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Protein AF-9 (ALL1-fused gene from chromosome 9 protein) (Myeloid/lymphoid or mixed-lineage leukemia translocated to chromosome 3 protein) (YEATS domain-containing protein 3)

 AF9_HUMAN               Reviewed;         568 AA.
P42568; B1AMQ2; B2R7B3; B7Z755; D3DRJ8; Q8IVB0;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 2.
11-DEC-2019, entry version 171.
RecName: Full=Protein AF-9;
AltName: Full=ALL1-fused gene from chromosome 9 protein;
AltName: Full=Myeloid/lymphoid or mixed-lineage leukemia translocated to chromosome 3 protein;
AltName: Full=YEATS domain-containing protein 3;
Name=MLLT3 {ECO:0000312|HGNC:HGNC:7136}; Synonyms=AF9, YEATS3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHROMOSOMAL TRANSLOCATION WITH
KMT2A.
PubMed=8506309; DOI=10.1073/pnas.90.10.4631;
Nakamura T., Alder H., Gu Y., Prasad R., Canaani O., Kamada N., Gale R.P.,
Lange B., Crist W.M., Nowell P.C., Croce C.M., Canaani E.;
"Genes on chromosomes 4, 9, and 19 involved in 11q23 abnormalities in acute
leukemia share sequence homology and/or common motifs.";
Proc. Natl. Acad. Sci. U.S.A. 90:4631-4635(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Synovium;
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH BCOR.
PubMed=10898795;
Huynh K.D., Fischle W., Verdin E., Bardwell V.J.;
"BCoR, a novel corepressor involved in BCL-6 repression.";
Genes Dev. 14:1810-1823(2000).
[7]
CHROMOSOMAL TRANSLOCATION.
PubMed=10861294; DOI=10.1093/hmg/9.11.1671;
Strissel P.L., Strick R., Tomek R.J., Roe B.A., Rowley J.D.,
Zeleznik-Le N.J.;
"DNA structural properties of AF9 are similar to MLL and could act as
recombination hot spots resulting in MLL/AF9 translocations and
leukemogenesis.";
Hum. Mol. Genet. 9:1671-1679(2000).
[8]
INTERACTION WITH CBX8.
PubMed=11313972; DOI=10.1038/sj.onc.1204108;
Garcia-Cuellar M.P., Zilles O., Schreiner S.A., Birke M., Winkler T.H.,
Slany R.K.;
"The ENL moiety of the childhood leukemia-associated MLL-ENL oncoprotein
recruits human Polycomb 3.";
Oncogene 20:411-419(2001).
[9]
CHROMOSOMAL TRANSLOCATION.
PubMed=16001262; DOI=10.1007/s00439-005-0004-1;
Pramparo T., Grosso S., Messa J., Zatterale A., Bonaglia M.C., Chessa L.,
Balestri P., Rocchi M., Zuffardi O., Giorda R.;
"Loss-of-function mutation of the AF9/MLLT3 gene in a girl with neuromotor
development delay, cerebellar ataxia, and epilepsy.";
Hum. Genet. 118:76-81(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294 AND SER-483, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the
kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288; SER-294 AND SER-483, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412 AND SER-419, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
FUNCTION, AND IDENTIFICATION IN THE SEC COMPLEX.
PubMed=20471948; DOI=10.1016/j.molcel.2010.04.013;
He N., Liu M., Hsu J., Xue Y., Chou S., Burlingame A., Krogan N.J.,
Alber T., Zhou Q.;
"HIV-1 Tat and host AFF4 recruit two transcription elongation factors into
a bifunctional complex for coordinated activation of HIV-1 transcription.";
Mol. Cell 38:428-438(2010).
[15]
FUNCTION, AND IDENTIFICATION IN THE SEC COMPLEX.
PubMed=20159561; DOI=10.1016/j.molcel.2010.01.026;
Lin C., Smith E.R., Takahashi H., Lai K.C., Martin-Brown S., Florens L.,
Washburn M.P., Conaway J.W., Conaway R.C., Shilatifard A.;
"AFF4, a component of the ELL/P-TEFb elongation complex and a shared
subunit of MLL chimeras, can link transcription elongation to leukemia.";
Mol. Cell 37:429-437(2010).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION IN THE SEC COMPLEX.
PubMed=22195968; DOI=10.1016/j.molcel.2011.12.008;
Smith E.R., Lin C., Garrett A.S., Thornton J., Mohaghegh N., Hu D.,
Jackson J., Saraf A., Swanson S.K., Seidel C., Florens L., Washburn M.P.,
Eissenberg J.C., Shilatifard A.;
"The little elongation complex regulates small nuclear RNA transcription.";
Mol. Cell 44:954-965(2011).
[18]
INTERACTION OF FUSION PROTEIN KMT2A-MLLT3 WITH MEN1.
PubMed=22936661; DOI=10.1182/blood-2012-05-429274;
Shi A., Murai M.J., He S., Lund G., Hartley T., Purohit T., Reddy G.,
Chruszcz M., Grembecka J., Cierpicki T.;
"Structural insights into inhibition of the bivalent menin-MLL interaction
by small molecules in leukemia.";
Blood 120:4461-4469(2012).
[19]
REVIEW ON THE SUPER ELONGATION COMPLEX.
PubMed=22895430; DOI=10.1038/nrm3417;
Luo Z., Lin C., Shilatifard A.;
"The super elongation complex (SEC) family in transcriptional control.";
Nat. Rev. Mol. Cell Biol. 13:543-547(2012).
[20]
INTERACTION WITH ALKBH4.
PubMed=23145062; DOI=10.1371/journal.pone.0049045;
Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M., Meza-Zepeda L.A.,
Falnes P.O.;
"Human ALKBH4 interacts with proteins associated with transcription.";
PLoS ONE 7:E49045-E49045(2012).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294 AND SER-483, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
INTERACTION OF FUSION PROTEIN KMT2A-MLLT3 WITH PSIP1 AND MEN1.
PubMed=25305204; DOI=10.1182/blood-2014-01-550079;
Murai M.J., Pollock J., He S., Miao H., Purohit T., Yokom A., Hess J.L.,
Muntean A.G., Grembecka J., Cierpicki T.;
"The same site on the integrase-binding domain of lens epithelium-derived
growth factor is a therapeutic target for MLL leukemia and HIV.";
Blood 124:3730-3737(2014).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-339, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-339, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-modification
with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[25]
STRUCTURE BY NMR OF 490-568 IN COMPLEX WITH AFF1.
PubMed=23260655; DOI=10.1016/j.str.2012.11.011;
Leach B.I., Kuntimaddi A., Schmidt C.R., Cierpicki T., Johnson S.A.,
Bushweller J.H.;
"Leukemia fusion target AF9 is an intrinsically disordered transcriptional
regulator that recruits multiple partners via coupled folding and
binding.";
Structure 21:176-183(2013).
[26]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-138 IN COMPLEX WITH H3K9AC
PEPTIDE, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF PHE-28;
HIS-56; SER-58; PHE-59; GLY-77; TYR-78; PHE-81 AND ASP-103.
PubMed=25417107; DOI=10.1016/j.cell.2014.09.049;
Li Y., Wen H., Xi Y., Tanaka K., Wang H., Peng D., Ren Y., Jin Q.,
Dent S.Y., Li W., Li H., Shi X.;
"AF9 YEATS domain links histone acetylation to DOT1L-mediated H3K79
methylation.";
Cell 159:558-571(2014).
[27]
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-138 IN COMPLEX WITH H3K9CR
PEPTIDE, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF PHE-28;
HIS-56; SER-58; PHE-59; GLY-77 AND TYR-78.
PubMed=27105114; DOI=10.1016/j.molcel.2016.03.028;
Li Y., Sabari B.R., Panchenko T., Wen H., Zhao D., Guan H., Wan L.,
Huang H., Tang Z., Zhao Y., Roeder R.G., Shi X., Allis C.D., Li H.;
"Molecular coupling of histone crotonylation and active transcription by
AF9 YEATS domain.";
Mol. Cell 62:181-193(2016).
[28]
STRUCTURE BY NMR OF 1-138, FUNCTION, DOMAIN, AND MUTAGENESIS OF PHE-59 AND
TYR-78.
PubMed=27545619; DOI=10.1016/j.str.2016.05.023;
Zhang Q., Zeng L., Zhao C., Ju Y., Konuma T., Zhou M.M.;
"Structural insights into histone crotonyl-lysine recognition by the AF9
YEATS domain.";
Structure 24:1606-1612(2016).
-!- FUNCTION: Chromatin reader component of the super elongation complex
(SEC), a complex required to increase the catalytic rate of RNA
polymerase II transcription by suppressing transient pausing by the
polymerase at multiple sites along the DNA (PubMed:20159561,
PubMed:20471948, PubMed:25417107, PubMed:27105114, PubMed:27545619).
Specifically recognizes and binds acylated histone H3, with a marked
preference for histone H3 that is crotonylated (PubMed:25417107,
PubMed:27105114, PubMed:27545619). Crotonylation marks active promoters
and enhancers and confers resistance to transcriptional repressors
(PubMed:25417107, PubMed:27105114, PubMed:27545619). Recognizes and
binds histone H3 crotonylated at 'Lys-9' (H3K9cr), and with slightly
lower affinity histone H3 crotonylated at 'Lys-18' (H3K18cr)
(PubMed:27105114). Also recognizes and binds histone H3 acetylated at
'Lys-9' (H3K9ac), but with lower affinity than crotonylated histone H3
(PubMed:25417107, PubMed:27105114). In the SEC complex, MLLT3 is
required to recruit the complex to crotonylated histones
(PubMed:27105114, PubMed:27545619). {ECO:0000269|PubMed:20159561,
ECO:0000269|PubMed:20471948, ECO:0000269|PubMed:25417107,
ECO:0000269|PubMed:27105114, ECO:0000269|PubMed:27545619}.
-!- SUBUNIT: Component of the super elongation complex (SEC), at least
composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb
complex and ELL (ELL, ELL2 or ELL3) (PubMed:20159561, PubMed:20471948,
PubMed:22195968, PubMed:23260655, PubMed:25417107). Interacts with BCOR
(PubMed:10898795). Interacts with CBX8 (PubMed:11313972). Interacts
with ALKBH4 (PubMed:23145062). {ECO:0000269|PubMed:10898795,
ECO:0000269|PubMed:11313972, ECO:0000269|PubMed:20159561,
ECO:0000269|PubMed:20471948, ECO:0000269|PubMed:22195968,
ECO:0000269|PubMed:23145062, ECO:0000269|PubMed:23260655,
ECO:0000269|PubMed:25417107}.
-!- INTERACTION:
P51825:AFF1; NbExp=7; IntAct=EBI-716132, EBI-2610180;
Q9UHB7:AFF4; NbExp=4; IntAct=EBI-716132, EBI-395282;
Q9NXW9:ALKBH4; NbExp=4; IntAct=EBI-716132, EBI-8637516;
Q92624:APPBP2; NbExp=3; IntAct=EBI-716132, EBI-743771;
Q6W2J9-1:BCOR; NbExp=2; IntAct=EBI-716132, EBI-16028932;
Q9HC52:CBX8; NbExp=2; IntAct=EBI-716132, EBI-712912;
Q8TEK3:DOT1L; NbExp=6; IntAct=EBI-716132, EBI-2619253;
Q8IZU1:FAM9A; NbExp=3; IntAct=EBI-716132, EBI-8468186;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00376,
ECO:0000269|PubMed:27105114}. Chromosome {ECO:0000269|PubMed:25417107,
ECO:0000269|PubMed:27105114}. Note=Colocalizes with acylated histone H3
(PubMed:25417107, PubMed:27105114). Colocalizes with histone H3
crotonylated at 'Lys-18' (H3K18cr) (PubMed:27105114).
{ECO:0000269|PubMed:25417107, ECO:0000269|PubMed:27105114}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P42568-1; Sequence=Displayed;
Name=2;
IsoId=P42568-2; Sequence=VSP_054924;
-!- DOMAIN: The YEATS domain specifically recognizes and binds acylated
histones, with a marked preference histones that are crotonylated
(PubMed:27105114, PubMed:27545619). Also binds histone H3 acetylated at
'Lys-9' (H3K9ac), but with lower affinity (PubMed:25417107,
PubMed:27105114). {ECO:0000269|PubMed:25417107,
ECO:0000269|PubMed:27105114, ECO:0000269|PubMed:27545619}.
-!- DISEASE: Note=A chromosomal aberration involving MLLT3 is associated
with acute leukemias. Translocation t(9;11)(p22;q23) with KMT2A/MLL1.
The result is a rogue activator protein. Fusion protein KMT2A-MLLT3
interacts with MEN1 and PSIP1 (PubMed:22936661, PubMed:25305204).
{ECO:0000269|PubMed:10861294, ECO:0000269|PubMed:22936661,
ECO:0000269|PubMed:25305204, ECO:0000269|PubMed:8506309}.
-!- DISEASE: Note=A chromosomal aberration involving MLLT3 was observed in
a patient with neuromotor development delay, cerebellar ataxia and
epilepsy. Translocation t(4;9)(q35;p22). {ECO:0000269|PubMed:16001262}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
Haematology;
URL="http://atlasgeneticsoncology.org/Genes/AF9ID5.html";
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EMBL; L13744; AAA58361.1; -; mRNA.
EMBL; AK301474; BAH13491.1; -; mRNA.
EMBL; AK312914; BAG35760.1; -; mRNA.
EMBL; AL354879; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL512635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL513498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL163193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL627410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471071; EAW58631.1; -; Genomic_DNA.
EMBL; CH471071; EAW58632.1; -; Genomic_DNA.
EMBL; BC036089; AAH36089.1; -; mRNA.
CCDS; CCDS6494.1; -. [P42568-1]
CCDS; CCDS69579.1; -. [P42568-2]
PIR; I39411; I39411.
RefSeq; NP_001273620.1; NM_001286691.1. [P42568-2]
RefSeq; NP_004520.2; NM_004529.3. [P42568-1]
PDB; 2LM0; NMR; -; A=490-568.
PDB; 2MV7; NMR; -; A=500-568.
PDB; 2N4Q; NMR; -; B=500-568.
PDB; 2NDF; NMR; -; A=1-138.
PDB; 2NDG; NMR; -; A=1-138.
PDB; 4TMP; X-ray; 2.30 A; A/C=1-138.
PDB; 5HJB; X-ray; 2.70 A; A=1-138.
PDB; 5HJD; X-ray; 2.81 A; A/C/E/G/K/N/Q/T=1-138.
PDB; 5YYF; X-ray; 1.90 A; A/C=1-138.
PDB; 6B7G; NMR; -; A=500-568.
PDB; 6MIL; X-ray; 1.93 A; A/C=1-138.
PDB; 6MIM; X-ray; 2.52 A; A/C=1-138.
PDBsum; 2LM0; -.
PDBsum; 2MV7; -.
PDBsum; 2N4Q; -.
PDBsum; 2NDF; -.
PDBsum; 2NDG; -.
PDBsum; 4TMP; -.
PDBsum; 5HJB; -.
PDBsum; 5HJD; -.
PDBsum; 5YYF; -.
PDBsum; 6B7G; -.
PDBsum; 6MIL; -.
PDBsum; 6MIM; -.
SMR; P42568; -.
BioGrid; 110446; 67.
CORUM; P42568; -.
DIP; DIP-56409N; -.
IntAct; P42568; 50.
MINT; P42568; -.
STRING; 9606.ENSP00000369695; -.
iPTMnet; P42568; -.
PhosphoSitePlus; P42568; -.
BioMuta; MLLT3; -.
DMDM; 215273971; -.
jPOST; P42568; -.
MassIVE; P42568; -.
MaxQB; P42568; -.
PaxDb; P42568; -.
PeptideAtlas; P42568; -.
PRIDE; P42568; -.
ProteomicsDB; 55517; -. [P42568-1]
ProteomicsDB; 6833; -.
Ensembl; ENST00000380338; ENSP00000369695; ENSG00000171843. [P42568-1]
Ensembl; ENST00000630269; ENSP00000485996; ENSG00000171843. [P42568-2]
GeneID; 4300; -.
KEGG; hsa:4300; -.
UCSC; uc003zoe.3; human. [P42568-1]
CTD; 4300; -.
DisGeNET; 4300; -.
EuPathDB; HostDB:ENSG00000171843.15; -.
GeneCards; MLLT3; -.
HGNC; HGNC:7136; MLLT3.
HPA; HPA001824; -.
MalaCards; MLLT3; -.
MIM; 159558; gene.
neXtProt; NX_P42568; -.
OpenTargets; ENSG00000171843; -.
Orphanet; 402017; Acute myeloid leukemia with t(9;11)(p22;q23).
PharmGKB; PA30852; -.
eggNOG; KOG3149; Eukaryota.
eggNOG; COG5033; LUCA.
GeneTree; ENSGT00940000155903; -.
InParanoid; P42568; -.
KO; K15187; -.
OMA; PNRSVHT; -.
OrthoDB; 727038at2759; -.
PhylomeDB; P42568; -.
TreeFam; TF314586; -.
Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
SIGNOR; P42568; -.
ChiTaRS; MLLT3; human.
GeneWiki; MLLT3; -.
GenomeRNAi; 4300; -.
Pharos; P42568; Tbio.
PRO; PR:P42568; -.
Proteomes; UP000005640; Chromosome 9.
RNAct; P42568; protein.
Bgee; ENSG00000171843; Expressed in 193 organ(s), highest expression level in frontal cortex.
ExpressionAtlas; P42568; baseline and differential.
Genevisible; P42568; HS.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0008023; C:transcription elongation factor complex; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISM:NTNU_SB.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB.
GO; GO:0140030; F:modification-dependent protein binding; IDA:UniProtKB.
GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:2000096; P:positive regulation of Wnt signaling pathway, planar cell polarity pathway; IGI:MGI.
GO; GO:0007379; P:segment specification; IEA:Ensembl.
GO; GO:0006366; P:transcription by RNA polymerase II; TAS:Reactome.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
DisProt; DP01070; -.
Gene3D; 2.60.40.1970; -; 1.
InterPro; IPR040930; AF-9_AHD.
InterPro; IPR038704; YEAST_sf.
InterPro; IPR005033; YEATS.
PANTHER; PTHR23195; PTHR23195; 1.
Pfam; PF17793; AHD; 1.
Pfam; PF03366; YEATS; 1.
PROSITE; PS51037; YEATS; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Chromosomal rearrangement;
Chromosome; Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1..568
/note="Protein AF-9"
/id="PRO_0000215921"
DOMAIN 8..112
/note="YEATS"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00376"
REGION 78..80
/note="Histone H3K9cr binding"
/evidence="ECO:0000244|PDB:5HJB, ECO:0000244|PDB:5HJD,
ECO:0000269|PubMed:27105114"
REGION 106..108
/note="Histone H3K9cr binding"
/evidence="ECO:0000244|PDB:5HJB, ECO:0000244|PDB:5HJD,
ECO:0000269|PubMed:27105114"
MOTIF 295..300
/note="Nuclear localization signal"
/evidence="ECO:0000255"
COMPBIAS 149..194
/note="Poly-Ser"
COMPBIAS 383..391
/note="Poly-Ser"
COMPBIAS 466..469
/note="Poly-Pro"
BINDING 58
/note="Histone H3K9cr"
/evidence="ECO:0000244|PDB:5HJB, ECO:0000244|PDB:5HJD,
ECO:0000269|PubMed:27105114"
BINDING 103
/note="Histone H3K9cr"
/evidence="ECO:0000244|PDB:5HJB, ECO:0000244|PDB:5HJD,
ECO:0000269|PubMed:27105114"
SITE 375
/note="KMT2A/MLL1 fusion point (in acute myeloid leukemia
patient CO)"
/evidence="ECO:0000269|PubMed:8506309"
SITE 481
/note="KMT2A/MLL1 fusion point (in acute myeloid leukemia
patient F1)"
/evidence="ECO:0000269|PubMed:8506309"
MOD_RES 288
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648"
MOD_RES 294
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976, ECO:0000244|PubMed:23186163"
MOD_RES 412
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19690332"
MOD_RES 419
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19690332"
MOD_RES 483
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976, ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163"
CROSSLNK 339
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733"
VAR_SEQ 1..4
/note="MASS -> M (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_054924"
MUTAGEN 28
/note="F->A: Decreased binding to crotonylated histone H3.
Decreased binding to acetylated histone H3."
/evidence="ECO:0000269|PubMed:25417107,
ECO:0000269|PubMed:27105114"
MUTAGEN 56
/note="H->A: Decreased binding to crotonylated histone H3.
Decreased binding to acetylated histone H3."
/evidence="ECO:0000269|PubMed:25417107,
ECO:0000269|PubMed:27105114"
MUTAGEN 58
/note="S->A: Decreased binding to crotonylated histone H3.
Decreased binding to acetylated histone H3."
/evidence="ECO:0000269|PubMed:25417107,
ECO:0000269|PubMed:27105114"
MUTAGEN 59
/note="F->A: Strongly decreased binding to crotonylated
histone H3. Decreased binding to acetylated histone H3."
/evidence="ECO:0000269|PubMed:25417107,
ECO:0000269|PubMed:27105114, ECO:0000269|PubMed:27545619"
MUTAGEN 77
/note="G->A: Decreased binding to crotonylated histone H3.
Decreased binding to acetylated histone H3."
/evidence="ECO:0000269|PubMed:25417107,
ECO:0000269|PubMed:27105114"
MUTAGEN 78
/note="Y->A: Strongly decreased binding to crotonylated
histone H3. Decreased binding to acetylated histone H3."
/evidence="ECO:0000269|PubMed:25417107,
ECO:0000269|PubMed:27105114, ECO:0000269|PubMed:27545619"
MUTAGEN 81
/note="F->A: Decreased binding to acetylated histone H3."
/evidence="ECO:0000269|PubMed:25417107"
MUTAGEN 103
/note="D->A: Decreased binding to acetylated histone H3."
/evidence="ECO:0000269|PubMed:25417107"
CONFLICT 6
/note="A -> S (in Ref. 1; AAA58361 and 2; BAG35760)"
/evidence="ECO:0000305"
CONFLICT 173
/note="S -> G (in Ref. 5; AAH36089)"
/evidence="ECO:0000305"
CONFLICT 419
/note="S -> P (in Ref. 2; BAG35760)"
/evidence="ECO:0000305"
STRAND 6..19
/evidence="ECO:0000244|PDB:5YYF"
STRAND 30..37
/evidence="ECO:0000244|PDB:5YYF"
HELIX 39..41
/evidence="ECO:0000244|PDB:5YYF"
TURN 45..47
/evidence="ECO:0000244|PDB:5YYF"
STRAND 48..54
/evidence="ECO:0000244|PDB:5YYF"
STRAND 59..61
/evidence="ECO:0000244|PDB:5YYF"
STRAND 63..90
/evidence="ECO:0000244|PDB:5YYF"
STRAND 92..94
/evidence="ECO:0000244|PDB:5YYF"
STRAND 97..104
/evidence="ECO:0000244|PDB:5YYF"
STRAND 114..126
/evidence="ECO:0000244|PDB:5YYF"
HELIX 129..135
/evidence="ECO:0000244|PDB:5YYF"
HELIX 504..515
/evidence="ECO:0000244|PDB:2LM0"
HELIX 523..531
/evidence="ECO:0000244|PDB:2LM0"
STRAND 536..538
/evidence="ECO:0000244|PDB:2LM0"
STRAND 543..545
/evidence="ECO:0000244|PDB:2LM0"
TURN 547..549
/evidence="ECO:0000244|PDB:2LM0"
HELIX 552..561
/evidence="ECO:0000244|PDB:2LM0"
SEQUENCE 568 AA; 63351 MW; 0A020B7FB34132F9 CRC64;
MASSCAVQVK LELGHRAQVR KKPTVEGFTH DWMVFVRGPE HSNIQHFVEK VVFHLHESFP
RPKRVCKDPP YKVEESGYAG FILPIEVYFK NKEEPRKVRF DYDLFLHLEG HPPVNHLRCE
KLTFNNPTED FRRKLLKAGG DPNRSIHTSS SSSSSSSSSS SSSSSSSSSS SSSSSSSSSS
SSSSSSSSSS TSFSKPHKLM KEHKEKPSKD SREHKSAFKE PSRDHNKSSK ESSKKPKENK
PLKEEKIVPK MAFKEPKPMS KEPKPDSNLL TITSGQDKKA PSKRPPISDS EELSAKKRKK
SSSEALFKSF SSAPPLILTC SADKKQIKDK SHVKMGKVKI ESETSEKKKS TLPPFDDIVD
PNDSDVEENI SSKSDSEQPS PASSSSSSSS SFTPSQTRQQ GPLRSIMKDL HSDDNEEESD
EVEDNDNDSE MERPVNRGGS RSRRVSLSDG SDSESSSASS PLHHEPPPPL LKTNNNQILE
VKSPIKQSKS DKQIKNGECD KAYLDELVEL HRRLMTLRER HILQQIVNLI EETGHFHITN
TTFDFDLCSL DKTTVRKLQS YLETSGTS


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Related Genes :
[MLLT3 AF9 YEATS3] Protein AF-9 (ALL1-fused gene from chromosome 9 protein) (Myeloid/lymphoid or mixed-lineage leukemia translocated to chromosome 3 protein) (YEATS domain-containing protein 3)
[KMT2A ALL1 CXXC7 HRX HTRX MLL MLL1 TRX1] Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.354) (ALL-1) (CXXC-type zinc finger protein 7) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]
[Kmt2a All1 Hrx Mll Mll1] Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.354) (ALL-1) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]
[KMT2D ALR MLL2 MLL4] Histone-lysine N-methyltransferase 2D (Lysine N-methyltransferase 2D) (EC 2.1.1.354) (ALL1-related protein) (Myeloid/lymphoid or mixed-lineage leukemia protein 2)
[KMT2C HALR KIAA1506 MLL3] Histone-lysine N-methyltransferase 2C (Lysine N-methyltransferase 2C) (EC 2.1.1.354) (Homologous to ALR protein) (Myeloid/lymphoid or mixed-lineage leukemia protein 3)
[Mllt3 Af9] Protein AF-9 (Myeloid/lymphoid or mixed-lineage leukemia translocated to chromosome 3 protein homolog)
[AFF4 AF5Q31 MCEF HSPC092] AF4/FMR2 family member 4 (ALL1-fused gene from chromosome 5q31 protein) (Protein AF-5q31) (Major CDK9 elongation factor-associated protein)
[KNL1 CASC5 KIAA1570] Kinetochore scaffold 1 (ALL1-fused gene from chromosome 15q14 protein) (AF15q14) (Bub-linking kinetochore protein) (Blinkin) (Cancer susceptibility candidate gene 5 protein) (Cancer/testis antigen 29) (CT29) (Kinetochore-null protein 1) (Protein CASC5) (Protein D40/AF15q14)
[Kmt2d Mll2 Mll4] Histone-lysine N-methyltransferase 2D (Lysine N-methyltransferase 2D) (EC 2.1.1.354) (ALL1-related protein) (Myeloid/lymphoid or mixed-lineage leukemia protein 2)
[AFF1 AF4 FEL MLLT2 PBM1] AF4/FMR2 family member 1 (ALL1-fused gene from chromosome 4 protein) (Protein AF-4) (Protein FEL) (Proto-oncogene AF4)
[MLLT10 AF10] Protein AF-10 (ALL1-fused gene from chromosome 10 protein)
[KMT2E MLL5] Inactive histone-lysine N-methyltransferase 2E (Inactive lysine N-methyltransferase 2E) (Myeloid/lymphoid or mixed-lineage leukemia protein 5)
[Kmt2c Mll3] Histone-lysine N-methyltransferase 2C (Lysine N-methyltransferase 2C) (EC 2.1.1.354) (Myeloid/lymphoid or mixed-lineage leukemia protein 3 homolog)
[KMT2B HRX2 KIAA0304 MLL2 MLL4 TRX2 WBP7] Histone-lysine N-methyltransferase 2B (Lysine N-methyltransferase 2B) (EC 2.1.1.354) (Myeloid/lymphoid or mixed-lineage leukemia protein 4) (Trithorax homolog 2) (WW domain-binding protein 7) (WBP-7)
[Kmt2e Mll5] Inactive histone-lysine N-methyltransferase 2E (Inactive lysine N-methyltransferase 2E) (Myeloid/lymphoid or mixed-lineage leukemia protein 5 homolog)
[Kmt2b Mll2 Trx2 Wbp7] Histone-lysine N-methyltransferase 2B (Lysine N-methyltransferase 2B) (EC 2.1.1.354) (Myeloid/lymphoid or mixed-lineage leukemia protein 4 homolog) (Trithorax homolog 2) (WW domain-binding protein 7) (WBP-7)
[RUNX1 AML1 CBFA2] Runt-related transcription factor 1 (Acute myeloid leukemia 1 protein) (Core-binding factor subunit alpha-2) (CBF-alpha-2) (Oncogene AML-1) (Polyomavirus enhancer-binding protein 2 alpha B subunit) (PEA2-alpha B) (PEBP2-alpha B) (SL3-3 enhancer factor 1 alpha B subunit) (SL3/AKV core-binding factor alpha B subunit)
[PICALM CALM] Phosphatidylinositol-binding clathrin assembly protein (Clathrin assembly lymphoid myeloid leukemia protein)
[MLLT1 ENL LTG19 YEATS1] Protein ENL (YEATS domain-containing protein 1)
[MAP3K20 MLTK ZAK HCCS4] Mitogen-activated protein kinase kinase kinase 20 (EC 2.7.11.25) (Human cervical cancer suppressor gene 4 protein) (HCCS-4) (Leucine zipper- and sterile alpha motif-containing kinase) (MLK-like mitogen-activated protein triple kinase) (Mitogen-activated protein kinase kinase kinase MLT) (Mixed lineage kinase-related kinase) (MLK-related kinase) (MRK) (Sterile alpha motif- and leucine zipper-containing kinase AZK)
[TET1 CXXC6 KIAA1676 LCX] Methylcytosine dioxygenase TET1 (EC 1.14.11.n2) (CXXC-type zinc finger protein 6) (Leukemia-associated protein with a CXXC domain) (Ten-eleven translocation 1 gene protein)
[MCL1 BCL2L3] Induced myeloid leukemia cell differentiation protein Mcl-1 (Bcl-2-like protein 3) (Bcl2-L-3) (Bcl-2-related protein EAT/mcl1) (mcl1/EAT)
[MAP3K9 MLK1 PRKE1] Mitogen-activated protein kinase kinase kinase 9 (EC 2.7.11.25) (Mixed lineage kinase 1)
[SETD2 HIF1 HYPB KIAA1732 KMT3A SET2 HSPC069] Histone-lysine N-methyltransferase SETD2 (EC 2.1.1.-) (HIF-1) (Huntingtin yeast partner B) (Huntingtin-interacting protein 1) (HIP-1) (Huntingtin-interacting protein B) (Lysine N-methyltransferase 3A) (Protein-lysine N-methyltransferase SETD2) (EC 2.1.1.-) (SET domain-containing protein 2) (hSET2) (p231HBP)
[RUNX2 AML3 CBFA1 OSF2 PEBP2A] Runt-related transcription factor 2 (Acute myeloid leukemia 3 protein) (Core-binding factor subunit alpha-1) (CBF-alpha-1) (Oncogene AML-3) (Osteoblast-specific transcription factor 2) (OSF-2) (Polyomavirus enhancer-binding protein 2 alpha A subunit) (PEA2-alpha A) (PEBP2-alpha A) (SL3-3 enhancer factor 1 alpha A subunit) (SL3/AKV core-binding factor alpha A subunit)
[PITX2 ARP1 RGS RIEG RIEG1] Pituitary homeobox 2 (ALL1-responsive protein ARP1) (Homeobox protein PITX2) (Paired-like homeodomain transcription factor 2) (RIEG bicoid-related homeobox transcription factor) (Solurshin)
[Pitx2 Arp1 Brx1 Otlx2 Ptx2 Rgs] Pituitary homeobox 2 (ALL1-responsive protein ARP1) (BRX1 homeoprotein) (Homeobox protein PITX2) (Orthodenticle-like homeobox 2) (Paired-like homeodomain transcription factor 2) (Paired-like homeodomain transcription factor Munc 30) (Solurshin)
[ABL1 ABL JTK7] Tyrosine-protein kinase ABL1 (EC 2.7.10.2) (Abelson murine leukemia viral oncogene homolog 1) (Abelson tyrosine-protein kinase 1) (Proto-oncogene c-Abl) (p150)
[BCL11A CTIP1 EVI9 KIAA1809 ZNF856] B-cell lymphoma/leukemia 11A (BCL-11A) (B-cell CLL/lymphoma 11A) (COUP-TF-interacting protein 1) (Ecotropic viral integration site 9 protein homolog) (EVI-9) (Zinc finger protein 856)
[NCKIPSD AF3P21 SPIN90] NCK-interacting protein with SH3 domain (54 kDa VacA-interacting protein) (54 kDa vimentin-interacting protein) (VIP54) (90 kDa SH3 protein interacting with Nck) (AF3p21) (Dia-interacting protein 1) (DIP-1) (Diaphanous protein-interacting protein) (SH3 adapter protein SPIN90) (WASP-interacting SH3-domain protein) (WISH) (Wiskott-Aldrich syndrome protein-interacting protein)

Bibliography :