Tag | Content |
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CPLM ID | CPLM-017684 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Histone-lysine N-methyltransferase 2C |
Protein Synonyms/Alias | Lysine N-methyltransferase 2C; Homologous to ALR protein; Myeloid/lymphoid or mixed-lineage leukemia protein 3 |
Gene Name | KMT2C |
Gene Synonyms/Alias | HALR; KIAA1506; MLL3 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
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870 | SEGREIFKPRQLPGS | ubiquitination | [1] |
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Reference | [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] |
Functional Description | 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. |
Sequence Annotation | DOMAIN 4545 4605 FYR N-terminal. DOMAIN 4606 4691 FYR C-terminal. DOMAIN 4771 4887 SET. DOMAIN 4895 4911 Post-SET. DNA_BIND 34 46 A.T hook. ZN_FING 341 391 PHD-type 1. ZN_FING 344 389 RING-type. ZN_FING 388 438 PHD-type 2. ZN_FING 436 489 DHHC-type. ZN_FING 464 520 PHD-type 3. ZN_FING 957 1010 PHD-type 4. ZN_FING 1007 1057 PHD-type 5. ZN_FING 1084 1139 PHD-type 6. REGION 4848 4849 S-adenosyl-L-methionine binding (By METAL 4851 4851 Zinc (By similarity). METAL 4899 4899 Zinc (By similarity). METAL 4901 4901 Zinc (By similarity). METAL 4906 4906 Zinc (By similarity). BINDING 4825 4825 S-adenosyl-L-methionine (By similarity). MOD_RES 46 46 Phosphoserine. MOD_RES 89 89 Phosphoserine. MOD_RES 758 758 N6-acetyllysine. MOD_RES 1301 1301 Phosphoserine. MOD_RES 1508 1508 N6-acetyllysine. MOD_RES 1772 1772 N6-acetyllysine. MOD_RES 2009 2009 N6-acetyllysine. MOD_RES 2802 2802 N6-acetyllysine. MOD_RES 2809 2809 N6-acetyllysine. MOD_RES 2832 2832 N6-acetyllysine. MOD_RES 3714 3714 N6-acetyllysine. |
Keyword | 3D-structure; Acetylation; Activator; Alternative splicing; Chromatin regulator; Coiled coil; Complete proteome; DNA-binding; Metal-binding; Methyltransferase; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; S-adenosyl-L-methionine; Transcription; Transcription regulation; Transferase; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 4911 AA |
Protein Sequence | MSSEEDKSVE QPQPPPPPPE EPGAPAPSPA AADKRPRGRP RKDGASPFQR ARKKPRSRGK 60 TAVEDEDSMD GLETTETETI VETEIKEQSA EEDAEAEVDN SKQLIPTLQR SVSEESANSL 120 VSVGVEAKIS EQLCAFCYCG EKSSLGQGDL KQFRITPGFI LPWRNQPSNK KDIDDNSNGT 180 YEKMQNSAPR KQRGQRKERS PQQNIVSCVS VSTQTASDDQ AGKLWDELSL VGLPDAIDIQ 240 ALFDSTGTCW AHHRCVEWSL GVCQMEEPLL VNVDKAVVSG STERCAFCKH LGATIKCCEE 300 KCTQMYHYPC AAGAGTFQDF SHIFLLCPEH IDQAPERSKE DANCAVCDSP GDLLDQFFCT 360 TCGQHYHGMC LDIAVTPLKR AGWQCPECKV CQNCKQSGED SKMLVCDTCD KGYHTFCLQP 420 VMKSVPTNGW KCKNCRICIE CGTRSSSQWH HNCLICDNCY QQQDNLCPFC GKCYHPELQK 480 DMLHCNMCKR WVHLECDKPT DHELDTQLKE EYICMYCKHL GAEMDRLQPG EEVEIAELTT 540 DYNNEMEVEG PEDQMVFSEQ AANKDVNGQE STPGIVPDAV QVHTEEQQKS HPSESLDTDS 600 LLIAVSSQHT VNTELEKQIS NEVDSEDLKM SSEVKHICGE DQIEDKMEVT ENIEVVTHQI 660 TVQQEQLQLL EEPETVVSRE ESRPPKLVME SVTLPLETLV SPHEESISLC PEEQLVIERL 720 QGEKEQKENS ELSTGLMDSE MTPTIEGCVK DVSYQGGKSI KLSSETESSF SSSADISKAD 780 VSSSPTPSSD LPSHDMLHNY PSALSSSAGN IMPTTYISVT PKIGMGKPAI TKRKFSPGRP 840 RSKQGAWSTH NTVSPPSWSP DISEGREIFK PRQLPGSAIW SIKVGRGSGF PGKRRPRGAG 900 LSGRGGRGRS KLKSGIGAVV LPGVSTADIS SNKDDEENSM HNTVVLFSSS DKFTLNQDMC 960 VVCGSFGQGA EGRLLACSQC GQCYHPYCVS IKITKVVLSK GWRCLECTVC EACGKATDPG 1020 RLLLCDDCDI SYHTYCLDPP LQTVPKGGWK CKWCVWCRHC GATSAGLRCE WQNNYTQCAP 1080 CASLSSCPVC YRNYREEDLI LQCRQCDRWM HAVCQNLNTE EEVENVADIG FDCSMCRPYM 1140 PASNVPSSDC CESSLVAQIV TKVKELDPPK TYTQDGVCLT ESGMTQLQSL TVTVPRRKRS 1200 KPKLKLKIIN QNSVAVLQTP PDIQSEHSRD GEMDDSREGE LMDCDGKSES SPEREAVDDE 1260 TKGVEGTDGV KKRKRKPYRP GIGGFMVRQR SRTGQGKTKR SVIRKDSSGS ISEQLPCRDD 1320 GWSEQLPDTL VDESVSVTES TEKIKKRYRK RKNKLEETFP AYLQEAFFGK DLLDTSRQSK 1380 ISLDNLSEDG AQLLYKTNMN TGFLDPSLDP LLSSSSAPTK SGTHGPADDP LADISEVLNT 1440 DDDILGIISD DLAKSVDHSD IGPVTDDPSS LPQPNVNQSS RPLSEEQLDG ILSPELDKMV 1500 TDGAILGKLY KIPELGGKDV EDLFTAVLSP ANTQPTPLPQ PPPPTQLLPI HNQDAFSRMP 1560 LMNGLIGSSP HLPHNSLPPG SGLGTFSAIA QSSYPDARDK NSAFNPMASD PNNSWTSSAP 1620 TVEGENDTMS NAQRSTLKWE KEEALGEMAT VAPVLYTNIN FPNLKEEFPD WTTRVKQIAK 1680 LWRKASSQER APYVQKARDN RAALRINKVQ MSNDSMKRQQ QQDSIDPSSR IDSELFKDPL 1740 KQRESEHEQE WKFRQQMRQK SKQQAKIEAT QKLEQVKNEQ QQQQQQQFGS QHLLVQSGSD 1800 TPSSGIQSPL TPQPGNGNMS PAQSFHKELF TKQPPSTPTS TSSDDVFVKP QAPPPPPAPS 1860 RIPIQDSLSQ AQTSQPPSPQ VFSPGSSNSR PPSPMDPYAK MVGTPRPPPV GHSFSRRNSA 1920 APVENCTPLS SVSRPLQMNE TTANRPSPVR DLCSSSTTNN DPYAKPPDTP RPVMTDQFPK 1980 SLGLSRSPVV SEQTAKGPIA AGTSDHFTKP SPRADVFQRQ RIPDSYARPL LTPAPLDSGP 2040 GPFKTPMQPP PSSQDPYGSV SQASRRLSVD PYERPALTPR PIDNFSHNQS NDPYSQPPLT 2100 PHPAVNESFA HPSRAFSQPG TISRPTSQDP YSQPPGTPRP VVDSYSQSSG TARSNTDPYS 2160 QPPGTPRPTT VDPYSQQPQT PRPSTQTDLF VTPVTNQRHS DPYAHPPGTP RPGISVPYSQ 2220 PPATPRPRIS EGFTRSSMTR PVLMPNQDPF LQAAQNRGPA LPGPLVRPPD TCSQTPRPPG 2280 PGLSDTFSRV SPSAARDPYD QSPMTPRSQS DSFGTSQTAH DVADQPRPGS EGSFCASSNS 2340 PMHSQGQQFS GVSQLPGPVP TSGVTDTQNT VNMAQADTEK LRQRQKLREI ILQQQQQKKI 2400 AGRQEKGSQD SPAVPHPGPL QHWQPENVNQ AFTRPPPPYP GNIRSPVAPP LGPRYAVFPK 2460 DQRGPYPPDV ASMGMRPHGF RFGFPGGSHG TMPSQERFLV PPQQIQGSGV SPQLRRSVSV 2520 DMPRPLNNSQ MNNPVGLPQH FSPQSLPVQQ HNILGQAYIE LRHRAPDGRQ RLPFSAPPGS 2580 VVEASSNLRH GNFIPRPDFP GPRHTDPMRR PPQGLPNQLP VHPDLEQVPP SQQEQGHSVH 2640 SSSMVMRTLN HPLGGEFSEA PLSTSVPSET TSDNLQITTQ PSDGLEEKLD SDDPSVKELD 2700 VKDLEGVEVK DLDDEDLENL NLDTEDGKVV ELDTLDNLET NDPNLDDLLR SGEFDIIAYT 2760 DPELDMGDKK SMFNEELDLP IDDKLDNQCV SVEPKKKEQE NKTLVLSDKH SPQKKSTVTN 2820 EVKTEVLSPN SKVESKCETE KNDENKDNVD TPCSQASAHS DLNDGEKTSL HPCDPDLFEK 2880 RTNRETAGPS ANVIQASTQL PAQDVINSCG ITGSTPVLSS LLANEKSDNS DIRPSGSPPP 2940 PTLPASPSNH VSSLPPFIAP PGRVLDNAMN SNVTVVSRVN HVFSQGVQVN PGLIPGQSTV 3000 NHSLGTGKPA TQTGPQTSQS GTSSMSGPQQ LMIPQTLAQQ NRERPLLLEE QPLLLQDLLD 3060 QERQEQQQQR QMQAMIRQRS EPFFPNIDFD AITDPIMKAK MVALKGINKV MAQNNLGMPP 3120 MVMSRFPFMG QVVTGTQNSE GQNLGPQAIP QDGSITHQIS RPNPPNFGPG FVNDSQRKQY 3180 EEWLQETQQL LQMQQKYLEE QIGAHRKSKK ALSAKQRTAK KAGREFPEED AEQLKHVTEQ 3240 QSMVQKQLEQ IRKQQKEHAE LIEDYRIKQQ QQCAMAPPTM MPSVQPQPPL IPGATPPTMS 3300 QPTFPMVPQQ LQHQQHTTVI SGHTSPVRMP SLPGWQPNSA PAHLPLNPPR IQPPIAQLPI 3360 KTCTPAPGTV SNANPQSGPP PRVEFDDNNP FSESFQERER KERLREQQER QRIQLMQEVD 3420 RQRALQQRME MEQHGMVGSE ISSSRTSVSQ IPFYSSDLPC DFMQPLGPLQ QSPQHQQQMG 3480 QVLQQQNIQQ GSINSPSTQT FMQTNERRQV GPPSFVPDSP SIPVGSPNFS SVKQGHGNLS 3540 GTSFQQSPVR PSFTPALPAA PPVANSSLPC GQDSTITHGH SYPGSTQSLI QLYSDIIPEE 3600 KGKKKRTRKK KRDDDAESTK APSTPHSDIT APPTPGISET TSTPAVSTPS ELPQQADQES 3660 VEPVGPSTPN MAAGQLCTEL ENKLPNSDFS QATPNQQTYA NSEVDKLSME TPAKTEEIKL 3720 EKAETESCPG QEEPKLEEQN GSKVEGNAVA CPVSSAQSPP HSAGAPAAKG DSGNELLKHL 3780 LKNKKSSSLL NQKPEGSICS EDDCTKDNKL VEKQNPAEGL QTLGAQMQGG FGCGNQLPKT 3840 DGGSETKKQR SKRTQRTGEK AAPRSKKRKK DEEEKQAMYS STDTFTHLKQ VRQLSLLPLM 3900 EPIIGVNFAH FLPYGSGQFN SGNRLLGTFG SATLEGVSDY YSQLIYKQNN LSNPPTPPAS 3960 LPPTPPPMAC QKMANGFATT EELAGKAGVL VSHEVTKTLG PKPFQLPFRP QDDLLARALA 4020 QGPKTVDVPA SLPTPPHNNQ EELRIQDHCG DRDTPDSFVP SSSPESVVGV EVSRYPDLSL 4080 VKEEPPEPVP SPIIPILPST AGKSSESRRN DIKTEPGTLY FASPFGPSPN GPRSGLISVA 4140 ITLHPTAAEN ISSVVAAFSD LLHVRIPNSY EVSSAPDVPS MGLVSSHRIN PGLEYRQHLL 4200 LRGPPPGSAN PPRLVSSYRL KQPNVPFPPT SNGLSGYKDS SHGIAESAAL RPQWCCHCKV 4260 VILGSGVRKS FKDLTLLNKD SRESTKRVEK DIVFCSNNCF ILYSSTAQAK NSENKESIPS 4320 LPQSPMRETP SKAFHQYSNN ISTLDVHCLP QLPEKASPPA SPPIAFPPAF EAAQVEAKPD 4380 ELKVTVKLKP RLRAVHGGFE DCRPLNKKWR GMKWKKWSIH IVIPKGTFKP PCEDEIDEFL 4440 KKLGTSLKPD PVPKDYRKCC FCHEEGDGLT DGPARLLNLD LDLWVHLNCA LWSTEVYETQ 4500 AGALINVELA LRRGLQMKCV FCHKTGATSG CHRFRCTNIY HFTCAIKAQC MFFKDKTMLC 4560 PMHKPKGIHE QELSYFAVFR RVYVQRDEVR QIASIVQRGE RDHTFRVGSL IFHTIGQLLP 4620 QQMQAFHSPK ALFPVGYEAS RLYWSTRYAN RRCRYLCSIE EKDGRPVFVI RIVEQGHEDL 4680 VLSDISPKGV WDKILEPVAC VRKKSEMLQL FPAYLKGEDL FGLTVSAVAR IAESLPGVEA 4740 CENYTFRYGR NPLMELPLAV NPTGCARSEP KMSAHVKRFV LRPHTLNSTS TSKSFQSTVT 4800 GELNAPYSKQ FVHSKSSQYR KMKTEWKSNV YLARSRIQGL GLYAARDIEK HTMVIEYIGT 4860 IIRNEVANRK EKLYESQNRG VYMFRMDNDH VIDATLTGGP ARYINHSCAP NCVAEVVTFE 4920 RGHKIIISSS RRIQKGEELC YDYKFDFEDD QHKIPCHCGA VNCRKWMN 4968 |
Gene Ontology | GO:0035097; C:histone methyltransferase complex; IDA:MGI. GO:0003677; F:DNA binding; IEA:UniProtKB-KW. GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IDA:MGI. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0035556; P:intracellular signal transduction; IEA:InterPro. GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW. GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. |
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PRINTS | |