ASH1L_MOUSE
ID ASH1L_MOUSE Reviewed; 2958 AA.
AC Q99MY8; E9QNM2; Q3U598; Q80VY5; Q8BM69; Q8BTX0; Q8BZY6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Histone-lysine N-methyltransferase ASH1L;
DE EC=2.1.1.359 {ECO:0000250|UniProtKB:Q9NR48};
DE EC=2.1.1.367 {ECO:0000269|PubMed:22939622};
DE AltName: Full=ASH1-like protein;
DE AltName: Full=Absent small and homeotic disks protein 1 homolog;
GN Name=Ash1l;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-2005 AND 2048-2465.
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Testis, and Thymus;
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 [3]
RP PROTEIN SEQUENCE OF 88-94; 1254-1265; 1730-1752 AND 2270-2277, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 290-2958.
RC TISSUE=Thymus;
RA Tanaka Y.;
RT "A novel SWI/SNF family gene in mammals reveals a bromodomain lost in
RT Drosophila ASH1.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1996-2958.
RC TISSUE=Limb;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1160 AND SER-1168, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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 [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22939622; DOI=10.1016/j.cell.2012.06.048;
RA Pinheiro I., Margueron R., Shukeir N., Eisold M., Fritzsch C.,
RA Richter F.M., Mittler G., Genoud C., Goyama S., Kurokawa M., Son J.,
RA Reinberg D., Lachner M., Jenuwein T.;
RT "Prdm3 and Prdm16 are H3K9me1 methyltransferases required for mammalian
RT heterochromatin integrity.";
RL Cell 150:948-960(2012).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2307; LYS-2309 AND LYS-2313, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Histone methyltransferase specifically trimethylating 'Lys-
CC 36' of histone H3 forming H3K36me3 (By similarity). Also monomethylates
CC 'Lys-9' of histone H3 (H3K9me1) in vitro (PubMed:22939622). The
CC physiological significance of the H3K9me1 activity is unclear
CC (Probable) (PubMed:22939622). {ECO:0000250|UniProtKB:Q9NR48,
CC ECO:0000269|PubMed:22939622, ECO:0000305|PubMed:22939622}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60324, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:15536, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.359;
CC Evidence={ECO:0000250|UniProtKB:Q9NR48};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60280, Rhea:RHEA-COMP:15542, Rhea:RHEA-COMP:15546,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.367;
CC Evidence={ECO:0000269|PubMed:22939622};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NR48}. Cell
CC junction, tight junction {ECO:0000250|UniProtKB:Q9NR48}. Chromosome
CC {ECO:0000250|UniProtKB:Q9NR48}. Note=The relevance of tight junction
CC localization is however unclear. {ECO:0000250|UniProtKB:Q9NR48}.
CC -!- PTM: Methylated at Gln-1218 by N6AMT1. {ECO:0000250|UniProtKB:Q9NR48}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. SET2 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK26242.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE32182.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC127377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC140468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK033177; BAC28183.2; -; mRNA.
DR EMBL; AK034679; BAC28795.2; -; mRNA.
DR EMBL; AK088497; BAC40390.1; -; mRNA.
DR EMBL; AK153783; BAE32182.1; ALT_INIT; mRNA.
DR EMBL; AF247132; AAK26242.1; ALT_INIT; mRNA.
DR EMBL; BC052194; AAH52194.1; -; mRNA.
DR CCDS; CCDS17487.1; -.
DR RefSeq; NP_619620.3; NM_138679.5.
DR RefSeq; XP_006501204.1; XM_006501141.2.
DR RefSeq; XP_006501205.1; XM_006501142.2.
DR SMR; Q99MY8; -.
DR BioGRID; 228672; 3.
DR IntAct; Q99MY8; 2.
DR STRING; 10090.ENSMUSP00000140251; -.
DR ChEMBL; CHEMBL4523437; -.
DR iPTMnet; Q99MY8; -.
DR PhosphoSitePlus; Q99MY8; -.
DR EPD; Q99MY8; -.
DR MaxQB; Q99MY8; -.
DR PaxDb; Q99MY8; -.
DR PeptideAtlas; Q99MY8; -.
DR PRIDE; Q99MY8; -.
DR ProteomicsDB; 281920; -.
DR Antibodypedia; 1436; 184 antibodies from 19 providers.
DR DNASU; 192195; -.
DR Ensembl; ENSMUST00000090933; ENSMUSP00000088451; ENSMUSG00000028053.
DR Ensembl; ENSMUST00000186583; ENSMUSP00000140251; ENSMUSG00000028053.
DR GeneID; 192195; -.
DR KEGG; mmu:192195; -.
DR UCSC; uc008pxi.1; mouse.
DR CTD; 55870; -.
DR MGI; MGI:2183158; Ash1l.
DR VEuPathDB; HostDB:ENSMUSG00000028053; -.
DR eggNOG; KOG1083; Eukaryota.
DR GeneTree; ENSGT00940000156698; -.
DR HOGENOM; CLU_000657_0_0_1; -.
DR InParanoid; Q99MY8; -.
DR OMA; EPQPACT; -.
DR OrthoDB; 507784at2759; -.
DR PhylomeDB; Q99MY8; -.
DR TreeFam; TF106416; -.
DR BRENDA; 2.1.1.357; 3474.
DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR BioGRID-ORCS; 192195; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Ash1l; mouse.
DR PRO; PR:Q99MY8; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q99MY8; protein.
DR Bgee; ENSMUSG00000028053; Expressed in ciliary body and 258 other tissues.
DR Genevisible; Q99MY8; MM.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); ISO:MGI.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IDA:MGI.
DR GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0046697; P:decidualization; IMP:MGI.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR GO; GO:0097676; P:histone H3-K36 dimethylation; ISO:MGI.
DR GO; GO:0051568; P:histone H3-K4 methylation; IDA:MGI.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IGI:MGI.
DR GO; GO:0000165; P:MAPK cascade; IMP:MGI.
DR GO; GO:0002674; P:negative regulation of acute inflammatory response; IMP:MGI.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IGI:MGI.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0048733; P:sebaceous gland development; IMP:MGI.
DR GO; GO:0007338; P:single fertilization; IMP:MGI.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR GO; GO:1903699; P:tarsal gland development; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:1903709; P:uterine gland development; IMP:MGI.
DR GO; GO:0061038; P:uterus morphogenesis; IMP:MGI.
DR CDD; cd05525; Bromo_ASH1; 1.
DR CDD; cd15548; PHD_ASH1L; 1.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR043320; Bromo_ASH1L.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR043319; PHD_ASH1L.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF17907; AWS; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00384; AT_hook; 4.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Bromodomain; Cell junction; Chromatin regulator;
KW Chromosome; Direct protein sequencing; Isopeptide bond; Metal-binding;
KW Methylation; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; S-adenosyl-L-methionine; Tight junction;
KW Transcription; Transcription regulation; Transferase; Ubl conjugation;
KW Zinc; Zinc-finger.
FT CHAIN 1..2958
FT /note="Histone-lysine N-methyltransferase ASH1L"
FT /id="PRO_0000259517"
FT DOMAIN 2081..2132
FT /note="AWS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00562"
FT DOMAIN 2135..2251
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 2259..2275
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT DOMAIN 2452..2522
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 2650..2787
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT DNA_BIND 885..897
FT /note="A.T hook 1"
FT DNA_BIND 1345..1357
FT /note="A.T hook 2"
FT DNA_BIND 1843..1855
FT /note="A.T hook 3"
FT ZN_FING 2574..2620
FT /note="PHD-type"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1243..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1579..1599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1613..1704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1722..1754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1921..1941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2059..2278
FT /note="Catalytic domain"
FT /evidence="ECO:0000250"
FT REGION 2278..2334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2814..2846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2861..2909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..935
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..963
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1653..1699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1730..1750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1921..1938
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2299..2316
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2827..2846
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2867..2893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR48"
FT MOD_RES 373
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR48"
FT MOD_RES 1160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1218
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR48"
FT MOD_RES 2307
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 2309
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 2313
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CROSSLNK 34
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NR48"
FT CROSSLNK 424
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NR48"
FT CONFLICT 331
FT /note="L -> M (in Ref. 2; BAC40390)"
FT /evidence="ECO:0000305"
FT CONFLICT 711..714
FT /note="RKGR -> EKEE (in Ref. 4; AAK26242)"
FT /evidence="ECO:0000305"
FT CONFLICT 1073
FT /note="Q -> K (in Ref. 4; AAK26242)"
FT /evidence="ECO:0000305"
FT CONFLICT 1095
FT /note="A -> V (in Ref. 4; AAK26242)"
FT /evidence="ECO:0000305"
FT CONFLICT 1994
FT /note="Y -> S (in Ref. 4; AAK26242)"
FT /evidence="ECO:0000305"
FT CONFLICT 2656
FT /note="D -> H (in Ref. 4; AAK26242)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2958 AA; 331333 MW; E8CA3E7AB72BEF2B CRC64;
MDPRNTAMLG LGSDSEGFSR KSPSTINPGT LASKREAEIE GATEEEDPRK RNRERGTEAG
KEDGSTDAQQ QFSVKETNFS EGNLKLKIGL QAKRTKKPPK NLENYVCRPA IKTTIKHSRK
ALKSGKMTDE KNEHCPSKWD SSKLFKKAGD ATAIDCQAEE SIHLHSQGES NPLSKKLSPV
HSQMADYISA APSLVGSRDP DIKDRALLNG GTSVTEKLAQ LIATCPPSKS SKAKPKKLGT
GTTVGLVSKD LIRKPGVGSI AGIIHKDLIK KPALSTAVGL VTKDPGKKPM FNAAVGLINK
DSVKKLGTGT TAVFINKDLG KKPGAITTVG LLSKESGKKL GIGIVPGLVN KESGKKLGLG
TVVGLVNKEL GKKLSSTVGL VAKDVTKKIV ASSAMGLVNK DIGKKLLNCP MAGQLGSKDA
LNLKSEALLP TQEQLKASCS ANISNHDSQE LPESLKDSAT GKAFEKSVMR HSKESMLEKF
SVRKEITNLE KEMFNEGTCI QQDNFSSSER GAFETSKHEK QPPVYCTSPD FQIGGASDAS
TAKSPFSAVG ESNLPSSSPT VSVNPVTRSP PEASSQLVPN PLLLNSTAEQ MEEISESIGK
SQFTAESTHL NVGHRSLGHS LSIECKGIDK ELNESKNTHL DIPRISSSLG KKPSLTSDSG
IHAITPSVVN FTSLFSNKPF LKLGAVTAPD KHCQVAESLS SSFQSKPLKK RKGRKPRWTK
VVARSTCRSP KGLDLERSEL FKNVSCSSLS NSSEPAKFMK TIGASSFVDH DFLKRRLPKL
SKSSAPSLAL LTDSEKPSHK SFITHKLSSS MCVTSDLLSD IYKPKRGRPK SKEMPQLEGP
PKRTLKIPAS KVFSLQSKEE QEPPILQPEI EIPSFKQSLS VSPFPKKRGR PKRQMRSPVK
MKPPVLSVAP FVATESPSKL ESESENHRSS SDFFESEDQL QDTDDLDDSH RQSVCSMSDL
EMEPDKKISK RNNGQLMKTI IRKINKMKTL KRKKLLNQIL SSSVESSNKG KVQSKLHNTV
SSLAATFGSK LGQQINVSKK GTIYIGKRRG RKPKTVLNGL LSGSPASLAV LEQTAQQAAG
SALGQILPPL LPSPASSSEI LPSPICSQSS GTSGGQSPVS SDAGFVEPSS VPYLHVHSRQ
GSMIQTLAMK KASKGRRRLS PPTLLPNSPS HLSELTSLKE ATPSPVSESH SDETIPSDSG
IGTDNNSTSD RAEKFCGQKK RRHSFEHISL IPPETSTVLN SLKEKHKHKC KRRSHDYLSY
DKMKRQKRKR KKKYPQLRNR QDPDFIAELE ELISRLSEIR ITHRSHHFIP RDLLPTIFRI
NFNSFYTHPS FPLDPLHYIR KPDLKKKRGR PPKMREAMAE MPFMHSLSFP LSSTGFYPSY
GMPYSPSPLT AAPIGLGYYG RYPPTLYPPP PSPSFTTPLP PPSYMHAGHL LLNPTKYHKK
KHKLLRQEAF LTTSRTPLLS MSTYPSVPPE MAYGWMVEHK HRHRHKHREH RSEQPQVSMD
SGSSRSVLES LKRYRFGKDT VGDRYKHKEK HRCHMSCPHL SPSKNLINRE EQWVSREPSE
SSSLALGLQT PLQIDCSESS PSLSLGGFTP NSEPASSDEH MNLFTSAIGS CRVSNPNSSC
RKKLTDSPGL FPVQDTALNR PHRKEPLPSS ERAIQSLAGS QSASDKPSQR SSESTNCSPT
RKRSSSESTS STVNGVPSRS PRLVASMDDS VDSLLQRIVH HDEQESMEKN GDASITTVSA
PPSSSPGHSY SKERALGKSD SLLVPAVPND SCSNIPLLSE KSASRCSPHH IKRSVVEAMQ
RQARKMCNYD KILATKKNLD HVNKILKAKK LQRQARTGNN FVKRRPGRPR KCPLQAVVSM
QAFQAAQFVS PELNEGEDMS LHLSPDTVTD VIEAVVQSVN LTSEHKKGVK RKNWLLEEQT
RKKQKTVPEE EEQENNKSFI ETPVEIPSPL ETPAEPSEPE NTLQPVLALI PREKKAPRPP
KKKYQRAGLY SDVYKTIDPK SRLIQLKKEK LEYTPGEHEY GLFPAPIHVG KYLRQKRIDF
QLPYDILWQW KHNQLYKKPD VPLYKKIRSN VYVDVKPLSG YEATTCNCKK PDDDTRKGCG
DDCLNRMIFA ECSPNTCPCG EQCCNQRIQR HEWVQCLERF RAEEKGWGIR TKEPLKAGQF
IIEYLGEVVS EQEFRNRMIE QYHNHSDHYC LNLDSGMVID SYRMGNEARF INHSCDPNCE
MQKWSVNGVY RIGLYALKDM PAGTELTYDY NFHSFNVEKQ QLCKCGFEKC RGIIGGKSQR
MNGLPSHKGS QSSSTHRKSA RAKEKRKSKH KLKKRKGHPS EEPSENINTP TRLTPQLQMK
PMSNRERNFV LKHHVFLVRN WEKIHQKQEE VKHTRDIHSA SLYTRWNGLC RDDGNIKSDV
FMTQFSALQT ARSVRTRRLA AAEENLEVAR AARLAQIFKE ICDGIISYRD SSQQTLAAPL
LNLPPKKKNA DYYEKISDPL DLSTIEKQIL IGYYKTVEAF DADMLKVFRN AEKYYGRKSP
IGRDVCRLRK AYYSARHEAS AQIDEIVGET ASEADSSETS VSEKESGHEK DDDVIRCICG
LYKDEGLMIQ CDKCMVWQHC DCMGVNTDVE HYLCEQCDPR PVDREVPMIP RPHYAQPGCV
YFICLLRDDL LLRQGDCVYL MRDSRRTPDG HPVRQSYRLL SHINRDKLDI FRIEKLWKNE
KEERFAFGHH YFRPHETHHS PSRRFYHNEL FRVPLYEIIP LEAVVGTCCV LDLYTYCKGR
PKGIKEQDVY ICDYRLDKSA HLFYKIHRNR YPVCTKPYAF DHFPKKLTPK RDFSPHYVPD
NYKRNGGRSS WKSERSKPPL KDLGQEDDAL PLIEEVLASQ EQAAREVPSP EEPDQERATG
DIGDAEKKPE ESSQEAQLAS TPEERRHSQR ERLNQILLNL LEKIPGKNAI DVTYLLEEGS
GRKLRRRTLF IPENSFRK
