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Protein

Histone-lysine N-methyltransferase 2C

Gene

Kmt2c

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei4817S-adenosyl-L-methioninePROSITE-ProRule annotation1
Metal bindingi4843ZincBy similarity1
Metal bindingi4891ZincBy similarity1
Metal bindingi4893ZincBy similarity1
Metal bindingi4898ZincBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi34 – 46A.T hookAdd BLAST13
Zinc fingeri226 – 261C2HC pre-PHD-type 1; degeneratePROSITE-ProRule annotationAdd BLAST36
Zinc fingeri282 – 330PHD-type 1PROSITE-ProRule annotationAdd BLAST49
Zinc fingeri340 – 390PHD-type 2PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri343 – 388RING-typePROSITE-ProRule annotationAdd BLAST46
Zinc fingeri387 – 437PHD-type 3PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri463 – 519PHD-type 4PROSITE-ProRule annotationAdd BLAST57
Zinc fingeri950 – 1003PHD-type 5PROSITE-ProRule annotationAdd BLAST54
Zinc fingeri1000 – 1050PHD-type 6PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri1077 – 1132PHD-type 7PROSITE-ProRule annotationAdd BLAST56
Zinc fingeri4391 – 4431C2HC pre-PHD-type 2PROSITE-ProRule annotationAdd BLAST41
Zinc fingeri4452 – 4499PHD-type 8PROSITE-ProRule annotationAdd BLAST48

GO - Molecular functioni

GO - Biological processi

  • eyelid development in camera-type eye Source: MGI
  • histone methylation Source: UniProtKB
  • multicellular organism growth Source: MGI
  • positive regulation of fibroblast proliferation Source: MGI
  • regulation of gene expression Source: MGI
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • single fertilization Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Chromatin regulator, Methyltransferase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiR-MMU-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.

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):
Myeloid/lymphoid or mixed-lineage leukemia protein 3 homolog
Gene namesi
Name:Kmt2c
Synonyms:Mll3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:2444959. Kmt2c.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001248801 – 4903Histone-lysine N-methyltransferase 2CAdd BLAST4903

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei28PhosphoserineBy similarity1
Modified residuei46PhosphoserineBy similarity1
Modified residuei89PhosphoserineBy similarity1
Modified residuei113PhosphoserineBy similarity1
Modified residuei751N6-acetyllysineBy similarity1
Modified residuei847PhosphoserineBy similarity1
Modified residuei1294PhosphoserineBy similarity1
Modified residuei1497N6-acetyllysineBy similarity1
Modified residuei1761N6-acetyllysineCombined sources1
Modified residuei1983PhosphoserineBy similarity1
Modified residuei2005N6-acetyllysineCombined sources1
Modified residuei2447Asymmetric dimethylarginineCombined sources1
Modified residuei2563Asymmetric dimethylarginineCombined sources1
Modified residuei2796N6-acetyllysineCombined sources1
Modified residuei2803N6-acetyllysineBy similarity1
Modified residuei2822PhosphoserineBy similarity1
Modified residuei2824PhosphotyrosineCombined sources1
Modified residuei2826N6-acetyllysineBy similarity1
Modified residuei2862N6-acetyllysineCombined sources1
Modified residuei3709N6-acetyllysineBy similarity1
Modified residuei4027PhosphoserineBy similarity1
Modified residuei4132Asymmetric dimethylarginineCombined sources1
Modified residuei4260PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiQ8BRH4.
PRIDEiQ8BRH4.

PTM databases

iPTMnetiQ8BRH4.
PhosphoSitePlusiQ8BRH4.

Expressioni

Tissue specificityi

In adult, detected in testis, kidney, spleen and lung, weakly expressed in brain and absent in heart and liver. First detected throughout the embryo at 8 dpc when expression is strong in forebrain neuroepithelium and absent in heart. Expressed in the eye lens between 10 and 14.5 dpc. By 13 dpc, expressed strongly in spinal cord, hand/foot plates and gonads.1 Publication

Gene expression databases

BgeeiENSMUSG00000038056.
CleanExiMM_MLL3.

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.By similarity

Protein-protein interaction databases

DIPiDIP-61282N.
IntActiQ8BRH4. 6 interactors.
STRINGi10090.ENSMUSP00000043874.

Structurei

3D structure databases

ProteinModelPortaliQ8BRH4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini435 – 488DHHCPROSITE-ProRule annotationAdd BLAST54
Domaini4537 – 4597FYR N-terminalPROSITE-ProRule annotationAdd BLAST61
Domaini4598 – 4683FYR C-terminalPROSITE-ProRule annotationAdd BLAST86
Domaini4763 – 4879SETPROSITE-ProRule annotationAdd BLAST117
Domaini4887 – 4903Post-SETPROSITE-ProRule annotationAdd BLAST17

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni4840 – 4841S-adenosyl-L-methionine bindingBy similarity2

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1330 – 1352Sequence analysisAdd BLAST23
Coiled coili1743 – 1790Sequence analysisAdd BLAST48
Coiled coili3047 – 3074Sequence analysisAdd BLAST28
Coiled coili3166 – 3193Sequence analysisAdd BLAST28
Coiled coili3224 – 3270Sequence analysisAdd BLAST47
Coiled coili3387 – 3432Sequence analysisAdd BLAST46

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi384 – 487Cys-richAdd BLAST104
Compositional biasi970 – 1099Cys-richAdd BLAST130
Compositional biasi1519 – 1568Pro-richAdd BLAST50
Compositional biasi1708 – 1787Gln-richAdd BLAST80
Compositional biasi1831 – 2622Pro-richAdd BLAST792
Compositional biasi2682 – 2780Asp-richAdd BLAST99
Compositional biasi3022 – 3504Gln-richAdd BLAST483

Domaini

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

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. TRX/MLL subfamily.PROSITE-ProRule annotation
Contains 1 A.T hook DNA-binding domain.Curated
Contains 2 C2HC pre-PHD-type zinc fingers.PROSITE-ProRule annotation
Contains 1 DHHC domain.PROSITE-ProRule annotation
Contains 1 FYR C-terminal domain.PROSITE-ProRule annotation
Contains 1 FYR N-terminal domain.PROSITE-ProRule annotation
Contains 8 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)DescriptionActionsGraphical viewLength
Zinc fingeri226 – 261C2HC pre-PHD-type 1; degeneratePROSITE-ProRule annotationAdd BLAST36
Zinc fingeri282 – 330PHD-type 1PROSITE-ProRule annotationAdd BLAST49
Zinc fingeri340 – 390PHD-type 2PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri343 – 388RING-typePROSITE-ProRule annotationAdd BLAST46
Zinc fingeri387 – 437PHD-type 3PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri463 – 519PHD-type 4PROSITE-ProRule annotationAdd BLAST57
Zinc fingeri950 – 1003PHD-type 5PROSITE-ProRule annotationAdd BLAST54
Zinc fingeri1000 – 1050PHD-type 6PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri1077 – 1132PHD-type 7PROSITE-ProRule annotationAdd BLAST56
Zinc fingeri4391 – 4431C2HC pre-PHD-type 2PROSITE-ProRule annotationAdd BLAST41
Zinc fingeri4452 – 4499PHD-type 8PROSITE-ProRule annotationAdd BLAST48

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG4443. Eukaryota.
COG2940. LUCA.
HOGENOMiHOG000113602.
HOVERGENiHBG045586.
InParanoidiQ8BRH4.
PhylomeDBiQ8BRH4.

Family and domain databases

Gene3Di3.30.40.10. 6 hits.
InterProiIPR003889. FYrich_C.
IPR003888. FYrich_N.
IPR009071. HMG_box_dom.
IPR000637. HMGI/Y_DNA-bd_CS.
IPR003616. Post-SET_dom.
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]
SMARTiSM00542. 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.
PROSITEiPS50216. DHHC. 1 hit.
PS51805. EPHD. 2 hits.
PS51543. FYRC. 1 hit.
PS51542. FYRN. 1 hit.
PS00354. HMGI_Y. 1 hit.
PS50868. POST_SET. 1 hit.
PS50280. SET. 1 hit.
PS01359. ZF_PHD_1. 5 hits.
PS50016. ZF_PHD_2. 6 hits.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8BRH4-1) [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

        10         20         30         40         50
MSSEEDRSAE QQQPPPAPPE EPGAPAPSPA AADKRPRGRP RKDGASPFQR
60 70 80 90 100
ARKKPRSRGK STVEDEDSMD GLETTETENI VETEIKEQSV EEDAETEVDS
110 120 130 140 150
SKQPVSALQR SVSEESANSL VSVGVEAKIS EQLCAFCYCG EKSSLGQGDL
160 170 180 190 200
KQFRVTPGLT LPWKDQPSNK DIDDNSSGTC EKIQNYAPRK QRGQRKERPP
210 220 230 240 250
QQSAVSCVSV STQTACEDQA GKLWDELSLV GLPDAIDVQA LFDSTGTCWA
260 270 280 290 300
HHRCVEWSLG ICQMEEPLLV NVDKAVVSGS TERCAFCKHL GATIKCCEEK
310 320 330 340 350
CTQMYHYPCA AGAGTFQDFS HFFLLCPEHI DQAPERSKED ANCAVCDSPG
360 370 380 390 400
DLLDQFFCTT CGQHYHGMCL DIAVTPLKRA GWQCPECKVC QNCKQSGEDS
410 420 430 440 450
KMLVCDTCDK GYHTFCLQPV MKSVPTNGWK CKNCRICIEC GTRSSTQWHH
460 470 480 490 500
NCLICDTCYQ QQDNLCPFCG KCYHPELQKD MLHCNMCKRW VHLECDKPTD
510 520 530 540 550
QELDSQLKED YICMYCKHLG AEIDPLHPGN EVEMPELPTD YASGMEIEGT
560 570 580 590 600
EDEVVFLEQT VNKDVSDHQC RPGIVPDVQV YTEEPQKSNP LESPDTVGLI
610 620 630 640 650
TSESSDNKMN PDLANEIAHE VDTEKTEMLS KGRHVCEEDQ NEDRMEVTEN
660 670 680 690 700
IEVLPHQTIV PQEDLLLSED SEVASKELSP PKSAPETAAP EALLSPHSER
710 720 730 740 750
SLSCKEPLLT ERVQEEMEQK ENSEFSTGCV DFEMTLAVDS CDKDSSCQGD
760 770 780 790 800
KYVELPAEEE STFSSATDLN KADVSSSSTL CSDLPSCDML HGYPPAFNSA
810 820 830 840 850
AGSIMPTTYI SVTPKIGMGK PAITKRKFSP GRPRSKQGAW SNHNTVSPPS
860 870 880 890 900
WAPDTSEGRE IFKPRQLSGS AIWSIKVGRG SGFPGKRRPR GAGLSGRGGR
910 920 930 940 950
GRSKLKSGIG AVVLPGVSAA DISSNKDEEE NSMHNTVVLF SSSDKFTLQQ
960 970 980 990 1000
DMCVVCGSFG QGAEGRLLAC SQCGQCYHPY CVSIKITKVV LSKGWRCLEC
1010 1020 1030 1040 1050
TVCEACGKAT DPGRLLLCDD CDISYHTYCL DPPLQTVPKG GWKCKWCVWC
1060 1070 1080 1090 1100
RHCGATSAGL RCEWQNNYTQ CAPCASLSSC PVCCRNYREE DLILQCRQCD
1110 1120 1130 1140 1150
RWMHAVCQNL NTEEEVENVA DIGFDCSMCR PYMPVSNVPS SDCCDSSLVA
1160 1170 1180 1190 1200
QIVTKVKELD PPKTYTQDGV CLTESGMSQL QSLTVTAPRR KRTKPKLKLK
1210 1220 1230 1240 1250
IINQNSVAVL QTPPDIQSEH SRDGEMDDSR EGELMDCDGK SESSPEREAG
1260 1270 1280 1290 1300
DDETKGIEGT DAIKKRKRKP YRPGIGGFMV RQRSRTGQGK AKRSVVRKDS
1310 1320 1330 1340 1350
SGSISEQLPS RDDGWREQLP DTLVDEPVSV AENTDKIKKR YRKRKNKLEE
1360 1370 1380 1390 1400
TFPAYLQEAF FGKDLLDTSR QNKLSVDNLS EDAAQLSFKT GFLDPSSDPL
1410 1420 1430 1440 1450
LSSSSTSAKP GTQGTADDPL ADISEVLNTD DDILGIISDD LAKSVDHSDI
1460 1470 1480 1490 1500
GPTTADASSL PQPGVSQSSR PLTEEQLDGI LSPELDKMVT DGAILGKLYK
1510 1520 1530 1540 1550
IPELGGKDVE DLFTAVLSPA TTQPAPLPQP PPPPQLLPMH NQDVFSRMPL
1560 1570 1580 1590 1600
MNGLIGPSPH LPHNSLPPGS GLGTFPAIAQ SPYTDVRDKS PAFNAIASDP
1610 1620 1630 1640 1650
NSSWAPTTPS MEGENDTLSN AQRSTLKWEK EEALGEMATV APVLYTNINF
1660 1670 1680 1690 1700
PNLKEEFPDW TTRVKQIAKL WRKASSQERA PYVQKARDNR AALRINKVQM
1710 1720 1730 1740 1750
SNDSMKRQQQ QDSIDPSSRI DSDLFKDPLK QRESEHEQEW KFRQQMRQKS
1760 1770 1780 1790 1800
KQQAKIEATQ KLEQVKNEQQ QQQQQQQQQQ QQQLASQHLL VAPGSDTPSS
1810 1820 1830 1840 1850
GAQSPLTPQA GNGNVSPAQT FHKDLFSKHL PGTPASTPSD GVFVKPQPPP
1860 1870 1880 1890 1900
PPSTPSRIPV QESLSQSQNS QPPSPQMFSP GSSHSRPPSP VDPYAKMVGT
1910 1920 1930 1940 1950
PRPPPGGHSF PRRNSVTPVE NCVPLSSVPR PIHMNETSAT RPSPARDLCA
1960 1970 1980 1990 2000
SSMTNSDPYA KPPDTPRPMM TDQFSKPFSL PRSPVISEQS TKGPLTTGTS
2010 2020 2030 2040 2050
DHFTKPSPRT DAFQRQRLPD PYAGPSLTPA PLGNGPFKTP LHPPPSQDPY
2060 2070 2080 2090 2100
GSVSQTSRRL SVDPYERPAL TPRPVDNFSH SQSNDPYSHP PLTPHPAMTE
2110 2120 2130 2140 2150
SFTHASRAFP QPGTISRSAS QDPYSQPPGT PRPLIDSYSQ TSGTARSNPD
2160 2170 2180 2190 2200
PYSQPPGTPR PNTIDPYSQQ PPTPRPSPQT DMFVSSVANQ RHTDPYTHHL
2210 2220 2230 2240 2250
GPPRPGISVP YSQPPAVPRP RTSEGFTRPS SARPALMPNQ DPFLQAAQNR
2260 2270 2280 2290 2300
VPGLPGPLIR PPDTCSQTPR PPGPGRIDTF THASSSAVRD PYDQPPVTPR
2310 2320 2330 2340 2350
PHSESFGTSQ VVHDLVDRPV PGSEGNFSTS SNLPVSSQGQ QFSSVSQLPG
2360 2370 2380 2390 2400
PVPTSGGTDT QNTVNMSQAD TEKLRQRQKL REIILQQQQQ KKIASRQEKG
2410 2420 2430 2440 2450
PQDTAVVPHP VPLPHWQPES INQAFTRPPP PYPGSTRSPV IPPLGPRYAV
2460 2470 2480 2490 2500
FPKDQRGPYP PEVAGMGMRP HGFRFGFPGA GHGPMPSQDR FHVPQQIQGS
2510 2520 2530 2540 2550
GIPPHIRRPM SMEMPRPSNN PPLNNPVGLP QHFPPQGLPV QQHNILGQAF
2560 2570 2580 2590 2600
IELRHRAPDG RSRLPFAASP SSVIESPSHP RHGNFLPRPD FPGPRHTDPI
2610 2620 2630 2640 2650
RQPSQCLSNQ LPVHPNLEQV PPSQQEQGHP AHQSSIVMRP LNHPLSGEFS
2660 2670 2680 2690 2700
EAPLSTSTPA ETSPDNLEIA GQSSAGLEEK LDSDDPSVKE LDVKDLEGVE
2710 2720 2730 2740 2750
VKDLDDEDLE NLNLDTEDGK GDDLDTLDNL ETNDPNLDDL LRSGEFDIIA
2760 2770 2780 2790 2800
YTDPELDLGD KKSMFNEELD LNVPIDDKLD NQCASVEPKT RDQGDKTMVL
2810 2820 2830 2840 2850
EDKDLPQRKS SVSSEIKTEA LSPYSKEEIQ SEIKNHDDSR GDADTACSQA
2860 2870 2880 2890 2900
ASAQTNHSDR GKTALLTTDQ DMLEKRCNQE NAGPVVSAIQ GSTPLPARDV
2910 2920 2930 2940 2950
MNSCDITGST PVLSSLLSNE KCDDSDIRPS GSSPPSLPIS PSTHGSSLPP
2960 2970 2980 2990 3000
TLIVPPSPLL DNTVNSNVTV VPRINHAFSQ GVPVNPGFIQ GQSSVNHNLG
3010 3020 3030 3040 3050
TGKPTNQTVP LTNQSSTMSG PQQLMIPQTL AQQNRERPLL LEEQPLLLQD
3060 3070 3080 3090 3100
LLDQERQEQQ QQRQMQAMIR QRSEPFFPNI DFDAITDPIM KAKMVALKGI
3110 3120 3130 3140 3150
NKVMAQNSLG MPPMVMSRFP FMGPSVAGTQ NNDGQTLVPQ AVAQDGSITH
3160 3170 3180 3190 3200
QISRPNPPNF GPGFVNDSQR KQYEEWLQET QQLLQMQQKY LEEQIGAHRK
3210 3220 3230 3240 3250
SKKALSAKQR TAKKAGREFP EEDAEQLKHV TEQQSMVQKQ LEQIRKQQKE
3260 3270 3280 3290 3300
HAELIEDYRI KQQQQQQQCA LAPPILMPGV QPQPPLVPGA TSLTMSQPNF
3310 3320 3330 3340 3350
PMVPQQLQHQ QHTAVISGHT SPARMPSLPG WQSNSASAHL PLNPPRIQPP
3360 3370 3380 3390 3400
IAQLSLKTCT PAPGTVSSAN PQNGPPPRVE FDDNNPFSES FQERERKERL
3410 3420 3430 3440 3450
REQQERQRVQ LMQEVDRQRA LQQRMEMEQH CLMGAELANR TPVSQMPFYG
3460 3470 3480 3490 3500
SDRPCDFLQP PRPLQQSPQH QQQIGPVLQQ QNVQQGSVNS PPNQTFMQTN
3510 3520 3530 3540 3550
EQRQVGPPSF VPDSPSASGG SPNFHSVKPG HGNLPGSSFQ QSPLRPPFTP
3560 3570 3580 3590 3600
ILPGTSPVAN SNVPCGQDPA VTQGQNYSGS SQSLIQLYSD IIPEEKGKKK
3610 3620 3630 3640 3650
RTRKKKKDDD AESGKAPSTP HSDCAAPLTP GLSETTSTPA VSSPSELPQQ
3660 3670 3680 3690 3700
RQQEPVEPVP VPTPNVSAGQ PCIESENKLP NSEFIKETSN QQTHVNAEAD
3710 3720 3730 3740 3750
KPSVETPNKT EEIKLEKAET QPSQEDTKVE EKTGNKIKDI VAGPVSSIQC
3760 3770 3780 3790 3800
PSHPVGTPTT KGDTGNELLK HLLKNKKASS LLTQKPEGTL SSDESSTKDG
3810 3820 3830 3840 3850
KLIEKQSPAE GLQTLGAQMQ GGFGGGNSQL PKTDGASENK KQRSKRTQRT
3860 3870 3880 3890 3900
GEKAAPRSKK RKKDEEEKQA MYSSSDSFTH LKQQNNLSNP PTPPASLPPT
3910 3920 3930 3940 3950
PPPMACQKMA NGFATTEELA GKAGVLVSHE VARALGPKPF QLPFRPQDDL
3960 3970 3980 3990 4000
LARAIAQGPK TVDVPASLPT PPHNNHEELR IQDHYGDRDT PDSFVPSSSP
4010 4020 4030 4040 4050
ESVVGVEVNK YPDLSLVKEE PPEPVPSPII PILPSISGKN SESRRNDIKT
4060 4070 4080 4090 4100
EPGTLFFTSP FGSSPNGPRS GLISVAITLH PTAAENISSV VAAFSDLLHV
4110 4120 4130 4140 4150
RIPNSYEVSN APDVPPMGLV SSHRVNPSLE YRQHLLLRGP PPGSANPPRL
4160 4170 4180 4190 4200
ATSYRLKQPN VPFPPTSNGL SGYKDSSHGP AEGASLRPQW CCHCKVVILG
4210 4220 4230 4240 4250
SGVRKSCKDL TFVNKGSREN TKRMEKDIVF CSNNCFILYS SAAQAKNSDN
4260 4270 4280 4290 4300
KESLPSLPQS PMKEPSKAFH QYSNNISTLD VHCLPQFQEK VSPPASPPIS
4310 4320 4330 4340 4350
FPPAFEAAKV ESKPDELKVT VKLKPRLRTV PVGLEDCRPL NKKWRGMKWK
4360 4370 4380 4390 4400
KWSIHIVIPK GTFKPPCEDE IDEFLKKLGT CLKPDPVPKD CRKCCFCHEE
4410 4420 4430 4440 4450
GDGLTDGPAR LLNLDLDLWV HLNCALWSTE VYETQAGALI NVELALRRGL
4460 4470 4480 4490 4500
QMKCVFCHKT GATSGCHRFR CTNIYHFTCA TKAQCMFFKD KTMLCPMHKP
4510 4520 4530 4540 4550
KGIHEQQLSY FAVFRRVYVQ RDEVRQIASI VQRGERDHTF RVGSLIFHTI
4560 4570 4580 4590 4600
GQLLPQQMQA FHSPKALFPV GYEASRLYWS TRYANRRCRY LCSIEEKDGR
4610 4620 4630 4640 4650
PVFVIRIVEQ GHEDLVLSDS SPKDVWDKIL EPVACVRKKS EMLQLFPAYL
4660 4670 4680 4690 4700
KGEDLFGLTV SAVARIAESL PGVEACENYT FRYGRNPLME LPLAVNPTGC
4710 4720 4730 4740 4750
ARSEPKMSAH VKRFVLRPHT LNSTSTSKSF QSTVTGELNA PYSKQFVHSK
4760 4770 4780 4790 4800
SSQYRRMKTE WKSNVYLARS RIQGLGLYAA RDIEKHTMVI EYIGTIIRNE
4810 4820 4830 4840 4850
VANRKEKLYE SQNRGVYMFR MDNDHVIDAT LTGGPARYIN HSCAPNCVAE
4860 4870 4880 4890 4900
VVTFERGHKI IISSNRRIQK GEELCYDYKF DFEDDQHKIP CHCGAVNCRK

WMN
Length:4,903
Mass (Da):540,187
Last modified:October 10, 2003 - v2
Checksum:i0B896490B081BA6C
GO
Isoform 2 (identifier: Q8BRH4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     839-878: Missing.
     1414-1448: Missing.
     1791-3080: Missing.
     3814-3884: Missing.
     4714-4717: Missing.

Show »
Length:3,463
Mass (Da):383,966
Checksum:iD14871D89FC23DAB
GO

Sequence cautioni

The sequence AAN11291 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti28 – 36SPAAADKRP → RSFVCGCGA in AAN11291 (PubMed:16459028).Curated9
Sequence conflicti276V → A in AAN11291 (PubMed:16459028).Curated1
Sequence conflicti433 – 440NCRICIEC → VSDFLICF in BAC32109 (PubMed:16141072).Curated8
Sequence conflicti533E → G in AAN11291 (PubMed:16459028).Curated1
Sequence conflicti577D → DA in AAN11291 (PubMed:16459028).Curated1
Sequence conflicti675S → C in BAC35712 (PubMed:16141072).Curated1
Sequence conflicti720K → E in AAN11291 (PubMed:16459028).Curated1
Sequence conflicti763F → L in AAN11291 (PubMed:16459028).Curated1
Sequence conflicti791H → Y in AAN11291 (PubMed:16459028).Curated1
Sequence conflicti1324 – 1325VD → LH in AAN11291 (PubMed:16459028).Curated2
Sequence conflicti1737E → V in AAN11291 (PubMed:16459028).Curated1
Sequence conflicti1776Q → R in AAN11291 (PubMed:16459028).Curated1
Sequence conflicti3236M → MM in AAN11291 (PubMed:16459028).Curated1
Sequence conflicti3423 – 3424QR → P in AAN11291 (PubMed:16459028).Curated2
Sequence conflicti3657E → G in AAN11291 (PubMed:16459028).Curated1
Sequence conflicti3668A → V in AAN11291 (PubMed:16459028).Curated1
Sequence conflicti4283C → Y in AAN11291 (PubMed:16459028).Curated1
Sequence conflicti4306E → D in AAN11291 (PubMed:16459028).Curated1
Sequence conflicti4520Q → R in AAN11291 (PubMed:16459028).Curated1
Sequence conflicti4531V → G in AAN11291 (PubMed:16459028).Curated1
Sequence conflicti4649Y → H in AAN11291 (PubMed:16459028).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_020568839 – 878Missing in isoform 2. 1 PublicationAdd BLAST40
Alternative sequenceiVSP_0205691414 – 1448Missing in isoform 2. 1 PublicationAdd BLAST35
Alternative sequenceiVSP_0205701791 – 3080Missing in isoform 2. 1 PublicationAdd BLAST1290
Alternative sequenceiVSP_0205713814 – 3884Missing in isoform 2. 1 PublicationAdd BLAST71
Alternative sequenceiVSP_0205724714 – 4717Missing in isoform 2. 1 Publication4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY138582 mRNA. Translation: AAN11291.1. Different initiation.
AC116469 Genomic DNA. No translation available.
AC127319 Genomic DNA. No translation available.
AC134910 Genomic DNA. No translation available.
AK044828 mRNA. Translation: BAC32109.1.
AK054270 mRNA. Translation: BAC35712.2.
AK077567 mRNA. Translation: BAC36867.1.
AY036886 mRNA. Translation: AAK70213.1.
AY036887 mRNA. Translation: AAK70214.1.
UniGeneiMm.332268.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY138582 mRNA. Translation: AAN11291.1. Different initiation.
AC116469 Genomic DNA. No translation available.
AC127319 Genomic DNA. No translation available.
AC134910 Genomic DNA. No translation available.
AK044828 mRNA. Translation: BAC32109.1.
AK054270 mRNA. Translation: BAC35712.2.
AK077567 mRNA. Translation: BAC36867.1.
AY036886 mRNA. Translation: AAK70213.1.
AY036887 mRNA. Translation: AAK70214.1.
UniGeneiMm.332268.

3D structure databases

ProteinModelPortaliQ8BRH4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61282N.
IntActiQ8BRH4. 6 interactors.
STRINGi10090.ENSMUSP00000043874.

PTM databases

iPTMnetiQ8BRH4.
PhosphoSitePlusiQ8BRH4.

Proteomic databases

PaxDbiQ8BRH4.
PRIDEiQ8BRH4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:2444959. Kmt2c.

Phylogenomic databases

eggNOGiKOG4443. Eukaryota.
COG2940. LUCA.
HOGENOMiHOG000113602.
HOVERGENiHBG045586.
InParanoidiQ8BRH4.
PhylomeDBiQ8BRH4.

Enzyme and pathway databases

ReactomeiR-MMU-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.

Miscellaneous databases

PROiQ8BRH4.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000038056.
CleanExiMM_MLL3.

Family and domain databases

Gene3Di3.30.40.10. 6 hits.
InterProiIPR003889. FYrich_C.
IPR003888. FYrich_N.
IPR009071. HMG_box_dom.
IPR000637. HMGI/Y_DNA-bd_CS.
IPR003616. Post-SET_dom.
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]
SMARTiSM00542. 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.
PROSITEiPS50216. DHHC. 1 hit.
PS51805. EPHD. 2 hits.
PS51543. FYRC. 1 hit.
PS51542. FYRN. 1 hit.
PS00354. HMGI_Y. 1 hit.
PS50868. POST_SET. 1 hit.
PS50280. SET. 1 hit.
PS01359. ZF_PHD_1. 5 hits.
PS50016. ZF_PHD_2. 6 hits.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKMT2C_MOUSE
AccessioniPrimary (citable) accession number: Q8BRH4
Secondary accession number(s): Q5YLV9
, Q8BK12, Q8C6M3, Q923H5, Q923H6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: October 10, 2003
Last modified: November 2, 2016
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.