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Q8NEZ4

- KMT2C_HUMAN

UniProt

Q8NEZ4 - KMT2C_HUMAN

Protein

Histone-lysine N-methyltransferase 2C

Gene

KMT2C

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 3 (20 Jan 2009)
      Previous versions | rss
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    Functioni

    Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Central component of the MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation. KMT2C/MLL3 may be a catalytic subunit of this complex. May be involved in leukemogenesis and developmental disorder.1 Publication

    Catalytic activityi

    S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei4825 – 48251S-adenosyl-L-methioninePROSITE-ProRule annotation
    Metal bindingi4851 – 48511ZincBy similarity
    Metal bindingi4899 – 48991ZincBy similarity
    Metal bindingi4901 – 49011ZincBy similarity
    Metal bindingi4906 – 49061ZincBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi34 – 4613A.T hookAdd
    BLAST
    Zinc fingeri341 – 39151PHD-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri344 – 38946RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri388 – 43851PHD-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri436 – 48954DHHC-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri464 – 52057PHD-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri957 – 101054PHD-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1007 – 105751PHD-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1084 – 113956PHD-type 6PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. histone methyltransferase activity (H3-K4 specific) Source: MGI
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: IntAct
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. histone H3-K4 methylation Source: GOC
    2. intracellular signal transduction Source: InterPro
    3. regulation of transcription, DNA-templated Source: UniProtKB-KW
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, 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 2C (EC:2.1.1.43)
    Short name:
    Lysine N-methyltransferase 2C
    Alternative name(s):
    Homologous to ALR protein
    Myeloid/lymphoid or mixed-lineage leukemia protein 3
    Gene namesi
    Name:KMT2C
    Synonyms:HALR, KIAA1506, MLL3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:13726. KMT2C.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30847.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 49114911Histone-lysine N-methyltransferase 2CPRO_0000124879Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei46 – 461Phosphoserine1 Publication
    Modified residuei89 – 891Phosphoserine1 Publication
    Modified residuei758 – 7581N6-acetyllysine1 Publication
    Modified residuei1301 – 13011Phosphoserine1 Publication
    Modified residuei1508 – 15081N6-acetyllysine1 Publication
    Modified residuei1772 – 17721N6-acetyllysine1 Publication
    Modified residuei2009 – 20091N6-acetyllysine1 Publication
    Modified residuei2802 – 28021N6-acetyllysine1 Publication
    Modified residuei2809 – 28091N6-acetyllysine1 Publication
    Modified residuei2832 – 28321N6-acetyllysine1 Publication
    Modified residuei2867 – 28671N6-acetyllysineBy similarity
    Modified residuei3714 – 37141N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8NEZ4.
    PaxDbiQ8NEZ4.
    PRIDEiQ8NEZ4.

    PTM databases

    PhosphoSiteiQ8NEZ4.

    Expressioni

    Tissue specificityi

    Highly expressed in testis and ovary, followed by brain and liver. Also expressed in placenta, peripherical blood, fetal thymus, heart, lung and kidney. Within brain, expression was highest in hippocampus, caudate nucleus, and substantia nigra. Not detected in skeletal muscle and fetal liver.

    Gene expression databases

    ArrayExpressiQ8NEZ4.
    BgeeiQ8NEZ4.
    CleanExiHS_MLL3.
    GenevestigatoriQ8NEZ4.

    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 histone H3.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NCOA6Q146865EBI-1042997,EBI-78670

    Protein-protein interaction databases

    BioGridi121835. 20 interactions.
    DIPiDIP-48649N.
    IntActiQ8NEZ4. 10 interactions.
    MINTiMINT-3042700.
    STRINGi9606.ENSP00000262189.

    Structurei

    Secondary structure

    1
    4911
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni345 – 3473
    Turni353 – 3553
    Beta strandi356 – 3583
    Beta strandi360 – 3623
    Turni368 – 3725
    Turni377 – 3793
    Turni386 – 3883
    Turni392 – 3943
    Beta strandi403 – 4053
    Beta strandi407 – 4093
    Beta strandi412 – 4143
    Helixi415 – 4173
    Beta strandi418 – 4203
    Helixi433 – 4364
    Helixi1636 – 164510
    Helixi1646 – 16483
    Beta strandi1650 – 16523
    Helixi1653 – 16608
    Helixi1664 – 16674
    Helixi1671 – 168414
    Helixi1687 – 170620
    Beta strandi4707 – 47093

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YSMNMR-A342-439[»]
    2YUKNMR-A1631-1713[»]
    3UVLX-ray2.20B4707-4717[»]
    4ERYX-ray1.30D4703-4716[»]
    ProteinModelPortaliQ8NEZ4.
    SMRiQ8NEZ4. Positions 245-331, 342-439, 482-518, 960-1057, 1086-1138, 1624-1713, 4399-4507, 4761-4911.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8NEZ4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4545 – 460561FYR N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini4606 – 469186FYR C-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini4771 – 4887117SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini4895 – 491117Post-SETPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni4848 – 48492S-adenosyl-L-methionine bindingBy similarity

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili92 – 11221Sequence AnalysisAdd
    BLAST
    Coiled coili644 – 67229Sequence AnalysisAdd
    BLAST
    Coiled coili1338 – 136629Sequence AnalysisAdd
    BLAST
    Coiled coili1754 – 178734Sequence AnalysisAdd
    BLAST
    Coiled coili3054 – 308128Sequence AnalysisAdd
    BLAST
    Coiled coili3173 – 3272100Sequence AnalysisAdd
    BLAST
    Coiled coili3391 – 343343Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1719 – 179678Gln-richAdd
    BLAST
    Compositional biasi1834 – 2281448Pro-richAdd
    BLAST
    Compositional biasi2412 – 2630219Pro-richAdd
    BLAST
    Compositional biasi2690 – 278697Asp-richAdd
    BLAST
    Compositional biasi3012 – 3509498Gln-richAdd
    BLAST
    Compositional biasi3277 – 3381105Pro-richAdd
    BLAST

    Domaini

    The SET domain interacts with histone H3 but not H2A, H2B and H4, and may have a H3 lysine specific methylation activity.

    Sequence similaritiesi

    Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. TRX/MLL subfamily.PROSITE-ProRule annotation
    Contains 1 A.T hook DNA-binding domain.Curated
    Contains 1 DHHC-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 6 PHD-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 post-SET domain.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
    Contains 1 SET domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri341 – 39151PHD-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri344 – 38946RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri388 – 43851PHD-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri436 – 48954DHHC-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri464 – 52057PHD-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri957 – 101054PHD-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1007 – 105751PHD-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1084 – 113956PHD-type 6PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG2940.
    HOVERGENiHBG045586.
    InParanoidiQ8NEZ4.
    KOiK09188.
    OMAiMPSLPGW.
    PhylomeDBiQ8NEZ4.
    TreeFamiTF354317.

    Family and domain databases

    Gene3Di3.30.40.10. 6 hits.
    InterProiIPR017956. AT_hook_DNA-bd_motif.
    IPR003889. FYrich_C.
    IPR003888. FYrich_N.
    IPR009071. HMG_box_dom.
    IPR000637. HMGI/Y_DNA-bd_CS.
    IPR003616. Post-SET_dom.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR001214. SET_dom.
    IPR001594. Znf_DHHC_palmitoyltrfase.
    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. 2 hits.
    PF00856. SET. 1 hit.
    [Graphical view]
    SMARTiSM00384. AT_hook. 2 hits.
    SM00109. C1. 2 hits.
    SM00542. FYRC. 1 hit.
    SM00541. FYRN. 1 hit.
    SM00398. HMG. 1 hit.
    SM00249. PHD. 8 hits.
    SM00508. PostSET. 1 hit.
    SM00184. RING. 4 hits.
    SM00317. SET. 1 hit.
    [Graphical view]
    SUPFAMiSSF47095. SSF47095. 1 hit.
    SSF57903. SSF57903. 6 hits.
    PROSITEiPS51543. FYRC. 1 hit.
    PS51542. FYRN. 1 hit.
    PS00354. HMGI_Y. 1 hit.
    PS50868. POST_SET. 1 hit.
    PS50280. SET. 1 hit.
    PS50216. ZF_DHHC. 1 hit.
    PS01359. ZF_PHD_1. 5 hits.
    PS50016. ZF_PHD_2. 6 hits.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8NEZ4-1) [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

    MSSEEDKSVE QPQPPPPPPE EPGAPAPSPA AADKRPRGRP RKDGASPFQR     50
    ARKKPRSRGK TAVEDEDSMD GLETTETETI VETEIKEQSA EEDAEAEVDN 100
    SKQLIPTLQR SVSEESANSL VSVGVEAKIS EQLCAFCYCG EKSSLGQGDL 150
    KQFRITPGFI LPWRNQPSNK KDIDDNSNGT YEKMQNSAPR KQRGQRKERS 200
    PQQNIVSCVS VSTQTASDDQ AGKLWDELSL VGLPDAIDIQ ALFDSTGTCW 250
    AHHRCVEWSL GVCQMEEPLL VNVDKAVVSG STERCAFCKH LGATIKCCEE 300
    KCTQMYHYPC AAGAGTFQDF SHIFLLCPEH IDQAPERSKE DANCAVCDSP 350
    GDLLDQFFCT TCGQHYHGMC LDIAVTPLKR AGWQCPECKV CQNCKQSGED 400
    SKMLVCDTCD KGYHTFCLQP VMKSVPTNGW KCKNCRICIE CGTRSSSQWH 450
    HNCLICDNCY QQQDNLCPFC GKCYHPELQK DMLHCNMCKR WVHLECDKPT 500
    DHELDTQLKE EYICMYCKHL GAEMDRLQPG EEVEIAELTT DYNNEMEVEG 550
    PEDQMVFSEQ AANKDVNGQE STPGIVPDAV QVHTEEQQKS HPSESLDTDS 600
    LLIAVSSQHT VNTELEKQIS NEVDSEDLKM SSEVKHICGE DQIEDKMEVT 650
    ENIEVVTHQI TVQQEQLQLL EEPETVVSRE ESRPPKLVME SVTLPLETLV 700
    SPHEESISLC PEEQLVIERL QGEKEQKENS ELSTGLMDSE MTPTIEGCVK 750
    DVSYQGGKSI KLSSETESSF SSSADISKAD VSSSPTPSSD LPSHDMLHNY 800
    PSALSSSAGN IMPTTYISVT PKIGMGKPAI TKRKFSPGRP RSKQGAWSTH 850
    NTVSPPSWSP DISEGREIFK PRQLPGSAIW SIKVGRGSGF PGKRRPRGAG 900
    LSGRGGRGRS KLKSGIGAVV LPGVSTADIS SNKDDEENSM HNTVVLFSSS 950
    DKFTLNQDMC VVCGSFGQGA EGRLLACSQC GQCYHPYCVS IKITKVVLSK 1000
    GWRCLECTVC EACGKATDPG RLLLCDDCDI SYHTYCLDPP LQTVPKGGWK 1050
    CKWCVWCRHC GATSAGLRCE WQNNYTQCAP CASLSSCPVC YRNYREEDLI 1100
    LQCRQCDRWM HAVCQNLNTE EEVENVADIG FDCSMCRPYM PASNVPSSDC 1150
    CESSLVAQIV TKVKELDPPK TYTQDGVCLT ESGMTQLQSL TVTVPRRKRS 1200
    KPKLKLKIIN QNSVAVLQTP PDIQSEHSRD GEMDDSREGE LMDCDGKSES 1250
    SPEREAVDDE TKGVEGTDGV KKRKRKPYRP GIGGFMVRQR SRTGQGKTKR 1300
    SVIRKDSSGS ISEQLPCRDD GWSEQLPDTL VDESVSVTES TEKIKKRYRK 1350
    RKNKLEETFP AYLQEAFFGK DLLDTSRQSK ISLDNLSEDG AQLLYKTNMN 1400
    TGFLDPSLDP LLSSSSAPTK SGTHGPADDP LADISEVLNT DDDILGIISD 1450
    DLAKSVDHSD IGPVTDDPSS LPQPNVNQSS RPLSEEQLDG ILSPELDKMV 1500
    TDGAILGKLY KIPELGGKDV EDLFTAVLSP ANTQPTPLPQ PPPPTQLLPI 1550
    HNQDAFSRMP LMNGLIGSSP HLPHNSLPPG SGLGTFSAIA QSSYPDARDK 1600
    NSAFNPMASD PNNSWTSSAP TVEGENDTMS NAQRSTLKWE KEEALGEMAT 1650
    VAPVLYTNIN FPNLKEEFPD WTTRVKQIAK LWRKASSQER APYVQKARDN 1700
    RAALRINKVQ MSNDSMKRQQ QQDSIDPSSR IDSELFKDPL KQRESEHEQE 1750
    WKFRQQMRQK SKQQAKIEAT QKLEQVKNEQ QQQQQQQFGS QHLLVQSGSD 1800
    TPSSGIQSPL TPQPGNGNMS PAQSFHKELF TKQPPSTPTS TSSDDVFVKP 1850
    QAPPPPPAPS RIPIQDSLSQ AQTSQPPSPQ VFSPGSSNSR PPSPMDPYAK 1900
    MVGTPRPPPV GHSFSRRNSA APVENCTPLS SVSRPLQMNE TTANRPSPVR 1950
    DLCSSSTTNN DPYAKPPDTP RPVMTDQFPK SLGLSRSPVV SEQTAKGPIA 2000
    AGTSDHFTKP SPRADVFQRQ RIPDSYARPL LTPAPLDSGP GPFKTPMQPP 2050
    PSSQDPYGSV SQASRRLSVD PYERPALTPR PIDNFSHNQS NDPYSQPPLT 2100
    PHPAVNESFA HPSRAFSQPG TISRPTSQDP YSQPPGTPRP VVDSYSQSSG 2150
    TARSNTDPYS QPPGTPRPTT VDPYSQQPQT PRPSTQTDLF VTPVTNQRHS 2200
    DPYAHPPGTP RPGISVPYSQ PPATPRPRIS EGFTRSSMTR PVLMPNQDPF 2250
    LQAAQNRGPA LPGPLVRPPD TCSQTPRPPG PGLSDTFSRV SPSAARDPYD 2300
    QSPMTPRSQS DSFGTSQTAH DVADQPRPGS EGSFCASSNS PMHSQGQQFS 2350
    GVSQLPGPVP TSGVTDTQNT VNMAQADTEK LRQRQKLREI ILQQQQQKKI 2400
    AGRQEKGSQD SPAVPHPGPL QHWQPENVNQ AFTRPPPPYP GNIRSPVAPP 2450
    LGPRYAVFPK DQRGPYPPDV ASMGMRPHGF RFGFPGGSHG TMPSQERFLV 2500
    PPQQIQGSGV SPQLRRSVSV DMPRPLNNSQ MNNPVGLPQH FSPQSLPVQQ 2550
    HNILGQAYIE LRHRAPDGRQ RLPFSAPPGS VVEASSNLRH GNFIPRPDFP 2600
    GPRHTDPMRR PPQGLPNQLP VHPDLEQVPP SQQEQGHSVH SSSMVMRTLN 2650
    HPLGGEFSEA PLSTSVPSET TSDNLQITTQ PSDGLEEKLD SDDPSVKELD 2700
    VKDLEGVEVK DLDDEDLENL NLDTEDGKVV ELDTLDNLET NDPNLDDLLR 2750
    SGEFDIIAYT DPELDMGDKK SMFNEELDLP IDDKLDNQCV SVEPKKKEQE 2800
    NKTLVLSDKH SPQKKSTVTN EVKTEVLSPN SKVESKCETE KNDENKDNVD 2850
    TPCSQASAHS DLNDGEKTSL HPCDPDLFEK RTNRETAGPS ANVIQASTQL 2900
    PAQDVINSCG ITGSTPVLSS LLANEKSDNS DIRPSGSPPP PTLPASPSNH 2950
    VSSLPPFIAP PGRVLDNAMN SNVTVVSRVN HVFSQGVQVN PGLIPGQSTV 3000
    NHSLGTGKPA TQTGPQTSQS GTSSMSGPQQ LMIPQTLAQQ NRERPLLLEE 3050
    QPLLLQDLLD QERQEQQQQR QMQAMIRQRS EPFFPNIDFD AITDPIMKAK 3100
    MVALKGINKV MAQNNLGMPP MVMSRFPFMG QVVTGTQNSE GQNLGPQAIP 3150
    QDGSITHQIS RPNPPNFGPG FVNDSQRKQY EEWLQETQQL LQMQQKYLEE 3200
    QIGAHRKSKK ALSAKQRTAK KAGREFPEED AEQLKHVTEQ QSMVQKQLEQ 3250
    IRKQQKEHAE LIEDYRIKQQ QQCAMAPPTM MPSVQPQPPL IPGATPPTMS 3300
    QPTFPMVPQQ LQHQQHTTVI SGHTSPVRMP SLPGWQPNSA PAHLPLNPPR 3350
    IQPPIAQLPI KTCTPAPGTV SNANPQSGPP PRVEFDDNNP FSESFQERER 3400
    KERLREQQER QRIQLMQEVD RQRALQQRME MEQHGMVGSE ISSSRTSVSQ 3450
    IPFYSSDLPC DFMQPLGPLQ QSPQHQQQMG QVLQQQNIQQ GSINSPSTQT 3500
    FMQTNERRQV GPPSFVPDSP SIPVGSPNFS SVKQGHGNLS GTSFQQSPVR 3550
    PSFTPALPAA PPVANSSLPC GQDSTITHGH SYPGSTQSLI QLYSDIIPEE 3600
    KGKKKRTRKK KRDDDAESTK APSTPHSDIT APPTPGISET TSTPAVSTPS 3650
    ELPQQADQES VEPVGPSTPN MAAGQLCTEL ENKLPNSDFS QATPNQQTYA 3700
    NSEVDKLSME TPAKTEEIKL EKAETESCPG QEEPKLEEQN GSKVEGNAVA 3750
    CPVSSAQSPP HSAGAPAAKG DSGNELLKHL LKNKKSSSLL NQKPEGSICS 3800
    EDDCTKDNKL VEKQNPAEGL QTLGAQMQGG FGCGNQLPKT DGGSETKKQR 3850
    SKRTQRTGEK AAPRSKKRKK DEEEKQAMYS STDTFTHLKQ QNNLSNPPTP 3900
    PASLPPTPPP MACQKMANGF ATTEELAGKA GVLVSHEVTK TLGPKPFQLP 3950
    FRPQDDLLAR ALAQGPKTVD VPASLPTPPH NNQEELRIQD HCGDRDTPDS 4000
    FVPSSSPESV VGVEVSRYPD LSLVKEEPPE PVPSPIIPIL PSTAGKSSES 4050
    RRNDIKTEPG TLYFASPFGP SPNGPRSGLI SVAITLHPTA AENISSVVAA 4100
    FSDLLHVRIP NSYEVSSAPD VPSMGLVSSH RINPGLEYRQ HLLLRGPPPG 4150
    SANPPRLVSS YRLKQPNVPF PPTSNGLSGY KDSSHGIAES AALRPQWCCH 4200
    CKVVILGSGV RKSFKDLTLL NKDSRESTKR VEKDIVFCSN NCFILYSSTA 4250
    QAKNSENKES IPSLPQSPMR ETPSKAFHQY SNNISTLDVH CLPQLPEKAS 4300
    PPASPPIAFP PAFEAAQVEA KPDELKVTVK LKPRLRAVHG GFEDCRPLNK 4350
    KWRGMKWKKW SIHIVIPKGT FKPPCEDEID EFLKKLGTSL KPDPVPKDYR 4400
    KCCFCHEEGD GLTDGPARLL NLDLDLWVHL NCALWSTEVY ETQAGALINV 4450
    ELALRRGLQM KCVFCHKTGA TSGCHRFRCT NIYHFTCAIK AQCMFFKDKT 4500
    MLCPMHKPKG IHEQELSYFA VFRRVYVQRD EVRQIASIVQ RGERDHTFRV 4550
    GSLIFHTIGQ LLPQQMQAFH SPKALFPVGY EASRLYWSTR YANRRCRYLC 4600
    SIEEKDGRPV FVIRIVEQGH EDLVLSDISP KGVWDKILEP VACVRKKSEM 4650
    LQLFPAYLKG EDLFGLTVSA VARIAESLPG VEACENYTFR YGRNPLMELP 4700
    LAVNPTGCAR SEPKMSAHVK RFVLRPHTLN STSTSKSFQS TVTGELNAPY 4750
    SKQFVHSKSS QYRKMKTEWK SNVYLARSRI QGLGLYAARD IEKHTMVIEY 4800
    IGTIIRNEVA NRKEKLYESQ NRGVYMFRMD NDHVIDATLT GGPARYINHS 4850
    CAPNCVAEVV TFERGHKIII SSSRRIQKGE ELCYDYKFDF EDDQHKIPCH 4900
    CGAVNCRKWM N 4911
    Length:4,911
    Mass (Da):541,370
    Last modified:January 20, 2009 - v3
    Checksum:i898CEE324772BD75
    GO
    Isoform 2 (identifier: Q8NEZ4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-939: Missing.
         3890-3890: Q → QVRQLSLLPLMEPIIGVNFAHFLPYGSGQFNSGNRLLGTFGSATLEGVSDYYSQLIYK
         4721-4724: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:4,025
    Mass (Da):443,538
    Checksum:i41624149C28E4BDE
    GO
    Isoform 3 (identifier: Q8NEZ4-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         3890-3890: Q → QVRQLSLLPLMEPIIGVNFAHFLPYGSGQFNSGNRLLGTFGSATLEGVSDYYSQLIYK

    Note: No experimental confirmation available.

    Show »
    Length:4,968
    Mass (Da):547,633
    Checksum:i7D6E36D9FA78714B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti579 – 5791A → T in AAK00583. (PubMed:11891048)Curated
    Sequence conflicti1286 – 12861M → V in AAK00583. (PubMed:11891048)Curated
    Sequence conflicti2360 – 23601P → S in AAK00583. (PubMed:11891048)Curated
    Sequence conflicti2797 – 27971K → R in AAK00583. (PubMed:11891048)Curated
    Sequence conflicti2882 – 28821T → A in AAK00583. (PubMed:11891048)Curated
    Sequence conflicti3289 – 32891P → S in BAC11409. (PubMed:14702039)Curated
    Sequence conflicti3428 – 34281R → W in BAC11409. (PubMed:14702039)Curated
    Sequence conflicti4613 – 46131I → V in AK022687. (PubMed:14702039)Curated
    Sequence conflicti4866 – 48661H → P in AK022687. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti291 – 2911L → F.
    Corresponds to variant rs56850341 [ dbSNP | Ensembl ].
    VAR_061911
    Natural varianti316 – 3161T → S.
    Corresponds to variant rs10454320 [ dbSNP | Ensembl ].
    VAR_061912
    Natural varianti347 – 3471C → G in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036311
    Natural varianti400 – 4001D → N in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036312
    Natural varianti478 – 4781L → W in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036313
    Natural varianti526 – 5261R → P.1 Publication
    Corresponds to variant rs3735156 [ dbSNP | Ensembl ].
    VAR_057360
    Natural varianti823 – 8231I → N.
    Corresponds to variant rs2838171 [ dbSNP | Ensembl ].
    VAR_017118
    Natural varianti823 – 8231I → T.
    Corresponds to variant rs2838171 [ dbSNP | Ensembl ].
    VAR_017117
    Natural varianti1836 – 18361S → N.
    Corresponds to variant rs11771635 [ dbSNP | Ensembl ].
    VAR_057361
    Natural varianti2008 – 20081T → A.
    Corresponds to variant rs6951159 [ dbSNP | Ensembl ].
    VAR_057362
    Natural varianti2412 – 24121P → T.
    Corresponds to variant rs13231116 [ dbSNP | Ensembl ].
    VAR_057363
    Natural varianti2600 – 26001P → A.
    Corresponds to variant rs2270234 [ dbSNP | Ensembl ].
    VAR_057364
    Natural varianti3698 – 36981T → S in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036314

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 939939Missing in isoform 2. 1 PublicationVSP_008561Add
    BLAST
    Alternative sequencei3890 – 38901Q → QVRQLSLLPLMEPIIGVNFA HFLPYGSGQFNSGNRLLGTF GSATLEGVSDYYSQLIYK in isoform 2 and isoform 3. 1 PublicationVSP_008562
    Alternative sequencei4721 – 47244Missing in isoform 2. 1 PublicationVSP_036223

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY024361 mRNA. Translation: AAK00583.1.
    AF264750 mRNA. Translation: AAF74766.2.
    AC006017 Genomic DNA. Translation: AAD45822.1.
    AC104692 Genomic DNA. No translation available.
    AC005631 Genomic DNA. No translation available.
    AB040939 mRNA. Translation: BAA96030.2.
    AK022687 mRNA. No translation available.
    AK075113 mRNA. Translation: BAC11409.1.
    AL833924 mRNA. Translation: CAD38780.1.
    CCDSiCCDS5931.1. [Q8NEZ4-1]
    RefSeqiNP_733751.2. NM_170606.2. [Q8NEZ4-1]
    UniGeneiHs.647120.

    Genome annotation databases

    EnsembliENST00000262189; ENSP00000262189; ENSG00000055609. [Q8NEZ4-1]
    ENST00000355193; ENSP00000347325; ENSG00000055609. [Q8NEZ4-3]
    GeneIDi58508.
    KEGGihsa:58508.
    UCSCiuc003wkz.3. human. [Q8NEZ4-2]
    uc003wla.3. human. [Q8NEZ4-1]

    Polymorphism databases

    DMDMi221222521.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY024361 mRNA. Translation: AAK00583.1 .
    AF264750 mRNA. Translation: AAF74766.2 .
    AC006017 Genomic DNA. Translation: AAD45822.1 .
    AC104692 Genomic DNA. No translation available.
    AC005631 Genomic DNA. No translation available.
    AB040939 mRNA. Translation: BAA96030.2 .
    AK022687 mRNA. No translation available.
    AK075113 mRNA. Translation: BAC11409.1 .
    AL833924 mRNA. Translation: CAD38780.1 .
    CCDSi CCDS5931.1. [Q8NEZ4-1 ]
    RefSeqi NP_733751.2. NM_170606.2. [Q8NEZ4-1 ]
    UniGenei Hs.647120.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YSM NMR - A 342-439 [» ]
    2YUK NMR - A 1631-1713 [» ]
    3UVL X-ray 2.20 B 4707-4717 [» ]
    4ERY X-ray 1.30 D 4703-4716 [» ]
    ProteinModelPortali Q8NEZ4.
    SMRi Q8NEZ4. Positions 245-331, 342-439, 482-518, 960-1057, 1086-1138, 1624-1713, 4399-4507, 4761-4911.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121835. 20 interactions.
    DIPi DIP-48649N.
    IntActi Q8NEZ4. 10 interactions.
    MINTi MINT-3042700.
    STRINGi 9606.ENSP00000262189.

    Chemistry

    ChEMBLi CHEMBL2189113.

    PTM databases

    PhosphoSitei Q8NEZ4.

    Polymorphism databases

    DMDMi 221222521.

    Proteomic databases

    MaxQBi Q8NEZ4.
    PaxDbi Q8NEZ4.
    PRIDEi Q8NEZ4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262189 ; ENSP00000262189 ; ENSG00000055609 . [Q8NEZ4-1 ]
    ENST00000355193 ; ENSP00000347325 ; ENSG00000055609 . [Q8NEZ4-3 ]
    GeneIDi 58508.
    KEGGi hsa:58508.
    UCSCi uc003wkz.3. human. [Q8NEZ4-2 ]
    uc003wla.3. human. [Q8NEZ4-1 ]

    Organism-specific databases

    CTDi 58508.
    GeneCardsi GC07M151835.
    H-InvDB HIX0007238.
    HIX0016202.
    HIX0080234.
    HGNCi HGNC:13726. KMT2C.
    MIMi 606833. gene.
    neXtProti NX_Q8NEZ4.
    PharmGKBi PA30847.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2940.
    HOVERGENi HBG045586.
    InParanoidi Q8NEZ4.
    KOi K09188.
    OMAi MPSLPGW.
    PhylomeDBi Q8NEZ4.
    TreeFami TF354317.

    Miscellaneous databases

    ChiTaRSi MLL3. human.
    EvolutionaryTracei Q8NEZ4.
    GeneWikii MLL3.
    GenomeRNAii 58508.
    NextBioi 65023.
    PROi Q8NEZ4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8NEZ4.
    Bgeei Q8NEZ4.
    CleanExi HS_MLL3.
    Genevestigatori Q8NEZ4.

    Family and domain databases

    Gene3Di 3.30.40.10. 6 hits.
    InterProi IPR017956. AT_hook_DNA-bd_motif.
    IPR003889. FYrich_C.
    IPR003888. FYrich_N.
    IPR009071. HMG_box_dom.
    IPR000637. HMGI/Y_DNA-bd_CS.
    IPR003616. Post-SET_dom.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR001214. SET_dom.
    IPR001594. Znf_DHHC_palmitoyltrfase.
    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. 2 hits.
    PF00856. SET. 1 hit.
    [Graphical view ]
    SMARTi SM00384. AT_hook. 2 hits.
    SM00109. C1. 2 hits.
    SM00542. FYRC. 1 hit.
    SM00541. FYRN. 1 hit.
    SM00398. HMG. 1 hit.
    SM00249. PHD. 8 hits.
    SM00508. PostSET. 1 hit.
    SM00184. RING. 4 hits.
    SM00317. SET. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47095. SSF47095. 1 hit.
    SSF57903. SSF57903. 6 hits.
    PROSITEi PS51543. FYRC. 1 hit.
    PS51542. FYRN. 1 hit.
    PS00354. HMGI_Y. 1 hit.
    PS50868. POST_SET. 1 hit.
    PS50280. SET. 1 hit.
    PS50216. ZF_DHHC. 1 hit.
    PS01359. ZF_PHD_1. 5 hits.
    PS50016. ZF_PHD_2. 6 hits.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "MLL3, a new human member of the TRX/MLL gene family, maps to 7q36, a chromosome region frequently deleted in myeloid leukaemia."
      Ruault M., Brun M.-E., Ventura M., Roizes G., De Sario A.
      Gene 284:73-81(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PRO-526.
      Tissue: Fetal thymus.
    2. "Novel human HALR (MLL3) gene encodes a protein homologous to ALR and to ALL-1 involved in leukemia, and maps to chromosome 7q36 associated with leukemia and developmental defects."
      Tan Y.C., Chow V.T.
      Cancer Detect. Prev. 25:454-469(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Cervix carcinoma.
    3. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 556-3865 (ISOFORM 1).
      Tissue: Brain.
    5. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3193-3865 AND 4460-4911.
      Tissue: Placenta.
    7. Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Testis.
    8. "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: INTERACTION WITH MLL2/3 COMPLEX (ISOFORM 2).
      Tissue: Cervix carcinoma.
    9. "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.
    10. "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.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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-758; LYS-1508; LYS-1772; LYS-2009; LYS-2802; LYS-2809; LYS-2832 AND LYS-3714, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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-89 AND SER-1301, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Solution structure of the first and second PHD domain from myeloid/lymphoid or mixed-lineage leukemia protein 3 homolog."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 342-439.
    16. "Solution structure of the HMG box of human myeloid/lymphoid or mixed-lineage leukemia protein 3 homolog."
      RIKEN structural genomics initiative (RSGI)
      Submitted (APR-2008) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1624-1713.
    17. Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLY-347; ASN-400; TRP-478 AND SER-3698.

    Entry informationi

    Entry nameiKMT2C_HUMAN
    AccessioniPrimary (citable) accession number: Q8NEZ4
    Secondary accession number(s): Q8NC02
    , Q8NDF6, Q9H9P4, Q9NR13, Q9P222, Q9UDR7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2003
    Last sequence update: January 20, 2009
    Last modified: October 1, 2014
    This is version 131 of the entry and version 3 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

    Found in a critical region of chromosome 7, which is commonly deleted in malignant myeloid disorders. Partial duplication of the KMT2C gene are found in the juxtacentromeric region of chromosomes 1, 2, 13 and 21. Juxtacentromeric reshuffling of the KMT2C gene has generated the BAGE genes.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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