ASXL2_MOUSE
ID ASXL2_MOUSE Reviewed; 1370 AA.
AC Q8BZ32; Q3TRU9; Q80TA5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Putative Polycomb group protein ASXL2;
DE AltName: Full=Additional sex combs-like protein 2;
GN Name=Asxl2; Synonyms=Kiaa1685;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Vagina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 311-1370.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1121, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-594, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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. Involved in transcriptional regulation mediated by
CC ligand-bound nuclear hormone receptors, such as peroxisome
CC proliferator-activated receptor gamma (PPARG). Acts as coactivator for
CC PPARG and enhances its adipocyte differentiation-inducing activity; the
CC function seems to involve differential recruitment of acetylated and
CC methylated histone H3 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PPARA and PPARG. {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; AK036839; BAC29602.1; -; mRNA.
DR EMBL; AK162455; BAE36927.1; -; mRNA.
DR EMBL; AK122540; BAC65822.1; -; mRNA.
DR RefSeq; NP_001257917.1; NM_001270988.1.
DR RefSeq; NP_766009.2; NM_172421.5.
DR AlphaFoldDB; Q8BZ32; -.
DR SMR; Q8BZ32; -.
DR BioGRID; 217375; 4.
DR STRING; 10090.ENSMUSP00000106846; -.
DR iPTMnet; Q8BZ32; -.
DR PhosphoSitePlus; Q8BZ32; -.
DR jPOST; Q8BZ32; -.
DR MaxQB; Q8BZ32; -.
DR PaxDb; Q8BZ32; -.
DR PRIDE; Q8BZ32; -.
DR ProteomicsDB; 265120; -.
DR DNASU; 75302; -.
DR GeneID; 75302; -.
DR KEGG; mmu:75302; -.
DR CTD; 55252; -.
DR MGI; MGI:1922552; Asxl2.
DR eggNOG; ENOG502QWPH; Eukaryota.
DR InParanoid; Q8BZ32; -.
DR OrthoDB; 123355at2759; -.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR BioGRID-ORCS; 75302; 12 hits in 75 CRISPR screens.
DR ChiTaRS; Asxl2; mouse.
DR PRO; PR:Q8BZ32; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BZ32; protein.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0035517; C:PR-DUB complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
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; ISS:UniProtKB.
DR GO; GO:0007512; P:adult heart development; IMP:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0035630; P:bone mineralization involved in bone maturation; IMP:MGI.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR GO; GO:0098532; P:histone H3-K27 trimethylation; IMP:MGI.
DR GO; GO:0030225; P:macrophage differentiation; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0030316; P:osteoclast differentiation; IMP:MGI.
DR GO; GO:1900159; P:positive regulation of bone mineralization involved in bone maturation; IMP:MGI.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:1902466; P:positive regulation of histone H3-K27 trimethylation; IMP:MGI.
DR GO; GO:0010884; P:positive regulation of lipid storage; ISO:MGI.
DR GO; GO:0045651; P:positive regulation of macrophage differentiation; IMP:MGI.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IMP:MGI.
DR GO; GO:0035360; P:positive regulation of peroxisome proliferator activated receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
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; 2.
DR PANTHER; PTHR13578:SF11; PTHR13578:SF11; 2.
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 1: Evidence at protein level;
KW Metal-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1370
FT /note="Putative Polycomb group protein ASXL2"
FT /id="PRO_0000313827"
FT DOMAIN 11..86
FT /note="HTH HARE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01261"
FT DOMAIN 229..338
FT /note="DEUBAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01264"
FT ZN_FING 1332..1369
FT /note="PHD-type; atypical"
FT REGION 92..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 178..182
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 258..262
FT /note="LXXLL motif"
FT COMPBIAS 92..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q76L83"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q76L83"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q76L83"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q76L83"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q76L83"
FT MOD_RES 594
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q76L83"
FT MOD_RES 1121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q76L83"
FT CONFLICT 564
FT /note="V -> S (in Ref. 1; BAE36927)"
FT /evidence="ECO:0000305"
FT CONFLICT 621
FT /note="E -> K (in Ref. 1; BAE36927 and 2; BAC65822)"
FT /evidence="ECO:0000305"
FT CONFLICT 627
FT /note="A -> P (in Ref. 1; BAE36927)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="P -> L (in Ref. 2; BAC65822)"
FT /evidence="ECO:0000305"
FT CONFLICT 686
FT /note="G -> V (in Ref. 1; BAE36927)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1370 AA; 147107 MW; 5E93DCF61F64861B CRC64;
MREKGRRKKG RTWAEAAKTV LEKYPNTPMS HKEILQVIQR EGLKEIRSGT SPLACLNAML
HTNSRGEEGI FYKVPGRMGV YTLKKDVPDG VKELSECSEE SSDGQSDSHS SDNSSSSDGG
SNKEGRKSRW KRKVSSRLSH PPSPPSGCPS PTIPASKVIS PSQKHSKKAL KQALKQQQQK
KKQQQCRPSM SISNQHLSLK TVKAASDSVP AKPGQMKRTK CADIDVETPD SILVNTNLRA
LINKHTFSVL PGDCQQRLLL LLPEVDRQVG PDGLMKLNGS ALNNEFFTSA AQGWKERLSE
GEFTPEMQVR IRQEIEKEKK VELWKEQFFE NYYGQSSGLS LEDSQKLTAS SSDPKAKKTP
AEQPKSILPS EASPVRIVPV VPQSECKEEA VQIPSPSQKE ENQDEARPDS KSPEPVLASA
SNTNELITMK PIKSPKDEGL LEQKPVACAE QESEKENHVT TTSRNNKSEN QEALAISPSK
SKNAGLQKPI IKPVAEASPL NPDMKMPPAT VTDQIQESLK RKSSLTDEEA TSSWEKRPRI
TENRQHQQPF QVSPQPFLNR GDRVQVRKVP PLKIPVSRIS PMLFSTSQVS PRARFPISIT
SPYRTGARTL ADIKAKAQLV EAQKAAAAAA AAAAAAASVG GTIPGPGPGG GQSPREGGER
KIAGGGSAGS DPVSTNGKGP TLELAGTGSR GGTRELLPCG PQPETNMPGQ AQPPGISGAQ
LQQTSSVPTG LASSGACTSV PLPAHIEISN SEKPNLHKAT ATAASPCHLQ DPRSCRLEKA
LSPTGPPLIS GASTVYFVAD GTVEPKAGSN KNAPKPSALA KTTAPAPLDM TSSPVTTASL
EKLPVPQISG TATSTGSAPS SSTLPAASSL KTPGTSANMN GPISRTSSSI PANNPLVTQL
LQGKDVPLEQ ILPKPLTKIE MKTVPLTTKE EKGIGIFPGI SVMESSSREE VNGRQAHLAI
PQLGKPLQSK QLSQVPRPVF TAKDRKDPCI DTHQYREGLS KTTQDQLFQT LIQRAQRQSV
LSFVPPSQFN FAHSGFHLED ISTSQKFMLG FAGRRTSKPA MAGHYLLNIS TYGRGTENIK
RTHSVNPDDR FCLSSPTEAL RMGHADYKNT TGEISSKEDE SDEDRVGDEQ EPISVKEEPW
ASQSSGRHPH HGEASSTNDC LASKNGKTEA PVSEQTTLGQ ENYIFSRGQA SDEKSLPRDF
IPAAHKQMTH AVRGKTVCSS PELFNSTALS LPADSPTHQP LLLPPLQTPK LYGSPTQIGP
SYRGMINVST SSDMDHNSAI PGSQVSSNVG DVMSFSVTVT TIPASQAMNP SSHGQTIPVQ
TFPDDNSIED TPSKCYCRLK AMIMCKGCGA FCHDDCIGPS KLCVSCLVVR
