Histone-lysine N-methyltransferase MLL4

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O08550 (MLL4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 94. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Histone-lysine N-methyltransferase MLL4
EC=2.1.1.43

Alternative name(s):
Myeloid/lymphoid or mixed-lineage leukemia protein 4 homolog
Trithorax homolog 2
WW domain-binding protein 7
Short name=WBP-7

Gene names

Name:	Wbp7
Synonyms:	Mll2, Trx2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	2713 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. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation By similarity.
Catalytic activity	S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
Subunit structure	Component of the MLL3/MLL4 complex, at least composed of MLL3, MLL4, ASH2L, RBBP5, DPY30, WDR5, NCOA6, KDM6A (or KDM6B), PAXIP1/PTIP and C16orf53/PA1 By similarity.
Subcellular location	Nucleus By similarity.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.4 Ref.5
Sequence similarities	Belongs to the histone-lysine methyltransferase family. TRX/MLL subfamily. Contains 3 A.T hook DNA-binding domains. 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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding S-adenosyl-L-methionine Zinc
Molecular function	Chromatin regulator Methyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	histone methyltransferase complex Inferred from direct assay. Source: MGI
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW histone methyltransferase activity (H3-K4 specific) Inferred from direct assay. Source: MGI zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 2713

2712

Histone-lysine N-methyltransferase MLL4

PRO_0000124882

Regions

Domain

1733 – 1789

FYR N-terminal

Domain

2409 – 2490

FYR C-terminal

Domain

2572 – 2693

122

SET

Domain

2697 – 2713

Post-SET

DNA binding

37 – 44

A.T hook 1

DNA binding

110 – 117

A.T hook 2

DNA binding

357 – 365

A.T hook 3

Zinc finger

964 – 1011

CXXC-type

Zinc finger

1207 – 1258

PHD-type 1

Zinc finger

1255 – 1309

PHD-type 2

Zinc finger

1341 – 1402

PHD-type 3

Region

2650 – 2651

S-adenosyl-L-methionine binding By similarity

Compositional bias

6 – 106

101

Gly-rich

Compositional bias

272 – 300

Gly-rich

Compositional bias

347 – 410

Glu-rich

Compositional bias

414 – 776

363

Pro-rich

Compositional bias

1814 – 2296

483

Pro-rich

Sites

Metal binding

2653

Zinc By similarity

Metal binding

2701

Zinc By similarity

Metal binding

2703

Zinc By similarity

Metal binding

2708

Zinc By similarity

Binding site

2583

S-adenosyl-L-methionine By similarity

Binding site

2585

S-adenosyl-L-methionine By similarity

Binding site

2627

S-adenosyl-L-methionine By similarity

Binding site

2702

S-adenosyl-L-methionine By similarity

Amino acid modifications

Modified residue

N-acetylalanine By similarity

Modified residue

159

Phosphothreonine By similarity

Modified residue

320

Phosphoserine Ref.5

Modified residue

826

Phosphoserine By similarity

Modified residue

849

Phosphoserine By similarity

Modified residue

866

Phosphoserine By similarity

Modified residue

931

N6-acetyllysine By similarity

Modified residue

1037

Phosphoserine By similarity

Modified residue

1040

Phosphoserine By similarity

Modified residue

1170

Phosphoserine By similarity

Modified residue

1926

Phosphoserine By similarity

Modified residue

1927

Phosphoserine Ref.4

Modified residue

1931

Phosphothreonine By similarity

Modified residue

2079

Phosphothreonine By similarity

Modified residue

2294

N6-acetyllysine By similarity

Experimental info

Sequence conflict

G → V in BAD81031. Ref.1

Sequence conflict

25 – 27

RGS → LGC in BAD81031. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

O08550 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 2AD4343C5C081933
Show »

FASTA

2,713

294,821

        10         20         30         40         50         60 
MAAAAGGGSC PGPGSARGRF PGRPRGSGGG GGRGGRGNGA ERVRVALRRG GGAAGPGGAE 

        70         80         90        100        110        120 
PGEDTALLRL LGLRRGLRRL RRLWAGARVQ RGRGRGRGRG WGPNRGCMPE EESSDGESEE 

       130        140        150        160        170        180 
EEFQGFHSDE DVAPSSLRSA LRSQRGRAPR GRGRKHKTTP LPPRLADVTP VPPKAPTRKR 

       190        200        210        220        230        240 
GEEGTERMVQ ALTELLRRSQ APQPPRSRAR AREPSTPRRS RGRPPGRPAG PCRKKQQAVV 

       250        260        270        280        290        300 
LAEAAVTIPK PEPPPPVVPV KNKAGSWKCK EGPGPGPGTP KRGGQPGRGG RGGRGRGRGG 

       310        320        330        340        350        360 
LPLMIKFVSK AKKVKMGQLS QELESGQGHG QRGESWQDAP QRKDGDEPER GSCRKKQEQK 

       370        380        390        400        410        420 
LEEEEEEEEK EGEEKEEKDD NEDNNKQEEE EETERAVAEE EAMLAKEKEE AKLPSPPLTP 

       430        440        450        460        470        480 
PVPSPPPPLP PPSTSPPPPA SPLPPPVSPP PPLSPPPYPA PEKQEESPPL VPATCSRKRG 

       490        500        510        520        530        540 
RPPLTPSQRA EREAARSGPE GTLSPTPNPS TTTGSPLEDS PTVVPKSTTF LKNIRQFIMP 

       550        560        570        580        590        600 
VVSARSSRVI KTPRRFMDED PPKPPKVEAS IVRPPVATSP PAPQEPVPVS SPPRVPTPPS 

       610        620        630        640        650        660 
TPVPLPEKRR SILREPTFRW TSLTRELPPP PPAPPPAPSP PPAPATPSRR PLLLRAPQFT 

       670        680        690        700        710        720 
PSEAHLKIYE SVLTPPPLGA LETPEPELPP ADDSPAEPEP RAVGRTNHLS LPRFVPVVTS 

       730        740        750        760        770        780 
PVKVEVPPHG APALSEGQQL QLQQPPQALQ TQLLPQALPP QQPQAQPPPS PQHTPPLEKA 

       790        800        810        820        830        840 
RVASLGSLPL SGVEEKMFSL LKRAKVQLFK IDQQQQQKVA ASMPLSPAVQ TEEAVGTVKQ 

       850        860        870        880        890        900 
TPDRGCVRSE DESMEAKRDR ASGPESPLQG PRIKHVCRHA AVALGQARAM VPEDVPRLSA 

       910        920        930        940        950        960 
LPLRDRQDLA TEDTSSASET ESVPSRSQRE KVESAGPGGD SEPTGSTGAL AHTPRRSLPS 

       970        980        990       1000       1010       1020 
HHGKKMRMAR CGHCRGCLRV QDCGSCVNCL DKPKFGGPNT KKQCCVYRKC DKIEARKMER 

      1030       1040       1050       1060       1070       1080 
LAKKGRTIVK TLLPWDSDES PEASPGPPGP RRGAGAGGSR EEVGATPGPE EQDSLLLQRK 

      1090       1100       1110       1120       1130       1140 
SARRCVKQRP SYDVFEDSDD SEPGGPPAPR RRTPREHELP VLEPEEQSRP RKPTLQPVLQ 

      1150       1160       1170       1180       1190       1200 
LKARRRLDKD ALAPGPFASF PNGWTGKQKS PDGVHRVRVD FKEDCDLENV WLMGGLSVLT 

      1210       1220       1230       1240       1250       1260 
SVPGGPPMVC LLCASKGLHE LVFCQVCCDP FHPFCLEEAE RPSPQHRDTW CCRRCKFCHV 

      1270       1280       1290       1300       1310       1320 
CGRKGRGSKH LLECERCRHA YHPACLGPSY PTRATRRRRH WICSACVRCK SCGATPGKNW 

      1330       1340       1350       1360       1370       1380 
DVEWSGDYSL CPRCTELYEK GNYCPICTRC YEDNDYESKM MQCAQCDHWV HAKCEGLSDE 

      1390       1400       1410       1420       1430       1440 
DYEILSGLPD SVLYTCGPCA GATQPRWREA LSGALQGGLR QVLQGLLSSK VAGPLLLCTQ 

      1450       1460       1470       1480       1490       1500 
CGQDGKQLHP GPCDLQAVGK RFEEGLYKSV HSFMEDVVAI LMRHSEEGET PERRAGSQMK 

      1510       1520       1530       1540       1550       1560 
GLLLKLLESA FCWFDAHDPK YWRRSTRLPN GVLPNAVLPP SLDHVYAQWR QQESETPESG 

      1570       1580       1590       1600       1610       1620 
QPPGDPSAAF QSKDPAAFSH LDDPRQCALC LKYGDADSKE AGRLLYIGQN EWTHVNCAIW 

      1630       1640       1650       1660       1670       1680 
SAEVFEENDG SLKNVHAAVA RGRQMRCELC LKPGATVGCC LSSCLSNFHF MCARASYCIF 

      1690       1700       1710       1720       1730       1740 
QDDKKVFCQK HTDLLDGKEI VTPDGFDVLR RVYVDFEGIN FKRKFLTGLE PDVINVLIGS 

      1750       1760       1770       1780       1790       1800 
IRINSLGTLS DLSDCEGRLF PIGYQCSRLY WSTVDARRRC WYRCRILEYR PWGPREEPVH 

      1810       1820       1830       1840       1850       1860 
LEAAEENQTI VHSPTPSSDT DSLIPGDPVH HSPIQNLDPP LRTDSSNGPP PTPRSFSGAR 

      1870       1880       1890       1900       1910       1920 
IKVPNYSPSR RPLGGVSFGP LPSPGSPSSL THHIPTVGDS DFPAPPRRSR RPSPLATRPP 

      1930       1940       1950       1960       1970       1980 
PSRRTSSPLR TSPQLRVPLS TSVTALTPTS GELAPPDLAP SPLPPSEDLG PDFEDMEVVS 

      1990       2000       2010       2020       2030       2040 
GLSAADLDFA ASLLGTEPFQ EEIVAAGAVG SSQGGPGDSS EEEASPTTHY VHFPVTVVSG 

      2050       2060       2070       2080       2090       2100 
PALAPSSLAG APRIEQLDGV DDGTDSEAEA VQQPRGQGTP PSGPGVGRGG VLGAAGDRAQ 

      2110       2120       2130       2140       2150       2160 
PPEDLPSEIV DFVLKNLGGP GEGAAGPRED SLPSAPPLAN GSQPPQSLST SPADPTRTFA 

      2170       2180       2190       2200       2210       2220 
WLPGAPGVRV LSLGPAPEPP KPATSKIILV NKLGQVFVKM AGEGEPVAPP VKQPPLPPII 

      2230       2240       2250       2260       2270       2280 
PPTAPTSWTL PPGPLLSVLP VVGVGVVRPA PPPPPPPLTL VFSSGPPSPP RQAIRVKRVS 

      2290       2300       2310       2320       2330       2340 
TFSGRSPPVP PPNKTPRLDE DGESLEDAHH VPGISGSGFS RVRMKTPTVR GVLDLNNPGE 

      2350       2360       2370       2380       2390       2400 
QPEEESPGRP QDRCPLLPLA EAPSQALDGS SDLLFESQWH HYSAGEASSS EEEPPSPEDK 

      2410       2420       2430       2440       2450       2460 
ENQVPKRVGP HLRFEISSDD GFSVEAESLE VAWRTLIEKV QEARGHARLR HLSFSGMSGA 

      2470       2480       2490       2500       2510       2520 
RLLGIHHDAV IFLAEQLPGA QRCQHYKFRY HQQGEGQEEP PLNPHGAARA EVYLRKCTFD 

      2530       2540       2550       2560       2570       2580 
MFNFLASQHR VLPEGATCDE EEDEVQLRST RRATSLELPM AMRFRHLKKT SKEAVGVYRS 

      2590       2600       2610       2620       2630       2640 
AIHGRGLFCK RNIDAGEMVI EYSGIVIRSV LTDKREKFYD GKGIGCYMFR MDDFDVVDAT 

      2650       2660       2670       2680       2690       2700 
MHGNAARFIN HSCEPNCFSR VIHVEGQKHI VIFALRRILR GEELTYDYKF PIEDASNKLP 

      2710 
CNCGAKRCRR FLN

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Murine MLL2 gene and its expression." Yoshida K. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6.
[3]	"FBP WW domains and the Abl SH3 domain bind to a specific class of proline-rich ligands." Bedford M.T., Chan D.C., Leder P. EMBO J. 16:2376-2383(1997) [PubMed: 9171351] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 379-657.
[4]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1927, MASS SPECTROMETRY. Tissue: Liver.
[5]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, MASS SPECTROMETRY. Tissue: Embryonic kidney.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB182318 mRNA. Translation: BAD81031.1. AC167970 Genomic DNA. No translation available. U92455 mRNA. Translation: AAC53192.1. Sequence problems.
IPI	IPI00229651.
RefSeq	NP_083550.2. NM_029274.2.
UniGene	Mm.168688.
3D structure databases
ProteinModelPortal	O08550.
SMR	O08550. Positions 964-1014, 1360-1399, 2539-2713.
ModBase	Search...
Proteomic databases
PRIDE	O08550.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000108154; ENSMUSP00000103789; ENSMUSG00000006307.
GeneID	75410.
KEGG	mmu:75410.
UCSC	uc009gff.1. mouse.
Organism-specific databases
CTD	75410.
MGI	MGI:109565. Wbp7.
Phylogenomic databases
HOVERGEN	HBG100043.
OrthoDB	EOG43XV2J.
Gene expression databases
ArrayExpress	O08550.
Bgee	O08550.
CleanEx	MM_WBP7.
Genevestigator	O08550.
GermOnline	ENSMUSG00000006307. Mus musculus.
Family and domain databases
InterPro	IPR017956. AT_hook_DNA-bd_motif. IPR003889. FYrich_C. IPR018516. FYrich_C_subgr. IPR003888. FYrich_N. IPR018518. FYrich_N_subgr. 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]
Gene3D	G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 2 hits.
KO	K14959.
Pfam	PF05965. FYRC. 1 hit. PF05964. FYRN. 1 hit. PF00628. PHD. 2 hits. PF00856. SET. 1 hit. PF02008. zf-CXXC. 1 hit. [Graphical view]
SMART	SM00384. AT_hook. 4 hits. SM00542. FYRC. 1 hit. SM00541. FYRN. 1 hit. SM00249. PHD. 4 hits. SM00508. PostSET. 1 hit. SM00317. SET. 1 hit. [Graphical view]
SUPFAM	SSF57903. FYVE_PHD_ZnF. 2 hits.
PROSITE	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	342938.
SOURCE	Search...

Entry information

Entry name

MLL4_MOUSE

Accession

Primary (citable) accession number: O08550
Secondary accession number(s): E9QKF4, Q5NU09

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	July 27, 2011
Last modified:	November 16, 2011
This is version 94 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents