ASXL2_CHICK
ID ASXL2_CHICK Reviewed; 1412 AA.
AC Q5ZM88;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Putative Polycomb group protein ASXL2;
DE AltName: Full=Additional sex combs-like protein 2;
GN Name=ASXL2; ORFNames=RCJMB04_2n14;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins act by
CC forming multiprotein complexes, which are required to maintain the
CC transcriptionally repressive state of homeotic genes throughout
CC development. PcG proteins are not required to initiate repression, but
CC to maintain it during later stages of development. They probably act
CC via methylation of histones, rendering chromatin heritably changed in
CC its expressibility. heritably changed in its expressibility. Involved
CC in transcriptional regulation mediated by ligand-bound nuclear hormone
CC receptors (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: Contains one Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif, which may be
CC required for an association with nuclear receptors. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Asx family. {ECO:0000305}.
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DR EMBL; AJ719496; CAG31155.1; -; mRNA.
DR RefSeq; NP_001026267.1; NM_001031096.1.
DR AlphaFoldDB; Q5ZM88; -.
DR SMR; Q5ZM88; -.
DR STRING; 9031.ENSGALP00000036004; -.
DR PaxDb; Q5ZM88; -.
DR GeneID; 421993; -.
DR KEGG; gga:421993; -.
DR CTD; 55252; -.
DR VEuPathDB; HostDB:geneid_421993; -.
DR eggNOG; ENOG502QWPH; Eukaryota.
DR InParanoid; Q5ZM88; -.
DR OrthoDB; 123355at2759; -.
DR PhylomeDB; Q5ZM88; -.
DR PRO; PR:Q5ZM88; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0035517; C:PR-DUB complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR026905; ASX-like_PHD.
DR InterPro; IPR024811; ASX/ASX-like.
DR InterPro; IPR028020; ASX_DEUBAD_dom.
DR InterPro; IPR024817; ASXL2.
DR InterPro; IPR007759; Asxl_HARE-HTH.
DR InterPro; IPR044867; DEUBAD_dom.
DR PANTHER; PTHR13578; PTHR13578; 1.
DR PANTHER; PTHR13578:SF11; PTHR13578:SF11; 1.
DR Pfam; PF13919; ASXH; 1.
DR Pfam; PF05066; HARE-HTH; 1.
DR Pfam; PF13922; PHD_3; 1.
DR PROSITE; PS51916; DEUBAD; 1.
DR PROSITE; PS51913; HTH_HARE; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1412
FT /note="Putative Polycomb group protein ASXL2"
FT /id="PRO_0000313828"
FT DOMAIN 11..86
FT /note="HTH HARE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01261"
FT DOMAIN 280..389
FT /note="DEUBAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01264"
FT ZN_FING 1374..1411
FT /note="PHD-type; atypical"
FT REGION 91..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1125..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1246..1289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 181..185
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 309..313
FT /note="LXXLL motif"
FT COMPBIAS 101..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..930
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1247..1277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1412 AA; 148669 MW; 3B3C7F3659C8DEF6 CRC64;
MREKGRRKKG RTWAEAARTV LEKYPNTPMS HKEILQVIQK EGLKEIRSGT SPLACLNAML
HTNSRGEEGI FYKVPGRMGV YTLKKDVPDG LKELSDGSEE SSDAQSDSQS SENSSSSSSS
DGCTNKDGRK SRWKRKVSSR LSQTSSPQTS CQSPSIQTGK VISSSQKHSK KALKQALKQQ
QQKQQQQQCR AGMPVSSNQH TLLKAVKAAS ASTPTKPAWI GKQSDGHSNS SQNSTFSSSA
SVKLDNSLPG LGKKPFQRSD RLHARQLKRT KCAEIDVETP DSILVNTNLR ALINKHTFSV
LPTECQQRLL LLLPEVDRQV GADGLMKLSG SALNNEFFTS AAQGWKERLS EGEFTPEMQL
RIRQEIEKEK KVELWKEHFF ESYYGQSSGL SPEESERLTA NTSADDGEAE KPAAEQPKCM
QVKEEITSPS ESKAQVVQEA PAVKKGEERR VEERREEMQP KAAKPAEASV SPAGCAVKPS
NPQIQERIQG EPIQENPQPA VSQKLEEERK HTASKEVKEA VRAPVLAPSK PKSPEAGEAA
AKVTSPVVVP PTPEKKPPVN EEMEVSVEGH KRKSESSEEA LTTPGKKPRI AEKCQQQQPA
FRSQTQSFPA AGPPVPRVPP LKIPVSRISP MPFPAGQVSP RVRFPASLIS PARTGARTLA
DIKAKAQQVR AQRAAAAAAA AAASSGGAVP GPGPGGGPAG GGGTGNAATS GAGETGTRGN
ALELAGTGSG GSSRRFLPRC PGTHSPMETQ EQPATPSLSR AQLQQTSVLQ SRSAAGNTGT
NCSSPAVSAI EQISGIKQSP PNVAINQVSG SSCAGGCDKQ EKAPSAPAGL GQACGASTVR
DGTTCVTVSS ADSNANITRV APAALGGTSS DVPKGTSPSP LMPSLTPTSS EAQAGGAVVS
APSAPCSNTL SAAPSLKTHP SSSGALPKAN SSIPANNPLV TQLLQGKSVP LEQILPKPLT
KAEMKTVPLA SNEEKGAAVP GVAGSGAGAE GGERQSALSP QQLGKIFCQS RPLPHIPRTF
VLPAGKEPGA DQHPEALSKT TQEQILQTLI KRVQRQNLLP VLQPSQVNVA HSGFQLENSS
TSQRFVLGFM GRRTSKPAMS GHYLLNISTY GRGSESLRRG FSLNPETRSC LNSPAGGPKA
ECGECEEMPD HGSSSEEEDA DNESTGDEHE HVSVKEEPQA SQVAAPCEKE QVSHGANSSD
YGILAKKGVK TEAAVSQQAA GSRENSQALD GTALARDFIQ AAQEQTVHAV KGKTHSSPEL
FSSSTPSSDS AQLQLPQLSH PHPPKLGGDA AAAQLIGPSY SGTINVSTSP DVNQGSLMSG
LSECNQLSSS MGNVMSFSVT VTTIPTSQAM NSGNHSQTIP VQAFAEDSSM EDSPSKCYCR
LKAMIMCKGC GAFCHDDCIG PSKLCVSCLV VR
