CHD9_MOUSE
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 03-AUG-2022, entry version 154.
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; 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 iPTMnet; Q8BYH8; -.
DR PhosphoSitePlus; Q8BYH8; -.
DR EPD; Q8BYH8; -.
DR jPOST; Q8BYH8; -.
DR MaxQB; Q8BYH8; -.
DR PaxDb; Q8BYH8; -.
DR PeptideAtlas; Q8BYH8; -.
DR PRIDE; Q8BYH8; -.
DR ProteomicsDB; 281609; -. [Q8BYH8-1]
DR ProteomicsDB; 281610; -. [Q8BYH8-2]
DR Antibodypedia; 28339; 74 antibodies from 22 providers.
DR DNASU; 109151; -.
DR Ensembl; ENSMUST00000048665; ENSMUSP00000046356; ENSMUSG00000056608. [Q8BYH8-2]
DR Ensembl; ENSMUST00000109614; ENSMUSP00000105243; ENSMUSG00000056608. [Q8BYH8-1]
DR Ensembl; ENSMUST00000209423; ENSMUSP00000148088; ENSMUSG00000056608. [Q8BYH8-1]
DR GeneID; 109151; -.
DR KEGG; mmu:109151; -.
DR UCSC; uc009msf.2; mouse. [Q8BYH8-2]
DR UCSC; uc009msi.2; mouse. [Q8BYH8-1]
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; KMAHSKT; -.
DR OrthoDB; 7181at2759; -.
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 76 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 221 other tissues.
DR ExpressionAtlas; Q8BYH8; baseline and differential.
DR Genevisible; Q8BYH8; MM.
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:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.5.120; -; 2.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR006576; BRK_domain.
DR InterPro; IPR037259; BRK_sf.
DR InterPro; IPR042850; CHD9.
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; IPR000330; SNF2_N.
DR PANTHER; PTHR45623:SF2; PTHR45623:SF2; 2.
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; SSF160481; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54160; SSF54160; 2.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
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..2787
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
