ID AF9_HUMAN Reviewed; 568 AA. AC P42568; B1AMQ2; B2R7B3; B7Z755; D3DRJ8; Q8IVB0; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 2. DT 27-MAR-2024, entry version 193. DE RecName: Full=Protein AF-9 {ECO:0000305}; DE AltName: Full=ALL1-fused gene from chromosome 9 protein {ECO:0000303|PubMed:10861294}; DE AltName: Full=Myeloid/lymphoid or mixed-lineage leukemia translocated to chromosome 3 protein {ECO:0000303|PubMed:16001262}; DE AltName: Full=YEATS domain-containing protein 3; GN Name=MLLT3 {ECO:0000303|PubMed:16001262, ECO:0000312|HGNC:HGNC:7136}; GN Synonyms=AF9 {ECO:0000303|PubMed:10861294}, YEATS3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHROMOSOMAL TRANSLOCATION WITH RP KMT2A. RX PubMed=8506309; DOI=10.1073/pnas.90.10.4631; RA Nakamura T., Alder H., Gu Y., Prasad R., Canaani O., Kamada N., Gale R.P., RA Lange B., Crist W.M., Nowell P.C., Croce C.M., Canaani E.; RT "Genes on chromosomes 4, 9, and 19 involved in 11q23 abnormalities in acute RT leukemia share sequence homology and/or common motifs."; RL Proc. Natl. Acad. Sci. U.S.A. 90:4631-4635(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, and Synovium; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP INTERACTION WITH BCOR. RX PubMed=10898795; RA Huynh K.D., Fischle W., Verdin E., Bardwell V.J.; RT "BCoR, a novel corepressor involved in BCL-6 repression."; RL Genes Dev. 14:1810-1823(2000). RN [7] RP CHROMOSOMAL TRANSLOCATION. RX PubMed=10861294; DOI=10.1093/hmg/9.11.1671; RA Strissel P.L., Strick R., Tomek R.J., Roe B.A., Rowley J.D., RA Zeleznik-Le N.J.; RT "DNA structural properties of AF9 are similar to MLL and could act as RT recombination hot spots resulting in MLL/AF9 translocations and RT leukemogenesis."; RL Hum. Mol. Genet. 9:1671-1679(2000). RN [8] RP INTERACTION WITH CBX8. RX PubMed=11313972; DOI=10.1038/sj.onc.1204108; RA Garcia-Cuellar M.P., Zilles O., Schreiner S.A., Birke M., Winkler T.H., RA Slany R.K.; RT "The ENL moiety of the childhood leukemia-associated MLL-ENL oncoprotein RT recruits human Polycomb 3."; RL Oncogene 20:411-419(2001). RN [9] RP CHROMOSOMAL TRANSLOCATION. RX PubMed=16001262; DOI=10.1007/s00439-005-0004-1; RA Pramparo T., Grosso S., Messa J., Zatterale A., Bonaglia M.C., Chessa L., RA Balestri P., Rocchi M., Zuffardi O., Giorda R.; RT "Loss-of-function mutation of the AF9/MLLT3 gene in a girl with neuromotor RT development delay, cerebellar ataxia, and epilepsy."; RL Hum. Genet. 118:76-81(2005). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294 AND SER-483, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288; SER-294 AND SER-483, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412 AND SER-419, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [14] RP FUNCTION, AND IDENTIFICATION IN THE SEC COMPLEX. RX PubMed=20471948; DOI=10.1016/j.molcel.2010.04.013; RA He N., Liu M., Hsu J., Xue Y., Chou S., Burlingame A., Krogan N.J., RA Alber T., Zhou Q.; RT "HIV-1 Tat and host AFF4 recruit two transcription elongation factors into RT a bifunctional complex for coordinated activation of HIV-1 transcription."; RL Mol. Cell 38:428-438(2010). RN [15] RP FUNCTION, AND IDENTIFICATION IN THE SEC COMPLEX. RX PubMed=20159561; DOI=10.1016/j.molcel.2010.01.026; RA Lin C., Smith E.R., Takahashi H., Lai K.C., Martin-Brown S., Florens L., RA Washburn M.P., Conaway J.W., Conaway R.C., Shilatifard A.; RT "AFF4, a component of the ELL/P-TEFb elongation complex and a shared RT subunit of MLL chimeras, can link transcription elongation to leukemia."; RL Mol. Cell 37:429-437(2010). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [17] RP IDENTIFICATION IN THE SEC COMPLEX. RX PubMed=22195968; DOI=10.1016/j.molcel.2011.12.008; RA Smith E.R., Lin C., Garrett A.S., Thornton J., Mohaghegh N., Hu D., RA Jackson J., Saraf A., Swanson S.K., Seidel C., Florens L., Washburn M.P., RA Eissenberg J.C., Shilatifard A.; RT "The little elongation complex regulates small nuclear RNA transcription."; RL Mol. Cell 44:954-965(2011). RN [18] RP INTERACTION OF FUSION PROTEIN KMT2A-MLLT3 WITH MEN1. RX PubMed=22936661; DOI=10.1182/blood-2012-05-429274; RA Shi A., Murai M.J., He S., Lund G., Hartley T., Purohit T., Reddy G., RA Chruszcz M., Grembecka J., Cierpicki T.; RT "Structural insights into inhibition of the bivalent menin-MLL interaction RT by small molecules in leukemia."; RL Blood 120:4461-4469(2012). RN [19] RP REVIEW ON THE SUPER ELONGATION COMPLEX. RX PubMed=22895430; DOI=10.1038/nrm3417; RA Luo Z., Lin C., Shilatifard A.; RT "The super elongation complex (SEC) family in transcriptional control."; RL Nat. Rev. Mol. Cell Biol. 13:543-547(2012). RN [20] RP INTERACTION WITH ALKBH4. RX PubMed=23145062; DOI=10.1371/journal.pone.0049045; RA Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M., Meza-Zepeda L.A., RA Falnes P.O.; RT "Human ALKBH4 interacts with proteins associated with transcription."; RL PLoS ONE 7:E49045-E49045(2012). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294 AND SER-483, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [22] RP INTERACTION OF FUSION PROTEIN KMT2A-MLLT3 WITH PSIP1 AND MEN1. RX PubMed=25305204; DOI=10.1182/blood-2014-01-550079; RA Murai M.J., Pollock J., He S., Miao H., Purohit T., Yokom A., Hess J.L., RA Muntean A.G., Grembecka J., Cierpicki T.; RT "The same site on the integrase-binding domain of lens epithelium-derived RT growth factor is a therapeutic target for MLL leukemia and HIV."; RL Blood 124:3730-3737(2014). RN [23] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-339, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [24] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-339, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [25] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=31776511; DOI=10.1038/s41586-019-1790-2; RA Calvanese V., Nguyen A.T., Bolan T.J., Vavilina A., Su T., Lee L.K., RA Wang Y., Lay F.D., Magnusson M., Crooks G.M., Kurdistani S.K., RA Mikkola H.K.A.; RT "MLLT3 governs human haematopoietic stem-cell self-renewal and RT engraftment."; RL Nature 576:281-286(2019). RN [26] RP INTERACTION WITH CDK9, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=30134174; DOI=10.1016/j.celrep.2018.07.064; RA Ghosh K., Tang M., Kumari N., Nandy A., Basu S., Mall D.P., Rai K., RA Biswas D.; RT "Positive Regulation of Transcription by Human ZMYND8 through Its RT Association with P-TEFb Complex."; RL Cell Rep. 24:2141-2154(2018). RN [27] {ECO:0007744|PDB:2LM0} RP STRUCTURE BY NMR OF 490-568 IN COMPLEX WITH AFF1. RX PubMed=23260655; DOI=10.1016/j.str.2012.11.011; RA Leach B.I., Kuntimaddi A., Schmidt C.R., Cierpicki T., Johnson S.A., RA Bushweller J.H.; RT "Leukemia fusion target AF9 is an intrinsically disordered transcriptional RT regulator that recruits multiple partners via coupled folding and RT binding."; RL Structure 21:176-183(2013). RN [28] {ECO:0007744|PDB:4TMP} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-138 IN COMPLEX WITH H3K9AC RP PEPTIDE, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF PHE-28; RP HIS-56; SER-58; PHE-59; GLY-77; TYR-78; PHE-81 AND ASP-103. RX PubMed=25417107; DOI=10.1016/j.cell.2014.09.049; RA Li Y., Wen H., Xi Y., Tanaka K., Wang H., Peng D., Ren Y., Jin Q., RA Dent S.Y., Li W., Li H., Shi X.; RT "AF9 YEATS domain links histone acetylation to DOT1L-mediated H3K79 RT methylation."; RL Cell 159:558-571(2014). RN [29] {ECO:0007744|PDB:5HJB, ECO:0007744|PDB:5HJD} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-138 IN COMPLEX WITH H3K9CR RP PEPTIDE, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF PHE-28; RP HIS-56; SER-58; PHE-59; GLY-77 AND TYR-78. RX PubMed=27105114; DOI=10.1016/j.molcel.2016.03.028; RA Li Y., Sabari B.R., Panchenko T., Wen H., Zhao D., Guan H., Wan L., RA Huang H., Tang Z., Zhao Y., Roeder R.G., Shi X., Allis C.D., Li H.; RT "Molecular coupling of histone crotonylation and active transcription by RT AF9 YEATS domain."; RL Mol. Cell 62:181-193(2016). RN [30] {ECO:0007744|PDB:2NDF, ECO:0007744|PDB:2NDG} RP STRUCTURE BY NMR OF 1-138, FUNCTION, DOMAIN, AND MUTAGENESIS OF PHE-59 AND RP TYR-78. RX PubMed=27545619; DOI=10.1016/j.str.2016.05.023; RA Zhang Q., Zeng L., Zhao C., Ju Y., Konuma T., Zhou M.M.; RT "Structural insights into histone crotonyl-lysine recognition by the AF9 RT YEATS domain."; RL Structure 24:1606-1612(2016). RN [31] {ECO:0007744|PDB:5YYF} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-138 IN COMPLEX WITH INHIBITOR, RP FUNCTION, DOMAIN, AND ACTIVITY REGULATION. RX PubMed=30374167; DOI=10.1038/s41589-018-0144-y; RA Li X., Li X.M., Jiang Y., Liu Z., Cui Y., Fung K.Y., van der Beelen S.H.E., RA Tian G., Wan L., Shi X., Allis C.D., Li H., Li Y., Li X.D.; RT "Structure-guided development of YEATS domain inhibitors by targeting pi- RT pi-pi stacking."; RL Nat. Chem. Biol. 14:1140-1149(2018). RN [32] {ECO:0007744|PDB:6MIL, ECO:0007744|PDB:6MIM} RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 1-138 IN COMPLEX WITH H3K9CR RP PEPTIDE, FUNCTION, DOMAIN, AND MUTAGENESIS OF 61-ARG--LYS-67; 78-TYR-ALA-79 RP AND TYR-78. RX PubMed=30385749; DOI=10.1038/s41467-018-07072-6; RA Klein B.J., Vann K.R., Andrews F.H., Wang W.W., Zhang J., Zhang Y., RA Beloglazkina A.A., Mi W., Li Y., Li H., Shi X., Kutateladze A.G., RA Strahl B.D., Liu W.R., Kutateladze T.G.; RT "Structural insights into the pi-pi-pi stacking mechanism and DNA-binding RT activity of the YEATS domain."; RL Nat. Commun. 9:4574-4574(2018). CC -!- FUNCTION: Chromatin reader component of the super elongation complex CC (SEC), a complex required to increase the catalytic rate of RNA CC polymerase II transcription by suppressing transient pausing by the CC polymerase at multiple sites along the DNA (PubMed:20159561, CC PubMed:20471948, PubMed:25417107, PubMed:27105114, PubMed:27545619). CC Specifically recognizes and binds acylated histone H3, with a CC preference for histone H3 that is crotonylated (PubMed:25417107, CC PubMed:27105114, PubMed:27545619, PubMed:30374167, PubMed:30385749). CC Crotonylation marks active promoters and enhancers and confers CC resistance to transcriptional repressors (PubMed:25417107, CC PubMed:27105114, PubMed:27545619). Recognizes and binds histone H3 CC crotonylated at 'Lys-9' (H3K9cr), and with slightly lower affinity CC histone H3 crotonylated at 'Lys-18' (H3K18cr) (PubMed:27105114). Also CC recognizes and binds histone H3 acetylated and butyrylated at 'Lys-9' CC (H3K9ac and H3K9bu, respectively), but with lower affinity than CC crotonylated histone H3 (PubMed:25417107, PubMed:27105114, CC PubMed:30385749). In the SEC complex, MLLT3 is required to recruit the CC complex to crotonylated histones (PubMed:27105114, PubMed:27545619). CC Recruitment of the SEC complex to crotonylated histones promotes CC recruitment of DOT1L on active chromatin to deposit histone H3 'Lys-79' CC methylation (H3K79me) (PubMed:25417107). Plays a key role in CC hematopoietic stem cell (HSC) maintenance by preserving, rather than CC conferring, HSC stemness (PubMed:31776511). Acts by binding to the CC transcription start site of active genes in HSCs and sustaining level CC of H3K79me2, probably by recruiting DOT1L (PubMed:31776511). CC {ECO:0000269|PubMed:20159561, ECO:0000269|PubMed:20471948, CC ECO:0000269|PubMed:25417107, ECO:0000269|PubMed:27105114, CC ECO:0000269|PubMed:27545619, ECO:0000269|PubMed:30374167, CC ECO:0000269|PubMed:30385749, ECO:0000269|PubMed:31776511}. CC -!- ACTIVITY REGULATION: Crotonylated lysine binding is strongly inhibited CC by the peptide XL-07i, carrying a 2-furancarbonyl side chain and capped CC with a hydrophobic carboxybenzyl group (PubMed:30374167). XL-07i CC targets the unique pi-pi-pi stacking interaction at the crotonylation CC recognition site (PubMed:30374167). {ECO:0000269|PubMed:30374167}. CC -!- SUBUNIT: Component of the super elongation complex (SEC), at least CC composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb CC complex and ELL (ELL, ELL2 or ELL3) (PubMed:20159561, PubMed:20471948, CC PubMed:22195968, PubMed:23260655, PubMed:25417107, PubMed:30134174). CC Interacts with BCOR (PubMed:10898795). Interacts with CBX8 CC (PubMed:11313972). Interacts with ALKBH4 (PubMed:23145062). CC {ECO:0000269|PubMed:10898795, ECO:0000269|PubMed:11313972, CC ECO:0000269|PubMed:20159561, ECO:0000269|PubMed:20471948, CC ECO:0000269|PubMed:22195968, ECO:0000269|PubMed:23145062, CC ECO:0000269|PubMed:23260655, ECO:0000269|PubMed:25417107, CC ECO:0000269|PubMed:30134174}. CC -!- INTERACTION: CC P42568; P51825: AFF1; NbExp=7; IntAct=EBI-716132, EBI-2610180; CC P42568; Q9UHB7: AFF4; NbExp=4; IntAct=EBI-716132, EBI-395282; CC P42568; Q9NXW9: ALKBH4; NbExp=5; IntAct=EBI-716132, EBI-8637516; CC P42568; Q92624: APPBP2; NbExp=4; IntAct=EBI-716132, EBI-743771; CC P42568; Q6W2J9-1: BCOR; NbExp=2; IntAct=EBI-716132, EBI-16028932; CC P42568; Q9HC52: CBX8; NbExp=2; IntAct=EBI-716132, EBI-712912; CC P42568; Q8TEK3: DOT1L; NbExp=6; IntAct=EBI-716132, EBI-2619253; CC P42568; Q8IZU1: FAM9A; NbExp=4; IntAct=EBI-716132, EBI-8468186; CC P42568; Q5JXC2: MIIP; NbExp=3; IntAct=EBI-716132, EBI-2801965; CC P42568; Q5SQQ9-2: VAX1; NbExp=3; IntAct=EBI-716132, EBI-12227803; CC P42568; Q7Z3I7: ZNF572; NbExp=3; IntAct=EBI-716132, EBI-10172590; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00376, CC ECO:0000269|PubMed:27105114}. Chromosome {ECO:0000269|PubMed:25417107, CC ECO:0000269|PubMed:27105114}. Note=Colocalizes with acylated histone H3 CC (PubMed:25417107, PubMed:27105114). Colocalizes with histone H3 CC crotonylated at 'Lys-18' (H3K18cr) (PubMed:27105114). CC {ECO:0000269|PubMed:25417107, ECO:0000269|PubMed:27105114}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P42568-1; Sequence=Displayed; CC Name=2; CC IsoId=P42568-2; Sequence=VSP_054924; CC -!- TISSUE SPECIFICITY: Enriched in undifferentiated hematopoietic stem CC cells in fetal liver, cord blood and bone marrow. CC {ECO:0000269|PubMed:31776511}. CC -!- DOMAIN: The YEATS domain specifically recognizes and binds acylated CC histones, with a marked preference for histones that are crotonylated CC (PubMed:27105114, PubMed:27545619). Also binds histone H3 acetylated at CC 'Lys-9' (H3K9ac), but with lower affinity (PubMed:25417107, CC PubMed:27105114). Binds crotonylated lysine through a non-canonical pi- CC pi-pi stacking mechanism (PubMed:30374167, PubMed:30385749). The YEATS CC domain also binds DNA (PubMed:30385749). {ECO:0000269|PubMed:25417107, CC ECO:0000269|PubMed:27105114, ECO:0000269|PubMed:27545619, CC ECO:0000269|PubMed:30374167, ECO:0000269|PubMed:30385749}. CC -!- DISEASE: Note=A chromosomal aberration involving MLLT3 is associated CC with acute leukemias. Translocation t(9;11)(p22;q23) with KMT2A/MLL1. CC The result is a rogue activator protein. Fusion protein KMT2A-MLLT3 CC interacts with MEN1 and PSIP1 (PubMed:22936661, PubMed:25305204). CC {ECO:0000269|PubMed:10861294, ECO:0000269|PubMed:22936661, CC ECO:0000269|PubMed:25305204, ECO:0000269|PubMed:8506309}. CC -!- DISEASE: Note=A chromosomal aberration involving MLLT3 was observed in CC a patient with neuromotor development delay, cerebellar ataxia and CC epilepsy. Translocation t(4;9)(q35;p22). {ECO:0000269|PubMed:16001262}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/5/mllt3"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L13744; AAA58361.1; -; mRNA. DR EMBL; AK301474; BAH13491.1; -; mRNA. DR EMBL; AK312914; BAG35760.1; -; mRNA. DR EMBL; AL354879; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL512635; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL513498; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL163193; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL627410; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471071; EAW58631.1; -; Genomic_DNA. DR EMBL; CH471071; EAW58632.1; -; Genomic_DNA. DR EMBL; BC036089; AAH36089.1; -; mRNA. DR CCDS; CCDS6494.1; -. [P42568-1] DR CCDS; CCDS69579.1; -. [P42568-2] DR PIR; I39411; I39411. DR RefSeq; NP_001273620.1; NM_001286691.1. [P42568-2] DR RefSeq; NP_004520.2; NM_004529.3. [P42568-1] DR PDB; 2LM0; NMR; -; A=490-568. DR PDB; 2MV7; NMR; -; A=500-568. DR PDB; 2N4Q; NMR; -; B=500-568. DR PDB; 2NDF; NMR; -; A=1-138. DR PDB; 2NDG; NMR; -; A=1-138. DR PDB; 4TMP; X-ray; 2.30 A; A/C=1-138. DR PDB; 5HJB; X-ray; 2.70 A; A=1-138. DR PDB; 5HJD; X-ray; 2.81 A; A/C/E/G/K/N/Q/T=1-138. DR PDB; 5YYF; X-ray; 1.90 A; A/C=1-138. DR PDB; 6B7G; NMR; -; A=500-568. DR PDB; 6L5Z; X-ray; 3.05 A; A=1-138. DR PDB; 6LS6; X-ray; 2.20 A; A/B=1-138. DR PDB; 6MIL; X-ray; 1.93 A; A/C=1-138. DR PDB; 6MIM; X-ray; 2.52 A; A/C=1-138. DR PDB; 7EIC; X-ray; 1.95 A; A/B=1-138. DR PDB; 7EID; X-ray; 2.00 A; A/B=1-138. DR PDB; 7VKG; X-ray; 1.83 A; A=1-138. DR PDB; 7VKH; X-ray; 2.25 A; A/B=1-138. DR PDB; 8PJ7; X-ray; 1.26 A; A=1-142. DR PDBsum; 2LM0; -. DR PDBsum; 2MV7; -. DR PDBsum; 2N4Q; -. DR PDBsum; 2NDF; -. DR PDBsum; 2NDG; -. DR PDBsum; 4TMP; -. DR PDBsum; 5HJB; -. DR PDBsum; 5HJD; -. DR PDBsum; 5YYF; -. DR PDBsum; 6B7G; -. DR PDBsum; 6L5Z; -. DR PDBsum; 6LS6; -. DR PDBsum; 6MIL; -. DR PDBsum; 6MIM; -. DR PDBsum; 7EIC; -. DR PDBsum; 7EID; -. DR PDBsum; 7VKG; -. DR PDBsum; 7VKH; -. DR PDBsum; 8PJ7; -. DR AlphaFoldDB; P42568; -. DR BMRB; P42568; -. DR SMR; P42568; -. DR BioGRID; 110446; 86. DR CORUM; P42568; -. DR DIP; DIP-56409N; -. DR IntAct; P42568; 53. DR MINT; P42568; -. DR STRING; 9606.ENSP00000369695; -. DR BindingDB; P42568; -. DR ChEMBL; CHEMBL4295761; -. DR GlyGen; P42568; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P42568; -. DR PhosphoSitePlus; P42568; -. DR BioMuta; MLLT3; -. DR DMDM; 215273971; -. DR jPOST; P42568; -. DR MassIVE; P42568; -. DR MaxQB; P42568; -. DR PaxDb; 9606-ENSP00000369695; -. DR PeptideAtlas; P42568; -. DR ProteomicsDB; 55517; -. [P42568-1] DR ProteomicsDB; 6833; -. DR Pumba; P42568; -. DR Antibodypedia; 1068; 320 antibodies from 29 providers. DR DNASU; 4300; -. DR Ensembl; ENST00000380338.9; ENSP00000369695.4; ENSG00000171843.17. [P42568-1] DR Ensembl; ENST00000630269.2; ENSP00000485996.1; ENSG00000171843.17. [P42568-2] DR GeneID; 4300; -. DR KEGG; hsa:4300; -. DR MANE-Select; ENST00000380338.9; ENSP00000369695.4; NM_004529.4; NP_004520.2. DR UCSC; uc003zoe.3; human. [P42568-1] DR AGR; HGNC:7136; -. DR CTD; 4300; -. DR DisGeNET; 4300; -. DR GeneCards; MLLT3; -. DR HGNC; HGNC:7136; MLLT3. DR HPA; ENSG00000171843; Low tissue specificity. DR MalaCards; MLLT3; -. DR MIM; 159558; gene. DR neXtProt; NX_P42568; -. DR OpenTargets; ENSG00000171843; -. DR Orphanet; 402017; Acute myeloid leukemia with t(9;11)(p22;q23). DR PharmGKB; PA30852; -. DR VEuPathDB; HostDB:ENSG00000171843; -. DR eggNOG; KOG3149; Eukaryota. DR GeneTree; ENSGT00940000155903; -. DR InParanoid; P42568; -. DR OMA; RIMYQYD; -. DR OrthoDB; 4267365at2759; -. DR PhylomeDB; P42568; -. DR TreeFam; TF314586; -. DR PathwayCommons; P42568; -. DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex. DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events. DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation. DR SignaLink; P42568; -. DR SIGNOR; P42568; -. DR BioGRID-ORCS; 4300; 25 hits in 1156 CRISPR screens. DR ChiTaRS; MLLT3; human. DR GeneWiki; MLLT3; -. DR GenomeRNAi; 4300; -. DR Pharos; P42568; Tchem. DR PRO; PR:P42568; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; P42568; Protein. DR Bgee; ENSG00000171843; Expressed in ganglionic eminence and 167 other cell types or tissues. DR ExpressionAtlas; P42568; baseline and differential. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. DR GO; GO:0008023; C:transcription elongation factor complex; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0042393; F:histone binding; IDA:UniProtKB. DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB. DR GO; GO:0140030; F:modification-dependent protein binding; IDA:UniProtKB. DR GO; GO:0060090; F:molecular adaptor activity; EXP:DisProt. DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl. DR GO; GO:0010467; P:gene expression; IEA:Ensembl. DR GO; GO:0060218; P:hematopoietic stem cell differentiation; IDA:UniProtKB. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:2000096; P:positive regulation of Wnt signaling pathway, planar cell polarity pathway; IGI:MGI. DR GO; GO:1902275; P:regulation of chromatin organization; IMP:UniProtKB. DR GO; GO:2000035; P:regulation of stem cell division; IDA:UniProtKB. DR GO; GO:0007379; P:segment specification; IEA:Ensembl. DR CDD; cd16906; YEATS_AF-9_like; 1. DR DisProt; DP01070; -. DR Gene3D; 1.20.1270.290; -; 1. DR Gene3D; 2.60.40.1970; YEATS domain; 1. DR IDEAL; IID00552; -. DR InterPro; IPR040930; AF-9_AHD. DR InterPro; IPR038704; YEAST_sf. DR InterPro; IPR005033; YEATS. DR PANTHER; PTHR47827; AHD DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR47827:SF5; PROTEIN AF-9; 1. DR Pfam; PF17793; AHD; 1. DR Pfam; PF03366; YEATS; 1. DR PROSITE; PS51037; YEATS; 1. DR Genevisible; P42568; HS. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; Chromosomal rearrangement; KW Chromosome; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; KW Proto-oncogene; Reference proteome; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..568 FT /note="Protein AF-9" FT /id="PRO_0000215921" FT DOMAIN 1..138 FT /note="YEATS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00376" FT REGION 78..80 FT /note="Histone H3K9cr binding" FT /evidence="ECO:0000269|PubMed:27105114, FT ECO:0000269|PubMed:30385749, ECO:0007744|PDB:5HJB, FT ECO:0007744|PDB:5HJD, ECO:0007744|PDB:6MIL, FT ECO:0007744|PDB:6MIM" FT REGION 106..108 FT /note="Histone H3K9cr binding" FT /evidence="ECO:0000269|PubMed:27105114, FT ECO:0000269|PubMed:30385749, ECO:0007744|PDB:5HJB, FT ECO:0007744|PDB:5HJD, ECO:0007744|PDB:6MIL, FT ECO:0007744|PDB:6MIM" FT REGION 137..475 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 295..300 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 143..195 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 196..262 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 282..304 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 323..354 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 373..403 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 414..428 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 441..461 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 58 FT /note="Histone H3K9cr binding" FT /evidence="ECO:0000269|PubMed:27105114, FT ECO:0000269|PubMed:30385749, ECO:0007744|PDB:5HJB, FT ECO:0007744|PDB:5HJD, ECO:0007744|PDB:6MIL, FT ECO:0007744|PDB:6MIM" FT SITE 103 FT /note="Histone H3K9cr binding" FT /evidence="ECO:0000269|PubMed:27105114, FT ECO:0000269|PubMed:30385749, ECO:0007744|PDB:5HJB, FT ECO:0007744|PDB:5HJD, ECO:0007744|PDB:6MIL, FT ECO:0007744|PDB:6MIM" FT SITE 375 FT /note="KMT2A/MLL1 fusion point (in acute myeloid leukemia FT patient CO)" FT /evidence="ECO:0000269|PubMed:8506309" FT SITE 481 FT /note="KMT2A/MLL1 fusion point (in acute myeloid leukemia FT patient F1)" FT /evidence="ECO:0000269|PubMed:8506309" FT MOD_RES 288 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 294 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163" FT MOD_RES 412 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 419 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 483 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT CROSSLNK 339 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..4 FT /note="MASS -> M (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054924" FT MUTAGEN 28 FT /note="F->A: Decreased binding to crotonylated histone H3. FT Decreased binding to acetylated histone H3." FT /evidence="ECO:0000269|PubMed:25417107, FT ECO:0000269|PubMed:27105114" FT MUTAGEN 56 FT /note="H->A: Decreased binding to crotonylated histone H3. FT Decreased binding to acetylated histone H3." FT /evidence="ECO:0000269|PubMed:25417107, FT ECO:0000269|PubMed:27105114" FT MUTAGEN 58 FT /note="S->A: Decreased binding to crotonylated histone H3. FT Decreased binding to acetylated histone H3." FT /evidence="ECO:0000269|PubMed:25417107, FT ECO:0000269|PubMed:27105114" FT MUTAGEN 59 FT /note="F->A: Strongly decreased binding to crotonylated FT histone H3. Decreased binding to acetylated histone H3." FT /evidence="ECO:0000269|PubMed:25417107, FT ECO:0000269|PubMed:27105114, ECO:0000269|PubMed:27545619" FT MUTAGEN 61..67 FT /note="RPKRVCK->EPERVCE: Decreased DNA-binding." FT /evidence="ECO:0000269|PubMed:30385749" FT MUTAGEN 77 FT /note="G->A: Decreased binding to crotonylated histone H3. FT Decreased binding to acetylated histone H3." FT /evidence="ECO:0000269|PubMed:25417107, FT ECO:0000269|PubMed:27105114" FT MUTAGEN 78..79 FT /note="YA->WG: Binds equally well acetylated and FT crotonylated histone H3." FT /evidence="ECO:0000269|PubMed:30385749" FT MUTAGEN 78 FT /note="Y->A: Strongly decreased binding to crotonylated FT histone H3. Decreased binding to acetylated histone H3." FT /evidence="ECO:0000269|PubMed:25417107, FT ECO:0000269|PubMed:27105114, ECO:0000269|PubMed:27545619" FT MUTAGEN 78 FT /note="Y->W: Does not affect ability to discriminate FT between acetylated and crotonylated histone H3." FT /evidence="ECO:0000269|PubMed:30385749" FT MUTAGEN 81 FT /note="F->A: Decreased binding to acetylated histone H3." FT /evidence="ECO:0000269|PubMed:25417107" FT MUTAGEN 103 FT /note="D->A: Decreased binding to acetylated histone H3." FT /evidence="ECO:0000269|PubMed:25417107" FT CONFLICT 6 FT /note="A -> S (in Ref. 1; AAA58361 and 2; BAG35760)" FT /evidence="ECO:0000305" FT CONFLICT 173 FT /note="S -> G (in Ref. 5; AAH36089)" FT /evidence="ECO:0000305" FT CONFLICT 419 FT /note="S -> P (in Ref. 2; BAG35760)" FT /evidence="ECO:0000305" FT STRAND 7..19 FT /evidence="ECO:0007829|PDB:7VKG" FT STRAND 30..37 FT /evidence="ECO:0007829|PDB:7VKG" FT HELIX 39..41 FT /evidence="ECO:0007829|PDB:5YYF" FT HELIX 44..46 FT /evidence="ECO:0007829|PDB:7VKG" FT STRAND 48..54 FT /evidence="ECO:0007829|PDB:7VKG" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:7VKG" FT STRAND 63..79 FT /evidence="ECO:0007829|PDB:7VKG" FT STRAND 81..94 FT /evidence="ECO:0007829|PDB:7VKG" FT STRAND 96..104 FT /evidence="ECO:0007829|PDB:7VKG" FT STRAND 114..126 FT /evidence="ECO:0007829|PDB:7VKG" FT HELIX 129..137 FT /evidence="ECO:0007829|PDB:7VKG" FT HELIX 504..515 FT /evidence="ECO:0007829|PDB:2LM0" FT HELIX 523..531 FT /evidence="ECO:0007829|PDB:2LM0" FT STRAND 536..538 FT /evidence="ECO:0007829|PDB:2LM0" FT STRAND 543..545 FT /evidence="ECO:0007829|PDB:2LM0" FT TURN 547..549 FT /evidence="ECO:0007829|PDB:2LM0" FT HELIX 552..561 FT /evidence="ECO:0007829|PDB:2LM0" SQ 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 //