CIC_MOUSE
ID CIC_MOUSE Reviewed; 2510 AA.
AC Q924A2; Q3UH79; Q3UHP4; Q6PDJ8; Q8CGE4; Q8CHH0; Q9CW61;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Protein capicua homolog;
GN Name=Cic; Synonyms=Kiaa0306;
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), POSSIBLE FUNCTION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12393275; DOI=10.1016/s0169-328x(02)00439-4;
RA Lee C.-J., Chan W.-I., Cheung M., Cheng Y.-C., Appleby V.J., Orme A.T.,
RA Scotting P.J.;
RT "CIC, a member of a novel subfamily of the HMG-box superfamily, is
RT transiently expressed in developing granule neurons.";
RL Brain Res. Mol. Brain Res. 106:151-156(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1056-2510 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1662-2510 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Kidney;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1162-2510 (ISOFORM 1).
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 [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=15981098; DOI=10.1007/s11060-004-4598-2;
RA Lee C.-J., Chan W.-I., Scotting P.J.;
RT "CIC, a gene involved in cerebellar development and ErbB signaling, is
RT significantly expressed in medulloblastomas.";
RL J. Neurooncol. 73:101-108(2005).
RN [7]
RP FUNCTION, INTERACTION WITH ATXN1, TISSUE SPECIFICITY, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17190598; DOI=10.1016/j.cell.2006.11.038;
RA Lam Y.C., Bowman A.B., Jafar-Nejad P., Lim J., Richman R., Fryer J.D.,
RA Hyun E.D., Duvick L.A., Orr H.T., Botas J., Zoghbi H.Y.;
RT "ATAXIN-1 interacts with the repressor Capicua in its native complex to
RT cause SCA1 neuropathology.";
RL Cell 127:1335-1347(2006).
RN [8]
RP INTERACTION WITH ATXN1L.
RX PubMed=17322884; DOI=10.1038/ng1977;
RA Bowman A.B., Lam Y.C., Jafar-Nejad P., Chen H.-K., Richman R., Samaco R.C.,
RA Fryer J.D., Kahle J.J., Orr H.T., Zoghbi H.Y.;
RT "Duplication of Atxn1l suppresses SCA1 neuropathology by decreasing
RT incorporation of polyglutamine-expanded ataxin-1 into native complexes.";
RL Nat. Genet. 39:373-379(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2299 AND SER-2304, AND
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-774; SER-778; SER-1053;
RP SER-1338; SER-1343; SER-1403; SER-1625; THR-2192; SER-2275; SER-2284;
RP SER-2299; SER-2304 AND SER-2311, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2169, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [12]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1097 AND ARG-1839, AND
RP IDENTIFICATION BY MASS 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 [13]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND IDENTIFICATION IN A
RP COMPLEX WITH ATXN1 AND ATXN1L.
RX PubMed=28288114; DOI=10.1038/ng.3808;
RA Lu H.C., Tan Q., Rousseaux M.W., Wang W., Kim J.Y., Richman R., Wan Y.W.,
RA Yeh S.Y., Patel J.M., Liu X., Lin T., Lee Y., Fryer J.D., Han J.,
RA Chahrour M., Finnell R.H., Lei Y., Zurita-Jimenez M.E., Ahimaz P.,
RA Anyane-Yeboa K., Van Maldergem L., Lehalle D., Jean-Marcais N.,
RA Mosca-Boidron A.L., Thevenon J., Cousin M.A., Bro D.E., Lanpher B.C.,
RA Klee E.W., Alexander N., Bainbridge M.N., Orr H.T., Sillitoe R.V.,
RA Ljungberg M.C., Liu Z., Schaaf C.P., Zoghbi H.Y.;
RT "Disruption of the ATXN1-CIC complex causes a spectrum of neurobehavioral
RT phenotypes in mice and humans.";
RL Nat. Genet. 49:527-536(2017).
CC -!- FUNCTION: Transcriptional repressor which plays a role in development
CC of the central nervous system (CNS) (PubMed:17190598). In concert with
CC ATXN1 and ATXN1L, involved in brain development (PubMed:28288114).
CC {ECO:0000269|PubMed:17190598, ECO:0000269|PubMed:28288114}.
CC -!- SUBUNIT: Isoform 1: Interacts with ATXN1 (PubMed:17190598). Isoform 2:
CC Interacts with ATXN1 (PubMed:17190598). Interacts with ATXN1L
CC (PubMed:17322884). Found in a complex with ATXN1 and ATXN1L
CC (PubMed:28288114). {ECO:0000269|PubMed:17190598,
CC ECO:0000269|PubMed:17322884, ECO:0000269|PubMed:28288114}.
CC -!- INTERACTION:
CC Q924A2; P54254: Atxn1; NbExp=2; IntAct=EBI-8412165, EBI-1169713;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=L;
CC IsoId=Q924A2-4; Sequence=Displayed;
CC Name=2; Synonyms=S;
CC IsoId=Q924A2-2; Sequence=VSP_026140, VSP_026141, VSP_039804;
CC -!- TISSUE SPECIFICITY: Expressed in the cortex and hypothalamus (at
CC protein level). Isoform 1: Present in cerebellum (at protein level)
CC (PubMed:17190598). Isoform 2: Present in cerebellum (at protein level)
CC (PubMed:17190598). {ECO:0000269|PubMed:17190598,
CC ECO:0000269|PubMed:28288114}.
CC -!- DEVELOPMENTAL STAGE: Expressed postnatally in the hippocampus,
CC neocortex, olfactory bulb and cerebellum. Expressed in the hippocampus
CC from P0 to P15. Expressed in the posterior region of the neocortex at
CC P4, the anterior region at P9, and is then lost by P15. Expressed in
CC the cerebellum from P0, specifically within the external granule layer
CC (EGL) which contains granule cell precursors. By P7 expression is
CC distributed throughout the EGL and is reduced in the inner granule cell
CC layer (IGL) where granule cells finally differentiate. Expression in
CC the IGL continues to diminish up to P15, when granule cell neurogenesis
CC is complete. {ECO:0000269|PubMed:12393275,
CC ECO:0000269|PubMed:15981098}.
CC -!- DISRUPTION PHENOTYPE: Mice with conditional knockouts of either ATXN1-
CC ATXN1L or CIC in the developing forebrain exhibit intellectual
CC disability, hyperactivity, social-behavioral deficits and reduced
CC thickness of upper cortical layers. {ECO:0000269|PubMed:28288114}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41408.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF363690; AAK73516.1; -; mRNA.
DR EMBL; AK004685; BAB23472.1; -; mRNA.
DR EMBL; AK147276; BAE27813.1; -; mRNA.
DR EMBL; AK147535; BAE27978.1; -; mRNA.
DR EMBL; AC156992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040463; AAH40463.1; -; mRNA.
DR EMBL; BC058665; AAH58665.1; -; mRNA.
DR EMBL; AB093224; BAC41408.1; ALT_SEQ; mRNA.
DR CCDS; CCDS52146.1; -. [Q924A2-2]
DR CCDS; CCDS80678.1; -. [Q924A2-4]
DR RefSeq; NP_001289740.1; NM_001302811.1. [Q924A2-4]
DR RefSeq; NP_082158.2; NM_027882.4. [Q924A2-2]
DR AlphaFoldDB; Q924A2; -.
DR BMRB; Q924A2; -.
DR SMR; Q924A2; -.
DR BioGRID; 214881; 3.
DR DIP; DIP-60650N; -.
DR IntAct; Q924A2; 3.
DR STRING; 10090.ENSMUSP00000126659; -.
DR iPTMnet; Q924A2; -.
DR PhosphoSitePlus; Q924A2; -.
DR EPD; Q924A2; -.
DR jPOST; Q924A2; -.
DR MaxQB; Q924A2; -.
DR PaxDb; Q924A2; -.
DR PeptideAtlas; Q924A2; -.
DR PRIDE; Q924A2; -.
DR ProteomicsDB; 283918; -. [Q924A2-4]
DR ProteomicsDB; 283919; -. [Q924A2-2]
DR Antibodypedia; 17427; 263 antibodies from 29 providers.
DR DNASU; 71722; -.
DR Ensembl; ENSMUST00000163320; ENSMUSP00000126659; ENSMUSG00000005442. [Q924A2-2]
DR Ensembl; ENSMUST00000169266; ENSMUSP00000132351; ENSMUSG00000005442. [Q924A2-4]
DR GeneID; 71722; -.
DR KEGG; mmu:71722; -.
DR UCSC; uc009fsa.3; mouse. [Q924A2-4]
DR UCSC; uc009fsc.3; mouse. [Q924A2-2]
DR CTD; 23152; -.
DR MGI; MGI:1918972; Cic.
DR VEuPathDB; HostDB:ENSMUSG00000005442; -.
DR eggNOG; KOG2746; Eukaryota.
DR GeneTree; ENSGT00940000159960; -.
DR HOGENOM; CLU_000921_0_0_1; -.
DR InParanoid; Q924A2; -.
DR OMA; IDRQTVM; -.
DR PhylomeDB; Q924A2; -.
DR TreeFam; TF323412; -.
DR BioGRID-ORCS; 71722; 10 hits in 75 CRISPR screens.
DR ChiTaRS; Cic; mouse.
DR PRO; PR:Q924A2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q924A2; protein.
DR Bgee; ENSMUSG00000005442; Expressed in embryonic brain and 137 other tissues.
DR ExpressionAtlas; Q924A2; baseline and differential.
DR Genevisible; Q924A2; MM.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR GO; GO:0007612; P:learning; IMP:UniProtKB.
DR GO; GO:0048286; P:lung alveolus development; IMP:MGI.
DR GO; GO:0007613; P:memory; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0035176; P:social behavior; IMP:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IGI:MGI.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR032147; DUF4819.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR Pfam; PF16090; DUF4819; 1.
DR Pfam; PF00505; HMG_box; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; DNA-binding; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..2510
FT /note="Protein capicua homolog"
FT /id="PRO_0000048599"
FT DNA_BIND 1107..1175
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..953
FT /note="Interaction with ATXN1"
FT /evidence="ECO:0000269|PubMed:17190598"
FT REGION 953..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1180..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1233..1272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1288..1348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1376..1536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1691..1712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1744..1773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1797..1819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2032..2057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2092..2248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2262..2336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2423..2510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..67
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..430
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..688
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1020
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1059
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1376..1396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1417..1432
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1435..1473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1759..1773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2092..2112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2125..2158
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2201..2216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2218..2232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2294..2321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2431..2460
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2473..2503
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1053
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1080
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RK0"
FT MOD_RES 1097
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RK0"
FT MOD_RES 1269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RK0"
FT MOD_RES 1338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1604
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RK0"
FT MOD_RES 1625
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1644
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RK0"
FT MOD_RES 1768
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96RK0"
FT MOD_RES 1839
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2169
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 2192
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RK0"
FT MOD_RES 2253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RK0"
FT MOD_RES 2275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RK0"
FT MOD_RES 2284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RK0"
FT MOD_RES 2299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 2300
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96RK0"
FT MOD_RES 2304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 2311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2497
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RK0"
FT VAR_SEQ 1..907
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12393275,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_026140"
FT VAR_SEQ 908..929
FT /note="VPSSYPSHPAPKKEVIMGRPGT -> MYSAHRPLIPASGAASRGLGMF (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:12393275,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_026141"
FT VAR_SEQ 2250
FT /note="K -> NR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12393275,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_039804"
FT CONFLICT 1089
FT /note="D -> E (in Ref. 2; BAE27978)"
FT /evidence="ECO:0000305"
FT CONFLICT 1963
FT /note="S -> SA (in Ref. 1; AAK73516)"
FT /evidence="ECO:0000305"
FT CONFLICT 2059
FT /note="T -> TA (in Ref. 1; AAK73516)"
FT /evidence="ECO:0000305"
FT CONFLICT 2115
FT /note="A -> P (in Ref. 2; BAB23472)"
FT /evidence="ECO:0000305"
FT CONFLICT 2156
FT /note="E -> G (in Ref. 2; BAE27978)"
FT /evidence="ECO:0000305"
FT CONFLICT 2212
FT /note="G -> V (in Ref. 2; BAE27813)"
FT /evidence="ECO:0000305"
FT CONFLICT 2364
FT /note="S -> L (in Ref. 2; BAB23472)"
FT /evidence="ECO:0000305"
FT CONFLICT 2401
FT /note="D -> N (in Ref. 2; BAB23472)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2510 AA; 258130 MW; 092C6CA3CC71B6D9 CRC64;
MKPMKKACPG LAGSASGSKS PPATRAKALR RRGAGEGDKP EEEEEAQPQE QAGPEEAEEG
EEEEAERDPG AEGTHPELQP NDPTPGLTED PKGDGEAGRW EPSLSRKTAT FKSRAPKKKY
VEEHGTGNVG VVGAPEERER TPEDASALGV PPRPPTSTRS SSTDTASEHS ADLEDEPPEA
CGPGPWPSTG TSEGYDLRQL RSQRVLARRG DGLFLPAVVR QVRRSQDLGV QFPGDRALTF
YEGVPGGGVD VVLDVTPPPG ALMVGTAVCT CVEPGVAAYR EGVVVEVATK PAAYKVRLSP
GPSSHAGPPG TLPQAQQTLH REPEEAVWVT RSSLRLLRPP WEPGALLRKH PAGPEEEQAE
PGPALPPCPS SVEPKQPEDA EVSNISFGSN LGTRCEEGEE KHPPSLGTPV LLPLPPPQLL
SPPPKSPAFG GPGRPSEQPS PCQEGSQGGS RSSSVASLEK GAAPAARART PLTAAQQKYK
KGDVVCTPNG IRKKFNGKQW RRLCSRDGCM KESQRRGYCS RHLSMRTKEM EGLADSGPGG
TGRPAGVAAR EGSTEFDWGD ETSRDSEASS VAARGDSRPR LVAPADLSRF EFDECEAAVM
LVSLGSSRSG TPSFSPVSTQ SPFSPAPSPS PSPLFGFRPA NFSPINASPV IQRTAVRSRH
LSASTPKAGV LTPPDLGPHP PPPAPRERHS SGILPTFQTN LTFTVPISPG RRKTELLPHP
GTLGASGAGG GGAAPDFPKS DSLDSGVDSV SHTPTPSTPA GFRAVSPAVP FSRSRQPSPL
LLLPPPAGLT SDPGPSVRRV PAVQRDSPVI VRNPDVPLPS KFPGEVGTAG EARAGGPGRS
CRETPVPPGV ASGKPGLPPP LPAPVPITVP PAAPTAVAQP MPTLGLASSP FQPVAFHPSP
AALLPVLVPS SYPSHPAPKK EVIMGRPGTV WTNVEPRSVA VFPWHSLVPF LAPSQPDPSV
QPSEAQQPAS HPVASNQSKE PAESAAVAHE QPPGGTGGAD PGRPPGAVCP ESPGPGPPLT
LGGVDPGKSL PPTTEEEAPG PPGEPRLDSE TESDHDDAFL SIMSPEIQLP LPPGKRRTQS
LSALPKERDS SSEKDGRSPN KREKDHIRRP MNAFMIFSKR HRALVHQRHP NQDNRTVSKI
LGEWWYALGP KEKQKYHDLA FQVKEAHFKA HPDWKWCNKD RKKSSSEAKP ASLGLAGGHK
ETRERSMSET GTAAAPGVSS ELLSVAAQTL LSSDTKVPGS GPCGAERLHA VGAPGSARPR
AFSHSGVHSL DGGEVDSQAL QELTQMVSGP ASYSGPKPSP QYGAPGSFAA PGEGGTLATS
GRPPLLPSRA SRSQRAASED MTSDEERMVI CEEEGDDDVI ADDSFGTTDI DLKCKERVTD
SESGDSSGED PEGNKGFGRK VFSPVIRSSF THCRPTLDPE PPGPPDPPAA FSKGYGPTPS
SSSSPASTSV SVSTSFSLGS GTFKTQESGQ GSTAVPLRPP PPGAGGPATP SKATRFPPTD
SATFRRKRPE SVGSLEAPGP SVIAAPPSGG GNLLQTLVLP PSKEDREGTR VPSAPAPPLA
YGAPAAPLCR PAATMVTNVV RPVSSTPVPI ASKPFPTSGR AEASSNDIAG ARTEMGTGSR
VPGGSPMGVS LVYSDKKSAA AATSPAPHLV AGPLLGTVGK APATVTNLLV GTPGYGAPAS
PAVQFIAQGA PGSATPAGSG ASTGSGPNGP VPLGILQPGA LGKAGGITQV QYILPTLPQQ
LQVAPAPAPA PGTKAAAPSG PAPTTSIRFT LPPGTSTNGK VLAATAPTAG IPILQSVPSA
PPPKAQSVSP VQATPSGGSA QLLPGKVLVP LAAPSMSVRG GGAGQPLPLV SSPFSVPVQN
GAQQPSKIIQ LTPVPVSTPS GLVPPLSPAT MPGPTSQPQK VLLPSSTRIT YVQSAGGHTL
PLGTSSACSQ TGTVTSYGPT SSVALGFTSL GPSGPAFVQP LLSGQAPLLA PGQVGVSPVP
SPQLPPACTA SGGPVITAFY PGSPAPTSAP LGPPSQAPPS LVYTVATSTT PPAATILPKG
PPASATATPA PTSPFPSATG SMTYSLVAPK AQRPSPKAPQ KVKAAIASIP VGSFESGTTG
RPGSTPRQSS DSGVAREPAA PESELEGQPT PPAPPPPTET WPPTARSSPP PPLPAEERPG
TKGPETASKF PSSSSDWRVP GLGLESRGEP PTPPSPAPAT GPSGSSSGSS EGSSGRAAGD
TPERKEVTSS GKKMKVRPPP LKKTFDSVDK VLSEVDFEER FAELPEFRPE EVLPSPTLQS
LATSPRAILG SYRKKRKNST DLDSAPEDPT SPKRKMRRRS SCSSEPNTPK SAKCEGDIFT
FDRTGTETED VLGELEYEKV PYSSLRRTLD QRRALVMQLF QDHGFFPSAQ ATAAFQARYA
DIFPSKVCLQ LKIREVRQKI MQAATPTEQP PGAEAPLPGP PPTGMAATPV PTPSPAGGPD
PTSPGSDSGT AQVAPPLPPP PEPGPGQPGW EGAPQPSPPP SGPSTAATGR
