Reviewed, UniProtKB/Swiss-Prot Q9UMN6 (MLL4_HUMAN)

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
    WW domain-binding protein 7
      Short name=WBP-7
    Trithorax homolog 2
    Lysine N-methyltransferase 2D

Gene names

Name:	WBP7
Synonyms:	HRX2, KIAA0304, KMT2D, MLL2, MLL4, TRX2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	2715 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. Ref.10
Catalytic activity	S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N(6)-methyl-L-lysine. Ref.10
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.
Subcellular location	Nucleus By similarity.
Tissue specificity	Widely expressed. Highest levels in testis. Also found in brain, bone marrow, heart, muscle, kidney, pancreas, spleen, thymus, prostate, ovary, intestine, colon, peripheral blood lymphocytes, and placenta.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR By similarity.
Involvement in disease	Often amplified in pancreatic carcinomas.
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 3 PHD-type zinc fingers. Contains 1 post-SET domain. Contains 1 SET domain.
Caution	This protein was first named MLL2 by Ref.3 and Ref.6. MLL2 corresponds to another protein located on chromosome 12 (see AC O14686).

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
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
Gene Ontology (GO)
Biological process	chromatin-mediated maintenance of transcription Ref.6 Non-traceable author statement. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	histone methyltransferase complex Inferred from electronic annotation. Source: InterPro
Molecular function	protein binding Inferred from physical interaction. Source: IntAct transcription factor activity Ref.6 Non-traceable author statement. Source: UniProtKB zinc ion binding Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ABL1	P00519	1	EBI-765774,EBI-375543
CRK	P46108	1	EBI-765774,EBI-886
FYN	P06241	1	EBI-765774,EBI-515315
GRB2	P62993	1	EBI-765774,EBI-401755
NCK1	P16333	1	EBI-765774,EBI-389883

Alternative products

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

Isoform 1 (identifier: Q9UMN6-1)

Also known as: Long;

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: Q9UMN6-2)

Also known as: Truncated;

The sequence of this isoform differs from the canonical sequence as follows:
     532-582: VSARSSRVIK...VPQEPAPVPS → PLSQSLLLPM...PRCPLTGLQL
     583-2715: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2715	2715	Histone-lysine N-methyltransferase MLL4		PRO_0000124881
Regions
	Domain	2574 – 2695	122	SET
	Domain	2699 – 2715	17	Post-SET
	DNA binding	37 – 44	8	A.T hook 1
	DNA binding	110 – 117	8	A.T hook 2
	DNA binding	357 – 365	9	A.T hook 3
	Zinc finger	959 – 1006	48	CXXC-type
	Zinc finger	1201 – 1252	52	PHD-type 1
	Zinc finger	1249 – 1303	55	PHD-type 2
	Zinc finger	1335 – 1396	62	PHD-type 3
	Compositional bias	26 – 37	12	Poly-Gly
	Compositional bias	248 – 255	8	Poly-Pro
	Compositional bias	362 – 398	37	Asp/Glu-rich (acidic)
	Compositional bias	402 – 771	370	Pro-rich
	Compositional bias	808 – 812	5	Poly-Gln
	Compositional bias	1963 – 1970	8	Poly-Pro
	Compositional bias	2251 – 2259	9	Poly-Pro
Amino acid modifications
	Modified residue	159	1	Phosphothreonine Ref.7
	Modified residue	172	1	Phosphothreonine Ref.11
	Modified residue	176	1	Phosphothreonine Ref.11
	Modified residue	320	1	Phosphoserine By similarity
	Modified residue	821	1	Phosphoserine Ref.11
	Modified residue	844	1	Phosphoserine Ref.11
	Modified residue	861	1	Phosphoserine Ref.8
	Modified residue	926	1	N6-acetyllysine Ref.12
	Modified residue	1032	1	Phosphoserine Ref.11
	Modified residue	1035	1	Phosphoserine Ref.11
	Modified residue	1164	1	Phosphoserine Ref.8
	Modified residue	1930	1	Phosphoserine Ref.11
	Modified residue	1935	1	Phosphothreonine Ref.11
	Modified residue	2296	1	N6-acetyllysine Ref.12
Natural variations
	Alternative sequence	532 – 582	51	VSARS…APVPS → PLSQSLLLPMTLQLSLSLGQ WAAPTTSACLDSPLWSPLLL RPRCPLTGLQL in isoform 2.		VSP_006668
	Alternative sequence	583 – 2715	2133	Missing in isoform 2.		VSP_006669
	Natural variant	587	1	P → R: dbSNP rs2242519.		VAR_046563
	Natural variant	754	1	P → L: dbSNP rs179686.		VAR_046564
	Natural variant	1097	1	P → L: dbSNP rs34014681.		VAR_046565
	Natural variant	1829	1	P → L: dbSNP rs16970649.		VAR_052653
	Natural variant	2364	1	D → G: dbSNP rs231591.		VAR_052654
	Natural variant	2408	1	K → N: dbSNP rs36062432.		VAR_052655
Experimental info
	Sequence conflict	834	1	K → E in AAD17932. Ref.6
	Sequence conflict	941	1	S → Y in AAD17932. Ref.6
	Sequence conflict	1317	1	E → Q in AAD17932. Ref.6
	Sequence conflict	1362	1	H → Y in AAD17932. Ref.6
	Sequence conflict	1438	1	D → N in AAD17932. Ref.6
	Sequence conflict	1918 – 1920	3	PLA → GTR in AAH09337. Ref.5
	Sequence conflict	2622	1	D → H in AAD26112. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) [UniParc]. Last modified May 1, 2000. Version 1. Checksum: C0615B981BBEB7BF	FASTA	2,715	293,515
	10 20 30 40 50 60 MAAAAGGGSC PGPGSARGRF PGRPRGAGGG GGRGGRGNGA ERVRVALRRG GGATGPGGAE 70 80 90 100 110 120 PGEDTALLRL LGLRRGLRRL RRLWAGPRVQ RGRGRGRGRG WGPSRGCVPE EESSDGESDE 130 140 150 160 170 180 EEFQGFHSDE DVAPSSLRSA LRSQRGRAPR GRGRKHKTTP LPPPRLADVA PTPPKTPARK 190 200 210 220 230 240 RGEEGTERMV QALTELLRRA QAPQAPRSRA CEPSTPRRSR GRPPGRPAGP CRRKQQAVVV 250 260 270 280 290 300 AEAAVTIPKP EPPPPVVPVK HQTGSWKCKE GPGPGPGTPR RGGQSSRGGR GGRGRGRGGG 310 320 330 340 350 360 LPFVIKFVSR AKKVKMGQLS LGLESGQGQG QHEESWQDVP QRRVGSGQGG SPCWKKQEQK 370 380 390 400 410 420 LDDEEEEKKE EEEKDKEGEE KEERAVAEEM MPAAEKEEAK LPPPPLTPPA PSPPPPLPPP 430 440 450 460 470 480 STSPPPPLCP PPPPPVSPPP LPSPPPPPAQ EEQEESPPPV VPATCSRKRG RPPLTPSQRA 490 500 510 520 530 540 EREAARAGPE GTSPPTPTPS TATGGPPEDS PTVAPKSTTF LKNIRQFIMP VVSARSSRVI 550 560 570 580 590 600 KTPRRFMDED PPKPPKVEVS PVLRPPITTS PPVPQEPAPV PSPPRAPTPP STPVPLPEKR 610 620 630 640 650 660 RSILREPTFR WTSLTRELPP PPPAPPPPPA PSPPPAPATS SRRPLLLRAP QFTPSEAHLK 670 680 690 700 710 720 IYESVLTPPP LGAPEAPEPE PPPADDSPAE PEPRAVGRTN HLSLPRFAPV VTTPVKAEVS 730 740 750 760 770 780 PHGAPALSNG PQTQAQLLQP LQALQTQLLP QALPPPQPQL QPPPSPQQMP PLEKARIAGV 790 800 810 820 830 840 GSLPLSGVEE KMFSLLKRAK VQLFKIDQQQ QQKVAASMPL SPGGQMEEVA GAVKQISDRG 850 860 870 880 890 900 PVRSEDESVE AKRERPSGPE SPVQGPRIKH VCRHAAVALG QARAMVPEDV PRLSALPLRD 910 920 930 940 950 960 RQDLATEDTS SASETESVPS RSRRGKVEAA GPGGESEPTG SGGTLAHTPR RSLPSHHGKK 970 980 990 1000 1010 1020 MRMARCGHCR GCLRVQDCGS CVNCLDKPKF GGPNTKKQCC VYRKCDKIEA RKMERLAKKG 1030 1040 1050 1060 1070 1080 RTIVKTLLPW DSDESPEASP GPPGPRRGAG AGGPREEVVA HPGPEEQDSL LQRKSARRCV 1090 1100 1110 1120 1130 1140 KQRPSYDIFE DSDDSEPGGP PAPRRRTPRE NELPLPEPEE QSRPRKPTLQ PVLQLKARRR 1150 1160 1170 1180 1190 1200 LDKDALAPGP FASFPNGWTG KQKSPDGVHR VRVDFKEDCD LENVWLMGGL SVLTSVPGGP 1210 1220 1230 1240 1250 1260 PMVCLLCASK GLHELVFCQV CCDPFHPFCL EEAERPLPQH HDTWCCRRCK FCHVCGRKGR 1270 1280 1290 1300 1310 1320 GSKHLLECER CRHAYHPACL GPSYPTRATR KRRHWICSAC VRCKSCGATP GKNWDVEWSG 1330 1340 1350 1360 1370 1380 DYSLCPRCTQ LYEKGNYCPI CTRCYEDNDY ESKMMQCAQC DHWVHAKCEG LSDEDYEILS 1390 1400 1410 1420 1430 1440 GLPDSVLYTC GPCAGAAQPR WREALSGALQ GGLRQVLQGL LSSKVVGPLL LCTQCGPDGK 1450 1460 1470 1480 1490 1500 QLHPGPCGLQ AVSQRFEDGH YKSVHSFMED MVGILMRHSE EGETPDRRAG GQMKGLLLKL 1510 1520 1530 1540 1550 1560 LESAFGWFDA HDPKYWRRST RLPNGVLPNA VLPPSLDHVY AQWRQQEPET PESGQPPGDP 1570 1580 1590 1600 1610 1620 SAAFQGKDPA AFSHLEDPRQ CALCLKYGDA DSKEAGRLLY IGQNEWTHVN CAIWSAEVFE 1630 1640 1650 1660 1670 1680 ENDGSLKNVH AAVARGRQMR CELCLKPGAT VGCCLSSCLS NFHFMCARAS YCIFQDDKKV 1690 1700 1710 1720 1730 1740 FCQKHTDLLD GKEIVNPDGF DVLRRVYVDF EGINFKRKFL TGLEPDAINV LIGSIRIDSL 1750 1760 1770 1780 1790 1800 GTLSDLSDCE GRLFPIGYQC SRLYWSTVDA RRRCWYRCRI LEYRPWGPRE EPAHLEAAEE 1810 1820 1830 1840 1850 1860 NQTIVHSPAP SSEPPGGEDP PLDTDVLVPG APERHSPIQN LDPPLRPDSG SAPPPAPRSF 1870 1880 1890 1900 1910 1920 SGARIKVPNY SPSRRPLGGV SFGPLPSPGS PSSLTHHIPT VGDPDFPAPP RRSRRPSPLA 1930 1940 1950 1960 1970 1980 PRPPPSRWAS PPLKTSPQLR VPPPTSVVTA LTPTSGELAP PGPAPSPPPP EDLGPDFEDM 1990 2000 2010 2020 2030 2040 EVVSGLSAAD LDFAASLLGT EPFQEEIVAA GAMGSSHGGP GDSSEEESSP TSRYIHFPVT 2050 2060 2070 2080 2090 2100 VVSAPGLAPS ATPGAPRIEQ LDGVDDGTDS EAEAVQQPRG QGTPPSGPGV VRAGVLGAAG 2110 2120 2130 2140 2150 2160 DRARPPEDLP SEIVDFVLKN LGGPGDGGAG PREESLPPAP PLANGSQPSQ GLTASPADPT 2170 2180 2190 2200 2210 2220 RTFAWLPGAP GVRVLSLGPA PEPPKPATSK IILVNKLGQV FVKMAGEGEP VPPPVKQPPL 2230 2240 2250 2260 2270 2280 PPTISPTAPT SWTLPPGPLL GVLPVVGVVR PAPPPPPPPL TLVLSSGPAS PPRQAIRVKR 2290 2300 2310 2320 2330 2340 VSTFSGRSPP APPPYKAPRL DEDGEASEDT PQVPGLGSGG FSRVRMKTPT VRGVLDLDRP 2350 2360 2370 2380 2390 2400 GEPAGEESPG PLQERSPLLP LPEDGPPQVP DGPPDLLLES QWHHYSGEAS SSEEEPPSPD 2410 2420 2430 2440 2450 2460 DKENQAPKRT GPHLRFEISS EDGFSVEAES LEGAWRTLIE KVQEARGHAR LRHLSFSGMS 2470 2480 2490 2500 2510 2520 GARLLGIHHD AVIFLAEQLP GAQRCQHYKF RYHQQGEGQE EPPLNPHGAA RAEVYLRKCT 2530 2540 2550 2560 2570 2580 FDMFNFLASQ HRVLPEGATC DEEEDEVQLR STRRATSLEL PMAMRFRHLK KTSKEAVGVY 2590 2600 2610 2620 2630 2640 RSAIHGRGLF CKRNIDAGEM VIEYSGIVIR SVLTDKREKF YDGKGIGCYM FRMDDFDVVD 2650 2660 2670 2680 2690 2700 ATMHGNAARF INHSCEPNCF SRVIHVEGQK HIVIFALRRI LRGEELTYDY KFPIEDASNK 2710 LPCNCGAKRC RRFLN
	Isoform 2 (Truncated). Checksum: 8B2EE4B04969CF76	FASTA	582	61,562
	10 20 30 40 50 60 MAAAAGGGSC PGPGSARGRF PGRPRGAGGG GGRGGRGNGA ERVRVALRRG GGATGPGGAE 70 80 90 100 110 120 PGEDTALLRL LGLRRGLRRL RRLWAGPRVQ RGRGRGRGRG WGPSRGCVPE EESSDGESDE 130 140 150 160 170 180 EEFQGFHSDE DVAPSSLRSA LRSQRGRAPR GRGRKHKTTP LPPPRLADVA PTPPKTPARK 190 200 210 220 230 240 RGEEGTERMV QALTELLRRA QAPQAPRSRA CEPSTPRRSR GRPPGRPAGP CRRKQQAVVV 250 260 270 280 290 300 AEAAVTIPKP EPPPPVVPVK HQTGSWKCKE GPGPGPGTPR RGGQSSRGGR GGRGRGRGGG 310 320 330 340 350 360 LPFVIKFVSR AKKVKMGQLS LGLESGQGQG QHEESWQDVP QRRVGSGQGG SPCWKKQEQK 370 380 390 400 410 420 LDDEEEEKKE EEEKDKEGEE KEERAVAEEM MPAAEKEEAK LPPPPLTPPA PSPPPPLPPP 430 440 450 460 470 480 STSPPPPLCP PPPPPVSPPP LPSPPPPPAQ EEQEESPPPV VPATCSRKRG RPPLTPSQRA 490 500 510 520 530 540 EREAARAGPE GTSPPTPTPS TATGGPPEDS PTVAPKSTTF LKNIRQFIMP VPLSQSLLLP 550 560 570 580 MTLQLSLSLG QWAAPTTSAC LDSPLWSPLL LRPRCPLTGL QL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mammalian trithorax- and ASH1-like proteins: putative chromatin regulators which contain PHD fingers and SET domains." Angrand P.-O., Valvatne H., Jeanmougin F., Adamson A., van der Hoeven F., Olsen L., Tekotte H., Huang N., Poch O., Lamerdin J., Chambon P., Losson R., Stewart A., Aasland R. Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed: 15057824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"MLL2, the second human homolog of the Drosophila trithorax gene, maps to 19q13.1 and is amplified in solid tumor cell lines." Huntsman D.G., Chin S.-F., Muleris M., Batley S.J., Collins V.P., Wiedemann L.M., Aparicio S., Caldas C. Oncogene 18:7975-7984(1999) [PubMed: 10637508] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 111-2715 (ISOFORM 1). Tissue: Leukocyte and Testis.
[4]	"Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 4:141-150(1997) [PubMed: 9205841] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 301-2715 (ISOFORM 1). Tissue: Brain.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1918-2715. Tissue: Brain and Skin.
[6]	"MLL2: a new mammalian member of the trx/MLL family of genes." FitzGerald K.T., Diaz M.O. Genomics 59:187-192(1999) [PubMed: 10409430] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Tissue: Bone marrow and Placenta.
[7]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-159, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"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 SER-861 AND SER-1164, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing." De Santa F., Totaro M.G., Prosperini E., Notarbartolo S., Testa G., Natoli G. Cell 130:1083-1094(2007) [PubMed: 17825402] [Abstract] Cited for: IDENTIFICATION IN THE PTIP COMPLEX.
[10]	"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.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-172; THR-176; SER-821; SER-844; SER-1032; SER-1035; SER-1930 AND THR-1935, MASS SPECTROMETRY.
[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-926 AND LYS-2296, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ007041 mRNA. Translation: CAB45385.1. AD000671 Genomic DNA. No translation available. AF186605 mRNA. Translation: AAD56420.1. AB002302 mRNA. Translation: BAA20763.3. BC009337 mRNA. Translation: AAH09337.2. BC007353 mRNA. Translation: AAH07353.3. AF104918 mRNA. Translation: AAD17932.1. AF105279 mRNA. Translation: AAD26113.1. AF105280 mRNA. Translation: AAD26112.1.
IPI	IPI00218823. IPI00220925.
RefSeq	NP_055542.1.
UniGene	Hs.676457 Hs.92236
3D structure databases
HSSP	HSSP built from PDB template 1MM2 based on UniProtKB Q14839.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UMN6. 8 interactions.
STRING	Q9UMN6.
PTM databases
PhosphoSite	Q9UMN6.
Proteomic databases
PRIDE	Q9UMN6.
Genome annotation databases
Ensembl	ENST00000222270; ENSP00000222270; ENSG00000105663; Homo sapiens. [Genome view] ENST00000341701; ENSP00000345761; ENSG00000105663; Homo sapiens. [Genome view] ENST00000396924; ENSP00000380130; ENSG00000105663; Homo sapiens. [Genome view] ENST00000420124; ENSP00000398837; ENSG00000105663; Homo sapiens. [Genome view]
GeneID	9757.
KEGG	hsa:9757.
Organism-specific databases
CTD	9757.
GeneCards	GC19P040900.
H-InvDB	HIX0015036.
HPA	HPA006487.
MIM	606834. gene.
HUGE	Search...
Phylogenomic databases
HOVERGEN	Q9UMN6.
OMA	EEFQGFH.
Gene expression databases
ArrayExpress	Q9UMN6.
Bgee	Q9UMN6.
CleanEx	HS_MLL2.
Genevestigator	Q9UMN6.
GermOnline	ENSG00000105663. Homo sapiens.
Family and domain databases
InterPro	IPR017956. AT_hook_DNA-bd_motif. IPR003889. FYrich_C. IPR018516. FYrich_C_sg. IPR003888. FYrich_N. IPR018518. FYrich_N_sg. IPR016569. MeTrfase_trithorax. IPR015722. MLL. IPR003616. Post-SET_Zn_bd. IPR001214. SET. IPR019786. Zinc_finger_PHD-type_CS. IPR002857. Znf_CXXC. IPR001965. Znf_PHD. IPR019787. Znf_PHD-finger. [Graphical view]
PANTHER	PTHR22884:SF10. MLL. 1 hit.
Pfam	PF02178. AT_hook. 1 hit. PF05965. FYRC. 1 hit. PF05964. FYRN. 1 hit. PF00628. PHD. 3 hits. PF00856. SET. 1 hit. PF02008. zf-CXXC. 1 hit. [Graphical view]
PIRSF	PIRSF010354. Methyltransferase_trithorax. 1 hit.
SMART	SM00384. AT_hook. 5 hits. SM00542. FYRC. 1 hit. SM00541. FYRN. 1 hit. SM00249. PHD. 4 hits. SM00508. PostSET. 1 hit. SM00317. SET. 1 hit. [Graphical view]
PROSITE	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 Resources
NextBio	36724.
SOURCE	Search...

Entry information

Entry name

MLL4_HUMAN

Accession

Primary (citable) accession number: Q9UMN6
Secondary accession number(s): O15022 , O95836, Q96GP2, Q96IP3, Q9UK25, Q9Y668, Q9Y669

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.