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Q8NEZ4 (MLL3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone-lysine N-methyltransferase MLL3

EC=2.1.1.43
Alternative name(s):
Homologous to ALR protein
Lysine N-methyltransferase 2C
Short name=KMT2C
Myeloid/lymphoid or mixed-lineage leukemia protein 3
Gene names
Name:MLL3
Synonyms:HALR, KIAA1506, KMT2C
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length4911 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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/MLL3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation. MLL3 may be a catalytic subunit of this complex. May be involved in leukemogenesis and developmental disorder. Ref.16

Catalytic activity

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. Ref.16

Subunit structure

Component of the MLL2/MLL3 complex (also named ASCOM complex), at least composed of MLL2, MLL3, ASH2L, RBBP5, DPY30, NCOA6, WDR5, MEN1, KDM6A and PAXIP1/PTIP. Component of the MLL3/MLL4 complex at least composed of MLL3, MLL4, ASH2L, RBBP5, DPY30, WDR5, NCOA6, KDM6A, PAXIP1/PTIP and C16orf53/PA1. Interacts with histone H3. Ref.8

Subcellular location

Nucleus Probable.

Tissue specificity

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.

Domain

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

Miscellaneous

Found in a critical region of chromosome 7, which is commonly deleted in malignant myeloid disorders. Partial duplication of the MLL3 gene are found in the juxtacentromeric region of chromosomes 1, 2, 13 and 21. Juxtacentromeric reshuffling of the MLL3 gene has generated the BAGE genes.

Sequence similarities

Belongs to the histone-lysine methyltransferase family. TRX/MLL subfamily.

Contains 1 A.T hook DNA-binding domain.

Contains 1 DHHC-type zinc finger.

Contains 1 FYR C-terminal domain.

Contains 1 FYR N-terminal domain.

Contains 6 PHD-type zinc fingers.

Contains 1 post-SET domain.

Contains 1 RING-type zinc finger.

Contains 1 SET domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NCOA6Q146864EBI-1042997,EBI-78670

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8NEZ4-1)

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.
Isoform 2 (identifier: Q8NEZ4-2)

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.
Isoform 3 (identifier: Q8NEZ4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     3890-3890: Q → QVRQLSLLPLMEPIIGVNFAHFLPYGSGQFNSGNRLLGTFGSATLEGVSDYYSQLIYK
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 49114911Histone-lysine N-methyltransferase MLL3
PRO_0000124879

Regions

Domain4545 – 460561FYR N-terminal
Domain4606 – 469186FYR C-terminal
Domain4770 – 4891122SET
Domain4895 – 491117Post-SET
DNA binding34 – 4613A.T hook
Zinc finger341 – 39151PHD-type 1
Zinc finger344 – 38946RING-type
Zinc finger388 – 43851PHD-type 2
Zinc finger436 – 48954DHHC-type
Zinc finger464 – 52057PHD-type 3
Zinc finger957 – 101054PHD-type 4
Zinc finger1007 – 105751PHD-type 5
Zinc finger1084 – 113956PHD-type 6
Region4848 – 48492S-adenosyl-L-methionine binding By similarity
Coiled coil92 – 11221 Potential
Coiled coil644 – 67229 Potential
Coiled coil1338 – 136629 Potential
Coiled coil1754 – 178734 Potential
Coiled coil3054 – 308128 Potential
Coiled coil3173 – 3272100 Potential
Coiled coil3391 – 343343 Potential
Compositional bias1719 – 179678Gln-rich
Compositional bias1834 – 2281448Pro-rich
Compositional bias2412 – 2630219Pro-rich
Compositional bias2690 – 278697Asp-rich
Compositional bias3012 – 3509498Gln-rich
Compositional bias3277 – 3381105Pro-rich

Sites

Metal binding48511Zinc By similarity
Metal binding48991Zinc By similarity
Metal binding49011Zinc By similarity
Metal binding49061Zinc By similarity
Binding site48251S-adenosyl-L-methionine By similarity

Amino acid modifications

Modified residue7581N6-acetyllysine Ref.12
Modified residue8271N6-acetyllysine Ref.12
Modified residue15081N6-acetyllysine Ref.12
Modified residue17721N6-acetyllysine Ref.12
Modified residue20091N6-acetyllysine Ref.12
Modified residue28021N6-acetyllysine Ref.12
Modified residue28091N6-acetyllysine Ref.10 Ref.12
Modified residue28321N6-acetyllysine Ref.12
Modified residue37141N6-acetyllysine Ref.12
Modified residue39451N6-acetyllysine Ref.12
Modified residue40181Phosphotyrosine Ref.9
Modified residue40221Phosphoserine Ref.9
Modified residue40341Phosphoserine Ref.11
Modified residue40501Phosphoserine Ref.11

Natural variations

Alternative sequence1 – 939939Missing in isoform 2.
VSP_008561
Alternative sequence38901Q → QVRQLSLLPLMEPIIGVNFA HFLPYGSGQFNSGNRLLGTF GSATLEGVSDYYSQLIYK in isoform 2 and isoform 3.
VSP_008562
Alternative sequence4721 – 47244Missing in isoform 2.
VSP_036223
Natural variant2911L → F.
Corresponds to variant rs56850341 [ dbSNP | Ensembl ].
VAR_061911
Natural variant3161T → S.
Corresponds to variant rs10454320 [ dbSNP | Ensembl ].
VAR_061912
Natural variant3471C → G in a colorectal cancer sample; somatic mutation. Ref.15
VAR_036311
Natural variant4001D → N in a colorectal cancer sample; somatic mutation. Ref.15
VAR_036312
Natural variant4781L → W in a colorectal cancer sample; somatic mutation. Ref.15
VAR_036313
Natural variant5261R → P. Ref.1
Corresponds to variant rs3735156 [ dbSNP | Ensembl ].
VAR_057360
Natural variant8231I → N.
Corresponds to variant rs2838171 [ dbSNP | Ensembl ].
VAR_017118
Natural variant8231I → T.
Corresponds to variant rs2838171 [ dbSNP | Ensembl ].
VAR_017117
Natural variant18361S → N.
Corresponds to variant rs11771635 [ dbSNP | Ensembl ].
VAR_057361
Natural variant20081T → A.
Corresponds to variant rs6951159 [ dbSNP | Ensembl ].
VAR_057362
Natural variant24121P → T.
Corresponds to variant rs13231116 [ dbSNP | Ensembl ].
VAR_057363
Natural variant26001P → A.
Corresponds to variant rs2270234 [ dbSNP | Ensembl ].
VAR_057364
Natural variant36981T → S in a colorectal cancer sample; somatic mutation. Ref.15
VAR_036314

Experimental info

Sequence conflict5791A → T in AAK00583. Ref.1
Sequence conflict12861M → V in AAK00583. Ref.1
Sequence conflict23601P → S in AAK00583. Ref.1
Sequence conflict27971K → R in AAK00583. Ref.1
Sequence conflict28821T → A in AAK00583. Ref.1
Sequence conflict32891P → S in BAC11409. Ref.6
Sequence conflict34281R → W in BAC11409. Ref.6
Sequence conflict46131I → V in AK022687. Ref.6
Sequence conflict48661H → P in AK022687. Ref.6

Secondary structure

.......................... 4911
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 20, 2009. Version 3.
Checksum: 898CEE324772BD75

FASTA4,911541,370
        10         20         30         40         50         60 
MSSEEDKSVE QPQPPPPPPE EPGAPAPSPA AADKRPRGRP RKDGASPFQR ARKKPRSRGK 

        70         80         90        100        110        120 
TAVEDEDSMD GLETTETETI VETEIKEQSA EEDAEAEVDN SKQLIPTLQR SVSEESANSL 

       130        140        150        160        170        180 
VSVGVEAKIS EQLCAFCYCG EKSSLGQGDL KQFRITPGFI LPWRNQPSNK KDIDDNSNGT 

       190        200        210        220        230        240 
YEKMQNSAPR KQRGQRKERS PQQNIVSCVS VSTQTASDDQ AGKLWDELSL VGLPDAIDIQ 

       250        260        270        280        290        300 
ALFDSTGTCW AHHRCVEWSL GVCQMEEPLL VNVDKAVVSG STERCAFCKH LGATIKCCEE 

       310        320        330        340        350        360 
KCTQMYHYPC AAGAGTFQDF SHIFLLCPEH IDQAPERSKE DANCAVCDSP GDLLDQFFCT 

       370        380        390        400        410        420 
TCGQHYHGMC LDIAVTPLKR AGWQCPECKV CQNCKQSGED SKMLVCDTCD KGYHTFCLQP 

       430        440        450        460        470        480 
VMKSVPTNGW KCKNCRICIE CGTRSSSQWH HNCLICDNCY QQQDNLCPFC GKCYHPELQK 

       490        500        510        520        530        540 
DMLHCNMCKR WVHLECDKPT DHELDTQLKE EYICMYCKHL GAEMDRLQPG EEVEIAELTT 

       550        560        570        580        590        600 
DYNNEMEVEG PEDQMVFSEQ AANKDVNGQE STPGIVPDAV QVHTEEQQKS HPSESLDTDS 

       610        620        630        640        650        660 
LLIAVSSQHT VNTELEKQIS NEVDSEDLKM SSEVKHICGE DQIEDKMEVT ENIEVVTHQI 

       670        680        690        700        710        720 
TVQQEQLQLL EEPETVVSRE ESRPPKLVME SVTLPLETLV SPHEESISLC PEEQLVIERL 

       730        740        750        760        770        780 
QGEKEQKENS ELSTGLMDSE MTPTIEGCVK DVSYQGGKSI KLSSETESSF SSSADISKAD 

       790        800        810        820        830        840 
VSSSPTPSSD LPSHDMLHNY PSALSSSAGN IMPTTYISVT PKIGMGKPAI TKRKFSPGRP 

       850        860        870        880        890        900 
RSKQGAWSTH NTVSPPSWSP DISEGREIFK PRQLPGSAIW SIKVGRGSGF PGKRRPRGAG 

       910        920        930        940        950        960 
LSGRGGRGRS KLKSGIGAVV LPGVSTADIS SNKDDEENSM HNTVVLFSSS DKFTLNQDMC 

       970        980        990       1000       1010       1020 
VVCGSFGQGA EGRLLACSQC GQCYHPYCVS IKITKVVLSK GWRCLECTVC EACGKATDPG 

      1030       1040       1050       1060       1070       1080 
RLLLCDDCDI SYHTYCLDPP LQTVPKGGWK CKWCVWCRHC GATSAGLRCE WQNNYTQCAP 

      1090       1100       1110       1120       1130       1140 
CASLSSCPVC YRNYREEDLI LQCRQCDRWM HAVCQNLNTE EEVENVADIG FDCSMCRPYM 

      1150       1160       1170       1180       1190       1200 
PASNVPSSDC CESSLVAQIV TKVKELDPPK TYTQDGVCLT ESGMTQLQSL TVTVPRRKRS 

      1210       1220       1230       1240       1250       1260 
KPKLKLKIIN QNSVAVLQTP PDIQSEHSRD GEMDDSREGE LMDCDGKSES SPEREAVDDE 

      1270       1280       1290       1300       1310       1320 
TKGVEGTDGV KKRKRKPYRP GIGGFMVRQR SRTGQGKTKR SVIRKDSSGS ISEQLPCRDD 

      1330       1340       1350       1360       1370       1380 
GWSEQLPDTL VDESVSVTES TEKIKKRYRK RKNKLEETFP AYLQEAFFGK DLLDTSRQSK 

      1390       1400       1410       1420       1430       1440 
ISLDNLSEDG AQLLYKTNMN TGFLDPSLDP LLSSSSAPTK SGTHGPADDP LADISEVLNT 

      1450       1460       1470       1480       1490       1500 
DDDILGIISD DLAKSVDHSD IGPVTDDPSS LPQPNVNQSS RPLSEEQLDG ILSPELDKMV 

      1510       1520       1530       1540       1550       1560 
TDGAILGKLY KIPELGGKDV EDLFTAVLSP ANTQPTPLPQ PPPPTQLLPI HNQDAFSRMP 

      1570       1580       1590       1600       1610       1620 
LMNGLIGSSP HLPHNSLPPG SGLGTFSAIA QSSYPDARDK NSAFNPMASD PNNSWTSSAP 

      1630       1640       1650       1660       1670       1680 
TVEGENDTMS NAQRSTLKWE KEEALGEMAT VAPVLYTNIN FPNLKEEFPD WTTRVKQIAK 

      1690       1700       1710       1720       1730       1740 
LWRKASSQER APYVQKARDN RAALRINKVQ MSNDSMKRQQ QQDSIDPSSR IDSELFKDPL 

      1750       1760       1770       1780       1790       1800 
KQRESEHEQE WKFRQQMRQK SKQQAKIEAT QKLEQVKNEQ QQQQQQQFGS QHLLVQSGSD 

      1810       1820       1830       1840       1850       1860 
TPSSGIQSPL TPQPGNGNMS PAQSFHKELF TKQPPSTPTS TSSDDVFVKP QAPPPPPAPS 

      1870       1880       1890       1900       1910       1920 
RIPIQDSLSQ AQTSQPPSPQ VFSPGSSNSR PPSPMDPYAK MVGTPRPPPV GHSFSRRNSA 

      1930       1940       1950       1960       1970       1980 
APVENCTPLS SVSRPLQMNE TTANRPSPVR DLCSSSTTNN DPYAKPPDTP RPVMTDQFPK 

      1990       2000       2010       2020       2030       2040 
SLGLSRSPVV SEQTAKGPIA AGTSDHFTKP SPRADVFQRQ RIPDSYARPL LTPAPLDSGP 

      2050       2060       2070       2080       2090       2100 
GPFKTPMQPP PSSQDPYGSV SQASRRLSVD PYERPALTPR PIDNFSHNQS NDPYSQPPLT 

      2110       2120       2130       2140       2150       2160 
PHPAVNESFA HPSRAFSQPG TISRPTSQDP YSQPPGTPRP VVDSYSQSSG TARSNTDPYS 

      2170       2180       2190       2200       2210       2220 
QPPGTPRPTT VDPYSQQPQT PRPSTQTDLF VTPVTNQRHS DPYAHPPGTP RPGISVPYSQ 

      2230       2240       2250       2260       2270       2280 
PPATPRPRIS EGFTRSSMTR PVLMPNQDPF LQAAQNRGPA LPGPLVRPPD TCSQTPRPPG 

      2290       2300       2310       2320       2330       2340 
PGLSDTFSRV SPSAARDPYD QSPMTPRSQS DSFGTSQTAH DVADQPRPGS EGSFCASSNS 

      2350       2360       2370       2380       2390       2400 
PMHSQGQQFS GVSQLPGPVP TSGVTDTQNT VNMAQADTEK LRQRQKLREI ILQQQQQKKI 

      2410       2420       2430       2440       2450       2460 
AGRQEKGSQD SPAVPHPGPL QHWQPENVNQ AFTRPPPPYP GNIRSPVAPP LGPRYAVFPK 

      2470       2480       2490       2500       2510       2520 
DQRGPYPPDV ASMGMRPHGF RFGFPGGSHG TMPSQERFLV PPQQIQGSGV SPQLRRSVSV 

      2530       2540       2550       2560       2570       2580 
DMPRPLNNSQ MNNPVGLPQH FSPQSLPVQQ HNILGQAYIE LRHRAPDGRQ RLPFSAPPGS 

      2590       2600       2610       2620       2630       2640 
VVEASSNLRH GNFIPRPDFP GPRHTDPMRR PPQGLPNQLP VHPDLEQVPP SQQEQGHSVH 

      2650       2660       2670       2680       2690       2700 
SSSMVMRTLN HPLGGEFSEA PLSTSVPSET TSDNLQITTQ PSDGLEEKLD SDDPSVKELD 

      2710       2720       2730       2740       2750       2760 
VKDLEGVEVK DLDDEDLENL NLDTEDGKVV ELDTLDNLET NDPNLDDLLR SGEFDIIAYT 

      2770       2780       2790       2800       2810       2820 
DPELDMGDKK SMFNEELDLP IDDKLDNQCV SVEPKKKEQE NKTLVLSDKH SPQKKSTVTN 

      2830       2840       2850       2860       2870       2880 
EVKTEVLSPN SKVESKCETE KNDENKDNVD TPCSQASAHS DLNDGEKTSL HPCDPDLFEK 

      2890       2900       2910       2920       2930       2940 
RTNRETAGPS ANVIQASTQL PAQDVINSCG ITGSTPVLSS LLANEKSDNS DIRPSGSPPP 

      2950       2960       2970       2980       2990       3000 
PTLPASPSNH VSSLPPFIAP PGRVLDNAMN SNVTVVSRVN HVFSQGVQVN PGLIPGQSTV 

      3010       3020       3030       3040       3050       3060 
NHSLGTGKPA TQTGPQTSQS GTSSMSGPQQ LMIPQTLAQQ NRERPLLLEE QPLLLQDLLD 

      3070       3080       3090       3100       3110       3120 
QERQEQQQQR QMQAMIRQRS EPFFPNIDFD AITDPIMKAK MVALKGINKV MAQNNLGMPP 

      3130       3140       3150       3160       3170       3180 
MVMSRFPFMG QVVTGTQNSE GQNLGPQAIP QDGSITHQIS RPNPPNFGPG FVNDSQRKQY 

      3190       3200       3210       3220       3230       3240 
EEWLQETQQL LQMQQKYLEE QIGAHRKSKK ALSAKQRTAK KAGREFPEED AEQLKHVTEQ 

      3250       3260       3270       3280       3290       3300 
QSMVQKQLEQ IRKQQKEHAE LIEDYRIKQQ QQCAMAPPTM MPSVQPQPPL IPGATPPTMS 

      3310       3320       3330       3340       3350       3360 
QPTFPMVPQQ LQHQQHTTVI SGHTSPVRMP SLPGWQPNSA PAHLPLNPPR IQPPIAQLPI 

      3370       3380       3390       3400       3410       3420 
KTCTPAPGTV SNANPQSGPP PRVEFDDNNP FSESFQERER KERLREQQER QRIQLMQEVD 

      3430       3440       3450       3460       3470       3480 
RQRALQQRME MEQHGMVGSE ISSSRTSVSQ IPFYSSDLPC DFMQPLGPLQ QSPQHQQQMG 

      3490       3500       3510       3520       3530       3540 
QVLQQQNIQQ GSINSPSTQT FMQTNERRQV GPPSFVPDSP SIPVGSPNFS SVKQGHGNLS 

      3550       3560       3570       3580       3590       3600 
GTSFQQSPVR PSFTPALPAA PPVANSSLPC GQDSTITHGH SYPGSTQSLI QLYSDIIPEE 

      3610       3620       3630       3640       3650       3660 
KGKKKRTRKK KRDDDAESTK APSTPHSDIT APPTPGISET TSTPAVSTPS ELPQQADQES 

      3670       3680       3690       3700       3710       3720 
VEPVGPSTPN MAAGQLCTEL ENKLPNSDFS QATPNQQTYA NSEVDKLSME TPAKTEEIKL 

      3730       3740       3750       3760       3770       3780 
EKAETESCPG QEEPKLEEQN GSKVEGNAVA CPVSSAQSPP HSAGAPAAKG DSGNELLKHL 

      3790       3800       3810       3820       3830       3840 
LKNKKSSSLL NQKPEGSICS EDDCTKDNKL VEKQNPAEGL QTLGAQMQGG FGCGNQLPKT 

      3850       3860       3870       3880       3890       3900 
DGGSETKKQR SKRTQRTGEK AAPRSKKRKK DEEEKQAMYS STDTFTHLKQ QNNLSNPPTP 

      3910       3920       3930       3940       3950       3960 
PASLPPTPPP MACQKMANGF ATTEELAGKA GVLVSHEVTK TLGPKPFQLP FRPQDDLLAR 

      3970       3980       3990       4000       4010       4020 
ALAQGPKTVD VPASLPTPPH NNQEELRIQD HCGDRDTPDS FVPSSSPESV VGVEVSRYPD 

      4030       4040       4050       4060       4070       4080 
LSLVKEEPPE PVPSPIIPIL PSTAGKSSES RRNDIKTEPG TLYFASPFGP SPNGPRSGLI 

      4090       4100       4110       4120       4130       4140 
SVAITLHPTA AENISSVVAA FSDLLHVRIP NSYEVSSAPD VPSMGLVSSH RINPGLEYRQ 

      4150       4160       4170       4180       4190       4200 
HLLLRGPPPG SANPPRLVSS YRLKQPNVPF PPTSNGLSGY KDSSHGIAES AALRPQWCCH 

      4210       4220       4230       4240       4250       4260 
CKVVILGSGV RKSFKDLTLL NKDSRESTKR VEKDIVFCSN NCFILYSSTA QAKNSENKES 

      4270       4280       4290       4300       4310       4320 
IPSLPQSPMR ETPSKAFHQY SNNISTLDVH CLPQLPEKAS PPASPPIAFP PAFEAAQVEA 

      4330       4340       4350       4360       4370       4380 
KPDELKVTVK LKPRLRAVHG GFEDCRPLNK KWRGMKWKKW SIHIVIPKGT FKPPCEDEID 

      4390       4400       4410       4420       4430       4440 
EFLKKLGTSL KPDPVPKDYR KCCFCHEEGD GLTDGPARLL NLDLDLWVHL NCALWSTEVY 

      4450       4460       4470       4480       4490       4500 
ETQAGALINV ELALRRGLQM KCVFCHKTGA TSGCHRFRCT NIYHFTCAIK AQCMFFKDKT 

      4510       4520       4530       4540       4550       4560 
MLCPMHKPKG IHEQELSYFA VFRRVYVQRD EVRQIASIVQ RGERDHTFRV GSLIFHTIGQ 

      4570       4580       4590       4600       4610       4620 
LLPQQMQAFH SPKALFPVGY EASRLYWSTR YANRRCRYLC SIEEKDGRPV FVIRIVEQGH 

      4630       4640       4650       4660       4670       4680 
EDLVLSDISP KGVWDKILEP VACVRKKSEM LQLFPAYLKG EDLFGLTVSA VARIAESLPG 

      4690       4700       4710       4720       4730       4740 
VEACENYTFR YGRNPLMELP LAVNPTGCAR SEPKMSAHVK RFVLRPHTLN STSTSKSFQS 

      4750       4760       4770       4780       4790       4800 
TVTGELNAPY SKQFVHSKSS QYRKMKTEWK SNVYLARSRI QGLGLYAARD IEKHTMVIEY 

      4810       4820       4830       4840       4850       4860 
IGTIIRNEVA NRKEKLYESQ NRGVYMFRMD NDHVIDATLT GGPARYINHS CAPNCVAEVV 

      4870       4880       4890       4900       4910 
TFERGHKIII SSSRRIQKGE ELCYDYKFDF EDDQHKIPCH CGAVNCRKWM N 

« Hide

Isoform 2 [UniParc].

Checksum: 41624149C28E4BDE
Show »

FASTA4,025443,538
Isoform 3 [UniParc].

Checksum: 7D6E36D9FA78714B
Show »

FASTA4,968547,633

References

« Hide 'large scale' references
[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: 11891048] [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: 11718452] [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. expand/collapse author list , 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: 12853948] [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: 10819331] [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: 12168954] [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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3193-3865 AND 4460-4911.
Tissue: Placenta.
[7]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
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: 12482968] [Abstract]
Cited for: INTERACTION WITH MLL2/MLL3 COMPLEX (ISOFORM 2).
Tissue: Cervix carcinoma.
[9]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-4018 AND SER-4022, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[10]"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.
Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2809, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[11]"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.
Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4034 AND SER-4050, MASS SPECTROMETRY.
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., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-758; LYS-827; LYS-1508; LYS-1772; LYS-2009; LYS-2802; LYS-2809; LYS-2832; LYS-3714 AND LYS-3945, MASS SPECTROMETRY.
[13]"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.
[14]"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.
[15]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLY-347; ASN-400; TRP-478 AND SER-3698.
[16]"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: 17500065] [Abstract]
Cited for: FUNCTION, ENZYME ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MLL3/MLL4 COMPLEX.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
IPIIPI00168806.
IPI00375729.
IPI00916332.
RefSeqNP_733751.2. NM_170606.2.
UniGeneHs.647120.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YSMNMR-A342-439[»]
2YUKNMR-A1631-1713[»]
ProteinModelPortalQ8NEZ4.
SMRQ8NEZ4. Positions 282-520, 956-1138, 1624-1713, 4542-4691, 4756-4911.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-48649N.
IntActQ8NEZ4. 9 interactions.
STRINGQ8NEZ4.

PTM databases

PhosphoSiteQ8NEZ4.

Polymorphism databases

DMDM221222521.

Proteomic databases

PRIDEQ8NEZ4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262189; ENSP00000262189; ENSG00000055609.
GeneID58508.
KEGGhsa:58508.
UCSCuc003wla.1. human.

Organism-specific databases

CTD58508.
GeneCardsGC07M151832.
H-InvDBHIX0007238.
HGNCHGNC:13726. MLL3.
MIM606833. gene.
neXtProtNX_Q8NEZ4.
PharmGKBPA30847.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

GeneTreeENSGT00580000081416.
HOVERGENHBG045586.
InParanoidQ8NEZ4.
OMADTSRQNK.
PhylomeDBQ8NEZ4.

Gene expression databases

ArrayExpressQ8NEZ4.
BgeeQ8NEZ4.
CleanExHS_MLL3.
GenevestigatorQ8NEZ4.
GermOnlineENSG00000055609. Homo sapiens.

Family and domain databases

InterProIPR017956. AT_hook_DNA-bd_motif.
IPR003889. FYrich_C.
IPR018516. FYrich_C_subgr.
IPR003888. FYrich_N.
IPR018518. FYrich_N_subgr.
IPR000910. HMG_HMG1/HMG2.
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]
Gene3DG3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 6 hits.
KOK09188.
PfamPF05965. FYRC. 1 hit.
PF05964. FYRN. 1 hit.
PF00628. PHD. 2 hits.
PF00856. SET. 1 hit.
[Graphical view]
SMARTSM00384. 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]
SUPFAMSSF57903. FYVE_PHD_ZnF. 6 hits.
PROSITEPS51543. 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]
ProtoNetSearch...

Other

NextBio65023.
SOURCESearch...

Entry information

Entry nameMLL3_HUMAN
AccessionPrimary (citable) accession number: Q8NEZ4
Secondary accession number(s): Q8NC02 expand/collapse secondary AC list , Q8NDF6, Q9H9P4, Q9NR13, Q9P222, Q9UDR7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: January 20, 2009
Last modified: December 14, 2011
This is version 106 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families