CHD7_MOUSE
ID CHD7_MOUSE Reviewed; 2986 AA.
AC A2AJK6; Q3TA86; Q3TAG7; Q3TBU4; Q8C986; Q8K244;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 7;
DE Short=CHD-7;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent helicase CHD7;
GN Name=Chd7;
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] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-590 (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum;
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 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2282-2986 (ISOFORM 3).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=16400610; DOI=10.1086/500273;
RA Lalani S.R., Safiullah A.M., Fernbach S.D., Harutyunyan K.G., Thaller C.,
RA Peterson L.E., McPherson J.D., Gibbs R.A., White L.D., Hefner M.,
RA Davenport S.L.H., Graham J.M., Bacino C.A., Glass N.L., Towbin J.A.,
RA Craigen W.J., Neish S.R., Lin A.E., Belmont J.W.;
RT "Spectrum of CHD7 mutations in 110 individuals with CHARGE syndrome and
RT genotype-phenotype correlation.";
RL Am. J. Hum. Genet. 78:303-314(2006).
RN [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-280, 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).
RN [6]
RP IDENTIFICATION IN A COMPLEX WITH FAM172A; AGO2 AND CHD7.
RX PubMed=29311329; DOI=10.1073/pnas.1715378115;
RA Belanger C., Berube-Simard F.A., Leduc E., Bernas G., Campeau P.M.,
RA Lalani S.R., Martin D.M., Bielas S., Moccia A., Srivastava A.,
RA Silversides D.W., Pilon N.;
RT "Dysregulation of cotranscriptional alternative splicing underlies CHARGE
RT syndrome.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E620-E629(2018).
CC -!- FUNCTION: Probable transcription regulator. Maybe involved in the in
CC 45S precursor rRNA production (By similarity). {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: May interact with CTCF. Interacts with CHD8. Interacts with
CC FAM124B. Found in a complex composed of AGO2, CHD7 and FAM172A
CC (PubMed:29311329). {ECO:0000250|UniProtKB:Q9P2D1,
CC ECO:0000269|PubMed:29311329}.
CC -!- INTERACTION:
CC A2AJK6; Q60I23: Sox2; NbExp=6; IntAct=EBI-6122905, EBI-6120118;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9P2D1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A2AJK6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AJK6-2; Sequence=VSP_026040, VSP_026041;
CC Name=3;
CC IsoId=A2AJK6-3; Sequence=VSP_026042;
CC -!- TISSUE SPECIFICITY: Expressed in the outflow tract of the heart, optic
CC vesicle, facio-acoustic preganglion complex, brain, olfactory pit, and
CC mandibular component of the first branchial arch.
CC {ECO:0000269|PubMed:16400610}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE42701.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE42701.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK042727; BAC31343.1; -; mRNA.
DR EMBL; AK171051; BAE42213.1; -; mRNA.
DR EMBL; AK171857; BAE42701.1; ALT_SEQ; mRNA.
DR EMBL; AK172025; BAE42783.1; -; mRNA.
DR EMBL; AL732627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL805903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034239; AAH34239.2; -; mRNA.
DR CCDS; CCDS38689.1; -. [A2AJK6-1]
DR RefSeq; NP_001264078.1; NM_001277149.1. [A2AJK6-1]
DR RefSeq; XP_006538067.1; XM_006538004.3. [A2AJK6-1]
DR SMR; A2AJK6; -.
DR BioGRID; 236292; 8.
DR IntAct; A2AJK6; 14.
DR MINT; A2AJK6; -.
DR STRING; 10090.ENSMUSP00000059079; -.
DR iPTMnet; A2AJK6; -.
DR PhosphoSitePlus; A2AJK6; -.
DR EPD; A2AJK6; -.
DR jPOST; A2AJK6; -.
DR MaxQB; A2AJK6; -.
DR PaxDb; A2AJK6; -.
DR PeptideAtlas; A2AJK6; -.
DR PRIDE; A2AJK6; -.
DR ProteomicsDB; 281604; -. [A2AJK6-1]
DR ProteomicsDB; 281605; -. [A2AJK6-2]
DR ProteomicsDB; 281606; -. [A2AJK6-3]
DR Antibodypedia; 24678; 158 antibodies from 30 providers.
DR Ensembl; ENSMUST00000039267; ENSMUSP00000043903; ENSMUSG00000041235. [A2AJK6-1]
DR Ensembl; ENSMUST00000051558; ENSMUSP00000059079; ENSMUSG00000041235. [A2AJK6-1]
DR GeneID; 320790; -.
DR KEGG; mmu:320790; -.
DR UCSC; uc008rxy.1; mouse. [A2AJK6-2]
DR UCSC; uc008rxz.2; mouse. [A2AJK6-1]
DR CTD; 55636; -.
DR MGI; MGI:2444748; Chd7.
DR VEuPathDB; HostDB:ENSMUSG00000041235; -.
DR eggNOG; KOG0384; Eukaryota.
DR GeneTree; ENSGT00940000153649; -.
DR HOGENOM; CLU_000315_5_0_1; -.
DR InParanoid; A2AJK6; -.
DR OMA; TMDMTGF; -.
DR OrthoDB; 7181at2759; -.
DR PhylomeDB; A2AJK6; -.
DR TreeFam; TF313572; -.
DR BioGRID-ORCS; 320790; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Chd7; mouse.
DR PRO; PR:A2AJK6; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2AJK6; protein.
DR Bgee; ENSMUSG00000041235; Expressed in retinal neural layer and 228 other tissues.
DR ExpressionAtlas; A2AJK6; baseline and differential.
DR Genevisible; A2AJK6; MM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0007512; P:adult heart development; IMP:MGI.
DR GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR GO; GO:0035904; P:aorta development; IMP:MGI.
DR GO; GO:0035909; P:aorta morphogenesis; IMP:MGI.
DR GO; GO:0048844; P:artery morphogenesis; IGI:MGI.
DR GO; GO:0036302; P:atrioventricular canal development; IMP:MGI.
DR GO; GO:0008015; P:blood circulation; IMP:MGI.
DR GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
DR GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR GO; GO:0060411; P:cardiac septum morphogenesis; IMP:MGI.
DR GO; GO:0007417; P:central nervous system development; ISO:MGI.
DR GO; GO:0043009; P:chordate embryonic development; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IMP:MGI.
DR GO; GO:0050890; P:cognition; ISO:MGI.
DR GO; GO:0021545; P:cranial nerve development; ISO:MGI.
DR GO; GO:0042471; P:ear morphogenesis; IMP:MGI.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
DR GO; GO:0060429; P:epithelium development; IMP:MGI.
DR GO; GO:0060324; P:face development; ISO:MGI.
DR GO; GO:0030540; P:female genitalia development; IMP:MGI.
DR GO; GO:0048806; P:genitalia development; ISO:MGI.
DR GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR GO; GO:0060384; P:innervation; IMP:MGI.
DR GO; GO:0060173; P:limb development; ISO:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0043584; P:nose development; IMP:MGI.
DR GO; GO:0042048; P:olfactory behavior; IMP:MGI.
DR GO; GO:0021772; P:olfactory bulb development; IMP:MGI.
DR GO; GO:0021553; P:olfactory nerve development; IMP:MGI.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0060123; P:regulation of growth hormone secretion; ISO:MGI.
DR GO; GO:0050767; P:regulation of neurogenesis; IMP:MGI.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IMP:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; ISO:MGI.
DR GO; GO:0003226; P:right ventricular compact myocardium morphogenesis; IMP:MGI.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0062009; P:secondary palate development; ISO:MGI.
DR GO; GO:0048752; P:semicircular canal morphogenesis; IGI:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR GO; GO:0001501; P:skeletal system development; ISO:MGI.
DR GO; GO:0030217; P:T cell differentiation; ISO:MGI.
DR GO; GO:0048771; P:tissue remodeling; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IMP:MGI.
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; 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 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; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chromatin regulator; Coiled coil;
KW DNA-binding; Helicase; Hydrolase; Methylation; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; rRNA processing; Transcription;
KW Transcription regulation.
FT CHAIN 1..2986
FT /note="Chromodomain-helicase-DNA-binding protein 7"
FT /id="PRO_0000289964"
FT DOMAIN 790..857
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 872..937
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 970..1144
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1284..1454
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 93..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1566..1590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1826..1851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2151..2274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2366..2393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2812..2861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2924..2986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2390..2420
FT /evidence="ECO:0000255"
FT MOTIF 1095..1098
FT /note="DEAH box"
FT COMPBIAS 194..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..410
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..522
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1566..1589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2152..2204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2366..2381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2812..2826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2827..2851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2925..2959
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2962..2986
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 983..990
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 147
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2D1"
FT MOD_RES 280
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2D1"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2D1"
FT MOD_RES 1567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2D1"
FT MOD_RES 1571
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2D1"
FT MOD_RES 1864
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2D1"
FT MOD_RES 2220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2D1"
FT MOD_RES 2222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2D1"
FT MOD_RES 2226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2D1"
FT MOD_RES 2240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2D1"
FT MOD_RES 2261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2D1"
FT MOD_RES 2264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2D1"
FT MOD_RES 2345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2D1"
FT MOD_RES 2384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2D1"
FT MOD_RES 2461
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2D1"
FT MOD_RES 2524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2D1"
FT MOD_RES 2540
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2D1"
FT MOD_RES 2548
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2D1"
FT MOD_RES 2608
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2D1"
FT MOD_RES 2945
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2D1"
FT VAR_SEQ 549..558
FT /note="HSPSEPFLEK -> VRGADACPVA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026040"
FT VAR_SEQ 559..2986
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026041"
FT VAR_SEQ 2526..2551
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026042"
FT CONFLICT 102
FT /note="S -> T (in Ref. 1; BAE42783)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="N -> D (in Ref. 1; BAE42783)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="V -> I (in Ref. 1; BAE42213)"
FT /evidence="ECO:0000305"
FT CONFLICT 2343
FT /note="V -> M (in Ref. 3; AAH34239)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2986 AA; 334061 MW; 3CDDC3914E6640EB CRC64;
MADPGMMSLF GEDGSLFSEG LEGLGECGYP ENPVNPMGQQ MPIDQGFPSL QPSLHHPSPN
QNQTKLTHFD HYSQYEQKMH LMDQPNRMMG SAPGNGLASP HSQYHTPPVP QVPHGGGGGG
QMGVYPGIQN ERHGQSFVDG GSMWGPRAVQ VPDQIRAPYQ QQQPQPAPSG PPAQGHPQHM
QQMGSYLARG DFSMQQHGQP QQRMGQFSQG QEGLSQGSPF IATSGPGHLS HMPQQSPSMA
PSLRHPVQQQ FHHHPAALHG ESVAHSPRFS PNPPQQGAVR PQTLNFSSRN QTVPSPTVNN
SGQYSRYPYS NLNQGLVNST GMNQNLGLTN STPMNQSVPR YPNAVGFPSN SGQGLVHQQP
IHSSGSLNQM NTQTMHPSQP QGTYASPPPM SPMKAMSNPA GTPPPQVRPG SAGMPMEVGS
YPNMPHPQPS HQPPGAMGIG QRNMGPRNMQ QPRSFMGMSS APRELTGHMR PNGCPGVGLA
DPQAIQERLI PGQQHPGQQP SFQQLPTCPP LQPHPGLHQS SPPHPHHQPW AQLHPSPQNT
PQKVPVHQHS PSEPFLEKPV PDMTQVSAQN AQLVKSDDYL PSIEQQPQQK KKKKKNNHIA
AGDSSKGFGK DDFPGGVENQ ELRRNSLDVS QEEKKKKKRP KVKKDPKESK EPKEKKEPKT
PKAPKIPKEP KEKKAKTVTP KPKSSKKSSN KKPDSEASAL KKKVNKGKTE GSENSDLDKT
PPPSPAPEED EDPGVQKRRS SRQVKRKRYT EDLEFKISDE EADDADAAGR DSPSNTSQSE
QQESVDAEGP VVEKIMSSRL VKKQKESGEE VEVEEFYVKY KNFSYLHCQW ASVEDLEKDK
RIQQKIKRFK SKQGQSKFLS EIEDDLFNPD YVEVDRIMDF ARSTDDRGEP VIHYLVKWCS
LPYEDSTWEL KQDIDQTKIE EFEKLMSREP ETERVERPPA DDWKKSESSR EYKNNNKLRE
YQLEGVNWLL FNWYNMRNCI LADEMGLGKT IQSITFLYEI YLKGIHGPFL VIAPLSTIPN
WEREFRTWTE LNVVVYHGSQ ASRRTIQLYE MYFKDPQGRV IKGSYKFHAI ITTFEMILTD
CPELRNIPWR CVVIDEAHRL KNRNCKLLEG LKMMDLEHKV LLTGTPLQNT VEELFSLLHF
LEPSRFPSET TFMQEFGDLK TEEQVQKLQA ILKPMMLRRL KEDVEKNLAP KEETIIEVEL
TNIQKKYYRA ILEKNFTFLS KGGGQANVPN LLNTMMELRK CCNHPYLING AEEKILEEFK
ETHNAESPDF QLQAMIQAAG KLVLIDKLLP KLKAGGHRVL IFSQMVRCLD ILEDYLIQRR
YPYERIDGRV RGNLRQAAID RFSKPDSDRF VFLLCTRAGG LGINLTAADT CIIFDSDWNP
QNDLQAQARC HRIGQSKSVK IYRLITRNSY EREMFDKASL KLGLDKAVLQ SMSGRENATN
GVQQLSKKEI EDLLRKGAYG ALMDEEDEGS KFCEEDIDQI LLRRTHTITI ESEGKGSTFA
KASFVASGNR TDISLDDPNF WQKWAKKAEL DIDALNGRNN LVIDTPRVRK QTRLYSAVKE
DELMEFSDLE SDSEEKPCAK PRRPQDKSQG YARSECFRVE KNLLVYGWGR WTDILSHGRY
KRQLTEQDVE TICRAILVYC LNHYRGDENI KSFIWDLITP TADGQTRALL NHSGLSAPVP
RGRKGKKVKA QSTQPVVHDA HWLASCNPDA LFQEDSYKKH LKHHCNKVLL RVRMLYYLRQ
EVIGDQAEKI LEGADSSEAD VWIPEPFHAE VPTDWWDREA DKSLLIGVFK HGYEKYNSMR
ADPALCFLER VGMPDAKAIA AEQRGTDMLA DGGDGGEFDR EDEDPEYKPT RAPFKDEIDE
FANSPAEDKE ESMEVHSSGK HSESNAELGQ LYWPNTSTLT TRLRRLITAY QRSYKRQQMR
QEALMKTDRR RRRPREEVRA LEAEREAIIS EKRQKWTRRE EADFYRVVST FGVIFDPVKQ
QFDWNQFRAF ARLDKKSDES LGKYFSCFVA MCRRVCRMPA KPEDEPPDLA SLIEPITEER
ASRTLYRIEL LRKIREQVLH HPQLSDRLKL CQPSLDLPEW WECGRHDRDL LVGAAKHGVS
RTDYHILNDP ELSFLDAHKS FAQNRGASTV PPLNTLAMGF GQTPPVISSA HVHEEKAMEQ
AEGKAEECEH SPAKERSDGK EEEEEAGGAK DGKQECEVEA SSVKGELKGV EGSADPGSKS
VSEKGSEEDE EEKLEDDDKS EESSQPEAGA VSRGKTFDEE SNASLSTARD ETRDGFYMED
GDASVAQLLH ERTFAFSFWP KDRVMINRLD NICEAVLKGK WPVNRRQMFD FQGLVPGYPP
SAVDSPLQKR SFAELSMVSQ ASISASEDIT TSPQLSKDDA LNLSVPRQRR RRRRKVEIEA
ERAAKRRNLM EMVAQLRESQ VVSENGQEKV VDLSKASREA TSSTSNFSSL TSKFILPNVS
TPVSDAFKSQ MELLQAGLSR TPTRHMLNGS LVDGEPPMKR RRGRRKNVEG LDLLFMSHKR
TPLSAEDAEV TKAFEEDIET PPIRNIPSPG QLDPDTRIPV INLEDGTRLV GEDAPKNKDL
VDWLKLHPTY TVDMPSYVPK NTDVLFSSFQ KPKQKRHRCR NPNKLDINTL TGEERVPVVN
KRNGKKMGGA MAPPMKDLPR WLEENPEFAV APDWTDIVKQ SGFVPESMFD RLLTGPVVRG
EGASRRGRRP KSEIARAAAA AAAVASTSGI NPLLVNSLFA GMDLTSLQNL QNLQSLQLAG
LMGFPPGLAT AATAGGDAKS PAAVLPLMLP GMAGLPNVFG LGGLLNNPLS AATGNTTTAS
SQGEPEDGTS KAEEKGNDNE DENRDSEKST DTVSAADSAN GSVGAATAPA ALPSNPLAFN
PFLLSTMAPG LFYPSMFLPP GLGGLTLPGF PALAGLQNAV GTSEEKAADK AEGGPCKDGE
TLEGSDAEEN LDKTVESSIL EDEVAQGEEL DSLEGGDEIE NTGNDE
