ASX_DROME
ID ASX_DROME Reviewed; 1669 AA.
AC Q9V727; O76930;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Polycomb protein Asx;
DE AltName: Full=Additional sex combs;
GN Name=Asx; ORFNames=CG8787;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Imaginal disk;
RX PubMed=9477319; DOI=10.1242/dev.125.7.1207;
RA Sinclair D.A.R., Milne T.A., Hodgson J.W., Shellard J., Salinas C.A.,
RA Kyba M., Randazzo F., Brock H.W.;
RT "The Additional sex combs gene of Drosophila encodes a chromatin protein
RT that binds to shared and unique Polycomb group sites on polytene
RT chromosomes.";
RL Development 125:1207-1216(1998).
RN [2]
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]
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]
RP INTERACTION WITH TANT.
RX PubMed=11397012; DOI=10.1006/dbio.2001.0255;
RA Dietrich B.H., Moore J., Kyba M., dosSantos G., McCloskey F., Milne T.A.,
RA Brock H.W., Krause H.M.;
RT "Tantalus, a novel ASX-interacting protein with tissue-specific
RT functions.";
RL Dev. Biol. 234:441-453(2001).
RN [5]
RP FUNCTION, IDENTIFICATION IN THE PR-DUB COMPLEX, AND INTERACTION WITH
RP CALYPSO.
RX PubMed=20436459; DOI=10.1038/nature08966;
RA Scheuermann J.C., de Ayala Alonso A.G., Oktaba K., Ly-Hartig N.,
RA McGinty R.K., Fraterman S., Wilm M., Muir T.W., Muller J.;
RT "Histone H2A deubiquitinase activity of the Polycomb repressive complex PR-
RT DUB.";
RL Nature 465:243-247(2010).
RN [6]
RP INTERACTION WITH CYCG.
RX PubMed=25995770; DOI=10.1186/s13072-015-0008-6;
RA Dupont C.A., Dardalhon-Cumenal D., Kyba M., Brock H.W., Randsholt N.B.,
RA Peronnet F.;
RT "Drosophila Cyclin G and epigenetic maintenance of gene expression during
RT development.";
RL Epigenetics Chromatin 8:18-18(2015).
CC -!- FUNCTION: Atypical Polycomb group protein, which may be involved in
CC both Polycomb group (PcG) and trithorax group (trxG) complexes. Non-
CC catalytic component of the PR-DUB complex, a complex that specifically
CC mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-118'
CC (H2AK118ub1). Does not deubiquitinate monoubiquitinated histone H2B.
CC Required to maintain the transcriptionally repressive state of homeotic
CC genes throughout development. The PR-DUB complex has weak or no
CC activity toward 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. PcG
CC and trxG proteins act by forming multiprotein complexes, which are
CC respectively required to maintain the transcriptionally repressive and
CC transcriptionally active state of homeotic genes throughout
CC development. PcG and trxG protein complexes are not required to
CC initiate repression and activation, but to maintain it during later
CC stages of development. {ECO:0000269|PubMed:20436459,
CC ECO:0000269|PubMed:9477319}.
CC -!- SUBUNIT: Component of the PR-DUB complex, at least composed of calypso
CC and Asx (PubMed:20436459). Interacts with tant (PubMed:11397012).
CC Interacts with cyclin CycG (PubMed:25995770).
CC {ECO:0000269|PubMed:11397012, ECO:0000269|PubMed:20436459,
CC ECO:0000269|PubMed:25995770}.
CC -!- INTERACTION:
CC Q9V727; Q7K5N4: calypso; NbExp=2; IntAct=EBI-103394, EBI-15851838;
CC Q9V727; Q8T0D4: tant; NbExp=3; IntAct=EBI-103394, EBI-139891;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9477319}. Chromosome
CC {ECO:0000269|PubMed:9477319}. Note=Associated with chromatin.
CC Colocalizes with many PcG sites on polytene chromosomes. It also
CC associates with many unique sites on polytene chromosomes.
CC -!- TISSUE SPECIFICITY: Highly expressed in nurse cells and deposited in
CC oocytes late in oogenesis. Ubiquitous in early embryos. Late embryos
CC show higher levels in CNS and neurectoderm.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Early
CC embryos have high levels of expression, this drops off and zygotic
CC expression begins at 3-6 hours embryos. Expression levels are low in
CC larvae and medium in pupae and adults. {ECO:0000269|PubMed:9477319}.
CC -!- DOMAIN: Contains two Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs, which may be
CC required for an association with nuclear receptors. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Asx family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA04568.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ001164; CAA04568.1; ALT_FRAME; mRNA.
DR EMBL; AE013599; AAF58239.1; -; Genomic_DNA.
DR PIR; T13748; T13748.
DR RefSeq; NP_725398.1; NM_166057.2.
DR PDB; 6CGA; X-ray; 3.50 A; B/D=207-340.
DR PDB; 6HGC; X-ray; 3.02 A; C=209-318.
DR PDBsum; 6CGA; -.
DR PDBsum; 6HGC; -.
DR AlphaFoldDB; Q9V727; -.
DR SMR; Q9V727; -.
DR BioGRID; 62360; 19.
DR DIP; DIP-22881N; -.
DR IntAct; Q9V727; 10.
DR STRING; 7227.FBpp0305149; -.
DR PaxDb; Q9V727; -.
DR EnsemblMetazoa; FBtr0087493; FBpp0086622; FBgn0261823.
DR GeneID; 36612; -.
DR KEGG; dme:Dmel_CG8787; -.
DR CTD; 36612; -.
DR FlyBase; FBgn0261823; Asx.
DR VEuPathDB; VectorBase:FBgn0261823; -.
DR eggNOG; ENOG502QWPH; Eukaryota.
DR GeneTree; ENSGT00520000055578; -.
DR InParanoid; Q9V727; -.
DR OMA; AHSEYGN; -.
DR OrthoDB; 552046at2759; -.
DR PhylomeDB; Q9V727; -.
DR Reactome; R-DME-5689603; UCH proteinases.
DR BioGRID-ORCS; 36612; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36612; -.
DR PRO; PR:Q9V727; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0261823; Expressed in cleaving embryo and 26 other tissues.
DR ExpressionAtlas; Q9V727; baseline and differential.
DR Genevisible; Q9V727; DM.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0035517; C:PR-DUB complex; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0035800; F:deubiquitinase activator activity; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0007469; P:antennal development; IMP:FlyBase.
DR GO; GO:0009948; P:anterior/posterior axis specification; IMP:UniProtKB.
DR GO; GO:0007475; P:apposition of dorsal and ventral imaginal disc-derived wing surfaces; IMP:FlyBase.
DR GO; GO:0001709; P:cell fate determination; IGI:FlyBase.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; IDA:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:2000152; P:regulation of ubiquitin-specific protease activity; IDA:FlyBase.
DR GO; GO:0045498; P:sex comb development; TAS:UniProtKB.
DR GO; GO:0035186; P:syncytial blastoderm mitotic cell cycle; IMP:FlyBase.
DR InterPro; IPR026905; ASX-like_PHD.
DR InterPro; IPR024811; ASX/ASX-like.
DR InterPro; IPR028020; ASX_DEUBAD_dom.
DR InterPro; IPR044867; DEUBAD_dom.
DR InterPro; IPR024814; Polycomb_ASX.
DR PANTHER; PTHR13578; PTHR13578; 3.
DR PANTHER; PTHR13578:SF20; PTHR13578:SF20; 3.
DR Pfam; PF13919; ASXH; 1.
DR Pfam; PF13922; PHD_3; 1.
DR PROSITE; PS51916; DEUBAD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Chromosome; Developmental protein;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1669
FT /note="Polycomb protein Asx"
FT /id="PRO_0000059323"
FT DOMAIN 215..338
FT /note="DEUBAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01264"
FT ZN_FING 1632..1669
FT /note="PHD-type; atypical"
FT REGION 90..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1174..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1398..1437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1482..1505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1587..1610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 224..228
FT /note="LXXLL motif 1"
FT MOTIF 244..248
FT /note="LXXLL motif 2"
FT COMPBIAS 336..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 14..15
FT /note="SQ -> CE (in Ref. 1; CAA04568)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="K -> N (in Ref. 1; CAA04568)"
FT /evidence="ECO:0000305"
FT CONFLICT 1253
FT /note="S -> T (in Ref. 1; CAA04568)"
FT /evidence="ECO:0000305"
FT CONFLICT 1520
FT /note="Missing (in Ref. 1; CAA04568)"
FT /evidence="ECO:0000305"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:6CGA"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:6HGC"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:6HGC"
FT HELIX 230..234
FT /evidence="ECO:0007829|PDB:6HGC"
FT HELIX 238..245
FT /evidence="ECO:0007829|PDB:6HGC"
FT HELIX 250..256
FT /evidence="ECO:0007829|PDB:6HGC"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:6HGC"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:6HGC"
FT HELIX 285..299
FT /evidence="ECO:0007829|PDB:6HGC"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:6HGC"
FT HELIX 304..317
FT /evidence="ECO:0007829|PDB:6HGC"
SQ SEQUENCE 1669 AA; 179842 MW; F65D87398D67D321 CRC64;
MKTITPDTTT TTSSQHQQLL IPQADQHHQP MLQQQSLLAA PPPTMIMEHV NLVDDDEKDP
LALEQLEVSP STKHTHSLRR HLPRIIVKPI PPEKKPMAPS EEAAVSTAPA PPTRLICSRR
IQQQQQVKAA AAAAAAAAAA AAAAAAAAQA QATSSYPSAI SPGSKAGTSQ ASTMREVLAS
IPGFSVKPRR RSNKKLTTAA QIEQTKDGKI DLETPDSILA STNLRALLNK QTFSLLPPLY
QYNLIQLLPS VDREASELEQ PSSSASGGSP SEAIRLSASC LNNEFFARAC LEWRERLSEG
EFTPENQLKL KTEAEREKNK LDPWKLKHFE PFWGEKNSRG KDKDKLESDC KNQKLSASIK
SEPKPPATSQ QKPLQQATCD NETELKFDLS TKCETTSAKT TVAVAVADKS STFPPTGSQN
NVLNEQQRRV LKRPSSSPSQ RKQAPTTIAT INLDDDLDEL PSTSKDSKQP KMDEIVPNAS
GNVVAAPMVD VVDHSAVEMK IKDEQQHQRQ HQPLINSTCD KIEPSECSKE MIVAMKQVDS
KEDVDSIASA AAMPAIAAVT PHTPKPEALA PNPDVANQFV SYLQNVELAA ETKAPLDNSN
EADITTGTNS HDFVFSDTID HAYFQEHQST INHNFFTSSS SSNTATTAAN KLEEHSDKPE
DSPLPIASSI SGSTPASSIT STSCTSSSSS SASMSSSCSS SNSGSTTTAP TTSSSAGAPT
APLTLAAAAE TTLANVQAML STVAKLQQQQ QELPVELNSN EMYQHVQHDW NFGDIKLSSS
QSSGDQQRNL SHEAIDLMDV VQDADVIDDI MHNDVCHDVL GDEDEGDQEE DEDDEVVECM
TEEQQLIDED SEAVREIVDK LQQHQQQQNQ QQHHQQLHIQ DVVQLAQHSF MPQAHSEFGN
DIGQEMLCDA VPMSAAEMEV SSTVITNSSN SNDSSNNISL CSSTNSLTIN QMPHQASQQP
QQNAQSNAQQ QRQILVDSNG QIIGNFLLQQ QRQQQQQQLL QQFTLQAAAA QQQQQQQQQH
QQQQQQQQQA TSSNSLGKTL PVALRNGTQQ FLSPNLIAQQ HQQQQQQQLE QHQQQATAQQ
KHQQIQQFAL QQAQLHQRQL LAQAANNNLL QQQQQQQQNV ALPTTQAKFI AKPLNIISMT
RPANASPTTA ATTANTASIP SAYANVVAVT GAQQQQSPPV PAPQQQTVQQ QQLANHNSNM
QQLPNVLTMK TLPPSGVPTT IAQQRLQPKM PTGKGRKATS NRLPPGAVNL ERSYQICQAV
IQNSPNRENL KAQLRPPAAI LNQHQPTTTT APAPINPVTL NVSTVAATPM SNITTATGSM
AAAVAAAPPQ NVLKQEELLV SGAVGAGALP AGLPPNVMGV GRPGVYKVIG PRMSGFPRKK
YVQRKPSPTT LIRHVFSPGP GGATATAQQL QMLQQHHQST TSPVPVQNPQ QPAPEQLIHQ
NGNGQYVLVH RANVGAADNQ APRASSAPPM HQNQFVTVQN PLHSINGIPM GGRGRPASVD
TTAGSGNVIA PPISATDALH HHHHEMQQQQ QHQQPQPLGN VGAAANIVRR NIAAGPNIAY
IDGSNTNSSA VALMEAGNNY IVTTNASPTA APSPINQQPQ SQPTGTQHQH PLLQLHQTGE
NTPPGNEATA TANNCACSLN AMVICQQCGA FCHDDCIGAA KLCVACVIR
