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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.
22-NOV-2017, entry version 152.
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;
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]
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).
[19]
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).
[20]
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).
[21]
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).
[22]
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).
[23]
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).
[24]
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).
[25]
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).
[26]
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;
-!- 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;
Note=No experimental confirmation available.;
-!- 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.
{ECO:0000269|PubMed:10861294, 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; AL512635; CAH70705.1; -; Genomic_DNA.
EMBL; AL354879; CAH70705.1; JOINED; Genomic_DNA.
EMBL; AL513498; CAH70705.1; JOINED; Genomic_DNA.
EMBL; AL354879; CAI14771.1; -; Genomic_DNA.
EMBL; AL512635; CAI14771.1; JOINED; Genomic_DNA.
EMBL; AL513498; CAI14771.1; JOINED; 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]
UniGene; Hs.317248; -.
UniGene; Hs.591085; -.
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.
PDBsum; 2LM0; -.
PDBsum; 2MV7; -.
PDBsum; 2N4Q; -.
PDBsum; 2NDF; -.
PDBsum; 2NDG; -.
PDBsum; 4TMP; -.
PDBsum; 5HJB; -.
PDBsum; 5HJD; -.
DisProt; DP01070; -.
ProteinModelPortal; P42568; -.
SMR; P42568; -.
BioGrid; 110446; 61.
CORUM; P42568; -.
DIP; DIP-56409N; -.
IntAct; P42568; 35.
MINT; MINT-1389464; -.
STRING; 9606.ENSP00000369695; -.
iPTMnet; P42568; -.
PhosphoSitePlus; P42568; -.
DMDM; 215273971; -.
MaxQB; P42568; -.
PaxDb; P42568; -.
PeptideAtlas; P42568; -.
PRIDE; P42568; -.
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; ENSGT00440000039936; -.
HOVERGEN; HBG004191; -.
InParanoid; P42568; -.
KO; K15187; -.
OMA; MSKEPKS; -.
OrthoDB; EOG091G06LN; -.
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; -.
PRO; PR:P42568; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000171843; -.
CleanEx; HS_MLLT3; -.
ExpressionAtlas; P42568; baseline and differential.
Genevisible; P42568; HS.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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: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:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:Reactome.
InterPro; IPR005033; YEATS.
PANTHER; PTHR23195; PTHR23195; 1.
Pfam; PF03366; YEATS; 1.
PROSITE; PS51037; YEATS; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing;
Chromosomal rearrangement; Chromosome; Complete proteome;
Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 568 Protein AF-9.
/FTId=PRO_0000215921.
DOMAIN 8 112 YEATS. {ECO:0000255|PROSITE-
ProRule:PRU00376}.
REGION 78 80 Histone H3K9cr binding.
{ECO:0000244|PDB:5HJB,
ECO:0000244|PDB:5HJD,
ECO:0000269|PubMed:27105114}.
REGION 106 108 Histone H3K9cr binding.
{ECO:0000244|PDB:5HJB,
ECO:0000244|PDB:5HJD,
ECO:0000269|PubMed:27105114}.
MOTIF 295 300 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 149 194 Poly-Ser.
COMPBIAS 383 391 Poly-Ser.
COMPBIAS 466 469 Poly-Pro.
BINDING 58 58 Histone H3K9cr. {ECO:0000244|PDB:5HJB,
ECO:0000244|PDB:5HJD,
ECO:0000269|PubMed:27105114}.
BINDING 103 103 Histone H3K9cr. {ECO:0000244|PDB:5HJB,
ECO:0000244|PDB:5HJD,
ECO:0000269|PubMed:27105114}.
SITE 375 375 KMT2A/MLL1 fusion point (in acute myeloid
leukemia patient CO).
{ECO:0000269|PubMed:8506309}.
SITE 481 481 KMT2A/MLL1 fusion point (in acute myeloid
leukemia patient F1).
{ECO:0000269|PubMed:8506309}.
MOD_RES 288 288 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 294 294 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163}.
MOD_RES 412 412 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 419 419 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 483 483 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
CROSSLNK 339 339 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 4 MASS -> M (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054924.
MUTAGEN 28 28 F->A: Decreased binding to crotonylated
histone H3. Decreased binding to
acetylated histone H3.
{ECO:0000269|PubMed:25417107,
ECO:0000269|PubMed:27105114}.
MUTAGEN 56 56 H->A: Decreased binding to crotonylated
histone H3. Decreased binding to
acetylated histone H3.
{ECO:0000269|PubMed:25417107,
ECO:0000269|PubMed:27105114}.
MUTAGEN 58 58 S->A: Decreased binding to crotonylated
histone H3. Decreased binding to
acetylated histone H3.
{ECO:0000269|PubMed:25417107,
ECO:0000269|PubMed:27105114}.
MUTAGEN 59 59 F->A: Strongly decreased binding to
crotonylated histone H3. Decreased
binding to acetylated histone H3.
{ECO:0000269|PubMed:25417107,
ECO:0000269|PubMed:27105114,
ECO:0000269|PubMed:27545619}.
MUTAGEN 77 77 G->A: Decreased binding to crotonylated
histone H3. Decreased binding to
acetylated histone H3.
{ECO:0000269|PubMed:25417107,
ECO:0000269|PubMed:27105114}.
MUTAGEN 78 78 Y->A: Strongly decreased binding to
crotonylated histone H3. Decreased
binding to acetylated histone H3.
{ECO:0000269|PubMed:25417107,
ECO:0000269|PubMed:27105114,
ECO:0000269|PubMed:27545619}.
MUTAGEN 81 81 F->A: Decreased binding to acetylated
histone H3.
{ECO:0000269|PubMed:25417107}.
MUTAGEN 103 103 D->A: Decreased binding to acetylated
histone H3.
{ECO:0000269|PubMed:25417107}.
CONFLICT 6 6 A -> S (in Ref. 1; AAA58361 and 2;
BAG35760). {ECO:0000305}.
CONFLICT 173 173 S -> G (in Ref. 5; AAH36089).
{ECO:0000305}.
CONFLICT 419 419 S -> P (in Ref. 2; BAG35760).
{ECO:0000305}.
STRAND 3 19 {ECO:0000244|PDB:4TMP}.
STRAND 30 37 {ECO:0000244|PDB:4TMP}.
HELIX 39 41 {ECO:0000244|PDB:4TMP}.
HELIX 44 46 {ECO:0000244|PDB:4TMP}.
STRAND 48 54 {ECO:0000244|PDB:4TMP}.
STRAND 59 61 {ECO:0000244|PDB:4TMP}.
STRAND 63 90 {ECO:0000244|PDB:4TMP}.
STRAND 92 94 {ECO:0000244|PDB:4TMP}.
STRAND 97 104 {ECO:0000244|PDB:4TMP}.
STRAND 114 126 {ECO:0000244|PDB:4TMP}.
HELIX 129 137 {ECO:0000244|PDB:4TMP}.
HELIX 504 515 {ECO:0000244|PDB:2LM0}.
HELIX 523 531 {ECO:0000244|PDB:2LM0}.
STRAND 536 538 {ECO:0000244|PDB:2LM0}.
STRAND 543 545 {ECO:0000244|PDB:2LM0}.
TURN 547 549 {ECO:0000244|PDB:2LM0}.
HELIX 552 561 {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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