CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017683
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
758DVSYQGGKSIKLSSEacetylation[1]
827TPKIGMGKPAITKRKacetylation[1]
870SEGREIFKPRQLPGSubiquitination[2]
1508TDGAILGKLYKIPELacetylation[1]
1766QKSKQQAKIEATQKLacetylation[3]
1772AKIEATQKLEQVKNEacetylation[1, 3]
2009GTSDHFTKPSPRADVacetylation[1, 3, 4, 5]
2795QCVSVEPKKKEQENKacetylation[6]
2802KKKEQENKTLVLSDKacetylation[1]
2809KTLVLSDKHSPQKKSacetylation[1, 7]
2814SDKHSPQKKSTVTNEacetylation[1]
2832EVLSPNSKVESKCETacetylation[1]
3714LSMETPAKTEEIKLEacetylation[1]
3945VTKTLGPKPFQLPFRacetylation[1]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] 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]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [6] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [7] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647
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 QNNLSNPPTP 3900
PASLPPTPPP MACQKMANGF ATTEELAGKA GVLVSHEVTK TLGPKPFQLP FRPQDDLLAR 3960
ALAQGPKTVD VPASLPTPPH NNQEELRIQD HCGDRDTPDS FVPSSSPESV VGVEVSRYPD 4020
LSLVKEEPPE PVPSPIIPIL PSTAGKSSES RRNDIKTEPG TLYFASPFGP SPNGPRSGLI 4080
SVAITLHPTA AENISSVVAA FSDLLHVRIP NSYEVSSAPD VPSMGLVSSH RINPGLEYRQ 4140
HLLLRGPPPG SANPPRLVSS YRLKQPNVPF PPTSNGLSGY KDSSHGIAES AALRPQWCCH 4200
CKVVILGSGV RKSFKDLTLL NKDSRESTKR VEKDIVFCSN NCFILYSSTA QAKNSENKES 4260
IPSLPQSPMR ETPSKAFHQY SNNISTLDVH CLPQLPEKAS PPASPPIAFP PAFEAAQVEA 4320
KPDELKVTVK LKPRLRAVHG GFEDCRPLNK KWRGMKWKKW SIHIVIPKGT FKPPCEDEID 4380
EFLKKLGTSL KPDPVPKDYR KCCFCHEEGD GLTDGPARLL NLDLDLWVHL NCALWSTEVY 4440
ETQAGALINV ELALRRGLQM KCVFCHKTGA TSGCHRFRCT NIYHFTCAIK AQCMFFKDKT 4500
MLCPMHKPKG IHEQELSYFA VFRRVYVQRD EVRQIASIVQ RGERDHTFRV GSLIFHTIGQ 4560
LLPQQMQAFH SPKALFPVGY EASRLYWSTR YANRRCRYLC SIEEKDGRPV FVIRIVEQGH 4620
EDLVLSDISP KGVWDKILEP VACVRKKSEM LQLFPAYLKG EDLFGLTVSA VARIAESLPG 4680
VEACENYTFR YGRNPLMELP LAVNPTGCAR SEPKMSAHVK RFVLRPHTLN STSTSKSFQS 4740
TVTGELNAPY SKQFVHSKSS QYRKMKTEWK SNVYLARSRI QGLGLYAARD IEKHTMVIEY 4800
IGTIIRNEVA NRKEKLYESQ NRGVYMFRMD NDHVIDATLT GGPARYINHS CAPNCVAEVV 4860
TFERGHKIII SSSRRIQKGE ELCYDYKFDF EDDQHKIPCH CGAVNCRKWM N 4911 
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. 
Interpro
 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. 
Pfam
 PF05965; FYRC
 PF05964; FYRN
 PF00628; PHD
 PF00856; SET 
SMART
 SM00384; AT_hook
 SM00109; C1
 SM00542; FYRC
 SM00541; FYRN
 SM00398; HMG
 SM00249; PHD
 SM00508; PostSET
 SM00184; RING
 SM00317; SET 
PROSITE
 PS51543; FYRC
 PS51542; FYRN
 PS00354; HMGI_Y
 PS50868; POST_SET
 PS50280; SET
 PS50216; ZF_DHHC
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2
 PS50089; ZF_RING_2 
PRINTS