P55200 (MLL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone-lysine N-methyltransferase MLL
EC=2.1.1.43

Alternative name(s):
ALL-1
Zinc finger protein HRX

Cleaved into the following 2 chains:

1. MLL cleavage product N320
   Alternative name(s):
   N-terminal cleavage product of 320 kDa
   Short name=p320
2. MLL cleavage product C180
   Alternative name(s):
   C-terminal cleavage product of 180 kDa
   Short name=p180

Gene names

Name:	Mll
Synonyms:	All1, Hrx, Mll1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	3966 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Histone methyltransferase that plays an essential role in early development and hematopoiesis. Catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac). In the MLL1/MLL complex, it specifically mediates H3K4me, a specific tag for epigenetic transcriptional activation. Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity. Has no activity toward histone H3 phosphorylated on 'Thr-3', less activity toward H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher activity toward H3 acetylated on 'Lys-9'. Required for transcriptional activation of HOXA9. Promotes PPP1R15A-induced apoptosis By similarity.
Catalytic activity	S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
Subunit structure	MLL cleavage product N320 heterodimerizes with MLL cleavage product C180 (via SET and FYRC domains). Interacts with WDR5; the interaction is direct. Interacts with KAT8/MOF; the interaction is direct. Interacts with SBF1 and PPP1R15A By similarity. Component of some MLL1/MLL complex, at least composed of the core components MLL, ASH2L, HCFC1/HCF1, HCFC2, WDR5, DPY30 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Ref.4
Subcellular location	Nucleus By similarity. MLL cleavage product N320: Nucleus By similarity. MLL cleavage product C180: Nucleus By similarity. Note: Localizes to a diffuse nuclear pattern when not associated with MLL cleavage product N320.
Domain	The SET domain structure is atypical and is not in an optimal position to have methyltransferase activity. It requires other components of the MLL1/MLL complex, such as ASH2L or RBBP5, to order the active site and obtain optimal histone methyltransferase activity By similarity. The CXXC-type zinc finger binds bind to nonmethyl-CpG dinucleotides By similarity.
Post-translational modification	Proteolytic cleavage by TASP1 generates MLL cleavage product N320 and MLL cleavage product C180, which reassemble through a non-covalent association. 2 cleavage sites exist, cleavage site 1 (CS1) and cleavage site 2 (CS2), to generate MLL cleavage products N320 and C180. CS2 is the major site By similarity.
Sequence similarities	Belongs to the histone-lysine methyltransferase family. TRX/MLL subfamily. Contains 3 A.T hook DNA-binding domains. Contains 1 bromo domain. Contains 1 CXXC-type zinc finger. Contains 1 FYR C-terminal domain. Contains 1 FYR N-terminal domain. Contains 3 PHD-type zinc fingers. Contains 1 post-SET domain. Contains 1 SET domain.
Sequence caution	The sequence BAE24386.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Bromodomain Repeat Zinc-finger
Ligand	DNA-binding Metal-binding S-adenosyl-L-methionine Zinc
Molecular function	Chromatin regulator Methyltransferase Transferase
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA methylation Inferred from mutant phenotype PubMed 16618927. Source: MGI anterior/posterior pattern specification Inferred from mutant phenotype PubMed 16618927. Source: MGI embryonic hemopoiesis Inferred from mutant phenotype PubMed 9639506. Source: MGI histone H4-K16 acetylation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cell proliferation Inferred from mutant phenotype PubMed 15640349. Source: MGI positive regulation of transcription from RNA polymerase II promoter Inferred from genetic interaction PubMed 15640349. Source: MGI regulation of histone H3-K4 methylation Inferred from mutant phenotype PubMed 16618927. Source: MGI transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	MLL1 complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	chromatin binding Inferred from direct assay PubMed 15640349. Source: MGI histone acetyl-lysine binding Inferred from sequence or structural similarity. Source: UniProtKB histone methyltransferase activity (H3-K4 specific) Inferred from sequence or structural similarity. Source: UniProtKB unmethylated CpG binding Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P55200-1)

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: P55200-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1603-1605: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 3966	3966	Histone-lysine N-methyltransferase MLL		PRO_0000124877
	Chain	1 – 2714	2714	MLL cleavage product N320 By similarity		PRO_0000390951
	Chain	2715 – 3966	1252	MLL cleavage product C180 By similarity		PRO_0000390952
Regions
	Domain	1705 – 1750	46	Bromo; divergent
	Domain	2020 – 2076	57	FYR N-terminal
	Domain	3663 – 3744	82	FYR C-terminal
	Domain	3825 – 3946	122	SET
	Domain	3950 – 3966	17	Post-SET
	DNA binding	167 – 178	12	A.T hook 1
	DNA binding	215 – 225	11	A.T hook 2
	DNA binding	299 – 307	9	A.T hook 3
	Zinc finger	1144 – 1192	49	CXXC-type
	Zinc finger	1430 – 1481	52	PHD-type 1
	Zinc finger	1478 – 1532	55	PHD-type 2
	Zinc finger	1565 – 1629	65	PHD-type 3
	Region	3903 – 3904	2	S-adenosyl-L-methionine binding By similarity
	Compositional bias	14 – 150	137	Gly-rich
	Compositional bias	17 – 100	84	Ala/Gly/Ser-rich
	Compositional bias	80 – 99	20	Ser-rich
	Compositional bias	135 – 141	7	Poly-Gly
	Compositional bias	199 – 287	89	Lys-rich
	Compositional bias	443 – 491	49	Ser-rich
	Compositional bias	559 – 601	43	Pro-rich
	Compositional bias	559 – 562	4	Poly-Pro
	Compositional bias	566 – 569	4	Poly-Pro
	Compositional bias	703 – 807	105	Ser-rich
	Compositional bias	1234 – 1366	133	Pro-rich
	Compositional bias	1819 – 1867	49	Pro-rich
	Compositional bias	2185 – 2320	136	Ser-rich
Sites
	Metal binding	3906	1	Zinc By similarity
	Metal binding	3954	1	Zinc By similarity
	Metal binding	3956	1	Zinc By similarity
	Metal binding	3961	1	Zinc By similarity
	Binding site	3836	1	S-adenosyl-L-methionine By similarity
	Binding site	3838	1	S-adenosyl-L-methionine By similarity
	Binding site	3880	1	S-adenosyl-L-methionine By similarity
	Binding site	3955	1	S-adenosyl-L-methionine By similarity
	Site	2662 – 2663	2	Cleavage; by TASP1, site 1 By similarity
	Site	2714 – 2715	2	Cleavage; by TASP1, site 2 By similarity
	Site	3762	1	Important for WDR5-recognition and binding By similarity
Amino acid modifications
	Modified residue	151	1	Phosphoserine By similarity
	Modified residue	195	1	Phosphoserine By similarity
	Modified residue	516	1	Phosphoserine By similarity
	Modified residue	634	1	N6-acetyllysine By similarity
	Modified residue	678	1	Phosphoserine By similarity
	Modified residue	837	1	Phosphothreonine By similarity
	Modified residue	923	1	Phosphoserine By similarity
	Modified residue	1053	1	Phosphoserine By similarity
	Modified residue	1127	1	N6-acetyllysine By similarity
	Modified residue	1232	1	N6-acetyllysine By similarity
	Modified residue	1847	1	Phosphothreonine By similarity
	Modified residue	1860	1	Phosphoserine By similarity
	Modified residue	2100	1	Phosphoserine By similarity
	Modified residue	2148	1	Phosphothreonine By similarity
	Modified residue	2152	1	Phosphoserine By similarity
	Modified residue	2202	1	Phosphoserine By similarity
	Modified residue	2951	1	Phosphoserine By similarity
	Modified residue	3032	1	Phosphoserine By similarity
	Modified residue	3369	1	Phosphothreonine By similarity
	Modified residue	3510	1	Phosphoserine By similarity
	Cross-link	214		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
	Cross-link	218		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
	Cross-link	219		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Natural variations
	Alternative sequence	1603 – 1605	3	Missing in isoform 2.		VSP_006667
	Natural variant	1597	1	K → T.
Experimental info
	Sequence conflict	372	1	Q → E in BAE28820. Ref.3
	Sequence conflict	554	1	Q → K in AAA62593. Ref.2
	Sequence conflict	564	1	L → F in AAA62593. Ref.2
	Sequence conflict	797	1	P → S in BAE28820. Ref.3
	Sequence conflict	806	1	E → D in AAA62593. Ref.2
	Sequence conflict	806	1	E → D in BAE28820. Ref.3
	Sequence conflict	821	1	L → P in AAA62593. Ref.2
	Sequence conflict	821	1	L → P in BAE28820. Ref.3
	Sequence conflict	1069	1	C → Y in AAA62593. Ref.2
	Sequence conflict	1230	1	A → S in AAA62593. Ref.2
	Sequence conflict	1349	1	R → L in AAA62593. Ref.2
	Sequence conflict	1437	1	A → S in AAA62593. Ref.2
	Sequence conflict	1440	1	G → E in AAA62593. Ref.2
	Sequence conflict	1632	1	A → P in AAA62593. Ref.2
	Sequence conflict	2292	1	S → L in AAA62593. Ref.2
	Sequence conflict	3481	1	N → I in AAA62593. Ref.2
	Sequence conflict	3493	1	R → S in AAA62593. Ref.2
	Sequence conflict	3548	1	G → V in AAA62593. Ref.2
	Sequence conflict	3769	1	Q → K in AAA62593. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: EA9CB2A467AB3545	FASTA	3,966	429,649
	10 20 30 40 50 60 MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRVPALLL PPGPQAGGGG PGAPPSPPAV 70 80 90 100 110 120 AAAAAGSSGA GVPGGAAAAS AASSSSASSS SSSSSSASSG PALLRVGPGF DAALQVSAAI 130 140 150 160 170 180 GTNLRRFRAV FGESGGGGGS GEDEQFLGFG SDEEVRVRSP TRSPSVKASP RKPRGRPRSG 190 200 210 220 230 240 SDRNPAILSD PSVFSPLNKS ETKSADKIKK KDSKSIEKKR GRPPTFPGVK IKITHGKDIA 250 260 270 280 290 300 ELTQGSKEDS LKKVKRTPSA MFQQATKIKK LRAGKLSPLK SKFKTGKLQI GRKGVQIVRR 310 320 330 340 350 360 RGRPPSTERI KTPSGLLINS ELEKPQKVRK DKEGTPPLTK EDKTVVRQSP RRIKPVRIIP 370 380 390 400 410 420 SCKRTDATIA KQLLQRAKKG AQKKIEKEAA QLQGRKVKTQ VKNIRQFIMP VVSAISSRII 430 440 450 460 470 480 KTPRRFIEDE DYDPPMKIAR LESTPNSRFS ATSCGSSEKS SAASQHSSQM SSDSSRSSSP 490 500 510 520 530 540 SIDTTSDSQA SEEIQALPEE RSNTPEVHTP LPISQSPENE SNDRRSRRYS MSERSFGSRA 550 560 570 580 590 600 TKKLPTLQSA PQQQTSSSPP PPLLTPPPPL QPASGISDHT PWLMPPTIPL ASPFLPASAA 610 620 630 640 650 660 PMQGKRKSIL REPTFRWTSL KHSRSEPQYF SSAKYAKEGL IRKPIFDNFR PPPLTPEDVG 670 680 690 700 710 720 FASGFSASGT AASARLFSPL HSGTRFDIHK RSPILRAPRF TPSEAHSRIF ESVTLPSNRT 730 740 750 760 770 780 SSGASSSGVS NRKRKRKVFS PIRSEPRSPS HSMRTRSGRL STSELSPLTP PSSVSSSLSI 790 800 810 820 830 840 PVSPLAASAL NPTFTFPSHS LTQSGESTEK NQRARKQTSA LAEPFSSNSP ALFPWFTPGS 850 860 870 880 890 900 QTEKGRKKDT APEELSKDRD ADKSVEKDKS RERDREREKE NKRESRKEKR KKGSDIQSSS 910 920 930 940 950 960 ALYPVGRVSK EKVAGEDVGT SSSAKKATGR KKSSSLDSGA DVAPVTLGDT TAVKAKILIK 970 980 990 1000 1010 1020 KGRGNLEKNN LDLGPAAPSL EKERTPCLSA PSSSTVKHST SSIGSMLAQA DKLPMTDKRV 1030 1040 1050 1060 1070 1080 ASLLKKAKAQ LCKIEKSKSL KQTDQPKAQG QESDSSETSV RGPRIKHVCR RAAVALGRKR 1090 1100 1110 1120 1130 1140 AVFPDDMPTL SALPWEEREK ILSSMGNDDK SSVAGSEDAE PLAPPIKPIK PVTRNKAPQE 1150 1160 1170 1180 1190 1200 PPVKKGRRSR RCGQCPGCQV PEDCGICTNC LDKPKFGGRN IKKQCCKMRK CQNLQWMPSK 1210 1220 1230 1240 1250 1260 ASLQKQTKAV KKKEKKSKTT EKKESKESTA VKSPLEPAQK AAPPPREEPA PKKSSSEPPP 1270 1280 1290 1300 1310 1320 RKPVEEKSEE GGAPAPAPAP EPKQVSAPAS RKSSKQVSQP AAVVPPQPPS TAPQKKEAPK 1330 1340 1350 1360 1370 1380 AVPSEPKKKQ PPPPEPGPEQ SKQKKVAPRP SIPVKQKPKD KEKPPPVSKQ ENAGTLNILN 1390 1400 1410 1420 1430 1440 PLSNGISSKQ KIPADGVHRI RVDFKEDCEA ENVWEMGGLG ILTSVPITPR VVCFLCASSG 1450 1460 1470 1480 1490 1500 HVEFVYCQVC CEPFHKFCLE ENERPLEDQL ENWCCRRCKF CHVCGRQHQA TKQLLECNKC 1510 1520 1530 1540 1550 1560 RNSYHPECLG PNYPTKPTKK KKVWICTKCV RCKSCGSTTP GKGWDAQWSH DFSLCHDCAK 1570 1580 1590 1600 1610 1620 LFAKGNFCPL CDKCYDDDDY ESKMMQCGKC DRWVHSKCES LSGTEDEMYE ILSNLPESVA 1630 1640 1650 1660 1670 1680 YTCVNCTERH PAEWRLALEK ELQASLKQVL TALLNSRTTS HLLRYRQAAK PPDLNPETEE 1690 1700 1710 1720 1730 1740 SIPSRSSPEG PDPPVLTEVS KQDEQQPLDL EGVKKRMDQG SYVSVLEFSD DIVKIIQAAI 1750 1760 1770 1780 1790 1800 NSDGGQPEIK KANSMVKSFF IRQMERVFPW FSVKKSRFWE PNKVSNNSGM LPNAVLPPSL 1810 1820 1830 1840 1850 1860 DHNYAQWQER EESSHTEQPP LMKKIIPAPK PKGPGEPDSP TPLHPPTPPI LSTDRSREDS 1870 1880 1890 1900 1910 1920 PELNPPPGID DNRQCALCLM YGDDSANDAG RLLYIGQNEW THVNCALWSA EVFEDDDGSL 1930 1940 1950 1960 1970 1980 KNVHMAVIRG KQLRCEFCQK PGATVGCCLT SCTSNYHFMC SRAKNCVFLD DKKVYCQRHR 1990 2000 2010 2020 2030 2040 DLIKGEVVPE NGFEVFRRVF VDFEGISLRR KFLNGLEPEN IHMMIGSMTI DCLGILNDLS 2050 2060 2070 2080 2090 2100 DCEDKLFPIG YQCSRVYWST TDARKRCVYT CKIMECRPPV VEPDINSTVE HDDNRTIAHS 2110 2120 2130 2140 2150 2160 PSSFIDASCK DSQSTAAILS PPSPDRPHSQ TSGSCYYHVI SKVPRIRTPS YSPTQRSPGC 2170 2180 2190 2200 2210 2220 RPLPSAGSPT PTTHEIVTVG DPLLSSGLRS IGSRRHSTSS LSPLRSKLRI MSPVRTGSAY 2230 2240 2250 2260 2270 2280 SRSSVSSVPS LGTATDPEAS AKASDRGGLL SSSANLGHSA PPSSSSQRTV GGSKTSHLDG 2290 2300 2310 2320 2330 2340 SSPSEVKRCS ASDLVPKGSL VKGEKNRTSS SKSTDGSAHS TAYPGIPKLT PQVHNATPGE 2350 2360 2370 2380 2390 2400 LNISKIGSFA EPSTVPFSSK DTVSYPQLHL RGQRSDRDQH MDPSQSVKPS PNEDGEIKTL 2410 2420 2430 2440 2450 2460 KLPGMGHRPS ILHEHIGSSS RDRRQKGKKS SKETCKEKHS SKSYLEPGQV TTGEEGNLKP 2470 2480 2490 2500 2510 2520 EFADEVLTPG FLGQRPCNNV SSEKIGDKVL PLSGVPKGQS TQVEGSSKEL QAPRKCSVKV 2530 2540 2550 2560 2570 2580 TPLKMEGENQ SKNTQKESGP GSPAHIESVC PAEPVSASRS PGAGPGVQPS PNNTLSQDPQ 2590 2600 2610 2620 2630 2640 SNNYQNLPEQ DRNLMIPDGP KPQEDGSFKR RYPRRSARAR SNMFFGLTPL YGVRSYGEED 2650 2660 2670 2680 2690 2700 IPFYSNSTGK KRGKRSAEGQ VDGADDLSTS DEDDLYYYNF TRTVISSGGE ERLASHNLFR 2710 2720 2730 2740 2750 2760 EEEQCDLPKI SQLDGVDDGT ESDTSVTATS RKSSQIPKRN GKENGTENLK IDRPEDAGEK 2770 2780 2790 2800 2810 2820 EHVIKSAVGH KNEPKLDNCH SVSRVKAQGQ DSLEAQLSSL ESSRRVHTST PSDKNLLDTY 2830 2840 2850 2860 2870 2880 NAELLKSDSD NNNSDDCGNI LPSDIMDFVL KNTPSMQALG ESPESSSSEL LTLGEGLGLD 2890 2900 2910 2920 2930 2940 SNREKDIGLF EVFSQQLPAT EPVDSSVSSS ISAEEQFELP LELPSDLSVL TTRSPTVPSQ 2950 2960 2970 2980 2990 3000 NPSRLAVISD SGEKRVTITE KSVASSEGDP ALLSPGVDPA PEGHMTPDHF IQGHMDADHI 3010 3020 3030 3040 3050 3060 SSPPCGSVEQ GHGNSQDLTR NSGTPGLQVP VSPTVPVQNQ KYVPSSTDSP GPSQISNAAV 3070 3080 3090 3100 3110 3120 QTTPPHLKPA TEKLIVVNQN MQPLYVLQTL PNGVTQKIQL TSPVSSTPSV METNTSVLGP 3130 3140 3150 3160 3170 3180 MGSGLTLTTG LNPSLPPSPS LFPPASKGLL SVPHHQHLHS FPAAAQSSFP PNISSPPSGL 3190 3200 3210 3220 3230 3240 LIGVQPPPDP QLLGSEANQR TDLTTTVATP SSGLKKRPIS RLHTRKNKKL APSSAPSNIA 3250 3260 3270 3280 3290 3300 PSDVVSNMTL INFTPSQLSN HPSLLDLGSL NPSSHRTVPN IIKRSKSGIM YFEQAPLLPP 3310 3320 3330 3340 3350 3360 QSVGGTAATA AGSSTISQDT SHLTSGPVSA LASGSSVLNV VSMQTTAAPT SSTSVPGHVT 3370 3380 3390 3400 3410 3420 LANQRLLGTP DIGSISHLLI KASHQSLGIQ DQPVALPPSS GMFPQLGTSQ TPSAAAMTAA 3430 3440 3450 3460 3470 3480 SSICVLPSSQ TAGMTAASPP GEAEEHYKLQ RGNQLLAGKT GTLTSQRDRD PDSAPGTQPS 3490 3500 3510 3520 3530 3540 NFTQTAEAPN GVRLEQNKTL PSAKPASSAS PGSSPSSGQQ SGSSSVPGPT KPKPKAKRIQ 3550 3560 3570 3580 3590 3600 LPLDKGSGKK HKVSHLRTSS EAHIPHRDTD PAPQPSVTRT PRANREQQDA AGVEQPSQKE 3610 3620 3630 3640 3650 3660 CGQPAGPVAA LPEVQATQNP ANEQENAEPK AMEEEESGFS SPLMLWLQQE QKRKESITER 3670 3680 3690 3700 3710 3720 KPKKGLVFEI SSDDGFQICA ESIEDAWKSL TDKVQEARSN ARLKQLSFAG VNGLRMLGIL 3730 3740 3750 3760 3770 3780 HDAVVFLIEQ LAGAKHCRNY KFRFHKPEEA NEPPLNPHGS ARAEVHLRQS AFDMFNFLAS 3790 3800 3810 3820 3830 3840 KHRQPPEYNP NDEEEEEVQL KSARRATSMD LPMPMRFRHL KKTSKEAVGV YRSPIHGRGL 3850 3860 3870 3880 3890 3900 FCKRNIDAGE MVIEYAGNVI RSIQTDKREK YYDSKGIGCY MFRIDDSEVV DATMHGNAAR 3910 3920 3930 3940 3950 3960 FINHSCEPNC YSRVINIDGQ KHIVIFAMRK IYRGEELTYD YKFPIEDASN KLPCNCGAKK CRKFLN
	Isoform 2 [UniParc]. Checksum: 5E5106EB6EF1B932	FASTA	3,963	429,362
	10 20 30 40 50 60 MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRVPALLL PPGPQAGGGG PGAPPSPPAV 70 80 90 100 110 120 AAAAAGSSGA GVPGGAAAAS AASSSSASSS SSSSSSASSG PALLRVGPGF DAALQVSAAI 130 140 150 160 170 180 GTNLRRFRAV FGESGGGGGS GEDEQFLGFG SDEEVRVRSP TRSPSVKASP RKPRGRPRSG 190 200 210 220 230 240 SDRNPAILSD PSVFSPLNKS ETKSADKIKK KDSKSIEKKR GRPPTFPGVK IKITHGKDIA 250 260 270 280 290 300 ELTQGSKEDS LKKVKRTPSA MFQQATKIKK LRAGKLSPLK SKFKTGKLQI GRKGVQIVRR 310 320 330 340 350 360 RGRPPSTERI KTPSGLLINS ELEKPQKVRK DKEGTPPLTK EDKTVVRQSP RRIKPVRIIP 370 380 390 400 410 420 SCKRTDATIA KQLLQRAKKG AQKKIEKEAA QLQGRKVKTQ VKNIRQFIMP VVSAISSRII 430 440 450 460 470 480 KTPRRFIEDE DYDPPMKIAR LESTPNSRFS ATSCGSSEKS SAASQHSSQM SSDSSRSSSP 490 500 510 520 530 540 SIDTTSDSQA SEEIQALPEE RSNTPEVHTP LPISQSPENE SNDRRSRRYS MSERSFGSRA 550 560 570 580 590 600 TKKLPTLQSA PQQQTSSSPP PPLLTPPPPL QPASGISDHT PWLMPPTIPL ASPFLPASAA 610 620 630 640 650 660 PMQGKRKSIL REPTFRWTSL KHSRSEPQYF SSAKYAKEGL IRKPIFDNFR PPPLTPEDVG 670 680 690 700 710 720 FASGFSASGT AASARLFSPL HSGTRFDIHK RSPILRAPRF TPSEAHSRIF ESVTLPSNRT 730 740 750 760 770 780 SSGASSSGVS NRKRKRKVFS PIRSEPRSPS HSMRTRSGRL STSELSPLTP PSSVSSSLSI 790 800 810 820 830 840 PVSPLAASAL NPTFTFPSHS LTQSGESTEK NQRARKQTSA LAEPFSSNSP ALFPWFTPGS 850 860 870 880 890 900 QTEKGRKKDT APEELSKDRD ADKSVEKDKS RERDREREKE NKRESRKEKR KKGSDIQSSS 910 920 930 940 950 960 ALYPVGRVSK EKVAGEDVGT SSSAKKATGR KKSSSLDSGA DVAPVTLGDT TAVKAKILIK 970 980 990 1000 1010 1020 KGRGNLEKNN LDLGPAAPSL EKERTPCLSA PSSSTVKHST SSIGSMLAQA DKLPMTDKRV 1030 1040 1050 1060 1070 1080 ASLLKKAKAQ LCKIEKSKSL KQTDQPKAQG QESDSSETSV RGPRIKHVCR RAAVALGRKR 1090 1100 1110 1120 1130 1140 AVFPDDMPTL SALPWEEREK ILSSMGNDDK SSVAGSEDAE PLAPPIKPIK PVTRNKAPQE 1150 1160 1170 1180 1190 1200 PPVKKGRRSR RCGQCPGCQV PEDCGICTNC LDKPKFGGRN IKKQCCKMRK CQNLQWMPSK 1210 1220 1230 1240 1250 1260 ASLQKQTKAV KKKEKKSKTT EKKESKESTA VKSPLEPAQK AAPPPREEPA PKKSSSEPPP 1270 1280 1290 1300 1310 1320 RKPVEEKSEE GGAPAPAPAP EPKQVSAPAS RKSSKQVSQP AAVVPPQPPS TAPQKKEAPK 1330 1340 1350 1360 1370 1380 AVPSEPKKKQ PPPPEPGPEQ SKQKKVAPRP SIPVKQKPKD KEKPPPVSKQ ENAGTLNILN 1390 1400 1410 1420 1430 1440 PLSNGISSKQ KIPADGVHRI RVDFKEDCEA ENVWEMGGLG ILTSVPITPR VVCFLCASSG 1450 1460 1470 1480 1490 1500 HVEFVYCQVC CEPFHKFCLE ENERPLEDQL ENWCCRRCKF CHVCGRQHQA TKQLLECNKC 1510 1520 1530 1540 1550 1560 RNSYHPECLG PNYPTKPTKK KKVWICTKCV RCKSCGSTTP GKGWDAQWSH DFSLCHDCAK 1570 1580 1590 1600 1610 1620 LFAKGNFCPL CDKCYDDDDY ESKMMQCGKC DRWVHSKCES LSDEMYEILS NLPESVAYTC 1630 1640 1650 1660 1670 1680 VNCTERHPAE WRLALEKELQ ASLKQVLTAL LNSRTTSHLL RYRQAAKPPD LNPETEESIP 1690 1700 1710 1720 1730 1740 SRSSPEGPDP PVLTEVSKQD EQQPLDLEGV KKRMDQGSYV SVLEFSDDIV KIIQAAINSD 1750 1760 1770 1780 1790 1800 GGQPEIKKAN SMVKSFFIRQ MERVFPWFSV KKSRFWEPNK VSNNSGMLPN AVLPPSLDHN 1810 1820 1830 1840 1850 1860 YAQWQEREES SHTEQPPLMK KIIPAPKPKG PGEPDSPTPL HPPTPPILST DRSREDSPEL 1870 1880 1890 1900 1910 1920 NPPPGIDDNR QCALCLMYGD DSANDAGRLL YIGQNEWTHV NCALWSAEVF EDDDGSLKNV 1930 1940 1950 1960 1970 1980 HMAVIRGKQL RCEFCQKPGA TVGCCLTSCT SNYHFMCSRA KNCVFLDDKK VYCQRHRDLI 1990 2000 2010 2020 2030 2040 KGEVVPENGF EVFRRVFVDF EGISLRRKFL NGLEPENIHM MIGSMTIDCL GILNDLSDCE 2050 2060 2070 2080 2090 2100 DKLFPIGYQC SRVYWSTTDA RKRCVYTCKI MECRPPVVEP DINSTVEHDD NRTIAHSPSS 2110 2120 2130 2140 2150 2160 FIDASCKDSQ STAAILSPPS PDRPHSQTSG SCYYHVISKV PRIRTPSYSP TQRSPGCRPL 2170 2180 2190 2200 2210 2220 PSAGSPTPTT HEIVTVGDPL LSSGLRSIGS RRHSTSSLSP LRSKLRIMSP VRTGSAYSRS 2230 2240 2250 2260 2270 2280 SVSSVPSLGT ATDPEASAKA SDRGGLLSSS ANLGHSAPPS SSSQRTVGGS KTSHLDGSSP 2290 2300 2310 2320 2330 2340 SEVKRCSASD LVPKGSLVKG EKNRTSSSKS TDGSAHSTAY PGIPKLTPQV HNATPGELNI 2350 2360 2370 2380 2390 2400 SKIGSFAEPS TVPFSSKDTV SYPQLHLRGQ RSDRDQHMDP SQSVKPSPNE DGEIKTLKLP 2410 2420 2430 2440 2450 2460 GMGHRPSILH EHIGSSSRDR RQKGKKSSKE TCKEKHSSKS YLEPGQVTTG EEGNLKPEFA 2470 2480 2490 2500 2510 2520 DEVLTPGFLG QRPCNNVSSE KIGDKVLPLS GVPKGQSTQV EGSSKELQAP RKCSVKVTPL 2530 2540 2550 2560 2570 2580 KMEGENQSKN TQKESGPGSP AHIESVCPAE PVSASRSPGA GPGVQPSPNN TLSQDPQSNN 2590 2600 2610 2620 2630 2640 YQNLPEQDRN LMIPDGPKPQ EDGSFKRRYP RRSARARSNM FFGLTPLYGV RSYGEEDIPF 2650 2660 2670 2680 2690 2700 YSNSTGKKRG KRSAEGQVDG ADDLSTSDED DLYYYNFTRT VISSGGEERL ASHNLFREEE 2710 2720 2730 2740 2750 2760 QCDLPKISQL DGVDDGTESD TSVTATSRKS SQIPKRNGKE NGTENLKIDR PEDAGEKEHV 2770 2780 2790 2800 2810 2820 IKSAVGHKNE PKLDNCHSVS RVKAQGQDSL EAQLSSLESS RRVHTSTPSD KNLLDTYNAE 2830 2840 2850 2860 2870 2880 LLKSDSDNNN SDDCGNILPS DIMDFVLKNT PSMQALGESP ESSSSELLTL GEGLGLDSNR 2890 2900 2910 2920 2930 2940 EKDIGLFEVF SQQLPATEPV DSSVSSSISA EEQFELPLEL PSDLSVLTTR SPTVPSQNPS 2950 2960 2970 2980 2990 3000 RLAVISDSGE KRVTITEKSV ASSEGDPALL SPGVDPAPEG HMTPDHFIQG HMDADHISSP 3010 3020 3030 3040 3050 3060 PCGSVEQGHG NSQDLTRNSG TPGLQVPVSP TVPVQNQKYV PSSTDSPGPS QISNAAVQTT 3070 3080 3090 3100 3110 3120 PPHLKPATEK LIVVNQNMQP LYVLQTLPNG VTQKIQLTSP VSSTPSVMET NTSVLGPMGS 3130 3140 3150 3160 3170 3180 GLTLTTGLNP SLPPSPSLFP PASKGLLSVP HHQHLHSFPA AAQSSFPPNI SSPPSGLLIG 3190 3200 3210 3220 3230 3240 VQPPPDPQLL GSEANQRTDL TTTVATPSSG LKKRPISRLH TRKNKKLAPS SAPSNIAPSD 3250 3260 3270 3280 3290 3300 VVSNMTLINF TPSQLSNHPS LLDLGSLNPS SHRTVPNIIK RSKSGIMYFE QAPLLPPQSV 3310 3320 3330 3340 3350 3360 GGTAATAAGS STISQDTSHL TSGPVSALAS GSSVLNVVSM QTTAAPTSST SVPGHVTLAN 3370 3380 3390 3400 3410 3420 QRLLGTPDIG SISHLLIKAS HQSLGIQDQP VALPPSSGMF PQLGTSQTPS AAAMTAASSI 3430 3440 3450 3460 3470 3480 CVLPSSQTAG MTAASPPGEA EEHYKLQRGN QLLAGKTGTL TSQRDRDPDS APGTQPSNFT 3490 3500 3510 3520 3530 3540 QTAEAPNGVR LEQNKTLPSA KPASSASPGS SPSSGQQSGS SSVPGPTKPK PKAKRIQLPL 3550 3560 3570 3580 3590 3600 DKGSGKKHKV SHLRTSSEAH IPHRDTDPAP QPSVTRTPRA NREQQDAAGV EQPSQKECGQ 3610 3620 3630 3640 3650 3660 PAGPVAALPE VQATQNPANE QENAEPKAME EEESGFSSPL MLWLQQEQKR KESITERKPK 3670 3680 3690 3700 3710 3720 KGLVFEISSD DGFQICAESI EDAWKSLTDK VQEARSNARL KQLSFAGVNG LRMLGILHDA 3730 3740 3750 3760 3770 3780 VVFLIEQLAG AKHCRNYKFR FHKPEEANEP PLNPHGSARA EVHLRQSAFD MFNFLASKHR 3790 3800 3810 3820 3830 3840 QPPEYNPNDE EEEEVQLKSA RRATSMDLPM PMRFRHLKKT SKEAVGVYRS PIHGRGLFCK 3850 3860 3870 3880 3890 3900 RNIDAGEMVI EYAGNVIRSI QTDKREKYYD SKGIGCYMFR IDDSEVVDAT MHGNAARFIN 3910 3920 3930 3940 3950 3960 HSCEPNCYSR VINIDGQKHI VIFAMRKIYR GEELTYDYKF PIEDASNKLP CNCGAKKCRK FLN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[2]	"Analysis of the murine All-1 gene reveals conserved domains with human ALL-1 and identifies a motif shared with DNA methyltransferases." Ma Q., Alder H., Nelson K.K., Chatterjee D., Gu Y., Nakamura T., Canaani E., Croce C.M., Siracusa L.D., Buchberg A.M. Proc. Natl. Acad. Sci. U.S.A. 90:6350-6354(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 101-3966 (ISOFORMS 1 AND 2). Strain: C57BL/6 X CBA and C57BL/6J. Tissue: Lung and Spleen.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 372-1517 (ISOFORM 1). Strain: C57BL/6J. Tissue: Medulla oblongata and Retina.
[4]	"Role for Dpy-30 in ES cell-fate specification by regulation of H3K4 methylation within bivalent domains." Jiang H., Shukla A., Wang X., Chen W.Y., Bernstein B.E., Roeder R.G. Cell 144:513-525(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN MLL COMPLEX, INTERACTION WITH ASH2L; DPY30; MLL2; RRBP5 AND WDR5.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC061963 Genomic DNA. No translation available. AC142113 Genomic DNA. No translation available. L17069 mRNA. Translation: AAA62593.1. AK140439 mRNA. Translation: BAE24386.1. Different initiation. AK149341 mRNA. Translation: BAE28820.1.
IPI	IPI00315032. IPI01007845.
RefSeq	NP_001074518.1. NM_001081049.1.
UniGene	Mm.2389.
3D structure databases
ProteinModelPortal	P55200.
SMR	P55200. Positions 6-39, 101-133, 1144-1200, 1563-1781, 2836-2865, 3787-3966.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-58597N.
IntAct	P55200. 1 interaction.
PTM databases
PhosphoSite	P55200.
Proteomic databases
PaxDb	P55200.
PRIDE	P55200.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000002095; ENSMUSP00000002095; ENSMUSG00000002028. ENSMUST00000114689; ENSMUSP00000110337; ENSMUSG00000002028.
GeneID	214162.
KEGG	mmu:214162.
UCSC	uc009pep.1. mouse. uc009peq.1. mouse.
Organism-specific databases
CTD	214162.
MGI	MGI:96995. Mll1.
Phylogenomic databases
eggNOG	COG2940.
GeneTree	ENSGT00690000101661.
HOGENOM	HOG000112954.
HOVERGEN	HBG051927.
InParanoid	P55200.
KO	K09186.
OMA	QYFSSAK.
OrthoDB	EOG47H5P3.
Gene expression databases
ArrayExpress	P55200.
Bgee	P55200.
CleanEx	MM_MLL1.
Genevestigator	P55200.
GermOnline	ENSMUSG00000002028. Mus musculus.
Family and domain databases
Gene3D	3.30.40.10. 2 hits.
InterPro	IPR017956. AT_hook_DNA-bd_motif. IPR001487. Bromodomain. IPR003889. FYrich_C. IPR003888. FYrich_N. IPR016569. MeTrfase_trithorax. IPR003616. Post-SET_dom. IPR001214. SET_dom. IPR002857. Znf_CXXC. IPR011011. Znf_FYVE_PHD. IPR001965. Znf_PHD. IPR019787. Znf_PHD-finger. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Pfam	PF05965. FYRC. 1 hit. PF05964. FYRN. 1 hit. PF00628. PHD. 2 hits. PF00856. SET. 1 hit. PF02008. zf-CXXC. 1 hit. [Graphical view]
PIRSF	PIRSF010354. Methyltransferase_trithorax. 1 hit.
SMART	SM00384. AT_hook. 3 hits. SM00297. BROMO. 1 hit. SM00542. FYRC. 1 hit. SM00541. FYRN. 1 hit. SM00249. PHD. 4 hits. SM00508. PostSET. 1 hit. SM00317. SET. 1 hit. [Graphical view]
SUPFAM	SSF47370. Bromodomain. 1 hit. SSF57903. FYVE_PHD_ZnF. 2 hits.
PROSITE	PS00633. BROMODOMAIN_1. False negative. PS50014. BROMODOMAIN_2. 1 hit. PS51543. FYRC. 1 hit. PS51542. FYRN. 1 hit. PS50868. POST_SET. 1 hit. PS50280. SET. 1 hit. PS51058. ZF_CXXC. 1 hit. PS01359. ZF_PHD_1. 3 hits. PS50016. ZF_PHD_2. 3 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	374214.
SOURCE	Search...

Entry information

Entry name

MLL1_MOUSE

Accession

Primary (citable) accession number: P55200
Secondary accession number(s): E9QNE7, Q3UEU1, Q3USE7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	July 27, 2011
Last modified:	April 3, 2013
This is version 123 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program