Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O14686

- KMT2D_HUMAN

UniProt

O14686 - KMT2D_HUMAN

Protein

Histone-lysine N-methyltransferase 2D

Gene

KMT2D

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (30 Nov 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.3 Publications

    Catalytic activityi

    S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei5451 – 54511S-adenosyl-L-methioninePROSITE-ProRule annotation
    Metal bindingi5477 – 54771ZincBy similarity
    Metal bindingi5525 – 55251ZincBy similarity
    Metal bindingi5527 – 55271ZincBy similarity
    Metal bindingi5532 – 55321ZincBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri226 – 27651PHD-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri229 – 27446RING-type 1; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri273 – 32351PHD-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri276 – 32146RING-type 2; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1377 – 143054PHD-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1427 – 147751PHD-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1504 – 155956PHD-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1507 – 155751RING-type 3; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri5092 – 513746RING-type 4; degeneratePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB
    2. histone-lysine N-methyltransferase activity Source: UniProtKB-EC
    3. protein binding Source: IntAct
    4. transcription regulatory region DNA binding Source: UniProtKB
    5. 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: Ensembl
    4. oocyte growth Source: UniProtKB
    5. oogenesis Source: UniProtKB
    6. positive regulation of cell proliferation Source: UniProtKB
    7. positive regulation of intracellular estrogen receptor signaling pathway Source: UniProtKB
    8. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    9. regulation of transcription, DNA-templated Source: UniProtKB
    10. response to estrogen Source: UniProtKB
    11. 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_200731. deactivation of the beta-catenin transactivating complex.
    REACT_200753. formation of the beta-catenin:TCF 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:ALR, MLL2, MLL4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:7133. KMT2D.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Kabuki syndrome 1 (KABUK1) [MIM:147920]: A congenital mental retardation syndrome with additional features, including postnatal dwarfism, a peculiar facies characterized by long palpebral fissures with eversion of the lateral third of the lower eyelids, a broad and depressed nasal tip, large prominent earlobes, a cleft or high-arched palate, scoliosis, short fifth finger, persistence of fingerpads, radiographic abnormalities of the vertebrae, hands, and hip joints, and recurrent otitis media in infancy.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti5109 – 51091C → F in KABUK1. 1 Publication
    VAR_063830
    Natural varianti5179 – 51791R → H in KABUK1. 1 Publication
    VAR_063831
    Natural varianti5210 – 52101Y → C in KABUK1. 1 Publication
    VAR_064378
    Natural varianti5214 – 52141R → H in KABUK1. 1 Publication
    VAR_063832
    Natural varianti5340 – 53401R → L in KABUK1. 1 Publication
    VAR_063833
    Natural varianti5428 – 54281G → D in KABUK1. 1 Publication
    VAR_064379
    Natural varianti5464 – 54641T → M in KABUK1. 1 Publication
    VAR_063834

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    MIMi147920. phenotype.
    Orphaneti2322. Kabuki syndrome.
    PharmGKBiPA30846.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 55375537Histone-lysine N-methyltransferase 2DPRO_0000124878Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei27 – 271Phosphoserine1 Publication
    Modified residuei1606 – 16061Phosphoserine1 Publication
    Modified residuei1671 – 16711Phosphoserine2 Publications
    Modified residuei2246 – 22461N6-acetyllysine1 Publication
    Modified residuei2274 – 22741Phosphoserine3 Publications
    Modified residuei2309 – 23091Phosphoserine1 Publication
    Modified residuei2311 – 23111Phosphoserine1 Publication
    Modified residuei3079 – 30791N6-acetyllysine1 Publication
    Modified residuei3130 – 31301Phosphoserine1 Publication
    Modified residuei3197 – 31971Phosphothreonine3 Publications
    Modified residuei3199 – 31991Phosphoserine1 Publication
    Modified residuei3433 – 34331N6-acetyllysine1 Publication
    Modified residuei4215 – 42151Phosphoserine1 Publication
    Modified residuei4359 – 43591Phosphoserine2 Publications
    Modified residuei4465 – 44651N6-acetyllysine1 Publication
    Modified residuei4738 – 47381Phosphoserine3 Publications
    Modified residuei4776 – 47761N6-acetyllysine1 Publication
    Modified residuei4822 – 48221Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO14686.
    PaxDbiO14686.
    PRIDEiO14686.

    PTM databases

    PhosphoSiteiO14686.

    Expressioni

    Tissue specificityi

    Expressed in most adult tissues, including a variety of hematoipoietic cells, with the exception of the liver.

    Gene expression databases

    BgeeiO14686.
    CleanExiHS_MLL2.
    GenevestigatoriO14686.

    Organism-specific databases

    HPAiHPA035977.

    Interactioni

    Subunit structurei

    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. Interacts with ESR1; interaction is direct.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ESR1P033723EBI-996065,EBI-78473
    NCOA6Q146866EBI-996065,EBI-78670

    Protein-protein interaction databases

    BioGridi113758. 26 interactions.
    DIPiDIP-37875N.
    IntActiO14686. 16 interactions.
    MINTiMINT-1192941.
    STRINGi9606.ENSP00000301067.

    Structurei

    Secondary structure

    1
    5537
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5339 – 53413

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3UVKX-ray1.40B5337-5347[»]
    4ERQX-ray1.91D/E/F5333-5346[»]
    ProteinModelPortaliO14686.
    SMRiO14686. Positions 220-323, 2000-2077.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati442 – 44651
    Repeati460 – 46452
    Repeati469 – 47353
    Repeati496 – 50054
    Repeati504 – 50855
    Repeati521 – 52556
    Repeati555 – 55957
    Repeati564 – 56858
    Repeati573 – 57759
    Repeati582 – 586510
    Repeati609 – 613511
    Repeati618 – 622512
    Repeati627 – 631513
    Repeati645 – 649514
    Repeati663 – 667515
    Domaini5175 – 523561FYR N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini5236 – 532186FYR C-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini5397 – 5513117SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini5521 – 553717Post-SETPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni439 – 66823015 X 5 AA repeats of S/P-P-P-E/P-E/AAdd
    BLAST
    Regioni5474 – 54752S-adenosyl-L-methionine bindingBy similarity

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili2669 – 270739Sequence AnalysisAdd
    BLAST
    Coiled coili3249 – 328234Sequence AnalysisAdd
    BLAST
    Coiled coili3562 – 361453Sequence AnalysisAdd
    BLAST
    Coiled coili3714 – 375037Sequence AnalysisAdd
    BLAST
    Coiled coili3897 – 397579Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi2686 – 26905LXXLL motif 1
    Motifi3038 – 30425LXXLL motif 2
    Motifi4222 – 423615LXXLL motif 3Add
    BLAST
    Motifi4253 – 42575LXXLL motif 4
    Motifi4463 – 44675LXXLL motif 5
    Motifi4990 – 49945LXXLL motif 6

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi229 – 32698Cys-richAdd
    BLAST
    Compositional biasi374 – 1197824Pro-richAdd
    BLAST
    Compositional biasi1290 – 132839Arg-richAdd
    BLAST
    Compositional biasi1351 – 13555Poly-Glu
    Compositional biasi1397 – 1510114Cys-richAdd
    BLAST
    Compositional biasi2107 – 2626520Pro-richAdd
    BLAST
    Compositional biasi2385 – 23928Poly-Pro
    Compositional biasi2707 – 27137Poly-Ala
    Compositional biasi2811 – 282212Gln-richAdd
    BLAST
    Compositional biasi2862 – 2978117Pro-richAdd
    BLAST
    Compositional biasi3261 – 42751015Gln-richAdd
    BLAST
    Compositional biasi4241 – 4360120Pro-richAdd
    BLAST
    Compositional biasi4909 – 497769Pro-richAdd
    BLAST
    Compositional biasi5494 – 54974Poly-Ile

    Domaini

    LXXLL motifs 5 and 6 are essential for the association with ESR1 nuclear receptor.

    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 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri229 – 27446RING-type 1; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri273 – 32351PHD-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri276 – 32146RING-type 2; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1377 – 143054PHD-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1427 – 147751PHD-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1504 – 155956PHD-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1507 – 155751RING-type 3; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri5092 – 513746RING-type 4; degeneratePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG2940.
    HOVERGENiHBG006738.
    InParanoidiO14686.
    KOiK09187.
    OMAiPTQHSYT.
    OrthoDBiEOG7N63KQ.
    PhylomeDBiO14686.
    TreeFamiTF354317.

    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. 5 hits.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O14686-1) [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

    MDSQKLAGED KDSEPAADGP AASEDPSATE SDLPNPHVGE VSVLSSGSPR     50
    LQETPQDCSG GPVRRCALCN CGEPSLHGQR ELRRFELPFD WPRCPVVSPG 100
    GSPGPNEAVL PSEDLSQIGF PEGLTPAHLG EPGGSCWAHH WCAAWSAGVW 150
    GQEGPELCGV DKAIFSGISQ RCSHCTRLGA SIPCRSPGCP RLYHFPCATA 200
    SGSFLSMKTL QLLCPEHSEG AAYLEEARCA VCEGPGELCD LFFCTSCGHH 250
    YHGACLDTAL TARKRAGWQC PECKVCQACR KPGNDSKMLV CETCDKGYHT 300
    FCLKPPMEEL PAHSWKCKAC RVCRACGAGS AELNPNSEWF ENYSLCHRCH 350
    KAQGGQTIRS VAEQHTPVCS RFSPPEPGDT PTDEPDALYV ACQGQPKGGH 400
    VTSMQPKEPG PLQCEAKPLG KAGVQLEPQL EAPLNEEMPL LPPPEESPLS 450
    PPPEESPTSP PPEASRLSPP PEELPASPLP EALHLSRPLE ESPLSPPPEE 500
    SPLSPPPESS PFSPLEESPL SPPEESPPSP ALETPLSPPP EASPLSPPFE 550
    ESPLSPPPEE LPTSPPPEAS RLSPPPEESP MSPPPEESPM SPPPEASRLF 600
    PPFEESPLSP PPEESPLSPP PEASRLSPPP EDSPMSPPPE ESPMSPPPEV 650
    SRLSPLPVVS RLSPPPEESP LSPPPEESPT SPPPEASRLS PPPEDSPTSP 700
    PPEDSPASPP PEDSLMSLPL EESPLLPLPE EPQLCPRSEG PHLSPRPEEP 750
    HLSPRPEEPH LSPQAEEPHL SPQPEEPCLC AVPEEPHLSP QAEGPHLSPQ 800
    PEELHLSPQT EEPHLSPVPE EPCLSPQPEE SHLSPQSEEP CLSPRPEESH 850
    LSPELEKPPL SPRPEKPPEE PGQCPAPEEL PLFPPPGEPS LSPLLGEPAL 900
    SEPGEPPLSP LPEELPLSPS GEPSLSPQLM PPDPLPPPLS PIITAAAPPA 950
    LSPLGELEYP FGAKGDSDPE SPLAAPILET PISPPPEANC TDPEPVPPMI 1000
    LPPSPGSPVG PASPILMEPL PPQCSPLLQH SLVPQNSPPS QCSPPALPLS 1050
    VPSPLSPIGK VVGVSDEAEL HEMETEKVSE PECPALEPSA TSPLPSPMGD 1100
    LSCPAPSPAP ALDDFSGLGE DTAPLDGIDA PGSQPEPGQT PGSLASELKG 1150
    SPVLLDPEEL APVTPMEVYP ECKQTAGQGS PCEEQEEPRA PVAPTPPTLI 1200
    KSDIVNEISN LSQGDASASF PGSEPLLGSP DPEGGGSLSM ELGVSTDVSP 1250
    ARDEGSLRLC TDSLPETDDS LLCDAGTAIS GGKAEGEKGR RRSSPARSRI 1300
    KQGRSSSFPG RRRPRGGAHG GRGRGRARLK STASSIETLV VADIDSSPSK 1350
    EEEEEDDDTM QNTVVLFSNT DKFVLMQDMC VVCGSFGRGA EGHLLACSQC 1400
    SQCYHPYCVN SKITKVMLLK GWRCVECIVC EVCGQASDPS RLLLCDDCDI 1450
    SYHTYCLDPP LLTVPKGGWK CKWCVSCMQC GAASPGFHCE WQNSYTHCGP 1500
    CASLVTCPIC HAPYVEEDLL IQCRHCERWM HAGCESLFTE DDVEQAADEG 1550
    FDCVSCQPYV VKPVAPVAPP ELVPMKVKEP EPQYFRFEGV WLTETGMALL 1600
    RNLTMSPLHK RRQRRGRLGL PGEAGLEGSE PSDALGPDDK KDGDLDTDEL 1650
    LKGEGGVEHM ECEIKLEGPV SPDVEPGKEE TEESKKRKRK PYRPGIGGFM 1700
    VRQRKSHTRT KKGPAAQAEV LSGDGQPDEV IPADLPAEGA VEQSLAEGDE 1750
    KKKQQRRGRK KSKLEDMFPA YLQEAFFGKE LLDLSRKALF AVGVGRPSFG 1800
    LGTPKAKGDG GSERKELPTS QKGDDGPDIA DEESRGLEGK ADTPGPEDGG 1850
    VKASPVPSDP EKPGTPGEGM LSSDLDRIST EELPKMESKD LQQLFKDVLG 1900
    SEREQHLGCG TPGLEGSRTP LQRPFLQGGL PLGNLPSSSP MDSYPGLCQS 1950
    PFLDSRERGG FFSPEPGEPD SPWTGSGGTT PSTPTTPTTE GEGDGLSYNQ 2000
    RSLQRWEKDE ELGQLSTISP VLYANINFPN LKQDYPDWSS RCKQIMKLWR 2050
    KVPAADKAPY LQKAKDNRAA HRINKVQKQA ESQINKQTKV GDIARKTDRP 2100
    ALHLRIPPQP GALGSPPPAA APTIFIGSPT TPAGLSTSAD GFLKPPAGSV 2150
    PGPDSPGELF LKLPPQVPAQ VPSQDPFGLA PAYPLEPRFP TAPPTYPPYP 2200
    SPTGAPAQPP MLGASSRPGA GQPGEFHTTP PGTPRHQPST PDPFLKPRCP 2250
    SLDNLAVPES PGVGGGKASE PLLSPPPFGE SRKALEVKKE ELGASSPSYG 2300
    PPNLGFVDSP SSGTHLGGLE LKTPDVFKAP LTPRASQVEP QSPGLGLRPQ 2350
    EPPPAQALAP SPPSHPDIFR PGSYTDPYAQ PPLTPRPQPP PPESCCALPP 2400
    RSLPSDPFSR VPASPQSQSS SQSPLTPRPL SAEAFCPSPV TPRFQSPDPY 2450
    SRPPSRPQSR DPFAPLHKPP RPQPPEVAFK AGSLAHTSLG AGGFPAALPA 2500
    GPAGELHAKV PSGQPPNFVR SPGTGAFVGT PSPMRFTFPQ AVGEPSLKPP 2550
    VPQPGLPPPH GINSHFGPGP TLGKPQSTNY TVATGNFHPS GSPLGPSSGS 2600
    TGESYGLSPL RPPSVLPPPA PDGSLPYLSH GASQRSGITS PVEKREDPGT 2650
    GMGSSLATAE LPGTQDPGMS GLSQTELEKQ RQRQRLRELL IRQQIQRNTL 2700
    RQEKETAAAA AGAVGPPGSW GAEPSSPAFE QLSRGQTPFA GTQDKSSLVG 2750
    LPPSKLSGPI LGPGSFPSDD RLSRPPPPAT PSSMDVNSRQ LVGGSQAFYQ 2800
    RAPYPGSLPL QQQQQQLWQQ QQATAATSMR FAMSARFPST PGPELGRQAL 2850
    GSPLAGISTR LPGPGEPVPG PAGPAQFIEL RHNVQKGLGP GGTPFPGQGP 2900
    PQRPRFYPVS EDPHRLAPEG LRGLAVSGLP PQKPSAPPAP ELNNSLHPTP 2950
    HTKGPTLPTG LELVNRPPSS TELGRPNPLA LEAGKLPCED PELDDDFDAH 3000
    KALEDDEELA HLGLGVDVAK GDDELGTLEN LETNDPHLDD LLNGDEFDLL 3050
    AYTDPELDTG DKKDIFNEHL RLVESANEKA EREALLRGVE PGPLGPEERP 3100
    PPAADASEPR LASVLPEVKP KVEEGGRHPS PCQFTIATPK VEPAPAANSL 3150
    GLGLKPGQSM MGSRDTRMGT GPFSSSGHTA EKASFGATGG PPAHLLTPSP 3200
    LSGPGGSSLL EKFELESGAL TLPGGPAASG DELDKMESSL VASELPLLIE 3250
    DLLEHEKKEL QKKQQLSAQL QPAQQQQQQQ QQHSLLSAPG PAQAMSLPHE 3300
    GSSPSLAGSQ QQLSLGLAGA RQPGLPQPLM PTQPPAHALQ QRLAPSMAMV 3350
    SNQGHMLSGQ HGGQAGLVPQ QSSQPVLSQK PMGTMPPSMC MKPQQLAMQQ 3400
    QLANSFFPDT DLDKFAAEDI IDPIAKAKMV ALKGIKKVMA QGSIGVAPGM 3450
    NRQQVSLLAQ RLSGGPSSDL QNHVAAGSGQ ERSAGDPSQP RPNPPTFAQG 3500
    VINEADQRQY EEWLFHTQQL LQMQLKVLEE QIGVHRKSRK ALCAKQRTAK 3550
    KAGREFPEAD AEKLKLVTEQ QSKIQKQLDQ VRKQQKEHTN LMAEYRNKQQ 3600
    QQQQQQQQQQ QQHSAVLALS PSQSPRLLTK LPGQLLPGHG LQPPQGPPGG 3650
    QAGGLRLTPG GMALPGQPGG PFLNTALAQQ QQQQHSGGAG SLAGPSGGFF 3700
    PGNLALRSLG PDSRLLQERQ LQLQQQRMQL AQKLQQQQQQ QQQQQHLLGQ 3750
    VAIQQQQQQG PGVQTNQALG PKPQGLMPPS SHQGLLVQQL SPQPPQGPQG 3800
    MLGPAQVAVL QQQHPGALGP QGPHRQVLMT QSRVLSSPQL AQQGQGLMGH 3850
    RLVTAQQQQQ QQQHQQQGSM AGLSHLQQSL MSHSGQPKLS AQPMGSLQQL 3900
    QQQQQLQQQQ QLQQQQQQQL QQQQQLQQQQ LQQQQQQQQL QQQQQQQLQQ 3950
    QQQQLQQQQQ QQQQQFQQQQ QQQQMGLLNQ SRTLLSPQQQ QQQQVALGPG 4000
    MPAKPLQHFS SPGALGPTLL LTGKEQNTVD PAVSSEATEG PSTHQGGPLA 4050
    IGTTPESMAT EPGEVKPSLS GDSQLLLVQP QPQPQPSSLQ LQPPLRLPGQ 4100
    QQQQVSLLHT AGGGSHGQLG SGSSSEASSV PHLLAQPSVS LGDQPGSMTQ 4150
    NLLGPQQPML ERPMQNNTGP QPPKPGPVLQ SGQGLPGVGI MPTVGQLRAQ 4200
    LQGVLAKNPQ LRHLSPQQQQ QLQALLMQRQ LQQSQAVRQT PPYQEPGTQT 4250
    SPLQGLLGCQ PQLGGFPGPQ TGPLQELGAG PRPQGPPRLP APPGALSTGP 4300
    VLGPVHPTPP PSSPQEPKRP SQLPSPSSQL PTEAQLPPTH PGTPKPQGPT 4350
    LEPPPGRVSP AAAQLADTLF SKGLGPWDPP DNLAETQKPE QSSLVPGHLD 4400
    QVNGQVVPEA SQLSIKQEPR EEPCALGAQS VKREANGEPI GAPGTSNHLL 4450
    LAGPRSEAGH LLLQKLLRAK NVQLSTGRGS EGLRAEINGH IDSKLAGLEQ 4500
    KLQGTPSNKE DAAARKPLTP KPKRVQKASD RLVSSRKKLR KEDGVRASEA 4550
    LLKQLKQELS LLPLTEPAIT ANFSLFAPFG SGCPVNGQSQ LRGAFGSGAL 4600
    PTGPDYYSQL LTKNNLSNPP TPPSSLPPTP PPSVQQKMVN GVTPSEELGE 4650
    HPKDAASARD SERALRDTSE VKSLDLLAAL PTPPHNQTED VRMESDEDSD 4700
    SPDSIVPASS PESILGEEAP RFPHLGSGRW EQEDRALSPV IPLIPRASIP 4750
    VFPDTKPYGA LGLEVPGKLP VTTWEKGKGS EVSVMLTVSA AAAKNLNGVM 4800
    VAVAELLSMK IPNSYEVLFP ESPARAGTEP KKGEAEGPGG KEKGLEGKSP 4850
    DTGPDWLKQF DAVLPGYTLK SQLDILSLLK QESPAPEPPT QHSYTYNVSN 4900
    LDVRQLSAPP PEEPSPPPSP LAPSPASPPT EPLVELPTEP LAEPPVPSPL 4950
    PLASSPESAR PKPRARPPEE GEDSRPPRLK KWKGVRWKRL RLLLTIQKGS 5000
    GRQEDEREVA EFMEQLGTAL RPDKVPRDMR RCCFCHEEGD GATDGPARLL 5050
    NLDLDLWVHL NCALWSTEVY ETQGGALMNV EVALHRGLLT KCSLCQRTGA 5100
    TSSCNRMRCP NVYHFACAIR AKCMFFKDKT MLCPMHKIKG PCEQELSSFA 5150
    VFRRVYIERD EVKQIASIIQ RGERLHMFRV GGLVFHAIGQ LLPHQMADFH 5200
    SATALYPVGY EATRIYWSLR TNNRRCCYRC SIGENNGRPE FVIKVIEQGL 5250
    EDLVFTDASP QAVWNRIIEP VAAMRKEADM LRLFPEYLKG EELFGLTVHA 5300
    VLRIAESLPG VESCQNYLFR YGRHPLMELP LMINPTGCAR SEPKILTHYK 5350
    RPHTLNSTSM SKAYQSTFTG ETNTPYSKQF VHSKSSQYRR LRTEWKNNVY 5400
    LARSRIQGLG LYAAKDLEKH TMVIEYIGTI IRNEVANRRE KIYEEQNRGI 5450
    YMFRINNEHV IDATLTGGPA RYINHSCAPN CVAEVVTFDK EDKIIIISSR 5500
    RIPKGEELTY DYQFDFEDDQ HKIPCHCGAW NCRKWMN 5537
    Length:5,537
    Mass (Da):593,389
    Last modified:November 30, 2010 - v2
    Checksum:i31C6DAB0A754F72A
    GO
    Isoform 3 (identifier: O14686-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1729-1729: E → EGET

    Show »
    Length:5,540
    Mass (Da):593,677
    Checksum:iBB9AC95AA8BC0DD4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51K → N in AAC51734. (PubMed:9247308)Curated
    Sequence conflicti14 – 141E → Q in AAC51734. (PubMed:9247308)Curated
    Sequence conflicti75 – 751S → A in AAC51734. (PubMed:9247308)Curated
    Sequence conflicti156 – 1561E → Q in AAC51734. (PubMed:9247308)Curated
    Sequence conflicti674 – 948275Missing in AAC51734. (PubMed:9247308)CuratedAdd
    BLAST
    Sequence conflicti1178 – 11781Q → R in AAC51734. (PubMed:9247308)Curated
    Sequence conflicti1178 – 11781Q → R in AAC51735. (PubMed:9247308)Curated
    Sequence conflicti1544 – 15474EQAA → DHAP in AAC51734. (PubMed:9247308)Curated
    Sequence conflicti1544 – 15474EQAA → DHAP in AAC51735. (PubMed:9247308)Curated
    Sequence conflicti1761 – 17611K → R in AAC51734. (PubMed:9247308)Curated
    Sequence conflicti1761 – 17611K → R in AAC51735. (PubMed:9247308)Curated
    Sequence conflicti1766 – 17661D → G in AAC51734. (PubMed:9247308)Curated
    Sequence conflicti1766 – 17661D → G in AAC51735. (PubMed:9247308)Curated
    Sequence conflicti2171 – 21711V → A in AAC51734. (PubMed:9247308)Curated
    Sequence conflicti2171 – 21711V → A in AAC51735. (PubMed:9247308)Curated
    Sequence conflicti2413 – 24131A → V in AAC51734. (PubMed:9247308)Curated
    Sequence conflicti2413 – 24131A → V in AAC51735. (PubMed:9247308)Curated
    Sequence conflicti3079 – 30791K → E in AAC51734. (PubMed:9247308)Curated
    Sequence conflicti3079 – 30791K → E in AAC51735. (PubMed:9247308)Curated
    Sequence conflicti3287 – 32871S → P in AAC51734. (PubMed:9247308)Curated
    Sequence conflicti3287 – 32871S → P in AAC51735. (PubMed:9247308)Curated
    Sequence conflicti3319 – 33191G → V in AAC51734. (PubMed:9247308)Curated
    Sequence conflicti3319 – 33191G → V in AAC51735. (PubMed:9247308)Curated
    Sequence conflicti3422 – 34221D → G in AAC51734. (PubMed:9247308)Curated
    Sequence conflicti3422 – 34221D → G in AAC51735. (PubMed:9247308)Curated
    Sequence conflicti4478 – 44781R → Q in AAC51734. (PubMed:9247308)Curated
    Sequence conflicti4478 – 44781R → Q in AAC51735. (PubMed:9247308)Curated
    Sequence conflicti4747 – 47471A → D in AAC51734. (PubMed:9247308)Curated
    Sequence conflicti4747 – 47471A → D in AAC51735. (PubMed:9247308)Curated
    Sequence conflicti4793 – 47931A → D in AAC51734. (PubMed:9247308)Curated
    Sequence conflicti4793 – 47931A → D in AAC51735. (PubMed:9247308)Curated
    Sequence conflicti4826 – 48261A → G in AAC51734. (PubMed:9247308)Curated
    Sequence conflicti4826 – 48261A → G in AAC51735. (PubMed:9247308)Curated
    Sequence conflicti4865 – 48651P → A in AAC51734. (PubMed:9247308)Curated
    Sequence conflicti4865 – 48651P → A in AAC51735. (PubMed:9247308)Curated
    Sequence conflicti4871 – 48711S → R in AAC51734. (PubMed:9247308)Curated
    Sequence conflicti4871 – 48711S → R in AAC51735. (PubMed:9247308)Curated
    Sequence conflicti4893 – 48931S → R in AAC51734. (PubMed:9247308)Curated
    Sequence conflicti4893 – 48931S → R in AAC51735. (PubMed:9247308)Curated
    Sequence conflicti4974 – 49741S → T in AAC51734. (PubMed:9247308)Curated
    Sequence conflicti4974 – 49741S → T in AAC51735. (PubMed:9247308)Curated
    Sequence conflicti5116 – 51161A → G in AAC51734. (PubMed:9247308)Curated
    Sequence conflicti5116 – 51161A → G in AAC51735. (PubMed:9247308)Curated
    Sequence conflicti5522 – 55221K → E in AAC51734. (PubMed:9247308)Curated
    Sequence conflicti5522 – 55221K → E in AAC51735. (PubMed:9247308)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti476 – 4761A → T.
    Corresponds to variant rs1064210 [ dbSNP | Ensembl ].
    VAR_057359
    Natural varianti692 – 6921P → T.1 Publication
    Corresponds to variant rs202076833 [ dbSNP | Ensembl ].
    VAR_064370
    Natural varianti813 – 8131P → L.1 Publication
    Corresponds to variant rs75226229 [ dbSNP | Ensembl ].
    VAR_064371
    Natural varianti2382 – 23821P → S.1 Publication
    Corresponds to variant rs3741626 [ dbSNP | Ensembl ].
    VAR_064372
    Natural varianti2460 – 24601R → C.1 Publication
    VAR_064373
    Natural varianti2557 – 25571P → L.1 Publication
    Corresponds to variant rs189888707 [ dbSNP | Ensembl ].
    VAR_064374
    Natural varianti3398 – 33981M → V.1 Publication
    Corresponds to variant rs75937132 [ dbSNP | Ensembl ].
    VAR_064375
    Natural varianti3419 – 34191D → G.1 Publication
    Corresponds to variant rs146044282 [ dbSNP | Ensembl ].
    VAR_064376
    Natural varianti4357 – 43571R → S.1 Publication
    VAR_064377
    Natural varianti5109 – 51091C → F in KABUK1. 1 Publication
    VAR_063830
    Natural varianti5179 – 51791R → H in KABUK1. 1 Publication
    VAR_063831
    Natural varianti5210 – 52101Y → C in KABUK1. 1 Publication
    VAR_064378
    Natural varianti5214 – 52141R → H in KABUK1. 1 Publication
    VAR_063832
    Natural varianti5224 – 52241R → H.
    Corresponds to variant rs3782356 [ dbSNP | Ensembl ].
    VAR_017115
    Natural varianti5340 – 53401R → L in KABUK1. 1 Publication
    VAR_063833
    Natural varianti5428 – 54281G → D in KABUK1. 1 Publication
    VAR_064379
    Natural varianti5464 – 54641T → M in KABUK1. 1 Publication
    VAR_063834

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1729 – 17291E → EGET in isoform 3. 1 PublicationVSP_008560

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF010403 mRNA. Translation: AAC51734.1.
    AF010404 mRNA. Translation: AAC51735.1.
    AC011603 Genomic DNA. No translation available.
    CCDSiCCDS44873.1. [O14686-1]
    PIRiT03454.
    T03455.
    RefSeqiNP_003473.3. NM_003482.3. [O14686-1]
    XP_005269219.1. XM_005269162.2. [O14686-1]
    XP_006719677.1. XM_006719614.1. [O14686-3]
    UniGeneiHs.731384.

    Genome annotation databases

    EnsembliENST00000301067; ENSP00000301067; ENSG00000167548. [O14686-1]
    GeneIDi8085.
    KEGGihsa:8085.
    UCSCiuc001rta.4. human. [O14686-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF010403 mRNA. Translation: AAC51734.1 .
    AF010404 mRNA. Translation: AAC51735.1 .
    AC011603 Genomic DNA. No translation available.
    CCDSi CCDS44873.1. [O14686-1 ]
    PIRi T03454.
    T03455.
    RefSeqi NP_003473.3. NM_003482.3. [O14686-1 ]
    XP_005269219.1. XM_005269162.2. [O14686-1 ]
    XP_006719677.1. XM_006719614.1. [O14686-3 ]
    UniGenei Hs.731384.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3UVK X-ray 1.40 B 5337-5347 [» ]
    4ERQ X-ray 1.91 D/E/F 5333-5346 [» ]
    ProteinModelPortali O14686.
    SMRi O14686. Positions 220-323, 2000-2077.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113758. 26 interactions.
    DIPi DIP-37875N.
    IntActi O14686. 16 interactions.
    MINTi MINT-1192941.
    STRINGi 9606.ENSP00000301067.

    Chemistry

    ChEMBLi CHEMBL2189114.

    PTM databases

    PhosphoSitei O14686.

    Proteomic databases

    MaxQBi O14686.
    PaxDbi O14686.
    PRIDEi O14686.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000301067 ; ENSP00000301067 ; ENSG00000167548 . [O14686-1 ]
    GeneIDi 8085.
    KEGGi hsa:8085.
    UCSCi uc001rta.4. human. [O14686-1 ]

    Organism-specific databases

    CTDi 8085.
    GeneCardsi GC12M049413.
    GeneReviewsi KMT2D.
    HGNCi HGNC:7133. KMT2D.
    HPAi HPA035977.
    MIMi 147920. phenotype.
    602113. gene.
    neXtProti NX_O14686.
    Orphaneti 2322. Kabuki syndrome.
    PharmGKBi PA30846.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2940.
    HOVERGENi HBG006738.
    InParanoidi O14686.
    KOi K09187.
    OMAi PTQHSYT.
    OrthoDBi EOG7N63KQ.
    PhylomeDBi O14686.
    TreeFami TF354317.

    Enzyme and pathway databases

    Reactomei REACT_200731. deactivation of the beta-catenin transactivating complex.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.

    Miscellaneous databases

    ChiTaRSi MLL2. human.
    GeneWikii MLL2.
    GenomeRNAii 8085.
    NextBioi 30706.
    PROi O14686.
    SOURCEi Search...

    Gene expression databases

    Bgeei O14686.
    CleanExi HS_MLL2.
    Genevestigatori O14686.

    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. 5 hits.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure and expression pattern of human ALR, a novel gene with strong homology to ALL-1 involved in acute leukemia and to Drosophila trithorax."
      Prasad R., Zhadanov A.B., Sedkov Y., Bullrich F., Druck T., Rallapalli R., Yano T., Alder H., Croce C.M., Huebner K., Mazo A., Canaani E.
      Oncogene 15:549-560(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
    2. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins."
      Goo Y.-H., Sohn Y.C., Kim D.-H., Kim S.-W., Kang M.-J., Jung D.-J., Kwak E., Barlev N.A., Berger S.L., Chow V.T., Roeder R.G., Azorsa D.O., Meltzer P.S., Suh P.-G., Song E.J., Lee K.-J., Lee Y.C., Lee J.W.
      Mol. Cell. Biol. 23:140-149(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MLL2/3 COMPLEX.
      Tissue: Cervix carcinoma.
    4. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. "Identification of the MLL2 complex as a coactivator for estrogen receptor alpha."
      Mo R., Rao S.M., Zhu Y.-J.
      J. Biol. Chem. 281:15714-15720(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME ACTIVITY, IDENTIFICATION IN THE MLL2 COMPLEX, LXXLL MOTIFS, INTERACTION WITH ESR1.
    6. "Coactivator as a target gene specificity determinant for histone H3 lysine 4 methyltransferases."
      Lee S., Lee D.K., Dou Y., Lee J., Lee B., Kwak E., Kong Y.Y., Lee S.K., Roeder R.G., Lee J.W.
      Proc. Natl. Acad. Sci. U.S.A. 103:15392-15397(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MLL2/3 (ASCOM) COMPLEX.
    7. "PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex."
      Cho Y.-W., Hong T., Hong S., Guo H., Yu H., Kim D., Guszczynski T., Dressler G.R., Copeland T.D., Kalkum M., Ge K.
      J. Biol. Chem. 282:20395-20406(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MLL2/3 COMPLEX.
    8. Cited for: FUNCTION, IDENTIFICATION IN THE MLL2/3 COMPLEX.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    10. "Demethylation of H3K27 regulates polycomb recruitment and H2A ubiquitination."
      Lee M.G., Villa R., Trojer P., Norman J., Yan K.P., Reinberg D., Di Croce L., Shiekhattar R.
      Science 318:447-450(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MLL2/3 COMPLEX.
    11. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-2274; SER-2309; SER-2311; THR-3197 AND SER-4822, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1671; SER-2274; THR-3197; SER-4359 AND SER-4822, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2246; LYS-3079; LYS-3433; LYS-4465 AND LYS-4776, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1606; THR-3197; SER-3199; SER-4215; SER-4359 AND SER-4738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1671; SER-2274 AND SER-4738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: VARIANTS KABUK1 CYS-5210 AND ASP-5428, VARIANTS THR-692; LEU-813; SER-2382; CYS-2460; LEU-2557; VAL-3398; GLY-3419 AND SER-4357.
    19. Cited for: VARIANTS KABUK1 PHE-5109; HIS-5179; HIS-5214; LEU-5340 AND MET-5464.

    Entry informationi

    Entry nameiKMT2D_HUMAN
    AccessioniPrimary (citable) accession number: O14686
    Secondary accession number(s): O14687
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2003
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 138 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    This gene mapped to a chromosomal region involved in duplications and translocations associated with cancer.

    Caution

    Another protein KMT2B/MLL4, located on chromosome 19, was first named MLL2 (see AC Q9UMN6). Thus, KMT2B/MLL4 is often referred to as MLL2 and vice versa in the literature.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3