DIDO1_MOUSE
ID DIDO1_MOUSE Reviewed; 2256 AA.
AC Q8C9B9; A2AJ47; A2AJ48; B2RS46; Q05C59; Q3ZTP5; Q3ZTP6; Q4V9W1; Q6ZQD7;
AC Q80V34; Q8BMD0; Q8BRG2; Q8CHR5; Q9WV00;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 4.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Death-inducer obliterator 1;
DE Short=DIO-1;
DE AltName: Full=Death-associated transcription factor 1;
DE Short=DATF-1;
GN Name=Dido1; Synonyms=Datf1, Dio1;
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), AND CHARACTERIZATION.
RC TISSUE=Pre-B cell;
RX PubMed=10393935; DOI=10.1073/pnas.96.14.7992;
RA Garcia-Domingo D., Leonardo E., Grandien A., Martinez P., Albar J.P.,
RA Izpisua-Belmonte J.-C., Martinez-A C.;
RT "DIO-1 is a novel gene involved in onset of apoptosis in vitro, whose
RT misexpression disrupts limb development.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:7992-7997(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RX PubMed=16127461; DOI=10.1172/jci24177;
RA Futterer A., Campanero M.R., Leonardo E., Criado L.M., Flores J.M.,
RA Hernandez J.M., San Miguel J.F., Martinez-A C.;
RT "Dido gene expression alterations are implicated in the induction of
RT hematological myeloid neoplasms.";
RL J. Clin. Invest. 115:2351-2362(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1484-2256 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Thymus, and Wolffian duct;
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Mammary gland, and 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 [7]
RP PROTEIN SEQUENCE OF 540-548 AND 699-705, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-802, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; THR-148; SER-149;
RP SER-802; SER-806; SER-886; SER-1016; SER-1035; THR-1252 AND SER-1256, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [11]
RP STRUCTURE BY NMR OF 257-319.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of PHD domain in death inducer-obliterator 1(DIO-1).";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Required for early embryonic stem cell development (By
CC similarity). Putative transcription factor, weakly pro-apoptotic when
CC overexpressed. {ECO:0000250}.
CC -!- SUBUNIT: Interacts specifically (via PHD-type zinc finger) with histone
CC H3 that is trimethylated at 'Lys-4' (H3K4me3), histone phosphorylation
CC at 'Thr-3' or 'Thr-6' disrupts this binding and promotes translocation
CC of DIDO1 from chromatin to the mitotic spindle during mitosis.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250}. Note=Translocates to the mitotic spindle upon
CC loss of interaction with H3K4me3 during early mitosis (By similarity).
CC Translocates to the nucleus after pro-apoptotic stimuli. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Dido3;
CC IsoId=Q8C9B9-1; Sequence=Displayed;
CC Name=2; Synonyms=Dido1;
CC IsoId=Q8C9B9-2; Sequence=VSP_012363, VSP_012364;
CC Name=3; Synonyms=Dido2;
CC IsoId=Q8C9B9-3; Sequence=VSP_026606, VSP_026607;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at intermediate levels.
CC -!- INDUCTION: Up-regulated during apoptosis.
CC -!- DOMAIN: The PHD-type zinc finger forms an aromatic cage around H3K4me3.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH44755.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC28053.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC97927.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ238332; CAB48401.1; -; mRNA.
DR EMBL; AY425951; AAR84049.1; -; mRNA.
DR EMBL; AY425952; AAR84050.1; -; mRNA.
DR EMBL; AK129117; BAC97927.1; ALT_INIT; mRNA.
DR EMBL; AK032843; BAC28053.1; ALT_INIT; mRNA.
DR EMBL; AK042474; BAC31270.1; -; mRNA.
DR EMBL; AK044919; BAC32141.1; -; mRNA.
DR EMBL; AL732560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029110; AAH29110.1; -; mRNA.
DR EMBL; BC044755; AAH44755.1; ALT_INIT; mRNA.
DR EMBL; BC096662; AAH96662.1; -; mRNA.
DR EMBL; BC138712; AAI38713.1; -; mRNA.
DR EMBL; BC138713; AAI38714.1; -; mRNA.
DR CCDS; CCDS17182.1; -. [Q8C9B9-1]
DR CCDS; CCDS17183.1; -. [Q8C9B9-3]
DR CCDS; CCDS17184.1; -. [Q8C9B9-2]
DR RefSeq; NP_001278361.1; NM_001291432.1. [Q8C9B9-2]
DR RefSeq; NP_001278362.1; NM_001291433.1. [Q8C9B9-3]
DR RefSeq; NP_035935.2; NM_011805.3. [Q8C9B9-2]
DR RefSeq; NP_780760.2; NM_175551.4. [Q8C9B9-1]
DR RefSeq; NP_808520.2; NM_177852.4. [Q8C9B9-3]
DR RefSeq; XP_006500671.1; XM_006500608.3. [Q8C9B9-1]
DR RefSeq; XP_006500672.1; XM_006500609.3. [Q8C9B9-1]
DR RefSeq; XP_006500673.1; XM_006500610.3. [Q8C9B9-1]
DR RefSeq; XP_006500674.1; XM_006500611.3. [Q8C9B9-1]
DR RefSeq; XP_006500675.1; XM_006500612.3. [Q8C9B9-1]
DR RefSeq; XP_006500678.1; XM_006500615.3. [Q8C9B9-1]
DR RefSeq; XP_006500679.1; XM_006500616.3. [Q8C9B9-1]
DR PDB; 1WEM; NMR; -; A=257-319.
DR PDBsum; 1WEM; -.
DR AlphaFoldDB; Q8C9B9; -.
DR BMRB; Q8C9B9; -.
DR SMR; Q8C9B9; -.
DR BioGRID; 204761; 8.
DR IntAct; Q8C9B9; 4.
DR MINT; Q8C9B9; -.
DR STRING; 10090.ENSMUSP00000084794; -.
DR iPTMnet; Q8C9B9; -.
DR PhosphoSitePlus; Q8C9B9; -.
DR EPD; Q8C9B9; -.
DR jPOST; Q8C9B9; -.
DR MaxQB; Q8C9B9; -.
DR PaxDb; Q8C9B9; -.
DR PeptideAtlas; Q8C9B9; -.
DR PRIDE; Q8C9B9; -.
DR ProteomicsDB; 279662; -. [Q8C9B9-1]
DR ProteomicsDB; 279663; -. [Q8C9B9-2]
DR ProteomicsDB; 279664; -. [Q8C9B9-3]
DR Antibodypedia; 3820; 270 antibodies from 37 providers.
DR DNASU; 23856; -.
DR Ensembl; ENSMUST00000087517; ENSMUSP00000084794; ENSMUSG00000038914. [Q8C9B9-1]
DR Ensembl; ENSMUST00000103055; ENSMUSP00000099344; ENSMUSG00000038914. [Q8C9B9-2]
DR Ensembl; ENSMUST00000103056; ENSMUSP00000099345; ENSMUSG00000038914. [Q8C9B9-3]
DR Ensembl; ENSMUST00000103057; ENSMUSP00000099346; ENSMUSG00000038914. [Q8C9B9-3]
DR Ensembl; ENSMUST00000130986; ENSMUSP00000119689; ENSMUSG00000038914. [Q8C9B9-2]
DR GeneID; 23856; -.
DR KEGG; mmu:23856; -.
DR UCSC; uc008ojq.2; mouse. [Q8C9B9-1]
DR UCSC; uc008ojr.2; mouse. [Q8C9B9-3]
DR UCSC; uc008oju.2; mouse. [Q8C9B9-2]
DR CTD; 11083; -.
DR MGI; MGI:1344352; Dido1.
DR VEuPathDB; HostDB:ENSMUSG00000038914; -.
DR eggNOG; KOG1632; Eukaryota.
DR eggNOG; KOG1634; Eukaryota.
DR GeneTree; ENSGT00940000155532; -.
DR HOGENOM; CLU_000673_1_0_1; -.
DR InParanoid; Q8C9B9; -.
DR OMA; FPANRGP; -.
DR OrthoDB; 174961at2759; -.
DR PhylomeDB; Q8C9B9; -.
DR TreeFam; TF350578; -.
DR BioGRID-ORCS; 23856; 9 hits in 76 CRISPR screens.
DR ChiTaRS; Dido1; mouse.
DR EvolutionaryTrace; Q8C9B9; -.
DR PRO; PR:Q8C9B9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8C9B9; protein.
DR Bgee; ENSMUSG00000038914; Expressed in paneth cell and 259 other tissues.
DR ExpressionAtlas; Q8C9B9; baseline and differential.
DR Genevisible; Q8C9B9; MM.
DR GO; GO:0005737; C:cytoplasm; TAS:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0097190; P:apoptotic signaling pathway; IDA:MGI.
DR GO; GO:0006351; P:transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.10.472.30; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR033082; DIDO1.
DR InterPro; IPR012921; SPOC_C.
DR InterPro; IPR003618; TFIIS_cen_dom.
DR InterPro; IPR036575; TFIIS_cen_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11477:SF13; PTHR11477:SF13; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF07744; SPOC; 1.
DR Pfam; PF07500; TFIIS_M; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00510; TFS2M; 1.
DR SUPFAM; SSF46942; SSF46942; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51321; TFIIS_CENTRAL; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Isopeptide bond; Metal-binding;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation;
KW Zinc; Zinc-finger.
FT CHAIN 1..2256
FT /note="Death-inducer obliterator 1"
FT /id="PRO_0000059325"
FT DOMAIN 667..787
FT /note="TFIIS central"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00651"
FT ZN_FING 265..319
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1320..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1362..1421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1509..1609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1630..2256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 162..170
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 182..190
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..885
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1252..1268
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1521..1548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1549..1563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1569..1585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1662..1677
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1678..1717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1740..1754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1853..1871
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2027..2041
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2077..2245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTC0"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTC0"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 148
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTC0"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTC0"
FT MOD_RES 802
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 806
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 886
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1016
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1027
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTC0"
FT MOD_RES 1035
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1239
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTC0"
FT MOD_RES 1252
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTC0"
FT MOD_RES 1514
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTC0"
FT MOD_RES 1726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTC0"
FT MOD_RES 1848
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTC0"
FT MOD_RES 1904
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTC0"
FT MOD_RES 1905
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTC0"
FT MOD_RES 1988
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTC0"
FT MOD_RES 1993
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTC0"
FT MOD_RES 2004
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTC0"
FT MOD_RES 2019
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTC0"
FT MOD_RES 2035
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTC0"
FT CROSSLNK 876
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BTC0"
FT VAR_SEQ 529..614
FT /note="SMKDDRRVEDRTMAAVTIPKKALPSASLVGRQTSPRNLVPKKLPPYSNMAGA
FT KPAIKKLPSGFKGTIPKRPWPSATLSGTSARQAG -> CTYHPKAGFPGPSHHLGGCLG
FT LSRTRVLGVLVLIVASSSLPARSRYQDASGPQVFLPSLWSLSGWFLKSCVGLMLEAISY
FT FSFRPW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10393935,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_012363"
FT VAR_SEQ 615..2256
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10393935,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_012364"
FT VAR_SEQ 1177..1183
FT /note="LESPRPN -> KHPVSGR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16127461"
FT /id="VSP_026606"
FT VAR_SEQ 1184..2256
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16127461"
FT /id="VSP_026607"
FT CONFLICT 45
FT /note="V -> A (in Ref. 1; CAB48401)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="D -> N (in Ref. 1; CAB48401)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="V -> I (in Ref. 4; BAC31270)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="P -> K (in Ref. 6; AAH29110)"
FT /evidence="ECO:0000305"
FT CONFLICT 688
FT /note="D -> Y (in Ref. 2; AAR84049/AAR84050)"
FT /evidence="ECO:0000305"
FT CONFLICT 718
FT /note="Y -> F (in Ref. 2; AAR84049/AAR84050)"
FT /evidence="ECO:0000305"
FT CONFLICT 1739
FT /note="P -> L (in Ref. 2; AAR84050)"
FT /evidence="ECO:0000305"
FT CONFLICT 2046
FT /note="Q -> H (in Ref. 2; AAR84050)"
FT /evidence="ECO:0000305"
FT CONFLICT 2049
FT /note="K -> T (in Ref. 2; AAR84050)"
FT /evidence="ECO:0000305"
FT CONFLICT 2054
FT /note="E -> K (in Ref. 2; AAR84050)"
FT /evidence="ECO:0000305"
FT CONFLICT 2058
FT /note="A -> P (in Ref. 2; AAR84050)"
FT /evidence="ECO:0000305"
FT CONFLICT 2118
FT /note="Q -> L (in Ref. 4; BAC28053)"
FT /evidence="ECO:0000305"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:1WEM"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:1WEM"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:1WEM"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:1WEM"
FT HELIX 298..307
FT /evidence="ECO:0007829|PDB:1WEM"
FT HELIX 314..319
FT /evidence="ECO:0007829|PDB:1WEM"
SQ SEQUENCE 2256 AA; 247176 MW; CB4F6F6D3FE53747 CRC64;
MDDKGHLSNE EAPKAIKPTS KEFRKTWGFR RTTIAKREGA GDTEVDPSEQ QPQQHNLSLR
RSGRQPKRTE RVEEFLTTVR RRGKKNVPVS LEDSSEPTSS TVTDVETASE GSVESSSEIR
SGPVSDSLGK EHPASSEKAK GGEEEEDTSD SDSDGLTLKE LQNRLRRKRE QEPVERSLRG
SQNRLRKKRR EEDSAETGSV QIGSAEQDRP LCKQEPEASQ GPVSQSETDD IENQLEGKAT
QGNTEENPRE AGKPKPECEV YDPNALYCIC RQPHNNRFMI CCDRCEEWFH GDCVGISEAR
GRLLERNGED YICPNCTILQ VQDETNGSAT DEQDSGCRSV GADGTDCTSI GTVEQKSGED
QGIKGRIEKA ANPSGKKKLK IFQPVVEAPG APKCIGPGCS SVAQPDSVYC SNDCILKHAA
ATMRFLSSGK EQKTKPKEKV KTKPEKFSLP KCSVQVGIKI SSVHKRLASE KRENPVKKVM
LASRSETSGK EAACESSTPS WASDHNYNAV KPEKPEKPTA LSPTLLSKSM KDDRRVEDRT
MAAVTIPKKA LPSASLVGRQ TSPRNLVPKK LPPYSNMAGA KPAIKKLPSG FKGTIPKRPW
PSATLSGTSA RQAGPTPMTA ASKKLPGSAA VVGVTRKPMS ANVPAASPAP GRLGPVSPAP
SQPNSQIRQN IRRSLKEILW KRVNDSDDLI MTENEVGKIA LHIEKEMFNL FQVTDNRYKS
KYRSIMFNLK DPKNQGLFHR VLREEISLAK LVRMKPEELV SKELSMWTEK PTKSVIESRT
KLLNESKKNT TKPETIPDME DSPPVSDSEE QQESVRAAPE KSAAPLLDVF SSMLKDTTSQ
HRAHLFDLNC KICTGQVPSS EDEPAPKKQK LSASSKKEDF KPRHDSSPPN AVPNTADEGI
ADTLPENASE PDPESTSSLN QERKCFPESP GDSHPEPSSL GGLSPSSASG GSGVVTTVTM
SGRDPRTALS GSCTVTASMA AHLDNSQASE TKLDMIKPAL TSAVVPKSIL AKPSSSPDPR
YLSVPPSPSI SESRSPPEGD TTLFLSRLNT IWKGFINMQS VAKFVTKAYP VSGCLDYLSE
DLPDTIHIGG RIAPKTVWDY VGKLKSSVSK ELCLIRFHPA TEEEEVAYIS LYSYFSSRGR
FGVVANNNRH VKDLYLIPLS AKDPVPSKLL PFEGPGLESP RPNIILGLVI CQKVKRPSSA
GELDKTDEKR TRLQQEELET SVYPKVTAAL PSEKKPPKYS VHSIDTAATS TTPPGSPPPP
PPLPEPPVLK ILSSLKPGST STVTAPTTAA ITTTASPVTA ATSKTASPLE HILQTLFGKK
KSFEPSGKES VGSTLSPHQD SKAKGEDTMS AAPLLDPIVQ QFGQFSKDKA LEEEEEDDRP
YDPEEEYNPD RAFHTLLAEP GRPHDVQSVS ETAEREEVAY DPEDETILEE AKVTIDDLPN
RMCMKVSATE RPADFTTDAS SASLVEQQKM LEELNKQIEE QKRQLEEQEE ALRQQRAAVG
VSMAHFSVSD ALMSPPPKSS LGKTELFSQE QQAPDPSQGA PNTNHNLDSR QSRDPRQARR
LAAENTENES LPRAPTGSTP GPQGTLPARE TPAGTAVVQG PGLAAEAKES MAVPWAPGEN
AVLRPEHDIQ KCEHPGNPVS LPLDTSHLPT AGDGAARPAP PRRVLLPTPP STTFPPSFPL
QPKAQNFSSG SREPFSGPTF MSQETSLGSS QYEDPRGAQS AGKNDSPVAD MEDSREPQPR
PGESTTSFPQ PGQRGGGPQP QFPGQREPAP RTFGMSGHHG PSFPGPRGPV PPYSEENLVP
NSDGPRGPPP ARFGAQKPPI PSLFSGQHGP PPYGDNRGLS PSYLGGPRGG APAQFEDRKD
PHGEKREFQD TPYNEMTGAP AQCEGPDQAQ FMGNRAPFQF GGQRRPLLTQ MKGPRGGPPP
SQFGAQRGPP PGHFVGPRGP HPSQFENSRG THPGQFEGAR GQAPGFMPGP RGIQPQQFEE
QRVNSPPRFA GQRASAPLPY GGPRGPAPFP EKNEQPPSRF HFQGPSSQPV KPPPRPLLEL
PSHPPQHRKD RWDEAGPATA LPSSAGPGQG HEADGQWATS EFREGKGHEY RSPAFEGRQR
ERFEAGSKEK PLDEPEAQGL ESRQGRAFED RRRERERGRN WSRERDWERS RDWDRHREWD
KGRDRSSNRD RERDNDRAKE WDRSRERSRN RDRDRERRRD RDRSRSRDRD RDRERARDRD
RDRGRDRKDR SKSRESPRDQ KPEARTSEGG PAAAQA
