Reviewed, UniProtKB/Swiss-Prot Q3UG20 (MLL5_MOUSE)

Names and origin

Protein names

Recommended name:
    Histone-lysine N-methyltransferase MLL5
    EC=2.1.1.43
Alternative name(s):
    Myeloid/lymphoid or mixed-lineage leukemia protein 5 homolog

Gene names

Name:

Mll5

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

Protein attributes

Sequence length	1868 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Histone methyltransferase that specifically mono- and dimethylates 'Lys-4' of histone H3 (H3K4me1 and H3K4me2). H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Key regulator of hematopoiesis involved in terminal myeloid differentiation and in the regulation of hematopoietic stem cell (HSCs) self-renewal by a mechanism that involves DNA methylation. Plays an essential role in retinoic-acid-induced granulopoiesis by acting as a coactivator of RAR-alpha (RARA) in target gene promoters. Also acts as an important cell cycle regulator, participating in cell cycle regulatory network machinery at multiple cell cycle stages. Required to suppress inappropriate expression of S-phase-promoting genes and maintain expression of determination genes in quiescent cells. Overexpression inhibits cell cycle progression, while knockdown induces cell cycle arrest at both the G1 and G2/M phases. Ref.5 Ref.6 Ref.7 Ref.8
Catalytic activity	S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
Subunit structure	Component of the MLL5-L complex, at least composed of MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with RARA By similarity.
Subcellular location	Nucleus speckle By similarity. Note: Absent from the nucleolus By similarity. UniProtKB Q8IZD2
Induction	Up-regulated in reversibly arrested C2C12 myoblasts. Ref.4
Post-translational modification	O-glycosylation at Thr-440 in the SET domain by OGT is essential for the histone methyltransferase and the coactivator activity toward RARA in granulopoiesis By similarity. The absence of Thr-440 glycosylation in assays done in vitro may explain why Ref.6 and Ref.8 did not detected any histone methyltransferase activity for this protein.
Disruption phenotype	Defects in immunity and hematopoiesis. Adult homozygous mice are obtained at reduced frequency because of postnatal lethality. Surviving animals display a variety of abnormalities, including male infertility, retarded growth and defects in multiple hematopoietic lineages. They also show increased susceptibility to spontaneous eye infections associated with a cell-autonomous impairment of neutrophil function. They exhibit a mild impairment of erythropoiesis and hematopoietic stem cells (HSCs) have impaired competitive repopulating capacity both under normal conditions and when subjected to self-renewal stimulation by NUP98-HOXA10. Homozygous HSCs show a dramatic sensitivity to DNA demethylation-induced differentiation (5-azadeoxycytidine). Ref.5 Ref.6 Ref.7
Sequence similarities	Belongs to the histone-lysine methyltransferase family. TRX/MLL subfamily. Contains 1 PHD-type zinc finger. Contains 1 SET domain.
Sequence caution	The sequence AAH36286.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence starting in position 486. The sequence AAH64079.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence starting in position 803. The sequence AAH89356.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence starting in position 495. The sequence AAI03802.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence starting in position 492. The sequence BAE28389.1 differs from that shown. Reason: Frameshift at position 12.

Ontologies

Keywords
Biological process	Cell cycle Growth arrest Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding S-adenosyl-L-methionine Zinc
Molecular function	Chromatin regulator Methyltransferase Transferase
PTM	Glycoprotein Phosphoprotein
Gene Ontology (GO)
Biological process	DNA methylation Ref.5 Inferred from mutant phenotype. Source: UniProtKB cell cycle arrest Inferred from electronic annotation. Source: UniProtKB-KW erythrocyte differentiation Ref.5 Inferred from mutant phenotype. Source: UniProtKB histone methylation Inferred from sequence or structural similarity. Source: UniProtKB neutrophil activation Ref.5 Inferred from mutant phenotype. Source: UniProtKB neutrophil mediated immunity Ref.5 Inferred from mutant phenotype. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB response to retinoic acid Inferred from sequence or structural similarity. Source: UniProtKB retinoic acid receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	MLL5-L complex Inferred from sequence or structural similarity. Source: UniProtKB nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	histone methyltransferase activity (H3-K4 specific) Inferred from sequence or structural similarity. Source: UniProtKB transcription coactivator activity Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

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

Isoform 1 Ref.2 Ref.3 (identifier: Q3UG20-1)

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.

Note: No experimental confirmation available.

Isoform 2 Ref.2 (identifier: Q3UG20-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-580: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1868	1868	Histone-lysine N-methyltransferase MLL5		PRO_0000341420
Regions
	Domain	328 – 451	124	SET
	Zinc finger	118 – 166	49	PHD-type
	Coiled coil	559 – 613	55	Potential
	Compositional bias	1549 – 1856	308	Pro-rich
Amino acid modifications
	Modified residue	1410	1	Phosphoserine By similarity UniProtKB Q8IZD2
	Glycosylation	440	1	O-linked (GalNAc...) By similarity
Natural variations
	Alternative sequence	1 – 580	580	Missing in isoform 2. Ref.2		VSP_052813
Experimental info
	Mutagenesis	411	1	C → A: Unable to repress cell-cycle-regulated element. Ref.8
	Sequence conflict	62	1	A → S in BAE43262. Ref.2
	Sequence conflict	181	1	R → I in BAE28389. Ref.2
	Sequence conflict	320	1	E → G in BAE28389. Ref.2
	Sequence conflict	489	1	R → S in BAB25186. Ref.2
	Sequence conflict	512	1	D → Y in BAC28936. Ref.2
	Sequence conflict	550	1	E → G in BAE35839. Ref.2
	Sequence conflict	562	1	E → G in BAE28389. Ref.2
	Sequence conflict	1005	1	S → R in BAC28936. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 10, 2008. Version 2. Checksum: B676F509E965415C	FASTA	1,868	204,543
	10 20 30 40 50 60 MSIAIPLGVD TTETSYLEMA AGSEPESVEA SPVVVEKSNS FPHQLYTSSS HHSHSYIGLP 70 80 90 100 110 120 YADHNYGARP PPTPPASPPP SGLISKNEVG IFTTPNFDET SSATTISTSE DGSYGTDVTR 130 140 150 160 170 180 CICGFTHDDG YMICCDKCSV WQHIDCMGID RQHIPDTYLC ERCQPRSLDK ERAVLLQRRK 190 200 210 220 230 240 RENMSDGDTS ATESGDEVPV ELYTAFQHTP TSITLTASRV PKVTDKRRKK SGEKEQNFSK 250 260 270 280 290 300 CKKAFREGSR KSSRVKGSAP EIDPSSDSSN FVWETKIKAW MDRYEEANNN QYSEGVQREA 310 320 330 340 350 360 QRLAQRLGSG NDSKDMNKSE LSTNNSLFRP PVESHIQKNK KILKSAKDLP PDALIIEYRG 370 380 390 400 410 420 KFMLREQFEA NGYFFKRPYP FVLFYSKFHG LEMCVDARTF GNEARFIRRS CTPNAEVRHE 430 440 450 460 470 480 IEEGTIHLYI YSIQSIPKGT EITIAFDFDY GNCKYKVDCA CLKENPECPV LKRSSESTEN 490 500 510 520 530 540 INSGYETRRK KGKKEKDTSK EKDIQNQNMT LDCEGTNNKI RSPETKQRKL SPLRLSVSNN 550 560 570 580 590 600 QEPDFIDDME EKTPISNEVE MESEEQIAER KRKMTREERK MEAILQAFAR LEKREKRREQ 610 620 630 640 650 660 ALERISTAKT EVKPECKESQ VIADAEVVQE QVKEETAIKP AAAKVNRTKQ RKSFSRSRTH 670 680 690 700 710 720 IGQQRRRHRT VSMCSDIPPS SPDIEVLSQQ NEIENTVLAI EPETETAVAE IIPEAEVPAL 730 740 750 760 770 780 NKCPTKYPKT KKHLVNEWLS EKNEKTGKPS DSLSERPLRI TTDPEVLATQ LNSLPGLTYS 790 800 810 820 830 840 PHVYSTPKHY IRFTSPFLSE KKRRKETTEN ISGSCKKRWL KQALEEENST ILHRYHSPCQ 850 860 870 880 890 900 ERSRSPTVNG ENKSPLLLSD SCSLPDLTTP LKKRRLYQLL DTAYSESSTP TPSPYATPTH 910 920 930 940 950 960 TDITPTDPAF ATPPRIKSDD ETYRNGYKPI YSPVTPVTPG TPGNTMHFEN ISSPESSPEI 970 980 990 1000 1010 1020 KRCTYNQEGY DRPSNMLTLG PFRNSNLTEL GLQEIKTIGY TSPRSRTEVN RPCPGEKESV 1030 1040 1050 1060 1070 1080 SDLQLGLDAV EPAALQKSME TPAHDRTEPS NQLDSTHSGR GTMYSSWVKS PDRTGVNFSV 1090 1100 1110 1120 1130 1140 NSNLRDLTPS HQLETGGGFR VSESKCLIQQ DDTRGMFLGA AVFCTSEDGL ASGFGRTVND 1150 1160 1170 1180 1190 1200 NLIDGSCTPQ NPPQKKKVSL LEYRKRQREA RKSGSKPENF ALISVSPHPS GSLSSSGDGC 1210 1220 1230 1240 1250 1260 VHSSENGEQA ENQASLPLPP PAAAAAATAA AAYSASSEEG SSNCPVKDAN SSEKKDPEVQ 1270 1280 1290 1300 1310 1320 WTASTSVEQV RERSYQRALL LSDHRKDKDS GGESPCVSCS PSHVQSPPSS HSNHIPQVHA 1330 1340 1350 1360 1370 1380 QSLAPSLSEL MADPDAEGTE ATSTSECPSP DTSQSPSKTS KPGSPGPINP AQSHGKILTK 1390 1400 1410 1420 1430 1440 PDSHWEATAT VSEADNSVHQ NPEPQHRQLS SNTPALSQNH APQAHALSAN DQLPQKLPSA 1450 1460 1470 1480 1490 1500 PTKLHCPPSP HTENPPKSST PHTPVQHGYL SPKPPSQHLG SPFRPHHSQS PQVGTPQRET 1510 1520 1530 1540 1550 1560 QRNFYAAAQN LQANPQQATS GALFTQTPSG QSSATYSQFN QQSLNSTAPP PPPPPPPSSY 1570 1580 1590 1600 1610 1620 YQNQQPSANF QNYNQLKGSL SQQTVFTSGP NQALPGSTSQ QSVPGHHVTP GHFLPSQNPT 1630 1640 1650 1660 1670 1680 IHHQPAAAAV VPPPPPPPPA PGPHLIQQPS SHQQHSVAHG VGPVHAVTPG SHIHSQTAGH 1690 1700 1710 1720 1730 1740 HLPPPPPPPG PAPHHHPPPH PTTGLQSLQA QHQHVVNSAP PPPPPPPPPP PASVLVSGHH 1750 1760 1770 1780 1790 1800 SASGQALHHP PHQGPPLFPA SAHPAVPPYP SQATHHTTLG PGPQHQPSGT GPHCPLPVAG 1810 1820 1830 1840 1850 1860 PHLQPQGPNS IPTPTASGFC PHPHPGSVAL PHGVQGPQQA SPVPAQIPIH RAQVPPTFQN NYHGSGWH
	Isoform 2. Checksum: 2166B0C437DBCC75	FASTA	1,288	138,681
	10 20 30 40 50 60 MEAILQAFAR LEKREKRREQ ALERISTAKT EVKPECKESQ VIADAEVVQE QVKEETAIKP 70 80 90 100 110 120 AAAKVNRTKQ RKSFSRSRTH IGQQRRRHRT VSMCSDIPPS SPDIEVLSQQ NEIENTVLAI 130 140 150 160 170 180 EPETETAVAE IIPEAEVPAL NKCPTKYPKT KKHLVNEWLS EKNEKTGKPS DSLSERPLRI 190 200 210 220 230 240 TTDPEVLATQ LNSLPGLTYS PHVYSTPKHY IRFTSPFLSE KKRRKETTEN ISGSCKKRWL 250 260 270 280 290 300 KQALEEENST ILHRYHSPCQ ERSRSPTVNG ENKSPLLLSD SCSLPDLTTP LKKRRLYQLL 310 320 330 340 350 360 DTAYSESSTP TPSPYATPTH TDITPTDPAF ATPPRIKSDD ETYRNGYKPI YSPVTPVTPG 370 380 390 400 410 420 TPGNTMHFEN ISSPESSPEI KRCTYNQEGY DRPSNMLTLG PFRNSNLTEL GLQEIKTIGY 430 440 450 460 470 480 TSPRSRTEVN RPCPGEKESV SDLQLGLDAV EPAALQKSME TPAHDRTEPS NQLDSTHSGR 490 500 510 520 530 540 GTMYSSWVKS PDRTGVNFSV NSNLRDLTPS HQLETGGGFR VSESKCLIQQ DDTRGMFLGA 550 560 570 580 590 600 AVFCTSEDGL ASGFGRTVND NLIDGSCTPQ NPPQKKKVSL LEYRKRQREA RKSGSKPENF 610 620 630 640 650 660 ALISVSPHPS GSLSSSGDGC VHSSENGEQA ENQASLPLPP PAAAAAATAA AAYSASSEEG 670 680 690 700 710 720 SSNCPVKDAN SSEKKDPEVQ WTASTSVEQV RERSYQRALL LSDHRKDKDS GGESPCVSCS 730 740 750 760 770 780 PSHVQSPPSS HSNHIPQVHA QSLAPSLSEL MADPDAEGTE ATSTSECPSP DTSQSPSKTS 790 800 810 820 830 840 KPGSPGPINP AQSHGKILTK PDSHWEATAT VSEADNSVHQ NPEPQHRQLS SNTPALSQNH 850 860 870 880 890 900 APQAHALSAN DQLPQKLPSA PTKLHCPPSP HTENPPKSST PHTPVQHGYL SPKPPSQHLG 910 920 930 940 950 960 SPFRPHHSQS PQVGTPQRET QRNFYAAAQN LQANPQQATS GALFTQTPSG QSSATYSQFN 970 980 990 1000 1010 1020 QQSLNSTAPP PPPPPPPSSY YQNQQPSANF QNYNQLKGSL SQQTVFTSGP NQALPGSTSQ 1030 1040 1050 1060 1070 1080 QSVPGHHVTP GHFLPSQNPT IHHQPAAAAV VPPPPPPPPA PGPHLIQQPS SHQQHSVAHG 1090 1100 1110 1120 1130 1140 VGPVHAVTPG SHIHSQTAGH HLPPPPPPPG PAPHHHPPPH PTTGLQSLQA QHQHVVNSAP 1150 1160 1170 1180 1190 1200 PPPPPPPPPP PASVLVSGHH SASGQALHHP PHQGPPLFPA SAHPAVPPYP SQATHHTTLG 1210 1220 1230 1240 1250 1260 PGPQHQPSGT GPHCPLPVAG PHLQPQGPNS IPTPTASGFC PHPHPGSVAL PHGVQGPQQA 1270 1280 SPVPAQIPIH RAQVPPTFQN NYHGSGWH

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: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[2]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1153 (ISOFORM 1). Strain: C57BL/6J. Tissue: Embryo, Embryonic eye, Melanoma, Pancreas and Tongue.
[3]	"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 1-802 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-494 (ISOFORM 1). Strain: C57BL/6, C57BL/6J and FVB/N. Tissue: Eye, Mammary gland and Mammary tumor.
[4]	"A gene-trap strategy identifies quiescence-induced genes in synchronized myoblasts." Sambasivan R., Pavlath G.K., Dhawan J. J. Biosci. 33:27-44(2008) [PubMed: 18376068] [Abstract] Cited for: INDUCTION.
[5]	"Loss of MLL5 results in pleiotropic hematopoietic defects, reduced neutrophil immune function, and extreme sensitivity to DNA demethylation." Heuser M., Yap D.B., Leung M., de Algara T.R., Tafech A., McKinney S., Dixon J., Thresher R., Colledge B., Carlton M., Humphries R.K., Aparicio S.A. Blood 113:1432-1443(2009) [PubMed: 18854576] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[6]	"Impaired function of primitive hematopoietic cells in mice lacking the Mixed-Lineage-Leukemia homolog MLL5." Madan V., Madan B., Brykczynska U., Zilbermann F., Hogeveen K., Doehner K., Doehner H., Weber O., Blum C., Rodewald H.-R., Sassone-Corsi P., Peters A.H.F.M., Fehling H.J. Blood 113:1444-1454(2009) [PubMed: 18952892] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[7]	"MLL5 contributes to hematopoietic stem cell fitness and homeostasis." Zhang Y., Wong J., Klinger M., Tran M.T., Shannon K.M., Killeen N. Blood 113:1455-1463(2009) [PubMed: 18818388] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[8]	"MLL5, a trithorax homolog, indirectly regulates H3K4 methylation, represses cyclin A2 expression, and promotes myogenic differentiation." Sebastian S., Sreenivas P., Sambasivan R., Cheedipudi S., Kandalla P., Pavlath G.K., Dhawan J. Proc. Natl. Acad. Sci. U.S.A. 106:4719-4724(2009) [PubMed: 19264965] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF CYS-411.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC122022 Genomic DNA. No translation available. AK007682 mRNA. Translation: BAB25186.1. Different initiation. AK021284 mRNA. Translation: BAE43262.1. AK035078 mRNA. Translation: BAC28936.2. Different initiation. AK148169 mRNA. Translation: BAE28389.1. Frameshift. AK160519 mRNA. Translation: BAE35839.1. BC036286 mRNA. Translation: AAH36286.1. Sequence problems. BC064079 mRNA. Translation: AAH64079.1. Sequence problems. BC089356 mRNA. Translation: AAH89356.1. Sequence problems. BC103801 mRNA. Translation: AAI03802.1. Sequence problems.
IPI	IPI00660988. IPI00896088.
RefSeq	NP_081260.1.
UniGene	Mm.205190 Mm.403814 Mm.471659
3D structure databases
SMR	Q3UG20. Positions 106-166, 341-469.
ModBase	Search...
PTM databases
PhosphoSite	Q3UG20.
Proteomic databases
PRIDE	Q3UG20.
Genome annotation databases
Ensembl	ENSMUST00000056291; ENSMUSP00000054228; ENSMUSG00000029004; Mus musculus. [Genome view] ENSMUST00000094962; ENSMUSP00000092569; ENSMUSG00000029004; Mus musculus. [Genome view] ENSMUST00000115128; ENSMUSP00000110781; ENSMUSG00000029004; Mus musculus. [Genome view]
GeneID	69188.
KEGG	mmu:69188.
Organism-specific databases
CTD	69188.
MGI	MGI:1924825. Mll5.
Phylogenomic databases
eggNOG	roNOG11229.
HOVERGEN	Q3UG20.
InParanoid	Q3UG20.
OMA	PGHHVTP.
OrthoDB	EOG96Q9BT.
Gene expression databases
ArrayExpress	Q3UG20.
Bgee	Q3UG20.
Genevestigator	Q3UG20.
Family and domain databases
InterPro	IPR001214. SET_dom. IPR019786. Zinc_finger_PHD-type_CS. IPR011011. Znf_FYVE_PHD. IPR001965. Znf_PHD. IPR019787. Znf_PHD-finger. [Graphical view]
Pfam	PF00628. PHD. 1 hit. PF00856. SET. 1 hit. [Graphical view]
SMART	SM00249. PHD. 1 hit. SM00317. SET. 1 hit. [Graphical view]
PROSITE	PS50280. SET. 1 hit. PS01359. ZF_PHD_1. 1 hit. PS50016. ZF_PHD_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

MLL5_MOUSE

Accession

Primary (citable) accession number: Q3UG20
Secondary accession number(s): Q3SYI5 , Q3TUY2, Q3V410, Q5FWI1, Q6P3B3, Q8BS65, Q8CFX7, Q9CVK6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	June 10, 2008
Last modified:	February 9, 2010
This is version 40 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)