AF17_HUMAN
ID AF17_HUMAN Reviewed; 1093 AA.
AC P55198; Q59F28; Q96IU3; Q9H5F6; Q9UF49;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Protein AF-17;
DE AltName: Full=ALL1-fused gene from chromosome 17 protein;
GN Name=MLLT6; Synonyms=AF17;
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], AND CHROMOSOMAL TRANSLOCATION WITH KMT2A/MLL1.
RX PubMed=8058765; DOI=10.1073/pnas.91.17.8107;
RA Prasad R., Leshkowitz D., Gu Y., Alder H., Nakamura T., Saito H.,
RA Huebner K., Berger R., Croce C.M., Canaani E.;
RT "Leucine-zipper dimerization motif encoded by the AF17 gene fused to ALL-1
RT (MLL) in acute leukemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:8107-8111(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-1093.
RC TISSUE=Spleen;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 624-1093.
RC TISSUE=Ileal mucosa;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 624-1093.
RC TISSUE=Skin;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 648-1093.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-451, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-378 AND SER-423, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [9]
RP INTERACTION WITH HISTONE H3.
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).
CC -!- SUBUNIT: Interacts with histone H3; interaction is necessary for MLLT6
CC binding to nucleosomes; interaction is inhibited by histone H3 'Lys-27'
CC methylations (H3K27me1, H3K27me2 and H3K27me3).
CC {ECO:0000269|PubMed:26439302}.
CC -!- INTERACTION:
CC P55198; Q9UBB4: ATXN10; NbExp=3; IntAct=EBI-740216, EBI-702390;
CC P55198; Q02930-3: CREB5; NbExp=3; IntAct=EBI-740216, EBI-10192698;
CC P55198; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-740216, EBI-717919;
CC P55198; B7ZLY0: PHC2; NbExp=3; IntAct=EBI-740216, EBI-14568740;
CC P55198; Q13526: PIN1; NbExp=3; IntAct=EBI-740216, EBI-714158;
CC P55198; Q08117-2: TLE5; NbExp=3; IntAct=EBI-740216, EBI-11741437;
CC P55198; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-740216, EBI-10173939;
CC P55198; Q9NRR5: UBQLN4; NbExp=2; IntAct=EBI-740216, EBI-711226;
CC P55198; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-740216, EBI-746595;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DISEASE: Note=A chromosomal aberration involving MLLT6 is associated
CC with acute leukemias. Translocation t(11;17)(q23;q21) with KMT2A/MLL1.
CC The result is a rogue activator protein.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH07237.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15670.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/AF17ID7.html";
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; U07932; AAA21145.1; -; mRNA.
DR EMBL; AC006449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB209633; BAD92870.1; -; mRNA.
DR EMBL; AK027133; BAB15670.1; ALT_INIT; mRNA.
DR EMBL; BC007237; AAH07237.1; ALT_INIT; mRNA.
DR EMBL; AL133659; CAB63772.2; -; mRNA.
DR CCDS; CCDS11327.1; -.
DR PIR; I38533; I38533.
DR RefSeq; NP_005928.2; NM_005937.3.
DR AlphaFoldDB; P55198; -.
DR SMR; P55198; -.
DR BioGRID; 110448; 89.
DR IntAct; P55198; 51.
DR STRING; 9606.ENSP00000479910; -.
DR GlyGen; P55198; 18 sites, 2 O-linked glycans (18 sites).
DR iPTMnet; P55198; -.
DR PhosphoSitePlus; P55198; -.
DR BioMuta; MLLT6; -.
DR DMDM; 215273929; -.
DR EPD; P55198; -.
DR jPOST; P55198; -.
DR MassIVE; P55198; -.
DR PaxDb; P55198; -.
DR PeptideAtlas; P55198; -.
DR PRIDE; P55198; -.
DR ProteomicsDB; 56804; -.
DR Antibodypedia; 73458; 114 antibodies from 19 providers.
DR DNASU; 4302; -.
DR Ensembl; ENST00000618876.2; ENSP00000477969.1; ENSG00000275851.4.
DR Ensembl; ENST00000621332.5; ENSP00000479910.1; ENSG00000275023.5.
DR GeneID; 4302; -.
DR KEGG; hsa:4302; -.
DR MANE-Select; ENST00000621332.5; ENSP00000479910.1; NM_005937.4; NP_005928.2.
DR CTD; 4302; -.
DR DisGeNET; 4302; -.
DR GeneCards; MLLT6; -.
DR HGNC; HGNC:7138; MLLT6.
DR HPA; ENSG00000275023; Low tissue specificity.
DR MalaCards; MLLT6; -.
DR MIM; 600328; gene.
DR neXtProt; NX_P55198; -.
DR OpenTargets; ENSG00000275023; -.
DR PharmGKB; PA30854; -.
DR VEuPathDB; HostDB:ENSG00000275023; -.
DR eggNOG; KOG0956; Eukaryota.
DR GeneTree; ENSGT00940000158572; -.
DR InParanoid; P55198; -.
DR OMA; YQMIQQV; -.
DR OrthoDB; 327785at2759; -.
DR PhylomeDB; P55198; -.
DR TreeFam; TF316118; -.
DR PathwayCommons; P55198; -.
DR SignaLink; P55198; -.
DR BioGRID-ORCS; 4302; 30 hits in 1081 CRISPR screens.
DR ChiTaRS; MLLT6; human.
DR GenomeRNAi; 4302; -.
DR Pharos; P55198; Tdark.
DR PRO; PR:P55198; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P55198; protein.
DR Bgee; ENSG00000275023; Expressed in right uterine tube and 99 other tissues.
DR ExpressionAtlas; P55198; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0034729; P:histone H3-K79 methylation; IEA:Ensembl.
DR GO; GO:2001161; P:negative regulation of histone H3-K79 methylation; IEA:Ensembl.
DR GO; GO:0035811; P:negative regulation of urine volume; IEA:Ensembl.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
DR GO; GO:0036359; P:renal potassium excretion; IEA:Ensembl.
DR GO; GO:0035812; P:renal sodium excretion; IEA:Ensembl.
DR GO; GO:0070295; P:renal water absorption; IEA:Ensembl.
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 Chromosomal rearrangement; Metal-binding; Nucleus; Phosphoprotein;
KW Proto-oncogene; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..1093
FT /note="Protein AF-17"
FT /id="PRO_0000215937"
FT ZN_FING 5..57
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 62..95
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 118..181
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 185..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..764
FT /note="Leucine-zipper"
FT REGION 775..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..388
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..864
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 551
FT /note="KMT2A/MLL1 fusion point (in acute myeloid leukemia
FT patient)"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 451
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VARIANT 33
FT /note="A -> V (in dbSNP:rs17855918)"
FT /id="VAR_080170"
FT VARIANT 198
FT /note="A -> T (in dbSNP:rs2241012)"
FT /id="VAR_022076"
FT CONFLICT 126
FT /note="Q -> T (in Ref. 1; AAA21145)"
FT /evidence="ECO:0000305"
FT CONFLICT 735
FT /note="R -> W (in Ref. 3; BAD92870)"
FT /evidence="ECO:0000305"
FT CONFLICT 1065
FT /note="L -> P (in Ref. 4; BAB15670)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1093 AA; 112048 MW; C55F0801D9A0A5C1 CRC64;
MKEMVGGCCV CSDERGWAEN PLVYCDGHAC SVAVHQACYG IVQVPTGPWF CRKCESQERA
ARVRCELCPH KDGALKRTDN GGWAHVVCAL YIPEVQFANV LTMEPIVLQY VPHDRFNKTC
YICEEQGRES KAASGACMTC NRHGCRQAFH VTCAQMAGLL CEEEVLEVDN VKYCGYCKYH
FSKMKTSRHS SGGGGGGAGG GGGSMGGGGS GFISGRRSRS ASPSTQQEKH PTHHERGQKK
SRKDKERLKQ KHKKRPESPP SILTPPVVPT ADKVSSSASS SSHHEASTQE TSESSRESKG
KKSSSHSLSH KGKKLSSGKG VSSFTSASSS SSSSSSSSGG PFQPAVSSLQ SSPDFSAFPK
LEQPEEDKYS KPTAPAPSAP PSPSAPEPPK ADLFEQKVVF SGFGPIMRFS TTTSSSGRAR
APSPGDYKSP HVTGSGASAG THKRMPALSA TPVPADETPE TGLKEKKHKA SKRSRHGPGR
PKGSRNKEGT GGPAAPSLPS AQLAGFTATA ASPFSGGSLV SSGLGGLSSR TFGPSGSLPS
LSLESPLLGA GIYTSNKDPI SHSGGMLRAV CSTPLSSSLL GPPGTSALPR LSRSPFTSTL
PSSSASISTT QVFSLAGSTF SLPSTHIFGT PMGAVNPLLS QAESSHTEPD LEDCSFRCRG
TSPQESLSSM SPISSLPALF DQTASAPCGG GQLDPAAPGT TNMEQLLEKQ GDGEAGVNIV
EMLKALHALQ KENQRLQEQI LSLTAKKERL QILNVQLSVP FPALPAALPA ANGPVPGPYG
LPPQAGSSDS LSTSKSPPGK SSLGLDNSLS TSSEDPHSGC PSRSSSSLSF HSTPPPLPLL
QQSPATLPLA LPGAPAPLPP QPQNGLGRAP GAAGLGAMPM AEGLLGGLAG SGGLPLNGLL
GGLNGAAAPN PASLSQAGGA PTLQLPGCLN SLTEQQRHLL QQQEQQLQQL QQLLASPQLT
PEHQTVVYQM IQQIQQKREL QRLQMAGGSQ LPMASLLAGS STPLLSAGTP GLLPTASAPP
LLPAGALVAP SLGNNTSLMA AAAAAAAVAA AGGPPVLTAQ TNPFLSLSGA EGSGGGPKGG
TADKGASANQ EKG
