ID   CHD9_MOUSE              Reviewed;        2885 AA.
AC   Q8BYH8; Q7TMV5; Q8BJG8; Q8BZJ2; Q8CHG8;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=Chromodomain-helicase-DNA-binding protein 9;
DE            Short=CHD-9;
DE            EC=3.6.4.12;
DE   AltName: Full=ATP-dependent helicase CHD9;
DE   AltName: Full=PPAR-alpha-interacting complex protein 320 kDa;
DE   AltName: Full=Peroxisomal proliferator-activated receptor A-interacting complex 320 kDa protein;
GN   Name=Chd9; Synonyms=Kiaa0308, Pric320;
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 [MRNA] (ISOFORM 2).
RX   PubMed=16554032; DOI=10.1016/j.bbrc.2006.02.160;
RA   Surapureddi S., Viswakarma N., Yu S., Guo D., Rao M.S., Reddy J.K.;
RT   "PRIC320, a transcription coactivator, isolated from peroxisome
RT   proliferator-binding protein complex.";
RL   Biochem. Biophys. Res. Commun. 343:535-543(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1104 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Diencephalon, Spinal cord, and Spinal ganglion;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 980-2885 (ISOFORM 2).
RC   TISSUE=Pancreatic islet;
RX   PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT   The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [4]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2207-2885 (ISOFORM 1).
RC   STRAIN=C3H/He; TISSUE=Mesenchymal stem cell;
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   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=16419031; DOI=10.1002/jcp.20586;
RA   Shur I., Socher R., Benayahu D.;
RT   "In vivo association of CReMM/CHD9 with promoters in osteogenic cells.";
RL   J. Cell. Physiol. 207:374-378(2006).
CC   -!- FUNCTION: Acts as a transcriptional coactivator for PPARA and possibly
CC       other nuclear receptors. Proposed to be a ATP-dependent chromatin
CC       remodeling protein. Has DNA-dependent ATPase activity and binds to A/T-
CC       rich DNA (By similarity). Associates with A/T-rich regulatory regions
CC       in promoters of genes that participate in the differentiation of
CC       progenitors during osteogenesis. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC   -!- SUBUNIT: Interacts with PPARA. Probably interacts with ESR1 and NR1I3
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BYH8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BYH8-2; Sequence=VSP_018087;
CC   -!- TISSUE SPECIFICITY: Expressed in osteoprogenitor cells during
CC       development and in mature bone (at protein level).
CC       {ECO:0000269|PubMed:16419031}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from embryonic day 16.5 dpc in
CC       mesenchymal cartilage surrounding bone cartilage and newly formed bone
CC       trabecular spicules. Detected in bone sections of 4-day-old newborn and
CC       3-week-old mice. {ECO:0000269|PubMed:16419031}.
CC   -!- PTM: Phosphorylated on serine and tyrosine residues. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH52896.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; DQ127229; AAZ73184.2; -; mRNA.
DR   EMBL; AK034446; BAC28711.1; -; mRNA.
DR   EMBL; AK039562; BAC30385.1; -; mRNA.
DR   EMBL; AK084000; BAC39090.1; -; mRNA.
DR   EMBL; AB093226; BAC41410.3; -; mRNA.
DR   EMBL; BC052896; AAH52896.1; ALT_INIT; mRNA.
DR   CCDS; CCDS22517.1; -. [Q8BYH8-2]
DR   CCDS; CCDS80912.1; -. [Q8BYH8-1]
DR   RefSeq; NP_001297459.1; NM_001310530.1. [Q8BYH8-1]
DR   RefSeq; NP_796198.1; NM_177224.2. [Q8BYH8-2]
DR   RefSeq; XP_006530632.1; XM_006530569.2. [Q8BYH8-1]
DR   RefSeq; XP_011246574.1; XM_011248272.2. [Q8BYH8-1]
DR   RefSeq; XP_011246575.1; XM_011248273.2. [Q8BYH8-1]
DR   RefSeq; XP_011246576.1; XM_011248274.2. [Q8BYH8-1]
DR   RefSeq; XP_011246577.1; XM_011248275.2. [Q8BYH8-1]
DR   RefSeq; XP_017168006.1; XM_017312517.1. [Q8BYH8-1]
DR   RefSeq; XP_017168007.1; XM_017312518.1. [Q8BYH8-1]
DR   SMR; Q8BYH8; -.
DR   BioGRID; 224575; 5.
DR   CORUM; Q8BYH8; -.
DR   STRING; 10090.ENSMUSP00000105243; -.
DR   GlyGen; Q8BYH8; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8BYH8; -.
DR   PhosphoSitePlus; Q8BYH8; -.
DR   EPD; Q8BYH8; -.
DR   jPOST; Q8BYH8; -.
DR   MaxQB; Q8BYH8; -.
DR   PaxDb; 10090-ENSMUSP00000105243; -.
DR   PeptideAtlas; Q8BYH8; -.
DR   ProteomicsDB; 281609; -. [Q8BYH8-1]
DR   ProteomicsDB; 281610; -. [Q8BYH8-2]
DR   Pumba; Q8BYH8; -.
DR   Antibodypedia; 28339; 95 antibodies from 22 providers.
DR   DNASU; 109151; -.
DR   Ensembl; ENSMUST00000048665.8; ENSMUSP00000046356.7; ENSMUSG00000056608.15. [Q8BYH8-2]
DR   Ensembl; ENSMUST00000109614.9; ENSMUSP00000105243.3; ENSMUSG00000056608.15. [Q8BYH8-1]
DR   Ensembl; ENSMUST00000209423.2; ENSMUSP00000148088.2; ENSMUSG00000056608.15. [Q8BYH8-1]
DR   GeneID; 109151; -.
DR   KEGG; mmu:109151; -.
DR   UCSC; uc009msf.2; mouse. [Q8BYH8-2]
DR   UCSC; uc009msi.2; mouse. [Q8BYH8-1]
DR   AGR; MGI:1924001; -.
DR   CTD; 80205; -.
DR   MGI; MGI:1924001; Chd9.
DR   VEuPathDB; HostDB:ENSMUSG00000056608; -.
DR   eggNOG; KOG0384; Eukaryota.
DR   GeneTree; ENSGT00940000155706; -.
DR   HOGENOM; CLU_000315_5_1_1; -.
DR   InParanoid; Q8BYH8; -.
DR   OMA; PGTACQF; -.
DR   OrthoDB; 22878at2759; -.
DR   PhylomeDB; Q8BYH8; -.
DR   TreeFam; TF313572; -.
DR   Reactome; R-MMU-400206; Regulation of lipid metabolism by PPARalpha.
DR   Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR   BioGRID-ORCS; 109151; 2 hits in 82 CRISPR screens.
DR   ChiTaRS; Chd9; mouse.
DR   PRO; PR:Q8BYH8; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q8BYH8; Protein.
DR   Bgee; ENSMUSG00000056608; Expressed in right kidney and 224 other cell types or tissues.
DR   ExpressionAtlas; Q8BYH8; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   CDD; cd18668; CD1_tandem_CHD5-9_like; 1.
DR   CDD; cd18663; CD2_tandem_CHD5-9_like; 1.
DR   CDD; cd18061; DEXHc_CHD9; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 2.40.50.40; -; 2.
DR   Gene3D; 3.40.5.120; -; 2.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR006576; BRK_domain.
DR   InterPro; IPR037259; BRK_sf.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR46850; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 9; 1.
DR   PANTHER; PTHR46850:SF1; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 9; 1.
DR   Pfam; PF07533; BRK; 2.
DR   Pfam; PF00385; Chromo; 2.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00592; BRK; 2.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF160481; BRK domain-like; 2.
DR   SUPFAM; SSF54160; Chromo domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50013; CHROMO_2; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   Genevisible; Q8BYH8; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Chromatin regulator;
KW   Cytoplasm; DNA-binding; Helicase; Hydrolase; Isopeptide bond;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN           1..2885
FT                   /note="Chromodomain-helicase-DNA-binding protein 9"
FT                   /id="PRO_0000233173"
FT   DOMAIN          689..760
FT                   /note="Chromo 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT   DOMAIN          772..838
FT                   /note="Chromo 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT   DOMAIN          871..1045
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1185..1336
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          173..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          283..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          479..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1460..1484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2046..2238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2331..2471
FT                   /note="Binds A/T-rich DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          2428..2435
FT                   /note="A.T hook-like"
FT   REGION          2473..2494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2724..2770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2818..2885
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           867..871
FT                   /note="LXXLL motif 1"
FT   MOTIF           996..999
FT                   /note="DEAH box"
FT   MOTIF           1035..1039
FT                   /note="LXXLL motif 2"
FT   MOTIF           2030..2034
FT                   /note="LXXLL motif 3"
FT   MOTIF           2710..2714
FT                   /note="LXXLL motif 4"
FT   MOTIF           2782..2786
FT                   /note="LXXLL motif 5"
FT   COMPBIAS        244..263
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..506
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..545
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        557..596
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..632
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..662
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2079..2093
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2131..2193
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2197..2217
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2218..2238
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2725..2751
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2752..2770
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2818..2848
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2849..2878
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         884..891
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         498
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3L8U1"
FT   MOD_RES         549
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3L8U1"
FT   MOD_RES         610
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3L8U1"
FT   MOD_RES         1467
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3L8U1"
FT   MOD_RES         1471
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3L8U1"
FT   MOD_RES         2025
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3L8U1"
FT   MOD_RES         2057
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3L8U1"
FT   MOD_RES         2058
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3L8U1"
FT   MOD_RES         2074
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3L8U1"
FT   MOD_RES         2078
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3L8U1"
FT   CROSSLNK        197
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q3L8U1"
FT   CROSSLNK        595
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q3L8U1"
FT   CROSSLNK        1587
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q3L8U1"
FT   CROSSLNK        1737
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q3L8U1"
FT   CROSSLNK        1902
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q3L8U1"
FT   CROSSLNK        2037
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q3L8U1"
FT   CROSSLNK        2073
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q3L8U1"
FT   CROSSLNK        2349
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q3L8U1"
FT   CROSSLNK        2355
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q3L8U1"
FT   CROSSLNK        2360
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q3L8U1"
FT   CROSSLNK        2833
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q3L8U1"
FT   VAR_SEQ         2335..2350
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12465718,
FT                   ECO:0000303|PubMed:16554032"
FT                   /id="VSP_018087"
FT   CONFLICT        101
FT                   /note="N -> I (in Ref. 2; BAC39090)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        584
FT                   /note="Y -> D (in Ref. 2; BAC28711)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2885 AA;  323860 MW;  B820BE8EA9CC2915 CRC64;
     MTDPMMDFFD DANLFGETLE GLSDDTFVQP GPVSLVDELN LGAEFEPLHI DSLNHVQGTP
     THQKMADFEQ LSQFDSMKFH PVNQSFGSPV EHVLSPHSQF NCSPIHPPNQ PNGLFQDVAD
     GSPMWGHQTA TGLANQNGSP FHQPGHSHSL HQNKSFVAHP DFALFQASEH QTQCSSLHSQ
     QSRSNLNPGQ NSLGQAKNFL DANVSGAHRV NVNHLATAPS SQQTLPVQFS PTANPPAHFL
     KCSSHQEGNY NRPSPSMTSC SVSNSQQFPS HYSFSSGHVS PSSLLQSSAG LAPGHTNQAL
     SDFAGSNSFS PHRGMKQEPT QHLLNPTPSL NSNNFQILHS SHPQGNYSNS KLSPVHMNFP
     DPVDAGPPVG HFNDHAETNG FSSLEENLLH HVDSHAEPFA GLDPEDLLQE GLLPQFDESP
     FGQDNSNHVL DHDLDRQFTS HLVSRPSDMA QTQLQYQARG WPSPLSTNHQ HLHSRNHLCL
     QRQPPSSKKS DGSGTYTKLQ NTQVRVMSEK KPRKRVESES KQEKANRIIS EAIARAKERG
     ERNIPRVMSP ENFPSASVEG KEEKRGRRMK SKPKDRDNKK PKTYSKLKEK TKIGKLIITL
     GKKHKRRNES SDELSDAEQR SQHTFKEQHS QKRRSNRQIK RKKYAEDAEG KQSEEEVKGS
     LRVKRNSAPP PGEQPLQLFV ENPSEEDAAI VDKILACRTV KKEVSPGVML DIEEFFVKYK
     NYSYLHCEWA TEQQLLKDKR IQQKIKRFKL RQAQRAHFLA DMEEEPFNPD YVEVDRILEV
     SFCEDKDTGE SVIYYLVKWC SLPYEDSTWE LKEDVDLAKI EEFEQLQASR PDTRHLDRPP
     SNIWKKIEQS REYKNGNQLR EYQLEGLNWL LFNWYNRRNC ILADEMGLGK TIQSITFLYE
     ILLTGIRGPF LIIAPLSTIA NWEREFRTWT DINVVVYHGS LISRQMIQQY EMYFRDSQGR
     IIRGAYRFQA IITTFEMILG GCGELNAIDW RCVIIDEAHR LKNKNCKLLE GLKLMNLEHK
     VLLTGTPLQN TVEELFSLLH FLEPLRFPSE STFMQEFGDL KTEEQVQKLQ AILKPMMLRR
     LKEDVEKKLA PKEETIIEVE LTNIQKKYYR AILEKNFSFL SKGAGQTNVP NLVNTMMELR
     KCCNHPYLIK GAEEKILGEF RDTYNPSASD FHLQAMIQSA GKLVLIDKLL PKMKAGGHKV
     LIFSQMVRCL DILEDYLIHK RYLYERIDGR VRGNLRQAAI DRFSKPDSDR FVFLLCTRAG
     GLGINLTAAD TCIIFDSDWN PQNDLQAQAR CHRIGQNKAV KVYRLVTRNS YEREMFDRAS
     LKLGLDKAVL QSMSGRDSNV SGIQQLSKKE IEDLLRRGAY GAIMEEEDEG SKFCEEDIDQ
     ILLRRTKTIT IESEGRGSTF AKASFVASGN RTDISLDDPN FWQKWAKKAE LDIDTISGRN
     SLVIDTPRIR KQTRPFSATK DELAELSEAE SEGEEKPKLR RPCDRSGGYG RTECFRVEKN
     LLVYGWGRWR EILSHGRFKR QLNEHDVEVI CRALLAYCLI HYRGDEKIKG FIWDLITPTE
     DGQTRELQNH LGLSAPVPRG RKGKKVKTQT SSFDIQKAEW LRKYNPEQLL QDEGYKKHVK
     HHCNKVLLRV RMLYYLKQEV IGNESQKVFD GVDASDIDVW VPEPDHSEVP AAWWDFDADK
     SLLIGVFKHG YEKYNTIRAD PALCFLERVG KPDDKAVAAE QRANDYMDGD VEDPEYKPAP
     AIFKDDIEDD VSSPGDLVIA DGEGQLMEGD KVYWPTPSAL TTRLRRLITA YQRTNKNRHI
     QQMQPTFSLP ANAMQPLYEE ATLNPKMAAK IERQQRWTRR EEADFYRVVS TFGVVFDPDR
     GQFDWTKFRA LARLHKKTDN SLEKYLCAFM SMCRRVCRLP SKEELVDPNI FIQPITEERA
     SRTLYRIELL RKVREQALRH PQLFERLKLC HPNPDLPIWW ECGSHDRDLL IGAAKHGVSR
     TDYHILRDPE LSFMAAQRNY NQSKAAHSRT SAPLLQQYQV ALSASPLTSL PRLLGAKGTL
     LEDMKVKSES LTEEPQSSEE ESMSSMETRT RVKSEPVSPK NGVLSQATGD QKSGGKSETD
     RRMVAARTEP LTPNPASKKP RVHKRGSQSS SDSDSDSARS SCSSRSSSSS SSSSSCSHSR
     SGSSSSSSSS CSSASSSSSS SSSSSSSSSS SSSEESDSEE DVQKREGTPH RKAYDEESVA
     SLSTTQDETQ DSFQANNGTP ESAYLLQGGY MLAASYWPKD RVMINRLDSI CQTVLKGKWP
     SARRHYDANT VASFYTTKLL DSPGAATERG EPSVPTPPAV AVREEHEQSA QMSKVKKHVR
     EKEFTVKIKD EGGLKLTFQK QGLAQKRPFD GEDGALGQQQ YLTRLRELQS TSETSLVNLP
     KAVPASGTSI QPTLGANGAI LDSQPIVKKR RGRRRNVEGA DILFLNRNKP PNHIPTGMNP
     ALSYPQPQRI PDTESPVPVI NLKDGTRLAG DDAPKRKDLD RWLKEHPGYV EDLGAFIPRV
     QLHEGRPKQK RHRCRNPNKL DINSLTGEER VQLINRRNAR KVGGAFAPPL KDLCRFLKEN
     SEYGVAPEWG DVVKQSGFLP ESMFERILTG PVVREEVSRR GRRPKSGIAK ATTAAAVPAG
     SVPGNPLLAN GLLPGVDLTA LQALQQNLQN LQSLQVTAGL MGMPAGLSSG GETKNMAAMF
     PMLFSGMAGL PNLLGMGGLL SKTAESGAEE KRGNDSKELE GKKERTESQS PENGGERCVP
     GSPSTSSTAA LSSAAAAKPI ALNPLLLSNI LYPGMLLTPG LNLHLPTLSQ SNAFDVQKNK
     SDDLDSSKSV EIKEENSRVR DQEEKGGTEP SPLNENSTDE GSERASSGSD SSSSSSEDSD
     SSNED
//