CIC_HUMAN
ID CIC_HUMAN Reviewed; 1608 AA.
AC Q96RK0; Q7LGI1; Q9UEG5; Q9Y6T1;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Protein capicua homolog;
GN Name=CIC; Synonyms=KIAA0306;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], POSSIBLE FUNCTION, AND VARIANT GLY-982.
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 GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 158-1608, AND VARIANT GLY-982.
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [4]
RP TISSUE SPECIFICITY, AND EXPRESSION IN MEDULLOBLASTOMA.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1378, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-721; SER-1373 AND
RP SER-1382, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-721; SER-1373; SER-1382;
RP SER-1397; SER-1402 AND SER-1409, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-721 AND SER-1373, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1402, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-277; SER-721;
RP SER-739; SER-1294; SER-1351; SER-1373; SER-1389; SER-1397 AND SER-1409, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-362; SER-700;
RP SER-1397; THR-1398; SER-1409 AND SER-1595, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-863, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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 [14]
RP VARIANTS [LARGE SCALE ANALYSIS] LYS-104 AND THR-652.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [15]
RP VARIANT MRD45 TRP-492.
RX PubMed=21076407; DOI=10.1038/ng.712;
RA Vissers L.E., de Ligt J., Gilissen C., Janssen I., Steehouwer M.,
RA de Vries P., van Lier B., Arts P., Wieskamp N., del Rosario M.,
RA van Bon B.W., Hoischen A., de Vries B.B., Brunner H.G., Veltman J.A.;
RT "A de novo paradigm for mental retardation.";
RL Nat. Genet. 42:1109-1112(2010).
RN [16]
RP VARIANTS MRD45 353-ARG--ARG-1608 DEL AND 992-GLN--ARG-1608 DEL, AND
RP CHARACTERIZATION OF VARIANT MRD45 353-ARG--ARG-1608 DEL.
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).
RN [17]
RP VARIANT 492-ARG--ARG-1608 DEL.
RX PubMed=30397230; DOI=10.1038/s41467-018-06014-6;
RA Snijders Blok L., Rousseau J., Twist J., Ehresmann S., Takaku M.,
RA Venselaar H., Rodan L.H., Nowak C.B., Douglas J., Swoboda K.J.,
RA Steeves M.A., Sahai I., Stumpel C.T.R.M., Stegmann A.P.A., Wheeler P.,
RA Willing M., Fiala E., Kochhar A., Gibson W.T., Cohen A.S.A., Agbahovbe R.,
RA Innes A.M., Au P.Y.B., Rankin J., Anderson I.J., Skinner S.A., Louie R.J.,
RA Warren H.E., Afenjar A., Keren B., Nava C., Buratti J., Isapof A.,
RA Rodriguez D., Lewandowski R., Propst J., van Essen T., Choi M., Lee S.,
RA Chae J.H., Price S., Schnur R.E., Douglas G., Wentzensen I.M., Zweier C.,
RA Reis A., Bialer M.G., Moore C., Koopmans M., Brilstra E.H., Monroe G.R.,
RA van Gassen K.L.I., van Binsbergen E., Newbury-Ecob R., Bownass L.,
RA Bader I., Mayr J.A., Wortmann S.B., Jakielski K.J., Strand E.A., Kloth K.,
RA Bierhals T., Roberts J.D., Petrovich R.M., Machida S., Kurumizaka H.,
RA Lelieveld S., Pfundt R., Jansen S., Deriziotis P., Faive L., Thevenon J.,
RA Assoum M., Shriberg L., Kleefstra T., Brunner H.G., Wade P.A., Fisher S.E.,
RA Campeau P.M.;
RT "CHD3 helicase domain mutations cause a neurodevelopmental syndrome with
RT macrocephaly and impaired speech and language.";
RL Nat. Commun. 9:4619-4619(2018).
CC -!- FUNCTION: Transcriptional repressor which plays a role in development
CC of the central nervous system (CNS). In concert with ATXN1 and ATXN1L,
CC involved in brain development. {ECO:0000250|UniProtKB:Q924A2}.
CC -!- SUBUNIT: Interacts with ATXN1 and ATXN1L. Found in a complex with ATXN1
CC and ATXN1L. {ECO:0000250|UniProtKB:Q924A2}.
CC -!- INTERACTION:
CC Q96RK0; P54253: ATXN1; NbExp=8; IntAct=EBI-945857, EBI-930964;
CC Q96RK0; Q9HC77: CENPJ; NbExp=2; IntAct=EBI-945857, EBI-946194;
CC Q96RK0; Q08379: GOLGA2; NbExp=4; IntAct=EBI-945857, EBI-618309;
CC Q96RK0; Q99816: TSG101; NbExp=2; IntAct=EBI-945857, EBI-346882;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
CC -!- TISSUE SPECIFICITY: Expressed in fetal brain.
CC {ECO:0000269|PubMed:15981098}.
CC -!- DISEASE: Intellectual developmental disorder, autosomal dominant 45
CC (MRD45) [MIM:617600]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period. MRD45
CC patients manifest developmental delay, variable intellectual
CC disability, and behavioral disorders, including autistic features,
CC attention deficit, and hyperactivity. {ECO:0000269|PubMed:21076407,
CC ECO:0000269|PubMed:28288114}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Expressed in medulloblastoma, a pediatric brain tumor
CC which may arise from the granule cell lineage.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD11988.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF363689; AAK73515.1; -; mRNA.
DR EMBL; AC006486; AAD11988.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB002304; BAA20765.1; -; mRNA.
DR CCDS; CCDS12601.1; -.
DR RefSeq; NP_001291744.1; NM_001304815.1.
DR RefSeq; NP_055940.3; NM_015125.4.
DR PDB; 2M41; NMR; -; A=34-48.
DR PDB; 4J2J; X-ray; 2.50 A; D/E/F=28-48.
DR PDB; 4J2L; X-ray; 3.15 A; C/D=21-48.
DR PDB; 6JRP; X-ray; 3.00 A; A/D/G/J=199-276.
DR PDB; 6KZG; X-ray; 2.00 A; C/Q=298-305.
DR PDB; 6KZH; X-ray; 2.65 A; C/Q=170-177.
DR PDBsum; 2M41; -.
DR PDBsum; 4J2J; -.
DR PDBsum; 4J2L; -.
DR PDBsum; 6JRP; -.
DR PDBsum; 6KZG; -.
DR PDBsum; 6KZH; -.
DR AlphaFoldDB; Q96RK0; -.
DR BMRB; Q96RK0; -.
DR SMR; Q96RK0; -.
DR BioGRID; 116767; 662.
DR CORUM; Q96RK0; -.
DR DIP; DIP-49964N; -.
DR IntAct; Q96RK0; 78.
DR MINT; Q96RK0; -.
DR STRING; 9606.ENSP00000458663; -.
DR GlyGen; Q96RK0; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; Q96RK0; -.
DR PhosphoSitePlus; Q96RK0; -.
DR BioMuta; CIC; -.
DR DMDM; 116241300; -.
DR CPTAC; CPTAC-1346; -.
DR EPD; Q96RK0; -.
DR jPOST; Q96RK0; -.
DR MassIVE; Q96RK0; -.
DR MaxQB; Q96RK0; -.
DR PaxDb; Q96RK0; -.
DR PeptideAtlas; Q96RK0; -.
DR PRIDE; Q96RK0; -.
DR ProteomicsDB; 77973; -.
DR Antibodypedia; 17427; 263 antibodies from 29 providers.
DR DNASU; 23152; -.
DR Ensembl; ENST00000575354.6; ENSP00000458663.2; ENSG00000079432.9.
DR GeneID; 23152; -.
DR KEGG; hsa:23152; -.
DR UCSC; uc002otf.1; human.
DR CTD; 23152; -.
DR DisGeNET; 23152; -.
DR GeneCards; CIC; -.
DR HGNC; HGNC:14214; CIC.
DR HPA; ENSG00000079432; Low tissue specificity.
DR MalaCards; CIC; -.
DR MIM; 612082; gene.
DR MIM; 617600; phenotype.
DR neXtProt; NX_Q96RK0; -.
DR OpenTargets; ENSG00000079432; -.
DR Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability.
DR PharmGKB; PA26513; -.
DR VEuPathDB; HostDB:ENSG00000079432; -.
DR eggNOG; KOG2746; Eukaryota.
DR GeneTree; ENSGT00940000159960; -.
DR InParanoid; Q96RK0; -.
DR OrthoDB; 14207at2759; -.
DR PhylomeDB; Q96RK0; -.
DR TreeFam; TF323412; -.
DR PathwayCommons; Q96RK0; -.
DR SignaLink; Q96RK0; -.
DR SIGNOR; Q96RK0; -.
DR BioGRID-ORCS; 23152; 33 hits in 1103 CRISPR screens.
DR ChiTaRS; CIC; human.
DR GeneWiki; CIC_(gene); -.
DR GenomeRNAi; 23152; -.
DR Pharos; Q96RK0; Tbio.
DR PRO; PR:Q96RK0; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q96RK0; protein.
DR Bgee; ENSG00000079432; Expressed in right hemisphere of cerebellum and 189 other tissues.
DR ExpressionAtlas; Q96RK0; baseline and differential.
DR Genevisible; Q96RK0; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
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; ISS:UniProtKB.
DR GO; GO:0007612; P:learning; ISS:UniProtKB.
DR GO; GO:0007613; P:memory; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0035176; P:social behavior; ISS:UniProtKB.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
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 3D-structure; Acetylation; Disease variant; DNA-binding;
KW Intellectual disability; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..1608
FT /note="Protein capicua homolog"
FT /id="PRO_0000048598"
FT DNA_BIND 200..268
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 28..46
FT /note="Interaction with ATXN1"
FT /evidence="ECO:0000250"
FT REGION 48..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1130..1155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1521..1608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..113
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..522
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..905
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1148
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1255
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1300
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1336..1365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1392..1419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1529..1558
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1571..1608
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q924A2"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 190
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q924A2"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q924A2"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q924A2"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q924A2"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 721
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 863
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 934
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q924A2"
FT MOD_RES 1268
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q924A2"
FT MOD_RES 1291
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q924A2"
FT MOD_RES 1294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336"
FT MOD_RES 1382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 1389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1397
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1398
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 1409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1595
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 104
FT /note="E -> K (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035936"
FT VARIANT 353..1608
FT /note="Missing (in MRD45; decreased protein expression)"
FT /evidence="ECO:0000269|PubMed:28288114"
FT /id="VAR_079294"
FT VARIANT 492..1608
FT /note="Missing (probable disease-associated variant found
FT in a patient with Snijders Blok-Campeau syndrome; the
FT patient also carries a likely pathogenic variation in CHD3;
FT both variants may contribute to disease phenotype)"
FT /evidence="ECO:0000269|PubMed:30397230"
FT /id="VAR_081527"
FT VARIANT 492
FT /note="R -> W (in MRD45; unknown pathological significance;
FT dbSNP:rs373584239)"
FT /evidence="ECO:0000269|PubMed:21076407"
FT /id="VAR_065090"
FT VARIANT 652
FT /note="A -> T (in a breast cancer sample; somatic mutation;
FT dbSNP:rs770323488)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035937"
FT VARIANT 982
FT /note="S -> G (in dbSNP:rs17339472)"
FT /evidence="ECO:0000269|PubMed:12393275,
FT ECO:0000269|PubMed:9205841"
FT /id="VAR_028302"
FT VARIANT 992..1608
FT /note="Missing (in MRD45)"
FT /evidence="ECO:0000269|PubMed:28288114"
FT /id="VAR_079295"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:4J2J"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:4J2J"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:2M41"
FT HELIX 206..221
FT /evidence="ECO:0007829|PDB:6JRP"
FT HELIX 227..239
FT /evidence="ECO:0007829|PDB:6JRP"
FT HELIX 243..263
FT /evidence="ECO:0007829|PDB:6JRP"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:6JRP"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:6KZG"
SQ SEQUENCE 1608 AA; 163820 MW; 355603C8BD67244E CRC64;
MYSAHRPLMP ASSAASRGLG MFVWTNVEPR SVAVFPWHSL VPFLAPSQPD PSVQPSEAQQ
PASHPVASNQ SKEPAESAAV AHERPPGGTG SADPERPPGA TCPESPGPGP PHPLGVVESG
KGPPPTTEEE ASGPPGEPRL DSETESDHDD AFLSIMSPEI QLPLPPGKRR TQSLSALPKE
RDSSSEKDGR SPNKREKDHI RRPMNAFMIF SKRHRALVHQ RHPNQDNRTV SKILGEWWYA
LGPKEKQKYH DLAFQVKEAH FKAHPDWKWC NKDRKKSSSE AKPTSLGLAG GHKETRERSM
SETGTAAAPG VSSELLSVAA QTLLSSDTKA PGSSSCGAER LHTVGGPGSA RPRAFSHSGV
HSLDGGEVDS QALQELTQMV SGPASYSGPK PSTQYGAPGP FAAPGEGGAL AATGRPPLLP
TRASRSQRAA SEDMTSDEER MVICEEEGDD DVIADDGFGT TDIDLKCKER VTDSESGDSS
GEDPEGNKGF GRKVFSPVIR SSFTHCRPPL DPEPPGPPDP PVAFGKGYGS APSSSASSPA
SSSASAATSF SLGSGTFKAQ ESGQGSTAGP LRPPPPGAGG PATPSKATRF LPMDPATFRR
KRPESVGGLE PPGPSVIAAP PSGGGNILQT LVLPPNKEEQ EGGGARVPSA PAPSLAYGAP
AAPLSRPAAT MVTNVVRPVS STPVPIASKP FPTSGRAEAS PNDTAGARTE MGTGSRVPGG
SPLGVSLVYS DKKSAAATSP APHLVAGPLL GTVGKAPATV TNLLVGTPGY GAPAPPAVQF
IAQGAPGGGT TAGSGAGAGS GPNGPVPLGI LQPGALGKAG GITQVQYILP TLPQQLQVAP
APAPAPGTKA AAPSGPAPTT SIRFTLPPGT STNGKVLAAT APTPGIPILQ SVPSAPPPKA
QSVSPVQAPP PGGSAQLLPG KVLVPLAAPS MSVRGGGAGQ PLPLVSPPFS VPVQNGAQPP
SKIIQLTPVP VSTPSGLVPP LSPATLPGPT SQPQKVLLPS STRITYVQSA GGHALPLGTS
PASSQAGTVT SYGPTSSVAL GFTSLGPSGP AFVQPLLSAG QAPLLAPGQV GVSPVPSPQL
PPACAAPGGP VITAFYSGSP APTSSAPLAQ PSQAPPSLVY TVATSTTPPA ATILPKGPPA
PATATPAPTS PFPSATAGSM TYSLVAPKAQ RPSPKAPQKV KAAIASIPVG SFEAGASGRP
GPAPRQPLEP GPVREPTAPE SELEGQPTPP APPPLPETWT PTARSSPPLP PPAEERTSAK
GPETMASKFP SSSSDWRVPG QGLENRGEPP TPPSPAPAPA VAPGGSSESS SGRAAGDTPE
RKEAAGTGKK VKVRPPPLKK TFDSVDNRVL SEVDFEERFA ELPEFRPEEV LPSPTLQSLA
TSPRAILGSY RKKRKNSTDL DSAPEDPTSP KRKMRRRSSC SSEPNTPKSA KCEGDIFTFD
RTGTEAEDVL GELEYDKVPY SSLRRTLDQR RALVMQLFQD HGFFPSAQAT AAFQARYADI
FPSKVCLQLK IREVRQKIMQ AATPTEQPPG AEAPLPVPPP TGTAAAPAPT PSPAGGPDPT
SPSSDSGTAQ AAPPLPPPPE SGPGQPGWEG APQPSPPPPG PSTAATGR
