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Protein

Histone-lysine N-methyltransferase 2C

Gene

KMT2C

Organism
Homo sapiens (Human)
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. 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)DescriptionActionsGraphical viewLength
Binding sitei4825S-adenosyl-L-methioninePROSITE-ProRule annotation1
Metal bindingi4851ZincBy similarity1
Metal bindingi4899ZincBy similarity1
Metal bindingi4901ZincBy similarity1
Metal bindingi4906ZincBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi34 – 46A.T hookAdd BLAST13
Zinc fingeri227 – 262C2HC pre-PHD-type 1; degeneratePROSITE-ProRule annotationAdd BLAST36
Zinc fingeri283 – 331PHD-type 1PROSITE-ProRule annotationAdd BLAST49
Zinc fingeri341 – 391PHD-type 2PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri344 – 389RING-typePROSITE-ProRule annotationAdd BLAST46
Zinc fingeri388 – 438PHD-type 3PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri464 – 520PHD-type 4PROSITE-ProRule annotationAdd BLAST57
Zinc fingeri957 – 1010PHD-type 5PROSITE-ProRule annotationAdd BLAST54
Zinc fingeri1007 – 1057PHD-type 6PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri1084 – 1139PHD-type 7PROSITE-ProRule annotationAdd BLAST56
Zinc fingeri4399 – 4439C2HC pre-PHD-type 2PROSITE-ProRule annotationAdd BLAST41
Zinc fingeri4460 – 4507PHD-type 8PROSITE-ProRule annotationAdd BLAST48

GO - Molecular functioni

GO - Biological processi

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

BioCyciZFISH:HS00685-MONOMER.
ReactomeiR-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-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):
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
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:13726. KMT2C.

Subcellular locationi

GO - Cellular componenti

  • histone methyltransferase complex Source: MGI
  • MLL3/4 complex Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi58508.
OpenTargetsiENSG00000055609.
PharmGKBiPA30847.

Chemistry databases

ChEMBLiCHEMBL2189113.

Polymorphism and mutation databases

BioMutaiKMT2C.
DMDMi221222521.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001248791 – 4911Histone-lysine N-methyltransferase 2CAdd BLAST4911

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei28PhosphoserineCombined sources1
Modified residuei46PhosphoserineCombined sources1
Modified residuei89PhosphoserineCombined sources1
Modified residuei113PhosphoserineCombined sources1
Modified residuei200PhosphoserineCombined sources1
Modified residuei758N6-acetyllysineCombined sources1
Modified residuei854PhosphoserineCombined sources1
Modified residuei1301PhosphoserineCombined sources1
Modified residuei1508N6-acetyllysineCombined sources1
Modified residuei1772N6-acetyllysineCombined sources1
Modified residuei1987PhosphoserineCombined sources1
Modified residuei2009N6-acetyllysineCombined sources1
Modified residuei2454Asymmetric dimethylarginineBy similarity1
Modified residuei2571Asymmetric dimethylarginineBy similarity1
Modified residuei2802N6-acetyllysineCombined sources1
Modified residuei2809N6-acetyllysineCombined sources1
Modified residuei2828PhosphoserineCombined sources1
Modified residuei2832N6-acetyllysineCombined sources1
Modified residuei2867N6-acetyllysineBy similarity1
Modified residuei3714N6-acetyllysineCombined sources1
Modified residuei3758PhosphoserineCombined sources1
Modified residuei4034PhosphoserineCombined sources1
Modified residuei4139Asymmetric dimethylarginineBy similarity1
Modified residuei4267PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Palmitate, Phosphoprotein

Proteomic databases

EPDiQ8NEZ4.
MaxQBiQ8NEZ4.
PaxDbiQ8NEZ4.
PeptideAtlasiQ8NEZ4.
PRIDEiQ8NEZ4.

PTM databases

iPTMnetiQ8NEZ4.
PhosphoSitePlusiQ8NEZ4.

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

BgeeiENSG00000055609.
CleanExiHS_MLL3.
ExpressionAtlasiQ8NEZ4. baseline and differential.
GenevisibleiQ8NEZ4. HS.

Organism-specific databases

HPAiHPA071556.

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
WDR5P619644EBI-1042997,EBI-540834

Protein-protein interaction databases

BioGridi121835. 24 interactors.
DIPiDIP-48649N.
IntActiQ8NEZ4. 18 interactors.
MINTiMINT-3042700.
STRINGi9606.ENSP00000262189.

Chemistry databases

BindingDBiQ8NEZ4.

Structurei

Secondary structure

14911
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni345 – 347Combined sources3
Turni353 – 355Combined sources3
Beta strandi356 – 358Combined sources3
Beta strandi360 – 362Combined sources3
Turni368 – 372Combined sources5
Turni377 – 379Combined sources3
Turni386 – 388Combined sources3
Turni392 – 394Combined sources3
Beta strandi403 – 405Combined sources3
Beta strandi407 – 409Combined sources3
Beta strandi412 – 414Combined sources3
Helixi415 – 417Combined sources3
Beta strandi418 – 420Combined sources3
Helixi433 – 436Combined sources4
Helixi1636 – 1645Combined sources10
Helixi1646 – 1648Combined sources3
Beta strandi1650 – 1652Combined sources3
Helixi1653 – 1660Combined sources8
Helixi1664 – 1667Combined sources4
Helixi1671 – 1684Combined sources14
Helixi1687 – 1706Combined sources20
Beta strandi4707 – 4709Combined sources3
Helixi4758 – 4768Combined sources11
Helixi4769 – 4771Combined sources3
Beta strandi4773 – 4777Combined sources5
Beta strandi4779 – 4789Combined sources11
Beta strandi4796 – 4800Combined sources5
Beta strandi4802 – 4806Combined sources5
Helixi4807 – 4817Combined sources11
Turni4818 – 4821Combined sources4
Beta strandi4826 – 4828Combined sources3
Beta strandi4830 – 4841Combined sources12
Helixi4843 – 4846Combined sources4
Beta strandi4854 – 4862Combined sources9
Beta strandi4865 – 4874Combined sources10
Beta strandi4908 – 4910Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YSMNMR-A342-439[»]
2YUKNMR-A1631-1713[»]
3UVLX-ray2.20B4707-4717[»]
4ERYX-ray1.30D4703-4716[»]
5F59X-ray2.80A4757-4910[»]
5F6KX-ray2.41C/E4757-4911[»]
ProteinModelPortaliQ8NEZ4.
SMRiQ8NEZ4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8NEZ4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini436 – 489DHHCPROSITE-ProRule annotationAdd BLAST54
Domaini4545 – 4605FYR N-terminalPROSITE-ProRule annotationAdd BLAST61
Domaini4606 – 4691FYR C-terminalPROSITE-ProRule annotationAdd BLAST86
Domaini4771 – 4887SETPROSITE-ProRule annotationAdd BLAST117
Domaini4895 – 4911Post-SETPROSITE-ProRule annotationAdd BLAST17

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni4848 – 4849S-adenosyl-L-methionine bindingBy similarity2

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili92 – 112Sequence analysisAdd BLAST21
Coiled coili644 – 672Sequence analysisAdd BLAST29
Coiled coili1338 – 1366Sequence analysisAdd BLAST29
Coiled coili1754 – 1787Sequence analysisAdd BLAST34
Coiled coili3054 – 3081Sequence analysisAdd BLAST28
Coiled coili3173 – 3272Sequence analysisAdd BLAST100
Coiled coili3391 – 3433Sequence analysisAdd BLAST43

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1719 – 1796Gln-richAdd BLAST78
Compositional biasi1834 – 2281Pro-richAdd BLAST448
Compositional biasi2412 – 2630Pro-richAdd BLAST219
Compositional biasi2690 – 2786Asp-richAdd BLAST97
Compositional biasi3012 – 3509Gln-richAdd BLAST498
Compositional biasi3277 – 3381Pro-richAdd BLAST105

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 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 fingeri227 – 262C2HC pre-PHD-type 1; degeneratePROSITE-ProRule annotationAdd BLAST36
Zinc fingeri283 – 331PHD-type 1PROSITE-ProRule annotationAdd BLAST49
Zinc fingeri341 – 391PHD-type 2PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri344 – 389RING-typePROSITE-ProRule annotationAdd BLAST46
Zinc fingeri388 – 438PHD-type 3PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri464 – 520PHD-type 4PROSITE-ProRule annotationAdd BLAST57
Zinc fingeri957 – 1010PHD-type 5PROSITE-ProRule annotationAdd BLAST54
Zinc fingeri1007 – 1057PHD-type 6PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri1084 – 1139PHD-type 7PROSITE-ProRule annotationAdd BLAST56
Zinc fingeri4399 – 4439C2HC pre-PHD-type 2PROSITE-ProRule annotationAdd BLAST41
Zinc fingeri4460 – 4507PHD-type 8PROSITE-ProRule annotationAdd BLAST48

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG4443. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00760000119228.
HOVERGENiHBG045586.
InParanoidiQ8NEZ4.
KOiK09188.
OMAiMPSLPGW.
OrthoDBiEOG091G000H.
PhylomeDBiQ8NEZ4.
TreeFamiTF354317.

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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

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

        10         20         30         40         50
MSSEEDKSVE QPQPPPPPPE EPGAPAPSPA AADKRPRGRP RKDGASPFQR
60 70 80 90 100
ARKKPRSRGK TAVEDEDSMD GLETTETETI VETEIKEQSA EEDAEAEVDN
110 120 130 140 150
SKQLIPTLQR SVSEESANSL VSVGVEAKIS EQLCAFCYCG EKSSLGQGDL
160 170 180 190 200
KQFRITPGFI LPWRNQPSNK KDIDDNSNGT YEKMQNSAPR KQRGQRKERS
210 220 230 240 250
PQQNIVSCVS VSTQTASDDQ AGKLWDELSL VGLPDAIDIQ ALFDSTGTCW
260 270 280 290 300
AHHRCVEWSL GVCQMEEPLL VNVDKAVVSG STERCAFCKH LGATIKCCEE
310 320 330 340 350
KCTQMYHYPC AAGAGTFQDF SHIFLLCPEH IDQAPERSKE DANCAVCDSP
360 370 380 390 400
GDLLDQFFCT TCGQHYHGMC LDIAVTPLKR AGWQCPECKV CQNCKQSGED
410 420 430 440 450
SKMLVCDTCD KGYHTFCLQP VMKSVPTNGW KCKNCRICIE CGTRSSSQWH
460 470 480 490 500
HNCLICDNCY QQQDNLCPFC GKCYHPELQK DMLHCNMCKR WVHLECDKPT
510 520 530 540 550
DHELDTQLKE EYICMYCKHL GAEMDRLQPG EEVEIAELTT DYNNEMEVEG
560 570 580 590 600
PEDQMVFSEQ AANKDVNGQE STPGIVPDAV QVHTEEQQKS HPSESLDTDS
610 620 630 640 650
LLIAVSSQHT VNTELEKQIS NEVDSEDLKM SSEVKHICGE DQIEDKMEVT
660 670 680 690 700
ENIEVVTHQI TVQQEQLQLL EEPETVVSRE ESRPPKLVME SVTLPLETLV
710 720 730 740 750
SPHEESISLC PEEQLVIERL QGEKEQKENS ELSTGLMDSE MTPTIEGCVK
760 770 780 790 800
DVSYQGGKSI KLSSETESSF SSSADISKAD VSSSPTPSSD LPSHDMLHNY
810 820 830 840 850
PSALSSSAGN IMPTTYISVT PKIGMGKPAI TKRKFSPGRP RSKQGAWSTH
860 870 880 890 900
NTVSPPSWSP DISEGREIFK PRQLPGSAIW SIKVGRGSGF PGKRRPRGAG
910 920 930 940 950
LSGRGGRGRS KLKSGIGAVV LPGVSTADIS SNKDDEENSM HNTVVLFSSS
960 970 980 990 1000
DKFTLNQDMC VVCGSFGQGA EGRLLACSQC GQCYHPYCVS IKITKVVLSK
1010 1020 1030 1040 1050
GWRCLECTVC EACGKATDPG RLLLCDDCDI SYHTYCLDPP LQTVPKGGWK
1060 1070 1080 1090 1100
CKWCVWCRHC GATSAGLRCE WQNNYTQCAP CASLSSCPVC YRNYREEDLI
1110 1120 1130 1140 1150
LQCRQCDRWM HAVCQNLNTE EEVENVADIG FDCSMCRPYM PASNVPSSDC
1160 1170 1180 1190 1200
CESSLVAQIV TKVKELDPPK TYTQDGVCLT ESGMTQLQSL TVTVPRRKRS
1210 1220 1230 1240 1250
KPKLKLKIIN QNSVAVLQTP PDIQSEHSRD GEMDDSREGE LMDCDGKSES
1260 1270 1280 1290 1300
SPEREAVDDE TKGVEGTDGV KKRKRKPYRP GIGGFMVRQR SRTGQGKTKR
1310 1320 1330 1340 1350
SVIRKDSSGS ISEQLPCRDD GWSEQLPDTL VDESVSVTES TEKIKKRYRK
1360 1370 1380 1390 1400
RKNKLEETFP AYLQEAFFGK DLLDTSRQSK ISLDNLSEDG AQLLYKTNMN
1410 1420 1430 1440 1450
TGFLDPSLDP LLSSSSAPTK SGTHGPADDP LADISEVLNT DDDILGIISD
1460 1470 1480 1490 1500
DLAKSVDHSD IGPVTDDPSS LPQPNVNQSS RPLSEEQLDG ILSPELDKMV
1510 1520 1530 1540 1550
TDGAILGKLY KIPELGGKDV EDLFTAVLSP ANTQPTPLPQ PPPPTQLLPI
1560 1570 1580 1590 1600
HNQDAFSRMP LMNGLIGSSP HLPHNSLPPG SGLGTFSAIA QSSYPDARDK
1610 1620 1630 1640 1650
NSAFNPMASD PNNSWTSSAP TVEGENDTMS NAQRSTLKWE KEEALGEMAT
1660 1670 1680 1690 1700
VAPVLYTNIN FPNLKEEFPD WTTRVKQIAK LWRKASSQER APYVQKARDN
1710 1720 1730 1740 1750
RAALRINKVQ MSNDSMKRQQ QQDSIDPSSR IDSELFKDPL KQRESEHEQE
1760 1770 1780 1790 1800
WKFRQQMRQK SKQQAKIEAT QKLEQVKNEQ QQQQQQQFGS QHLLVQSGSD
1810 1820 1830 1840 1850
TPSSGIQSPL TPQPGNGNMS PAQSFHKELF TKQPPSTPTS TSSDDVFVKP
1860 1870 1880 1890 1900
QAPPPPPAPS RIPIQDSLSQ AQTSQPPSPQ VFSPGSSNSR PPSPMDPYAK
1910 1920 1930 1940 1950
MVGTPRPPPV GHSFSRRNSA APVENCTPLS SVSRPLQMNE TTANRPSPVR
1960 1970 1980 1990 2000
DLCSSSTTNN DPYAKPPDTP RPVMTDQFPK SLGLSRSPVV SEQTAKGPIA
2010 2020 2030 2040 2050
AGTSDHFTKP SPRADVFQRQ RIPDSYARPL LTPAPLDSGP GPFKTPMQPP
2060 2070 2080 2090 2100
PSSQDPYGSV SQASRRLSVD PYERPALTPR PIDNFSHNQS NDPYSQPPLT
2110 2120 2130 2140 2150
PHPAVNESFA HPSRAFSQPG TISRPTSQDP YSQPPGTPRP VVDSYSQSSG
2160 2170 2180 2190 2200
TARSNTDPYS QPPGTPRPTT VDPYSQQPQT PRPSTQTDLF VTPVTNQRHS
2210 2220 2230 2240 2250
DPYAHPPGTP RPGISVPYSQ PPATPRPRIS EGFTRSSMTR PVLMPNQDPF
2260 2270 2280 2290 2300
LQAAQNRGPA LPGPLVRPPD TCSQTPRPPG PGLSDTFSRV SPSAARDPYD
2310 2320 2330 2340 2350
QSPMTPRSQS DSFGTSQTAH DVADQPRPGS EGSFCASSNS PMHSQGQQFS
2360 2370 2380 2390 2400
GVSQLPGPVP TSGVTDTQNT VNMAQADTEK LRQRQKLREI ILQQQQQKKI
2410 2420 2430 2440 2450
AGRQEKGSQD SPAVPHPGPL QHWQPENVNQ AFTRPPPPYP GNIRSPVAPP
2460 2470 2480 2490 2500
LGPRYAVFPK DQRGPYPPDV ASMGMRPHGF RFGFPGGSHG TMPSQERFLV
2510 2520 2530 2540 2550
PPQQIQGSGV SPQLRRSVSV DMPRPLNNSQ MNNPVGLPQH FSPQSLPVQQ
2560 2570 2580 2590 2600
HNILGQAYIE LRHRAPDGRQ RLPFSAPPGS VVEASSNLRH GNFIPRPDFP
2610 2620 2630 2640 2650
GPRHTDPMRR PPQGLPNQLP VHPDLEQVPP SQQEQGHSVH SSSMVMRTLN
2660 2670 2680 2690 2700
HPLGGEFSEA PLSTSVPSET TSDNLQITTQ PSDGLEEKLD SDDPSVKELD
2710 2720 2730 2740 2750
VKDLEGVEVK DLDDEDLENL NLDTEDGKVV ELDTLDNLET NDPNLDDLLR
2760 2770 2780 2790 2800
SGEFDIIAYT DPELDMGDKK SMFNEELDLP IDDKLDNQCV SVEPKKKEQE
2810 2820 2830 2840 2850
NKTLVLSDKH SPQKKSTVTN EVKTEVLSPN SKVESKCETE KNDENKDNVD
2860 2870 2880 2890 2900
TPCSQASAHS DLNDGEKTSL HPCDPDLFEK RTNRETAGPS ANVIQASTQL
2910 2920 2930 2940 2950
PAQDVINSCG ITGSTPVLSS LLANEKSDNS DIRPSGSPPP PTLPASPSNH
2960 2970 2980 2990 3000
VSSLPPFIAP PGRVLDNAMN SNVTVVSRVN HVFSQGVQVN PGLIPGQSTV
3010 3020 3030 3040 3050
NHSLGTGKPA TQTGPQTSQS GTSSMSGPQQ LMIPQTLAQQ NRERPLLLEE
3060 3070 3080 3090 3100
QPLLLQDLLD QERQEQQQQR QMQAMIRQRS EPFFPNIDFD AITDPIMKAK
3110 3120 3130 3140 3150
MVALKGINKV MAQNNLGMPP MVMSRFPFMG QVVTGTQNSE GQNLGPQAIP
3160 3170 3180 3190 3200
QDGSITHQIS RPNPPNFGPG FVNDSQRKQY EEWLQETQQL LQMQQKYLEE
3210 3220 3230 3240 3250
QIGAHRKSKK ALSAKQRTAK KAGREFPEED AEQLKHVTEQ QSMVQKQLEQ
3260 3270 3280 3290 3300
IRKQQKEHAE LIEDYRIKQQ QQCAMAPPTM MPSVQPQPPL IPGATPPTMS
3310 3320 3330 3340 3350
QPTFPMVPQQ LQHQQHTTVI SGHTSPVRMP SLPGWQPNSA PAHLPLNPPR
3360 3370 3380 3390 3400
IQPPIAQLPI KTCTPAPGTV SNANPQSGPP PRVEFDDNNP FSESFQERER
3410 3420 3430 3440 3450
KERLREQQER QRIQLMQEVD RQRALQQRME MEQHGMVGSE ISSSRTSVSQ
3460 3470 3480 3490 3500
IPFYSSDLPC DFMQPLGPLQ QSPQHQQQMG QVLQQQNIQQ GSINSPSTQT
3510 3520 3530 3540 3550
FMQTNERRQV GPPSFVPDSP SIPVGSPNFS SVKQGHGNLS GTSFQQSPVR
3560 3570 3580 3590 3600
PSFTPALPAA PPVANSSLPC GQDSTITHGH SYPGSTQSLI QLYSDIIPEE
3610 3620 3630 3640 3650
KGKKKRTRKK KRDDDAESTK APSTPHSDIT APPTPGISET TSTPAVSTPS
3660 3670 3680 3690 3700
ELPQQADQES VEPVGPSTPN MAAGQLCTEL ENKLPNSDFS QATPNQQTYA
3710 3720 3730 3740 3750
NSEVDKLSME TPAKTEEIKL EKAETESCPG QEEPKLEEQN GSKVEGNAVA
3760 3770 3780 3790 3800
CPVSSAQSPP HSAGAPAAKG DSGNELLKHL LKNKKSSSLL NQKPEGSICS
3810 3820 3830 3840 3850
EDDCTKDNKL VEKQNPAEGL QTLGAQMQGG FGCGNQLPKT DGGSETKKQR
3860 3870 3880 3890 3900
SKRTQRTGEK AAPRSKKRKK DEEEKQAMYS STDTFTHLKQ QNNLSNPPTP
3910 3920 3930 3940 3950
PASLPPTPPP MACQKMANGF ATTEELAGKA GVLVSHEVTK TLGPKPFQLP
3960 3970 3980 3990 4000
FRPQDDLLAR ALAQGPKTVD VPASLPTPPH NNQEELRIQD HCGDRDTPDS
4010 4020 4030 4040 4050
FVPSSSPESV VGVEVSRYPD LSLVKEEPPE PVPSPIIPIL PSTAGKSSES
4060 4070 4080 4090 4100
RRNDIKTEPG TLYFASPFGP SPNGPRSGLI SVAITLHPTA AENISSVVAA
4110 4120 4130 4140 4150
FSDLLHVRIP NSYEVSSAPD VPSMGLVSSH RINPGLEYRQ HLLLRGPPPG
4160 4170 4180 4190 4200
SANPPRLVSS YRLKQPNVPF PPTSNGLSGY KDSSHGIAES AALRPQWCCH
4210 4220 4230 4240 4250
CKVVILGSGV RKSFKDLTLL NKDSRESTKR VEKDIVFCSN NCFILYSSTA
4260 4270 4280 4290 4300
QAKNSENKES IPSLPQSPMR ETPSKAFHQY SNNISTLDVH CLPQLPEKAS
4310 4320 4330 4340 4350
PPASPPIAFP PAFEAAQVEA KPDELKVTVK LKPRLRAVHG GFEDCRPLNK
4360 4370 4380 4390 4400
KWRGMKWKKW SIHIVIPKGT FKPPCEDEID EFLKKLGTSL KPDPVPKDYR
4410 4420 4430 4440 4450
KCCFCHEEGD GLTDGPARLL NLDLDLWVHL NCALWSTEVY ETQAGALINV
4460 4470 4480 4490 4500
ELALRRGLQM KCVFCHKTGA TSGCHRFRCT NIYHFTCAIK AQCMFFKDKT
4510 4520 4530 4540 4550
MLCPMHKPKG IHEQELSYFA VFRRVYVQRD EVRQIASIVQ RGERDHTFRV
4560 4570 4580 4590 4600
GSLIFHTIGQ LLPQQMQAFH SPKALFPVGY EASRLYWSTR YANRRCRYLC
4610 4620 4630 4640 4650
SIEEKDGRPV FVIRIVEQGH EDLVLSDISP KGVWDKILEP VACVRKKSEM
4660 4670 4680 4690 4700
LQLFPAYLKG EDLFGLTVSA VARIAESLPG VEACENYTFR YGRNPLMELP
4710 4720 4730 4740 4750
LAVNPTGCAR SEPKMSAHVK RFVLRPHTLN STSTSKSFQS TVTGELNAPY
4760 4770 4780 4790 4800
SKQFVHSKSS QYRKMKTEWK SNVYLARSRI QGLGLYAARD IEKHTMVIEY
4810 4820 4830 4840 4850
IGTIIRNEVA NRKEKLYESQ NRGVYMFRMD NDHVIDATLT GGPARYINHS
4860 4870 4880 4890 4900
CAPNCVAEVV TFERGHKIII SSSRRIQKGE ELCYDYKFDF EDDQHKIPCH
4910
CGAVNCRKWM N
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)DescriptionActionsGraphical viewLength
Sequence conflicti579A → T in AAK00583 (PubMed:11891048).Curated1
Sequence conflicti1286M → V in AAK00583 (PubMed:11891048).Curated1
Sequence conflicti2360P → S in AAK00583 (PubMed:11891048).Curated1
Sequence conflicti2797K → R in AAK00583 (PubMed:11891048).Curated1
Sequence conflicti2882T → A in AAK00583 (PubMed:11891048).Curated1
Sequence conflicti3289P → S in BAC11409 (PubMed:14702039).Curated1
Sequence conflicti3428R → W in BAC11409 (PubMed:14702039).Curated1
Sequence conflicti4613I → V in AK022687 (PubMed:14702039).Curated1
Sequence conflicti4866H → P in AK022687 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_061911291L → F.Corresponds to variant rs56850341dbSNPEnsembl.1
Natural variantiVAR_061912316T → S.Corresponds to variant rs10454320dbSNPEnsembl.1
Natural variantiVAR_036311347C → G in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_036312400D → N in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_036313478L → W in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_057360526R → P.1 PublicationCorresponds to variant rs3735156dbSNPEnsembl.1
Natural variantiVAR_017118823I → N.Corresponds to variant rs2838171dbSNPEnsembl.1
Natural variantiVAR_017117823I → T.Corresponds to variant rs2838171dbSNPEnsembl.1
Natural variantiVAR_0573611836S → N.Corresponds to variant rs11771635dbSNPEnsembl.1
Natural variantiVAR_0573622008T → A.Corresponds to variant rs6951159dbSNPEnsembl.1
Natural variantiVAR_0573632412P → T.Corresponds to variant rs13231116dbSNPEnsembl.1
Natural variantiVAR_0573642600P → A.Corresponds to variant rs2270234dbSNPEnsembl.1
Natural variantiVAR_0363143698T → S in a colorectal cancer sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0085611 – 939Missing in isoform 2. 1 PublicationAdd BLAST939
Alternative sequenceiVSP_0085623890Q → QVRQLSLLPLMEPIIGVNFA HFLPYGSGQFNSGNRLLGTF GSATLEGVSDYYSQLIYK in isoform 2 and isoform 3. 1 Publication1
Alternative sequenceiVSP_0362234721 – 4724Missing in isoform 2. 1 Publication4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [Q8NEZ4-1]
GeneIDi58508.
KEGGihsa:58508.
UCSCiuc003wla.3. human. [Q8NEZ4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YSMNMR-A342-439[»]
2YUKNMR-A1631-1713[»]
3UVLX-ray2.20B4707-4717[»]
4ERYX-ray1.30D4703-4716[»]
5F59X-ray2.80A4757-4910[»]
5F6KX-ray2.41C/E4757-4911[»]
ProteinModelPortaliQ8NEZ4.
SMRiQ8NEZ4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121835. 24 interactors.
DIPiDIP-48649N.
IntActiQ8NEZ4. 18 interactors.
MINTiMINT-3042700.
STRINGi9606.ENSP00000262189.

Chemistry databases

BindingDBiQ8NEZ4.
ChEMBLiCHEMBL2189113.

PTM databases

iPTMnetiQ8NEZ4.
PhosphoSitePlusiQ8NEZ4.

Polymorphism and mutation databases

BioMutaiKMT2C.
DMDMi221222521.

Proteomic databases

EPDiQ8NEZ4.
MaxQBiQ8NEZ4.
PaxDbiQ8NEZ4.
PeptideAtlasiQ8NEZ4.
PRIDEiQ8NEZ4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262189; ENSP00000262189; ENSG00000055609. [Q8NEZ4-1]
ENST00000355193; ENSP00000347325; ENSG00000055609. [Q8NEZ4-1]
GeneIDi58508.
KEGGihsa:58508.
UCSCiuc003wla.3. human. [Q8NEZ4-1]

Organism-specific databases

CTDi58508.
DisGeNETi58508.
GeneCardsiKMT2C.
H-InvDBHIX0007238.
HIX0016202.
HIX0080234.
HGNCiHGNC:13726. KMT2C.
HPAiHPA071556.
MIMi606833. gene.
neXtProtiNX_Q8NEZ4.
OpenTargetsiENSG00000055609.
PharmGKBiPA30847.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4443. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00760000119228.
HOVERGENiHBG045586.
InParanoidiQ8NEZ4.
KOiK09188.
OMAiMPSLPGW.
OrthoDBiEOG091G000H.
PhylomeDBiQ8NEZ4.
TreeFamiTF354317.

Enzyme and pathway databases

BioCyciZFISH:HS00685-MONOMER.
ReactomeiR-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.

Miscellaneous databases

EvolutionaryTraceiQ8NEZ4.
GeneWikiiMLL3.
GenomeRNAii58508.
PROiQ8NEZ4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000055609.
CleanExiHS_MLL3.
ExpressionAtlasiQ8NEZ4. baseline and differential.
GenevisibleiQ8NEZ4. HS.

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_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: November 30, 2016
This is version 155 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

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.