ASXL2_HUMAN
ID ASXL2_HUMAN Reviewed; 1435 AA.
AC Q76L83; Q53TC9; Q5H9U4; Q76L81; Q86XM1; Q9C0H8; Q9NV67;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Putative Polycomb group protein ASXL2;
DE AltName: Full=Additional sex combs-like protein 2;
GN Name=ASXL2; Synonyms=ASXH2, KIAA1685;
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] (ISOFORM 1), AND CHROMOSOMAL TRANSLOCATION WITH
RP KAT6A.
RC TISSUE=Bone marrow;
RA Hosoda F., Kitabayashi I., Kakazu N., Fukushima M., Aikawa Y., Abe T.,
RA Hibi S., Yagi T., Ohki M.;
RT "MOZ is fused to a novel Polycomb group gene in a therapy-related
RT myelodysplastic syndrome with t(2;8)(p23;p11.2).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [3]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT VAL-796.
RC TISSUE=Testis;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 890-1435 (ISOFORM 1).
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP IDENTIFICATION BY 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 [12]
RP FUNCTION, AND INTERACTION WITH PPARA AND PPARG.
RX PubMed=21047783; DOI=10.1074/jbc.m110.177816;
RA Park U.H., Yoon S.K., Park T., Kim E.J., Um S.J.;
RT "Additional sex comb-like (ASXL) proteins 1 and 2 play opposite roles in
RT adipogenesis via reciprocal regulation of peroxisome proliferator-activated
RT receptor {gamma}.";
RL J. Biol. Chem. 286:1354-1363(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524; SER-562; SER-571;
RP SER-600; SER-637; SER-648 AND SER-1319, AND IDENTIFICATION BY MASS
RP 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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP INVOLVEMENT IN SHAPNS.
RX PubMed=27693232; DOI=10.1016/j.ajhg.2016.08.017;
RG Undiagnosed Diseases Network;
RA Shashi V., Pena L.D., Kim K., Burton B., Hempel M., Schoch K.,
RA Walkiewicz M., McLaughlin H.M., Cho M., Stong N., Hickey S.E., Shuss C.M.,
RA Freemark M.S., Bellet J.S., Keels M.A., Bonner M.J., El-Dairi M.,
RA Butler M., Kranz P.G., Stumpel C.T., Klinkenberg S., Oberndorff K.,
RA Alawi M., Santer R., Petrovski S., Kuismin O., Korpi-Heikkilae S.,
RA Pietilainen O., Aarno P., Kurki M.I., Hoischen A., Need A.C.,
RA Goldstein D.B., Kortuem F.;
RT "De novo truncating variants in ASXL2 are associated with a unique and
RT recognizable clinical phenotype.";
RL Am. J. Hum. Genet. 99:991-999(2016).
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 (By similarity). Involved in transcriptional
CC regulation mediated by ligand-bound nuclear hormone receptors, such as
CC peroxisome proliferator-activated receptor gamma (PPARG). Acts as
CC coactivator for PPARG and enhances its adipocyte differentiation-
CC inducing activity; the function seems to involve differential
CC recruitment of acetylated and methylated histone H3. {ECO:0000250,
CC ECO:0000269|PubMed:21047783}.
CC -!- SUBUNIT: Interacts with PPARA and PPARG. {ECO:0000269|PubMed:21047783}.
CC -!- INTERACTION:
CC Q76L83-2; Q96DN6: MBD6; NbExp=4; IntAct=EBI-12043951, EBI-719591;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q76L83-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q76L83-2; Sequence=VSP_030163, VSP_030164;
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 -!- DISEASE: Shashi-Pena syndrome (SHAPNS) [MIM:617190]: An autosomal
CC dominant syndrome characterized by delayed psychomotor development,
CC intellectual disability of variable severity, macrocephaly, prominent
CC eyes, arched eyebrows, hypertelorism, a glabellar nevus flammeus,
CC neonatal feeding difficulties, and hypotonia. Some patients may also
CC have atrial septal defect, episodic hypoglycemia, changes in bone
CC mineral density, and/or seizures. {ECO:0000269|PubMed:27693232}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Note=A chromosomal aberration involving ASXL2 is a cause of
CC therapy-related myelodysplastic syndrome. Translocation
CC t(2;8)(p23;p11.2) with KAT6A generates a KAT6A-ASXL2 fusion protein.
CC -!- SIMILARITY: Belongs to the Asx family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91889.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB21776.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD00088.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB084279; BAD00086.1; -; mRNA.
DR EMBL; AB084281; BAD00088.1; ALT_INIT; mRNA.
DR EMBL; AB051472; BAB21776.2; ALT_INIT; mRNA.
DR EMBL; CR933613; CAI45930.1; -; mRNA.
DR EMBL; AC010150; AAY14841.1; -; Genomic_DNA.
DR EMBL; BC042999; AAH42999.1; -; mRNA.
DR EMBL; AK001760; BAA91889.1; ALT_INIT; mRNA.
DR RefSeq; NP_060733.4; NM_018263.4. [Q76L83-1]
DR AlphaFoldDB; Q76L83; -.
DR SMR; Q76L83; -.
DR BioGRID; 120543; 73.
DR IntAct; Q76L83; 30.
DR MINT; Q76L83; -.
DR CarbonylDB; Q76L83; -.
DR GlyGen; Q76L83; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q76L83; -.
DR PhosphoSitePlus; Q76L83; -.
DR BioMuta; ASXL2; -.
DR DMDM; 74712929; -.
DR EPD; Q76L83; -.
DR jPOST; Q76L83; -.
DR MassIVE; Q76L83; -.
DR MaxQB; Q76L83; -.
DR PaxDb; Q76L83; -.
DR PeptideAtlas; Q76L83; -.
DR PRIDE; Q76L83; -.
DR ProteomicsDB; 68680; -. [Q76L83-1]
DR ProteomicsDB; 68681; -. [Q76L83-2]
DR Antibodypedia; 27772; 58 antibodies from 17 providers.
DR DNASU; 55252; -.
DR Ensembl; ENST00000404843.5; ENSP00000383920.1; ENSG00000143970.18. [Q76L83-2]
DR Ensembl; ENST00000435504.9; ENSP00000391447.3; ENSG00000143970.18. [Q76L83-1]
DR GeneID; 55252; -.
DR KEGG; hsa:55252; -.
DR MANE-Select; ENST00000435504.9; ENSP00000391447.3; NM_018263.6; NP_060733.4.
DR UCSC; uc002rgt.2; human. [Q76L83-1]
DR CTD; 55252; -.
DR DisGeNET; 55252; -.
DR GeneCards; ASXL2; -.
DR HGNC; HGNC:23805; ASXL2.
DR HPA; ENSG00000143970; Low tissue specificity.
DR MalaCards; ASXL2; -.
DR MIM; 612991; gene.
DR MIM; 617190; phenotype.
DR neXtProt; NX_Q76L83; -.
DR OpenTargets; ENSG00000143970; -.
DR PharmGKB; PA134884863; -.
DR VEuPathDB; HostDB:ENSG00000143970; -.
DR eggNOG; ENOG502QWPH; Eukaryota.
DR GeneTree; ENSGT00520000055578; -.
DR HOGENOM; CLU_005155_0_0_1; -.
DR InParanoid; Q76L83; -.
DR OMA; TAEPMKT; -.
DR OrthoDB; 123355at2759; -.
DR PhylomeDB; Q76L83; -.
DR TreeFam; TF328464; -.
DR PathwayCommons; Q76L83; -.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR SignaLink; Q76L83; -.
DR SIGNOR; Q76L83; -.
DR BioGRID-ORCS; 55252; 19 hits in 331 CRISPR screens.
DR ChiTaRS; ASXL2; human.
DR GenomeRNAi; 55252; -.
DR Pharos; Q76L83; Tbio.
DR PRO; PR:Q76L83; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q76L83; protein.
DR Bgee; ENSG00000143970; Expressed in caput epididymis and 211 other tissues.
DR ExpressionAtlas; Q76L83; baseline and differential.
DR Genevisible; Q76L83; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; IDA:UniProtKB.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IDA:UniProtKB.
DR GO; GO:0035360; P:positive regulation of peroxisome proliferator activated receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA: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; 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 1: Evidence at protein level;
KW Alternative splicing; Chromosomal rearrangement; Intellectual disability;
KW Metal-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1435
FT /note="Putative Polycomb group protein ASXL2"
FT /id="PRO_0000313826"
FT DOMAIN 11..86
FT /note="HTH HARE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01261"
FT DOMAIN 274..383
FT /note="DEUBAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01264"
FT ZN_FING 1397..1434
FT /note="PHD-type; atypical"
FT REGION 91..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1166..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 174..178
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 303..307
FT /note="LXXLL motif 1"
FT MOTIF 887..891
FT /note="LXXLL motif 2"
FT COMPBIAS 101..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..775
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1032
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 20..21
FT /note="Breakpoint for translocation to form KAT6A-ASXL2
FT protein"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 637
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 641
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8BZ32"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..260
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030163"
FT VAR_SEQ 838..1094
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030164"
FT VARIANT 731
FT /note="L -> P (in dbSNP:rs13385963)"
FT /id="VAR_037773"
FT VARIANT 796
FT /note="A -> V (in dbSNP:rs17854251)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_037774"
FT VARIANT 1210
FT /note="T -> P (in dbSNP:rs12991178)"
FT /id="VAR_037775"
FT VARIANT 1242
FT /note="T -> P (in dbSNP:rs12990978)"
FT /id="VAR_037776"
FT CONFLICT 473
FT /note="E -> G (in Ref. 3; CAI45930)"
FT /evidence="ECO:0000305"
FT CONFLICT 651
FT /note="R -> K (in Ref. 3; CAI45930)"
FT /evidence="ECO:0000305"
FT CONFLICT 1334
FT /note="S -> P (in Ref. 7; BAA91889)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1435 AA; 153820 MW; A01026E3C2D1035D CRC64;
MREKGRRKKG RTWAEAAKTV LEKYPNTPMS HKEILQVIQR EGLKEIRSGT SPLACLNAML
HTNSRGEEGI FYKVPGRMGV YTLKKDVPDG VKELSEGSEE SSDGQSDSQS SENSSSSSDG
GSNKEGKKSR WKRKVSSSSP QSGCPSPTIP AGKVISPSQK HSKKALKQAL KQQQQKKQQQ
QCRPSISISS NQHLSLKTVK AASDSVPAKP ATWEGKQSDG QTGSPQNSNS SFSSSVKVEN
TLLGLGKKSF QRSERLHTRQ MKRTKCADID VETPDSILVN TNLRALINKH TFSVLPGDCQ
QRLLLLLPEV DRQVGPDGLM KLNGSALNNE FFTSAAQGWK ERLSEGEFTP EMQVRIRQEI
EKEKKVEPWK EQFFESYYGQ SSGLSLEDSK KLTASPSDPK VKKTPAEQPK SMPVSEASLI
RIVPVVSQSE CKEEALQMSS PGRKEECESQ GEVQPNFSTS SEPLLSSALN THELSSILPI
KCPKDEDLLE QKPVTSAEQE SEKNHLTTAS NYNKSESQES LVTSPSKPKS PGVEKPIVKP
TAGAGPQETN MKEPLATLVD QSPESLKRKS SLTQEEAPVS WEKRPRVTEN RQHQQPFQVS
PQPFLNRGDR IQVRKVPPLK IPVSRISPMP FHPSQVSPRA RFPVSITSPN RTGARTLADI
KAKAQLVKAQ RAAAAAAAAA AAAASVGGTI PGPGPGGGQG PGEGGEGQTA RGGSPGSDRV
SETGKGPTLE LAGTGSRGGT RELLPCGPET QPQSETKTTP SQAQPHSVSG AQLQQTPPVP
PTPAVSGACT SVPSPAHIEK LDNEKLNPTR ATATVASVSH PQGPSSCRQE KAPSPTGPAL
ISGASPVHCA ADGTVELKAG PSKNIPNPSA SSKTDASVPV AVTPSPLTSL LTTATLEKLP
VPQVSATTAP AGSAPPSSTL PAASSLKTPG TSLNMNGPTL RPTSSIPANN PLVTQLLQGK
DVPMEQILPK PLTKVEMKTV PLTAKEERGM GALIATNTTE NSTREEVNER QSHPATQQQL
GKTLQSKQLP QVPRPLQLFS AKELRDSSID THQYHEGLSK ATQDQILQTL IQRVRRQNLL
SVVPPSQFNF AHSGFQLEDI STSQRFMLGF AGRRTSKPAM AGHYLLNIST YGRGSESFRR
THSVNPEDRF CLSSPTEALK MGYTDCKNAT GESSSSKEDD TDEESTGDEQ ESVTVKEEPQ
VSQSAGKGDT SSGPHSRETL STSDCLASKN VKAEIPLNEQ TTLSKENYLF TRGQTFDEKT
LARDLIQAAQ KQMAHAVRGK AIRSSPELFS STVLPLPADS PTHQPLLLPP LQTPKLYGSP
TQIGPSYRGM INVSTSSDMD HNSAVPGSQV SSNVGDVMSF SVTVTTIPAS QAMNPSSHGQ
TIPVQAFSEE NSIEGTPSKC YCRLKAMIMC KGCGAFCHDD CIGPSKLCVS CLVVR
