLSM KIPNSYEVLF PDGPARAGLE PKKGEAEGPG GKEKGLSGKG 4900
    PDTGPDWLKQ FDAVLPGYTL KSQLDILSLL KQESPAPEPS IQHSYTYNVS 4950
    NLDVRQLSAP PPEEPSPPPS PLAPSPASPP AEPMVELQAE RPAEPPIPSP 5000
    LPLASSPESA RPKPRARPPE ESEDSRPPRL KKWKGVRWKR LRLLLTIQKG 5050
    SGHQEDEREV AEFMEQFGTA LRPSKVPRDN RRCCFCHEEG DGATDGPARL 5100
    LNLDLDLWVH LNCALWSTEV YETQGGALMN VEVALHRGLL TKCSLCQRTG 5150
    ATSSCNRMRC PNVYHFACAI RAKCMFFKDK TMLCPVHKIK GPCEQELSSF 5200
    AVFRRVYIER DEVKQIASII QRGERLHMFR VGGLVFHAIG QLLPHQMADF 5250
    HSATALYPVG YEATRIYWSL RTNNRRCCYR CSISENNGRP EFVIKVIEQG 5300
    LEDLVFTDAS PQAVWNRIIE PVAAMRKEAD MLRLFPEYLK GEELFGLTVH 5350
    AVLRIAESLP GVESCQNYLF RYGRHPLMEL PLMINPTGCA RSEPKILTHY 5400
    KRPHTLNSTS MSKAYQSTFT GETNTPYSKQ FVHSKSSQYR RLRTEWKNNV 5450
    YLARSRIQGL GLYAAKDLEK HTMVIEYIGT IIRNEVANRR EKIYEEQNRG 5500
    IYMFRINNEH VIDATLTGGP ARYINHSCAP NCVAEVVTFD KEDKIIIISS 5550
    RRIPKGEELT YDYQFDFEDD QHKIPCHCGA WNCRKWMN 5588
    Length:5,588
    Mass (Da):600,245
    Last modified:November 30, 2010 - v2
    Checksum:i37A0E5D319A5F1A6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC161165 Genomic DNA. No translation available.
    BC058659 mRNA. Translation: AAH58659.1.
    CCDSiCCDS49725.2.
    UniGeneiMm.264889.

    Genome annotation databases

    EnsembliENSMUST00000178486; ENSMUSP00000135941; ENSMUSG00000048154.
    UCSCiuc029suy.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC161165 Genomic DNA. No translation available.
    BC058659 mRNA. Translation: AAH58659.1 .
    CCDSi CCDS49725.2.
    UniGenei Mm.264889.

    3D structure databases

    ProteinModelPortali Q6PDK2.
    SMRi Q6PDK2. Positions 220-323, 1957-2034.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 237747. 9 interactions.
    IntActi Q6PDK2. 2 interactions.
    STRINGi 10090.ENSMUSP00000023741.

    PTM databases

    PhosphoSitei Q6PDK2.

    Proteomic databases

    MaxQBi Q6PDK2.
    PaxDbi Q6PDK2.
    PRIDEi Q6PDK2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000178486 ; ENSMUSP00000135941 ; ENSMUSG00000048154 .
    UCSCi uc029suy.1. mouse.

    Organism-specific databases

    MGIi MGI:2682319. Kmt2d.

    Phylogenomic databases

    eggNOGi COG2940.
    GeneTreei ENSGT00740000115009.
    HOGENOMi HOG000168503.
    InParanoidi Q6PDK2.
    PhylomeDBi Q6PDK2.

    Enzyme and pathway databases

    Reactomei REACT_216539. formation of the beta-catenin:TCF transactivating complex.
    REACT_219771. deactivation of the beta-catenin transactivating complex.

    Miscellaneous databases

    ChiTaRSi MLL2. mouse.
    PROi Q6PDK2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6PDK2.
    Bgeei Q6PDK2.
    Genevestigatori Q6PDK2.

    Family and domain databases

    Gene3Di 3.30.40.10. 5 hits.
    InterProi IPR003889. FYrich_C.
    IPR003888. FYrich_N.
    IPR009071. HMG_box_dom.
    IPR003616. Post-SET_dom.
    IPR001214. SET_dom.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF05965. FYRC. 1 hit.
    PF05964. FYRN. 1 hit.
    PF00628. PHD. 3 hits.
    PF00856. SET. 1 hit.
    [Graphical view ]
    SMARTi SM00542. FYRC. 1 hit.
    SM00541. FYRN. 1 hit.
    SM00398. HMG. 1 hit.
    SM00249. PHD. 7 hits.
    SM00508. PostSET. 1 hit.
    SM00184. RING. 6 hits.
    SM00317. SET. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47095. SSF47095. 1 hit.
    SSF57903. SSF57903. 5 hits.
    PROSITEi PS51543. FYRC. 1 hit.
    PS51542. FYRN. 1 hit.
    PS50868. POST_SET. 1 hit.
    PS50280. SET. 1 hit.
    PS01359. ZF_PHD_1. 5 hits.
    PS50016. ZF_PHD_2. 4 hits.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4339-5588.
      Strain: C57BL/6.
      Tissue: Brain.
    3. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4789, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1627, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    5. "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 THE MLL COMPLEX, INTERACTION WITH ASH2L; DPY30; KMT2A; RRBP5 AND WDR5.
    6. "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-3071, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiKMT2D_MOUSE
    AccessioniPrimary (citable) accession number: Q6PDK2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 30, 2010
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 91 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    Human protein KMT2B/MLL4 was first named MLL2 (see AC Q9UMN6). Thus, also mouse Mll4 is often referred to as Mll2 and vice versa in the literature.Curated

    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