ID ASH2_DROME Reviewed; 556 AA.
AC Q94545; D3DMU8; Q8IMW1; Q960W8;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 27-MAR-2024, entry version 181.
DE RecName: Full=Set1/Ash2 histone methyltransferase complex subunit ASH2 {ECO:0000303|PubMed:21694722};
DE AltName: Full=Absent, small, or homeotic discs protein 2 {ECO:0000312|EMBL:AAO41602.1};
GN Name=ash2 {ECO:0000312|EMBL:AAC47328.2, ECO:0000312|FlyBase:FBgn0000139};
GN ORFNames=CG6677;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC47328.2}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=8889525; DOI=10.1093/genetics/144.2.621;
RA Adamson A.L., Shearn A.;
RT "Molecular genetic analysis of Drosophila ash2, a member of the trithorax
RT group required for imaginal disc pattern formation.";
RL Genetics 144:621-633(1996).
RN [2] {ECO:0000312|EMBL:AAO41602.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000312|EMBL:AAO41602.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAK93227.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAR96120.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 217-556 (ISOFORM C).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Booth B., Carlson J., Chavez C., Frise E., George R.,
RA Pacleb J., Park S., Wan K., Yu C., Rubin G.M., Celniker S.;
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8555105; DOI=10.1016/0925-4773(95)00430-0;
RA LaJeunesse D., Shearn A.;
RT "Trans-regulation of thoracic homeotic selector genes of the Antennapedia
RT and bithorax complexes by the trithorax group genes: absent, small, and
RT homeotic discs 1 and 2.";
RL Mech. Dev. 53:123-139(1995).
RN [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12068954;
RA Amoros M., Corominas M., Deak P., Serras F.;
RT "The ash2 gene is involved in Drosophila wing development.";
RL Int. J. Dev. Biol. 46:321-324(2002).
RN [8] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=12626737; DOI=10.1073/pnas.0538075100;
RA Beltran S., Blanco E., Serras F., Perez-Villamil B., Guigo R.,
RA Artavanis-Tsakonas S., Corominas M.;
RT "Transcriptional network controlled by the trithorax-group gene ash2 in
RT Drosophila melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:3293-3298(2003).
RN [9]
RP ERRATUM OF PUBMED:12626737.
RA Beltran S., Blanco E., Serras F., Perez-Villamil B., Guigo R.,
RA Artavanis-Tsakonas S., Corominas M.;
RL Proc. Natl. Acad. Sci. U.S.A. 109:17141-17141(2012).
RN [10] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15371308; DOI=10.1242/dev.01380;
RA Angulo M., Corominas M., Serras F.;
RT "Activation and repression activities of ash2 in Drosophila wing imaginal
RT discs.";
RL Development 131:4943-4953(2004).
RN [11] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SKTL, AND DISRUPTION PHENOTYPE.
RX PubMed=15280236; DOI=10.1534/genetics.103.018721;
RA Cheng M.K., Shearn A.;
RT "The direct interaction between ASH2, a Drosophila trithorax group protein,
RT and SKTL, a nuclear phosphatidylinositol 4-phosphate 5-kinase, implies a
RT role for phosphatidylinositol 4,5-bisphosphate in maintaining
RT transcriptionally active chromatin.";
RL Genetics 167:1213-1223(2004).
RN [12] {ECO:0000305}
RP FUNCTION, INTERACTION WITH HCF, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17466076; DOI=10.1186/gb-2007-8-4-r67;
RA Beltran S., Angulo M., Pignatelli M., Serras F., Corominas M.;
RT "Functional dissection of the ash2 and ash1 transcriptomes provides
RT insights into the transcriptional basis of wing phenotypes and reveals
RT conserved protein interactions.";
RL Genome Biol. 8:R67.1-R67.15(2007).
RN [13] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE SET1 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=21694722; DOI=10.1038/emboj.2011.194;
RA Ardehali M.B., Mei A., Zobeck K.L., Caron M., Lis J.T., Kusch T.;
RT "Drosophila Set1 is the major histone H3 lysine 4 trimethyltransferase with
RT role in transcription.";
RL EMBO J. 30:2817-2828(2011).
RN [14] {ECO:0000305}
RP FUNCTION, AND IDENTIFICATION IN THE SET1 AND MLL3/4 COMPLEXES.
RX PubMed=21875999; DOI=10.1128/mcb.06092-11;
RA Mohan M., Herz H.M., Smith E.R., Zhang Y., Jackson J., Washburn M.P.,
RA Florens L., Eissenberg J.C., Shilatifard A.;
RT "The COMPASS family of H3K4 methylases in Drosophila.";
RL Mol. Cell. Biol. 31:4310-4318(2011).
RN [15] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21310711; DOI=10.1093/nar/gkq1322;
RA Perez-Lluch S., Blanco E., Carbonell A., Raha D., Snyder M., Serras F.,
RA Corominas M.;
RT "Genome-wide chromatin occupancy analysis reveals a role for ASH2 in
RT transcriptional pausing.";
RL Nucleic Acids Res. 39:4628-4639(2011).
RN [16] {ECO:0000305}
RP FUNCTION, INTERACTION WITH TRR, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23197473; DOI=10.1091/mbc.e12-04-0267;
RA Carbonell A., Mazo A., Serras F., Corominas M.;
RT "Ash2 acts as an ecdysone receptor coactivator by stabilizing the histone
RT methyltransferase Trr.";
RL Mol. Biol. Cell 24:361-372(2013).
CC -!- FUNCTION: Transcriptional regulator. Regulates a number of genes
CC involved in wing development including activation of net and bs and
CC repression of rho and kni and controls vein-intervein patterning during
CC wing development. Required for correct expression of a number of
CC homeotic genes including Scr in the first leg imaginal disk and Ubx in
CC the third leg imaginal disk and haltere disks. Required for
CC stabilization of the histone-lysine N-methyltransferase trr and for
CC trimethylation of 'Lys-4' of histone H3. Together with sktl probably
CC plays a role in maintenance of transcriptionally active chromatin
CC through down-regulation of histone H1 hyperphosphorylation
CC (PubMed:15280236). {ECO:0000269|PubMed:12068954,
CC ECO:0000269|PubMed:12626737, ECO:0000269|PubMed:15280236,
CC ECO:0000269|PubMed:15371308, ECO:0000269|PubMed:17466076,
CC ECO:0000269|PubMed:21310711, ECO:0000269|PubMed:21694722,
CC ECO:0000269|PubMed:21875999, ECO:0000269|PubMed:23197473,
CC ECO:0000269|PubMed:8555105}.
CC -!- SUBUNIT: Core component of several methyltransferase-containing
CC complexes. Component of the SET1C/COMPASS complex, composed at least of
CC the catalytic subunit Set1, wds/WDR5, Wdr82, Rbbp5, ash2, Cfp1/CXXC1,
CC hcf and Dpy-30L1 (PubMed:21694722, PubMed:21875999). Component of the
CC MLL3/4 (Histone-lysine N-methyltransferase/demethylase TRR) complex
CC composed at least of the catalytic subunit trr, ash2, Rbbp5, Dpy-30L1,
CC wds, hcf, ptip, Pa1, Utx, Lpt and Ncoa6 (PubMed:21875999). Interacts
CC with hcf (PubMed:17466076). Interacts with trr (PubMed:23197473).
CC {ECO:0000269|PubMed:15280236, ECO:0000269|PubMed:17466076,
CC ECO:0000269|PubMed:21694722, ECO:0000269|PubMed:21875999,
CC ECO:0000269|PubMed:23197473}.
CC -!- SUBUNIT: [Isoform B]: Interacts (via B30.2/SPRY domain) with sktl; the
CC interaction is direct. {ECO:0000269|PubMed:15280236}.
CC -!- INTERACTION:
CC Q94545; Q9VPH8: Rbbp5; NbExp=3; IntAct=EBI-6991562, EBI-163110;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17466076,
CC ECO:0000269|PubMed:21694722, ECO:0000269|PubMed:23197473,
CC ECO:0000269|PubMed:8889525}. Chromosome {ECO:0000269|PubMed:17466076,
CC ECO:0000269|PubMed:21694722, ECO:0000269|PubMed:23197473,
CC ECO:0000269|PubMed:8889525}. Note=Accumulates on salivary gland
CC polytene chromosomes. {ECO:0000269|PubMed:17466076,
CC ECO:0000269|PubMed:21694722, ECO:0000269|PubMed:23197473,
CC ECO:0000269|PubMed:8889525}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=C {ECO:0000269|PubMed:12537569};
CC IsoId=Q94545-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q94545-2; Sequence=VSP_054947, VSP_054948;
CC -!- TISSUE SPECIFICITY: In larvae and pupae, expressed in imaginal disks,
CC salivary gland and fat body cells. No expression detected in central
CC nervous system (at protein level). {ECO:0000269|PubMed:8889525}.
CC -!- DEVELOPMENTAL STAGE: Expressed in larval and pupal stages (at protein
CC level). Expression also detected at early embryonic stages and in
CC adult. {ECO:0000269|PubMed:12626737, ECO:0000269|PubMed:8889525}.
CC -!- DISRUPTION PHENOTYPE: Generally pupal-lethal with mutants showing a
CC wide array of homeotic transformations. Adult escapers are sterile and
CC show pattern formation abnormalities in legs, including tissue
CC overgrowth and small supernumerary legs. In wings, the pattern
CC formation defects observed include duplicated bristles and sockets,
CC transformation of campaniform sensilla (a class of sensory organ) to
CC bristles, ectopic campaniform sensilla and reduction of intervein
CC tissue with increase of longitudinal veins and cross-vein tissue.
CC Mutant wing imaginal disk shows ectopic expression of neur, normally
CC expressed in all sensory organ precursors in the posterior region of
CC the wing disk. Increased histone H1 hyperphosphorylation in polytene
CC chromosomes. Reduced trimethylation of histone H3 'Lys-4', reduced
CC levels of trr protein and severe defects in pupariation and
CC metamorphosis due to a lack of activation of ecdysone-responsive genes.
CC {ECO:0000269|PubMed:12068954, ECO:0000269|PubMed:15280236,
CC ECO:0000269|PubMed:15371308, ECO:0000269|PubMed:17466076,
CC ECO:0000269|PubMed:21310711, ECO:0000269|PubMed:23197473,
CC ECO:0000269|PubMed:8555105, ECO:0000269|PubMed:8889525}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ADC27634.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; U73809; AAC47328.2; -; mRNA.
DR EMBL; AE014297; AAN14010.1; -; Genomic_DNA.
DR EMBL; AE014297; AAO41602.1; -; Genomic_DNA.
DR EMBL; AY051803; AAK93227.1; -; mRNA.
DR EMBL; BT011328; AAR96120.1; -; mRNA.
DR EMBL; BT120264; ADC27634.1; ALT_SEQ; mRNA.
DR PIR; S72249; S72249.
DR RefSeq; NP_733024.1; NM_170160.2. [Q94545-2]
DR RefSeq; NP_788735.1; NM_176558.3. [Q94545-1]
DR AlphaFoldDB; Q94545; -.
DR SMR; Q94545; -.
DR BioGRID; 67862; 31.
DR ComplexPortal; CPX-2284; Histone-lysine N-methyltransferase/demethylase TRR complex.
DR ComplexPortal; CPX-2287; Histone-lysine N-methyltransferase TRX complex.
DR ComplexPortal; CPX-2798; COMPASS complex.
DR IntAct; Q94545; 9.
DR MINT; Q94545; -.
DR STRING; 7227.FBpp0084040; -.
DR PaxDb; 7227-FBpp0084040; -.
DR DNASU; 42936; -.
DR EnsemblMetazoa; FBtr0084659; FBpp0084039; FBgn0000139. [Q94545-2]
DR EnsemblMetazoa; FBtr0084660; FBpp0084040; FBgn0000139. [Q94545-1]
DR GeneID; 42936; -.
DR KEGG; dme:Dmel_CG6677; -.
DR UCSC; CG6677-RB; d. melanogaster.
DR UCSC; CG6677-RC; d. melanogaster. [Q94545-1]
DR AGR; FB:FBgn0000139; -.
DR CTD; 42936; -.
DR FlyBase; FBgn0000139; ash2.
DR VEuPathDB; VectorBase:FBgn0000139; -.
DR eggNOG; KOG2626; Eukaryota.
DR GeneTree; ENSGT00390000010474; -.
DR HOGENOM; CLU_032370_2_0_1; -.
DR InParanoid; Q94545; -.
DR OMA; CATCSRW; -.
DR OrthoDB; 5479497at2759; -.
DR PhylomeDB; Q94545; -.
DR Reactome; R-DME-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-DME-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-DME-9772755; Formation of WDR5-containing histone-modifying complexes.
DR SignaLink; Q94545; -.
DR BioGRID-ORCS; 42936; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 42936; -.
DR PRO; PR:Q94545; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0000139; Expressed in oviduct (Drosophila) and 23 other cell types or tissues.
DR ExpressionAtlas; Q94545; baseline and differential.
DR Genevisible; Q94545; DM.
DR GO; GO:0044665; C:MLL1/2 complex; IDA:FlyBase.
DR GO; GO:0044666; C:MLL3/4 complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:UniProtKB.
DR GO; GO:0005703; C:polytene chromosome puff; IDA:UniProtKB.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
DR GO; GO:0007420; P:brain development; TAS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IMP:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0007444; P:imaginal disc development; TAS:UniProtKB.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0007474; P:imaginal disc-derived wing vein specification; IMP:FlyBase.
DR GO; GO:0002168; P:instar larval development; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0035209; P:pupal development; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0035075; P:response to ecdysone; IDA:UniProtKB.
DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IMP:FlyBase.
DR CDD; cd15583; PHD_ash2p_like; 1.
DR CDD; cd12872; SPRY_Ash2; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.90.980.20; -; 1.
DR InterPro; IPR037353; ASH2.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR PANTHER; PTHR10598; SET1/ASH2 HISTONE METHYLTRANSFERASE COMPLEX SUBUNIT ASH2; 1.
DR PANTHER; PTHR10598:SF0; SET1_ASH2 HISTONE METHYLTRANSFERASE COMPLEX SUBUNIT ASH2; 1.
DR Pfam; PF21198; ASH2L-like_WH; 1.
DR Pfam; PF00622; SPRY; 2.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Developmental protein; DNA-binding;
KW Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..556
FT /note="Set1/Ash2 histone methyltransferase complex subunit
FT ASH2"
FT /id="PRO_0000429418"
FT DOMAIN 288..510
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 34..90
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT VAR_SEQ 1..206
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_054947"
FT VAR_SEQ 207..216
FT /note="RLTDDGYTQA -> MASSFTDEES (in isoform B)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_054948"
SQ SEQUENCE 556 AA; 63229 MW; 6F895B62853CD37E CRC64;
MEDSQMDTSS PTESSSEVNF TAEEDKSQET RSAAGVCYCG KERNLNIVEL LCATCSRWVH
ETCVSYQLGK GKLLPFITNY VFVCKNCSAS GLESFRKSQA TISQMCHCAI ANMQQAASRD
GRRQIQFSKD KEIIPYIEQY WEAMTTMPRR LTQSWYSTVQ RSLVKDVQTL FTYEEHAEHG
AMYGLFHQDL RIIKPNYESM SKSGALRLTD DGYTQASLSK NNRQKRKFPG TDSGPTGKKG
RPSSDITANV KLPPHGYPLE HPFNKDGYRY ILAEPDPHAP FRQEFDESSD WAGKPIPGWL
YRILVPHSVL LALHDRAPQL KISEDRLAVT GERGYCMVRA THSVNRGCWY FEVTIEEMPD
GAATRLGWGR EYGNLQAPLG YDKFGYSWRS RKGTKFTESH GKHYSDAYVE GDTLGFLIEL
PEEASLDYLP NTFKDRPLVK FKSHLYYEDK DKITETLKNL HILQGSRIEF FKNGQSQGVA
FEDIYAGSYF PAISIHKSAT VSVNFGPAFK YPEVLVEHKA KGMHDRVEEL ITEQCLADTL
YLTEHDGRLR LDNMGL
//
