AF10_HUMAN
ID AF10_HUMAN Reviewed; 1068 AA.
AC P55197; B1ANA8; Q5JT37; Q5VX90; Q66K63;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Protein AF-10 {ECO:0000305};
DE AltName: Full=ALL1-fused gene from chromosome 10 protein;
GN Name=MLLT10 {ECO:0000312|HGNC:HGNC:16063};
GN Synonyms=AF10 {ECO:0000303|PubMed:10860745};
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).
RX PubMed=7888665;
RA Chaplin T., Ayton P., Bernard O.A., Saha V., Della Valle V., Hillion J.,
RA Gregorini A., Lillington D., Berger R., Young B.D.;
RT "A novel class of zinc finger/leucine zipper genes identified from the
RT molecular cloning of the t(10;11) translocation in acute leukemia.";
RL Blood 85:1435-1441(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND INTERACTION WITH DOT1L.
RX PubMed=15851025; DOI=10.1016/j.cell.2005.02.020;
RA Okada Y., Feng Q., Lin Y., Jiang Q., Li Y., Coffield V.M., Su L., Xu G.,
RA Zhang Y.;
RT "hDOT1L links histone methylation to leukemogenesis.";
RL Cell 121:167-178(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC TISSUE=Ovary, and Prostate;
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 [5]
RP SELF-ASSOCIATION, SUBCELLULAR LOCATION, AND DNA-BINDING.
RX PubMed=10860745; DOI=10.1006/jmbi.2000.3766;
RA Linder B., Newman R., Jones L.K., Debernardi S., Young B.D., Freemont P.,
RA Verrijzer C.P., Saha V.;
RT "Biochemical analyses of the AF10 protein: the extended LAP/PHD-finger
RT mediates oligomerisation.";
RL J. Mol. Biol. 299:369-378(2000).
RN [6]
RP INTERACTION WITH SS18.
RX PubMed=11423977; DOI=10.1038/sj.onc.1204419;
RA de Bruijn D.R., dos Santos N.R., Thijssen J., Balemans M., Debernardi S.,
RA Linder B., Young B.D., Geurts van Kessel A.;
RT "The synovial sarcoma associated protein SYT interacts with the acute
RT leukemia associated protein AF10.";
RL Oncogene 20:3281-3289(2001).
RN [7]
RP INTERACTION WITH YEATS4.
RX PubMed=11756182; DOI=10.1182/blood.v99.1.275;
RA Debernardi S., Bassini A., Jones L.K., Chaplin T., Linder B.,
RA de Bruijn D.R.H., Meese E., Young B.D.;
RT "The MLL fusion partner AF10 binds GAS41, a protein that interacts with the
RT human SWI/SNF complex.";
RL Blood 99:275-281(2002).
RN [8]
RP TRANSACTIVATION DOMAIN.
RX PubMed=11986236; DOI=10.1182/blood.v99.10.3780;
RA DiMartino J.F., Ayton P.M., Chen E.H., Naftzger C.C., Young B.D.,
RA Cleary M.L.;
RT "The AF10 leucine zipper is required for leukemic transformation of myeloid
RT progenitors by MLL-AF10.";
RL Blood 99:3780-3785(2002).
RN [9]
RP FUNCTION, SELF-ASSOCIATION, AND INTERACTION WITH FSTL3.
RX PubMed=17868029; DOI=10.1042/bc20060131;
RA Forissier S., Razanajaona D., Ay A.S., Martel S., Bartholin L., Rimokh R.;
RT "AF10-dependent transcription is enhanced by its interaction with FLRG.";
RL Biol. Cell 99:563-571(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-684 AND SER-686, 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=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
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 IDENTIFICATION BY 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-252; SER-436;
RP SER-686 AND SER-689, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-280, 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 [17] {ECO:0007744|PDB:5DAG, ECO:0007744|PDB:5DAH}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-208 IN COMPLEX WITH HISTONE H3
RP PEPTIDE AND ZINC, INTERACTION WITH HISTONE H3, MUTAGENESIS OF ILE-22;
RP VAL-80; ALA-106; LEU-107; ILE-109; PHE-114; MET-120; GLU-179 AND TYR-190,
RP FUNCTION, AND REGION.
RX PubMed=26439302; DOI=10.1016/j.molcel.2015.08.019;
RA Chen S., Yang Z., Wilkinson A.W., Deshpande A.J., Sidoli S., Krajewski K.,
RA Strahl B.D., Garcia B.A., Armstrong S.A., Patel D.J., Gozani O.;
RT "The PZP Domain of AF10 Senses Unmodified H3K27 to Regulate DOT1L-Mediated
RT Methylation of H3K79.";
RL Mol. Cell 60:319-327(2015).
RN [18] {ECO:0007744|PDB:6CKN, ECO:0007744|PDB:6CKO}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 704-779.
RA Zhang H., Tempel W., Bountra C., Arrowsmith C.H., Edwards A.M., Min J.;
RT "Crystal structure of an AF10 fragment.";
RL Submitted (FEB-2018) to the PDB data bank.
CC -!- FUNCTION: Probably involved in transcriptional regulation. In vitro or
CC as fusion protein with KMT2A/MLL1 has transactivation activity. Binds
CC to cruciform DNA. In cells, binding to unmodified histone H3 regulates
CC DOT1L functions including histone H3 'Lys-79' dimethylation (H3K79me2)
CC and gene activation (PubMed:26439302). {ECO:0000269|PubMed:17868029,
CC ECO:0000269|PubMed:26439302}.
CC -!- SUBUNIT: Self-associates. Interacts with FSTL3 isoform 2; the
CC interaction enhances MLLT10 in vitro transcriptional activity and self-
CC association. Interacts with YEATS4. Interacts with SS18. Interacts with
CC DOT1L; this interaction also occurs with the KMT2A/MLL1 fusion protein.
CC Interacts with histone H3; interaction is necessary for MLLT10 binding
CC to nucleosomes; interaction is inhibited by histone H3 'Lys-27'
CC methylations (H3K27me1, H3K27me2 and H3K27me3) amd acetylation;
CC interaction stabilizes association of MLLT10 at chromatin; interaction
CC is essential for histone H3 'Lys-79' dimethylation (H3K79me2)
CC (PubMed:26439302). {ECO:0000269|PubMed:11423977,
CC ECO:0000269|PubMed:11756182, ECO:0000269|PubMed:15851025,
CC ECO:0000269|PubMed:17868029, ECO:0000269|PubMed:26439302}.
CC -!- INTERACTION:
CC P55197; P35222: CTNNB1; NbExp=4; IntAct=EBI-1104952, EBI-491549;
CC P55197; Q93009: USP7; NbExp=2; IntAct=EBI-1104952, EBI-302474;
CC P55197-2; Q12951-2: FOXI1; NbExp=3; IntAct=EBI-12853322, EBI-12018822;
CC P55197-2; P35680: HNF1B; NbExp=3; IntAct=EBI-12853322, EBI-2798841;
CC P55197-2; P84074: HPCA; NbExp=3; IntAct=EBI-12853322, EBI-12197079;
CC P55197-2; P61601: NCALD; NbExp=3; IntAct=EBI-12853322, EBI-749635;
CC P55197-2; P14859-6: POU2F1; NbExp=3; IntAct=EBI-12853322, EBI-11526590;
CC P55197-2; P78424: POU6F2; NbExp=3; IntAct=EBI-12853322, EBI-12029004;
CC P55197-2; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-12853322, EBI-740343;
CC P55197-2; Q14119: VEZF1; NbExp=3; IntAct=EBI-12853322, EBI-11980193;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10860745}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=4;
CC IsoId=P55197-4; Sequence=Displayed;
CC Name=1;
CC IsoId=P55197-1; Sequence=VSP_047517, VSP_047518, VSP_047519;
CC Name=2;
CC IsoId=P55197-2; Sequence=VSP_043044, VSP_043045;
CC Name=3;
CC IsoId=P55197-3; Sequence=VSP_044552, VSP_044553;
CC -!- TISSUE SPECIFICITY: Expressed abundantly in testis.
CC -!- DISEASE: Note=A chromosomal aberration involving MLLT10 is associated
CC with acute leukemias. Translocation t(10;11)(p12;q23) with KMT2A/MLL1.
CC The result is a rogue activator protein.
CC -!- DISEASE: Note=A chromosomal aberration involving MLLT10 is associated
CC with diffuse histiocytic lymphomas. Translocation t(10;11)(p13;q14)
CC with PICALM.
CC -!- SEQUENCE CAUTION:
CC Sequence=BC129946; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/AF10ID4.html";
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DR EMBL; U13948; AAA79972.1; -; mRNA.
DR EMBL; AY598745; AAT47519.1; -; mRNA.
DR EMBL; AL161799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL358780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359697; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL357372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC080577; AAH80577.1; -; mRNA.
DR EMBL; BC094844; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC129946; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS55706.1; -. [P55197-2]
DR CCDS; CCDS55707.1; -. [P55197-3]
DR CCDS; CCDS55708.1; -. [P55197-4]
DR CCDS; CCDS7135.1; -. [P55197-1]
DR PIR; I38759; I38759.
DR RefSeq; NP_001182555.1; NM_001195626.1. [P55197-4]
DR RefSeq; NP_001182556.1; NM_001195627.1. [P55197-2]
DR RefSeq; NP_001182557.1; NM_001195628.1. [P55197-3]
DR RefSeq; NP_001182559.1; NM_001195630.1. [P55197-3]
DR RefSeq; NP_001311225.1; NM_001324296.1. [P55197-3]
DR RefSeq; NP_004632.1; NM_004641.3. [P55197-1]
DR PDB; 5DAG; X-ray; 1.60 A; A=1-208.
DR PDB; 5DAH; X-ray; 2.61 A; A/B=1-208.
DR PDB; 6CKN; X-ray; 2.49 A; A/B=704-779.
DR PDB; 6CKO; X-ray; 2.00 A; A/B=704-779.
DR PDB; 6JN2; X-ray; 3.60 A; A=699-782.
DR PDB; 7MJU; X-ray; 2.10 A; A=19-208.
DR PDBsum; 5DAG; -.
DR PDBsum; 5DAH; -.
DR PDBsum; 6CKN; -.
DR PDBsum; 6CKO; -.
DR PDBsum; 6JN2; -.
DR PDBsum; 7MJU; -.
DR AlphaFoldDB; P55197; -.
DR SMR; P55197; -.
DR BioGRID; 113723; 45.
DR DIP; DIP-37633N; -.
DR IntAct; P55197; 39.
DR MINT; P55197; -.
DR STRING; 9606.ENSP00000307411; -.
DR GlyGen; P55197; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P55197; -.
DR PhosphoSitePlus; P55197; -.
DR BioMuta; MLLT10; -.
DR DMDM; 527504034; -.
DR EPD; P55197; -.
DR jPOST; P55197; -.
DR MassIVE; P55197; -.
DR MaxQB; P55197; -.
DR PaxDb; P55197; -.
DR PeptideAtlas; P55197; -.
DR PRIDE; P55197; -.
DR ProteomicsDB; 3249; -.
DR ProteomicsDB; 56802; -. [P55197-4]
DR ProteomicsDB; 56803; -. [P55197-2]
DR ProteomicsDB; 65583; -.
DR Antibodypedia; 1417; 392 antibodies from 33 providers.
DR DNASU; 8028; -.
DR Ensembl; ENST00000307729.12; ENSP00000307411.7; ENSG00000078403.17. [P55197-4]
DR Ensembl; ENST00000377059.7; ENSP00000366258.4; ENSG00000078403.17. [P55197-4]
DR Ensembl; ENST00000377072.8; ENSP00000366272.3; ENSG00000078403.17. [P55197-1]
DR Ensembl; ENST00000377091.7; ENSP00000366295.2; ENSG00000078403.17. [P55197-2]
DR Ensembl; ENST00000377100.8; ENSP00000366304.3; ENSG00000078403.17. [P55197-3]
DR Ensembl; ENST00000621220.4; ENSP00000484335.1; ENSG00000078403.17. [P55197-2]
DR Ensembl; ENST00000631589.1; ENSP00000488569.1; ENSG00000078403.17. [P55197-4]
DR Ensembl; ENST00000652497.1; ENSP00000498595.1; ENSG00000078403.17. [P55197-3]
DR GeneID; 8028; -.
DR KEGG; hsa:8028; -.
DR MANE-Select; ENST00000307729.12; ENSP00000307411.7; NM_001195626.3; NP_001182555.1.
DR UCSC; uc001iqq.3; human. [P55197-4]
DR CTD; 8028; -.
DR DisGeNET; 8028; -.
DR GeneCards; MLLT10; -.
DR HGNC; HGNC:16063; MLLT10.
DR HPA; ENSG00000078403; Tissue enhanced (testis).
DR MalaCards; MLLT10; -.
DR MIM; 602409; gene.
DR neXtProt; NX_P55197; -.
DR OpenTargets; ENSG00000078403; -.
DR Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia.
DR PharmGKB; PA30849; -.
DR VEuPathDB; HostDB:ENSG00000078403; -.
DR eggNOG; KOG0956; Eukaryota.
DR GeneTree; ENSGT00940000157711; -.
DR HOGENOM; CLU_128812_0_0_1; -.
DR InParanoid; P55197; -.
DR OMA; RNDSYAH; -.
DR OrthoDB; 327785at2759; -.
DR PhylomeDB; P55197; -.
DR TreeFam; TF316118; -.
DR PathwayCommons; P55197; -.
DR SignaLink; P55197; -.
DR SIGNOR; P55197; -.
DR BioGRID-ORCS; 8028; 17 hits in 1090 CRISPR screens.
DR ChiTaRS; MLLT10; human.
DR GeneWiki; MLLT10; -.
DR GenomeRNAi; 8028; -.
DR Pharos; P55197; Tbio.
DR PRO; PR:P55197; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P55197; protein.
DR Bgee; ENSG00000078403; Expressed in buccal mucosa cell and 185 other tissues.
DR ExpressionAtlas; P55197; baseline and differential.
DR Genevisible; P55197; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
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; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosomal rearrangement; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1068
FT /note="Protein AF-10"
FT /id="PRO_0000215935"
FT ZN_FING 22..74
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 79..112
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 135..198
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 80..287
FT /note="Self-association"
FT REGION 106..190
FT /note="Required for interaction with histone H3"
FT /evidence="ECO:0000269|PubMed:26439302"
FT REGION 141..233
FT /note="Interaction with FSTL3"
FT /evidence="ECO:0000269|PubMed:17868029"
FT REGION 206..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..674
FT /note="DNA-binding"
FT REGION 583..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..784
FT /note="Transactivation domain; required for DOT1L-binding"
FT REGION 750..778
FT /note="Leucine-zipper"
FT REGION 800..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 266
FT /note="KMT2A/MLL1 fusion point (in acute myeloid leukemia
FT patient B)"
FT SITE 627
FT /note="KMT2A/MLL1 fusion point (in acute myeloid leukemia
FT patient C)"
FT SITE 664
FT /note="KMT2A/MLL1 fusion point (in acute myeloid leukemia
FT patient A)"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54826"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 280
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT VAR_SEQ 81..179
FT /note="RCELCPHKDGALKRTDNGGWAHVVCALYIPEVQFANVSTMEPIVLQSVPHDR
FT YNKTCYICDEQGRESKAATGACMTCNKHGCRQAFHVTCAQFAGLLCE -> MVCNSCWL
FT ASSENVTPGYIEHHCACASPHPRCLVSNVPPVSGALMHCFWACLTTAAFFGPQSFTTCH
FT MSFLVSRDILFYIYGFMPFISVVIWRFKKERW (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044552"
FT VAR_SEQ 81..126
FT /note="RCELCPHKDGALKRTDNGGWAHVVCALYIPEVQFANVSTMEPIVLQ -> AE
FT SRSVAQAKVQWCDLSPLQPLLPGFKRFSCLSLPNGMQFLLVSLI (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043044"
FT VAR_SEQ 127..1068
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043045"
FT VAR_SEQ 180..1068
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044553"
FT VAR_SEQ 566
FT /note="N -> NDRGDSSTLTKQELKFI (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:7888665"
FT /id="VSP_047517"
FT VAR_SEQ 986..1011
FT /note="EQHQAFLYQLMQHHHQQHHQPELQQL -> VHRHPHFTQLPPTHFSPSMEIM
FT QVRK (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:7888665"
FT /id="VSP_047518"
FT VAR_SEQ 1012..1068
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:7888665"
FT /id="VSP_047519"
FT MUTAGEN 22
FT /note="I->A: Does not affect interaction with histone H3."
FT /evidence="ECO:0000269|PubMed:26439302"
FT MUTAGEN 80
FT /note="V->A: Does not affect interaction with histone H3."
FT /evidence="ECO:0000269|PubMed:26439302"
FT MUTAGEN 106
FT /note="A->V: Impairs interaction with histone H3."
FT /evidence="ECO:0000269|PubMed:26439302"
FT MUTAGEN 107
FT /note="L->A: Impairs interaction with histone H3. Reduces
FT association to chromatin. Does not rescued histone H3 'Lys-
FT 79' dimethylation (H3K79me2) levels in MLLT10-depleted
FT cells. Does not rescued DOT1L-target genes in MLLT10-
FT depleted cells."
FT /evidence="ECO:0000269|PubMed:26439302"
FT MUTAGEN 109
FT /note="I->A: Impairs interaction with histone H3."
FT /evidence="ECO:0000269|PubMed:26439302"
FT MUTAGEN 114
FT /note="F->A: Impairs interaction with histone H3."
FT /evidence="ECO:0000269|PubMed:26439302"
FT MUTAGEN 120
FT /note="M->A: Impairs interaction with histone H3."
FT /evidence="ECO:0000269|PubMed:26439302"
FT MUTAGEN 179
FT /note="E->A: Impairs interaction with histone H3."
FT /evidence="ECO:0000269|PubMed:26439302"
FT MUTAGEN 190
FT /note="Y->A: Impairs interaction with histone H3."
FT /evidence="ECO:0000269|PubMed:26439302"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:5DAG"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:5DAG"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:5DAG"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:5DAG"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:5DAG"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:5DAH"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:5DAG"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:5DAG"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:5DAG"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:5DAG"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:5DAG"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:5DAG"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:5DAG"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:5DAG"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:5DAG"
FT HELIX 138..142
FT /evidence="ECO:0007829|PDB:5DAG"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:5DAG"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:5DAH"
FT HELIX 168..174
FT /evidence="ECO:0007829|PDB:5DAG"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:5DAH"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:5DAH"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:5DAH"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:5DAG"
FT HELIX 716..733
FT /evidence="ECO:0007829|PDB:6CKO"
FT HELIX 738..778
FT /evidence="ECO:0007829|PDB:6CKO"
SQ SEQUENCE 1068 AA; 113320 MW; 0C4D9B77F61BFEEE CRC64;
MVSSDRPVSL EDEVSHSMKE MIGGCCVCSD ERGWAENPLV YCDGHGCSVA VHQACYGIVQ
VPTGPWFCRK CESQERAARV RCELCPHKDG ALKRTDNGGW AHVVCALYIP EVQFANVSTM
EPIVLQSVPH DRYNKTCYIC DEQGRESKAA TGACMTCNKH GCRQAFHVTC AQFAGLLCEE
EGNGADNVQY CGYCKYHFSK LKKSKRGSNR SYDQSLSDSS SHSQDKHHEK EKKKYKEKDK
HKQKHKKQPE PSPALVPSLT VTTEKTYTST SNNSISGSLK RLEDTTARFT NANFQEVSAH
TSSGKDVSET RGSEGKGKKS SAHSSGQRGR KPGGGRNPGT TVSAASPFPQ GSFSGTPGSV
KSSSGSSVQS PQDFLSFTDS DLRNDSYSHS QQSSATKDVH KGESGSQEGG VNSFSTLIGL
PSTSAVTSQP KSFENSPGDL GNSSLPTAGY KRAQTSGIEE ETVKEKKRKG NKQSKHGPGR
PKGNKNQENV SHLSVSSASP TSSVASAAGS ITSSSLQKSP TLLRNGSLQS LSVGSSPVGS
EISMQYRHDG ACPTTTFSEL LNAIHNGIYN SNDVAVSFPN VVSGSGSSTP VSSSHLPQQS
SGHLQQVGAL SPSAVSSAAP AVATTQANTL SGSSLSQAPS HMYGNRSNSS MAALIAQSEN
NQTDQDLGDN SRNLVGRGSS PRGSLSPRSP VSSLQIRYDQ PGNSSLENLP PVAASIEQLL
ERQWSEGQQF LLEQGTPSDI LGMLKSLHQL QVENRRLEEQ IKNLTAKKER LQLLNAQLSV
PFPTITANPS PSHQIHTFSA QTAPTTDSLN SSKSPHIGNS FLPDNSLPVL NQDLTSSGQS
TSSSSALSTP PPAGQSPAQQ GSGVSGVQQV NGVTVGALAS GMQPVTSTIP AVSAVGGIIG
ALPGNQLAIN GIVGALNGVM QTPVTMSQNP TPLTHTTVPP NATHPMPATL TNSASGLGLL
SDQQRQILIH QQQFQQLLNS QQLTPEQHQA FLYQLMQHHH QQHHQPELQQ LQIPGPTQIP
INNLLAGTQA PPLHTATTNP FLTIHGDNAS QKVARLSDKT GPVAQEKS
