CECR2_HUMAN
ID CECR2_HUMAN Reviewed; 1484 AA.
AC Q9BXF3; A8MS90; A8MX16; Q658Z4; Q96P58; Q9C0C3;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Chromatin remodeling regulator CECR2 {ECO:0000305};
DE AltName: Full=Cat eye syndrome critical region protein 2;
GN Name=CECR2; Synonyms=KIAA1740;
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] (ISOFORM A), AND VARIANT LEU-674.
RX PubMed=11381032; DOI=10.1101/gr.154901;
RA Footz T.K., Brinkman-Mills P., Banting G.S., Maier S.A., Riazi M.A.,
RA Bridgland L.J., Hu S., Birren B., Minoshima S., Shimizu N., Pan H.,
RA Nguyen T., Fang F., Fu Y., Ray L., Wu H., Shaull S., Phan S., Yao Z.,
RA Chen F., Huan A., Hu P., Wang Q., Loh P., Qi S., Roe B.A., McDermid H.E.;
RT "Analysis of the cat eye syndrome critical region in humans and the region
RT of conserved synteny in mice: a search for candidate genes at or near the
RT human chromosome 22 pericentromere.";
RL Genome Res. 11:1053-1070(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-1484 (ISOFORM C).
RC TISSUE=Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 346-1484 (ISOFORM C), AND VARIANT
RP LEU-674.
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 168-1484 (ISOFORM B), FUNCTION, AND
RP INTERACTION WITH LRPPRC.
RC TISSUE=Liver;
RX PubMed=11827465; DOI=10.1006/geno.2001.6679;
RA Liu L., McKeehan W.L.;
RT "Sequence analysis of LRPPRC and its SEC1 domain interaction partners
RT suggests roles in cytoskeletal organization, vesicular trafficking,
RT nucleocytosolic shuttling, and chromosome activity.";
RL Genomics 79:124-136(2002).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE CERF COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15640247; DOI=10.1093/hmg/ddi048;
RA Banting G.S., Barak O., Ames T.M., Burnham A.C., Kardel M.D., Cooch N.S.,
RA Davidson C.E., Godbout R., McDermid H.E., Shiekhattar R.;
RT "CECR2, a protein involved in neurulation, forms a novel chromatin
RT remodeling complex with SNF2L.";
RL Hum. Mol. Genet. 14:513-524(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422; THR-546; SER-571;
RP SER-1014 AND SER-1312, METHYLATION AT ARG-1197 AND ARG-1203, AND
RP IDENTIFICATION BY 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 [9]
RP FUNCTION, AND DOMAIN.
RX PubMed=26365797; DOI=10.1016/j.str.2015.08.004;
RA Flynn E.M., Huang O.W., Poy F., Oppikofer M., Bellon S.F., Tang Y.,
RA Cochran A.G.;
RT "A subset of human bromodomains recognizes butyryllysine and crotonyllysine
RT histone peptide modifications.";
RL Structure 23:1801-1814(2015).
RN [10]
RP FUNCTION, IDENTIFICATION IN THE CERF-1 ISWI CHROMATIN REMODELING COMPLEX,
RP IDENTIFICATION IN THE CERF-5 CHROMATIN REMODELING COMPLEX, AND INTERACTION
RP WITH SMARCA1 AND SMARCA5.
RX PubMed=28801535; DOI=10.15252/embr.201744011;
RA Oppikofer M., Bai T., Gan Y., Haley B., Liu P., Sandoval W., Ciferri C.,
RA Cochran A.G.;
RT "Expansion of the ISWI chromatin remodeler family with new active
RT complexes.";
RL EMBO Rep. 18:1697-1706(2017).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 424-538, FUNCTION, DOMAIN, AND
RP SUBUNIT.
RX PubMed=22464331; DOI=10.1016/j.cell.2012.02.013;
RA Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P.,
RA Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T.,
RA Gingras A.C., Arrowsmith C.H., Knapp S.;
RT "Histone recognition and large-scale structural analysis of the human
RT bromodomain family.";
RL Cell 149:214-231(2012).
CC -!- FUNCTION: Regulatory subunit of the ATP-dependent CERF-1 and CERF-5
CC ISWI chromatin remodeling complexes, which form ordered nucleosome
CC arrays on chromatin and facilitate access to DNA during DNA-templated
CC processes such as DNA replication, transcription, and repair
CC (PubMed:15640247, PubMed:26365797, PubMed:28801535, PubMed:22464331).
CC The complexes do not have the ability to slide mononucleosomes to the
CC center of a DNA template (PubMed:28801535). The CERF-1 ISWI chromatin
CC remodeling complex has a lower ATP hydrolysis rate than the CERF-5 ISWI
CC chromatin remodeling complex (PubMed:28801535). Plays a role in various
CC processes during development: required during embryogenesis for neural
CC tube closure and inner ear development. In adults, required for
CC spermatogenesis, via the formation of ISWI-type chromatin complexes (By
CC similarity). In histone-modifying complexes, CECR2 recognizes and binds
CC acylated histones: binds histones that are acetylated and/or
CC butyrylated (PubMed:26365797, PubMed:22464331). May also be involved
CC through its interaction with LRPPRC in the integration of cytoskeletal
CC network with vesicular trafficking, nucleocytosolic shuttling,
CC transcription, chromosome remodeling and cytokinesis (PubMed:11827465).
CC {ECO:0000250|UniProtKB:E9Q2Z1, ECO:0000269|PubMed:11827465,
CC ECO:0000269|PubMed:15640247, ECO:0000269|PubMed:22464331,
CC ECO:0000269|PubMed:26365797, ECO:0000269|PubMed:28801535}.
CC -!- SUBUNIT: Component of the CERF-1 ISWI chromatin remodeling complex
CC (also called the CECR2-containing remodeling factor (CERF) complex) at
CC least composed of CECR2 and SMARCA1 (PubMed:15640247, PubMed:28801535).
CC Component of the CERF-5 ISWI chromatin remodeling complex at least
CC composed of SMARCA5/SNF2H and CECR2 (PubMed:28801535). Within the CERF-
CC 1 and CERF-5 ISWI chromatin remodeling complexes interacts with SMARCA1
CC and SMARCA5/SNF2H, respectively (PubMed:28801535). Interacts with
CC acetylated lysine residues on histone H2A and H3 (in vitro)
CC (PubMed:26365797, PubMed:22464331). Interacts with LRPPRC
CC (PubMed:11827465). {ECO:0000269|PubMed:11827465,
CC ECO:0000269|PubMed:15640247, ECO:0000269|PubMed:22464331,
CC ECO:0000269|PubMed:26365797, ECO:0000269|PubMed:28801535}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A;
CC IsoId=Q9BXF3-1; Sequence=Displayed;
CC Name=B; Synonyms=CECR2B;
CC IsoId=Q9BXF3-2; Sequence=VSP_000571, VSP_000572, VSP_000573;
CC Name=C;
CC IsoId=Q9BXF3-3; Sequence=VSP_020407;
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle, thymus,
CC placenta and lung. Expressed at lower level in brain, heart, colon,
CC spleen, kidney.
CC -!- DOMAIN: The Bromo domain recognizes and binds acetylated histones
CC (PubMed:22464331). Also recognizes and binds histones that are
CC butyrylated (PubMed:26365797). {ECO:0000269|PubMed:22464331,
CC ECO:0000269|PubMed:26365797}.
CC -!- MISCELLANEOUS: Candidate gene for the Cat Eye Syndrome (CES), a
CC developmental disorder associated with the duplication of a 2 Mb region
CC of 22q11.2. Duplication usually takes in the form of a surpernumerary
CC bisatellited isodicentric chromosome, resulting in four copies of the
CC region (represents an inv dup(22)(q11)). CES is characterized
CC clinically by the combination of coloboma of the iris and anal atresia
CC with fistula, downslanting palpebral fissures, preauricular tags and/or
CC pits, frequent occurrence of heart and renal malformations, and normal
CC or near-normal mental development. {ECO:0000305|PubMed:11381032}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH56122.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAH56212.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAW57756.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF336133; AAK15343.1; -; mRNA.
DR EMBL; AC004019; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471193; EAW57756.1; ALT_INIT; Genomic_DNA.
DR EMBL; BX647449; CAH56122.1; ALT_INIT; mRNA.
DR EMBL; AL832377; CAH56212.1; ALT_INIT; mRNA.
DR EMBL; AB051527; BAB21831.1; -; mRNA.
DR EMBL; AF411609; AAL07393.1; -; mRNA.
DR RefSeq; NP_001276975.1; NM_001290046.1.
DR RefSeq; NP_001276976.1; NM_001290047.1. [Q9BXF3-3]
DR PDB; 3NXB; X-ray; 1.83 A; A/B=424-538.
DR PDB; 5V84; X-ray; 2.70 A; A/B/C/D=424-538.
DR PDBsum; 3NXB; -.
DR PDBsum; 5V84; -.
DR AlphaFoldDB; Q9BXF3; -.
DR SMR; Q9BXF3; -.
DR BioGRID; 118176; 39.
DR ComplexPortal; CPX-446; CERF chromatin remodelling complex.
DR CORUM; Q9BXF3; -.
DR IntAct; Q9BXF3; 5.
DR STRING; 9606.ENSP00000341219; -.
DR BindingDB; Q9BXF3; -.
DR ChEMBL; CHEMBL3108639; -.
DR GuidetoPHARMACOLOGY; 2733; -.
DR iPTMnet; Q9BXF3; -.
DR PhosphoSitePlus; Q9BXF3; -.
DR BioMuta; CECR2; -.
DR DMDM; 114152782; -.
DR EPD; Q9BXF3; -.
DR jPOST; Q9BXF3; -.
DR MassIVE; Q9BXF3; -.
DR PaxDb; Q9BXF3; -.
DR PeptideAtlas; Q9BXF3; -.
DR PRIDE; Q9BXF3; -.
DR ProteomicsDB; 79417; -. [Q9BXF3-1]
DR ProteomicsDB; 79418; -. [Q9BXF3-2]
DR ProteomicsDB; 79419; -. [Q9BXF3-3]
DR ABCD; Q9BXF3; 1 sequenced antibody.
DR Antibodypedia; 283; 66 antibodies from 22 providers.
DR DNASU; 27443; -.
DR Ensembl; ENST00000262608.13; ENSP00000262608.11; ENSG00000099954.19. [Q9BXF3-3]
DR Ensembl; ENST00000342247.10; ENSP00000341219.6; ENSG00000099954.19. [Q9BXF3-1]
DR GeneID; 27443; -.
DR KEGG; hsa:27443; -.
DR MANE-Select; ENST00000262608.13; ENSP00000262608.11; NM_001290047.2; NP_001276976.1. [Q9BXF3-3]
DR UCSC; uc062bgi.1; human. [Q9BXF3-1]
DR CTD; 27443; -.
DR DisGeNET; 27443; -.
DR GeneCards; CECR2; -.
DR HGNC; HGNC:1840; CECR2.
DR HPA; ENSG00000099954; Tissue enhanced (brain, retina, skeletal muscle).
DR MIM; 607576; gene.
DR neXtProt; NX_Q9BXF3; -.
DR OpenTargets; ENSG00000099954; -.
DR PharmGKB; PA26383; -.
DR VEuPathDB; HostDB:ENSG00000099954; -.
DR eggNOG; KOG1472; Eukaryota.
DR GeneTree; ENSGT00940000160360; -.
DR InParanoid; Q9BXF3; -.
DR OrthoDB; 379050at2759; -.
DR PhylomeDB; Q9BXF3; -.
DR TreeFam; TF324727; -.
DR PathwayCommons; Q9BXF3; -.
DR SignaLink; Q9BXF3; -.
DR SIGNOR; Q9BXF3; -.
DR BioGRID-ORCS; 27443; 17 hits in 334 CRISPR screens.
DR ChiTaRS; CECR2; human.
DR EvolutionaryTrace; Q9BXF3; -.
DR GenomeRNAi; 27443; -.
DR Pharos; Q9BXF3; Tchem.
DR PRO; PR:Q9BXF3; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9BXF3; protein.
DR Bgee; ENSG00000099954; Expressed in tibialis anterior and 146 other tissues.
DR ExpressionAtlas; Q9BXF3; baseline and differential.
DR Genevisible; Q9BXF3; HS.
DR GO; GO:0090537; C:CERF complex; IDA:MGI.
DR GO; GO:0000791; C:euchromatin; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IDA:MGI.
DR GO; GO:0006309; P:apoptotic DNA fragmentation; TAS:HGNC-UCL.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0090102; P:cochlea development; IEA:Ensembl.
DR GO; GO:0007010; P:cytoskeleton organization; NAS:UniProtKB.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; NAS:UniProtKB.
DR GO; GO:0097194; P:execution phase of apoptosis; IDA:BHF-UCL.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IEA:Ensembl.
DR GO; GO:0001842; P:neural fold formation; IEA:Ensembl.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:0007338; P:single fertilization; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; NAS:UniProtKB.
DR Gene3D; 1.20.920.10; -; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR029614; CECR2.
DR PANTHER; PTHR47092; PTHR47092; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Bromodomain; Chromatin regulator;
KW Methylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..1484
FT /note="Chromatin remodeling regulator CECR2"
FT /id="PRO_0000211192"
FT DOMAIN 451..521
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 170..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1287..1320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1442..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..937
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1253
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1448..1468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 546
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1014
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1197
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:E9Q2Z1"
FT MOD_RES 1203
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:E9Q2Z1"
FT MOD_RES 1312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 291..318
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:11827465"
FT /id="VSP_000571"
FT VAR_SEQ 370..389
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:11214970,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_020407"
FT VAR_SEQ 519..526
FT /note="EYTKMSDN -> GKQGRSLC (in isoform B)"
FT /evidence="ECO:0000303|PubMed:11827465"
FT /id="VSP_000572"
FT VAR_SEQ 527..1484
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:11827465"
FT /id="VSP_000573"
FT VARIANT 293
FT /note="R -> H (in dbSNP:rs5747211)"
FT /id="VAR_027411"
FT VARIANT 674
FT /note="P -> L (in dbSNP:rs1296794)"
FT /evidence="ECO:0000269|PubMed:11214970,
FT ECO:0000269|PubMed:11381032"
FT /id="VAR_027412"
FT CONFLICT 352
FT /note="M -> I (in Ref. 4; CAH56122/CAH56212)"
FT /evidence="ECO:0000305"
FT CONFLICT 1029
FT /note="S -> C (in Ref. 1; AAK15343)"
FT /evidence="ECO:0000305"
FT CONFLICT 1045
FT /note="W -> R (in Ref. 1; AAK15343)"
FT /evidence="ECO:0000305"
FT CONFLICT 1441
FT /note="M -> T (in Ref. 4; CAH56122/CAH56212)"
FT /evidence="ECO:0000305"
FT HELIX 439..452
FT /evidence="ECO:0007829|PDB:3NXB"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:3NXB"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:5V84"
FT TURN 465..467
FT /evidence="ECO:0007829|PDB:3NXB"
FT HELIX 471..474
FT /evidence="ECO:0007829|PDB:3NXB"
FT HELIX 481..489
FT /evidence="ECO:0007829|PDB:3NXB"
FT HELIX 496..514
FT /evidence="ECO:0007829|PDB:3NXB"
FT HELIX 519..536
FT /evidence="ECO:0007829|PDB:3NXB"
SQ SEQUENCE 1484 AA; 164213 MW; 8680DB16A0B90D0D CRC64;
MCPEEGGAAG LGELRSWWEV PAIAHFCSLF RTAFRLPDFE IEELEAALHR DDVEFISDLI
ACLLQGCYQR RDITPQTFHS YLEDIINYRW ELEEGKPNPL REASFQDLPL RTRVEILHRL
CDYRLDADDV FDLLKGLDAD SLRVEPLGED NSGALYWYFY GTRMYKEDPV QGKSNGELSL
SRESEGQKNV SSIPGKTGKR RGRPPKRKKL QEEILLSEKQ EENSLASEPQ TRHGSQGPGQ
GTWWLLCQTE EEWRQVTESF RERTSLRERQ LYKLLSEDFL PEICNMIAQK GKRPQRTKAE
LHPRWMSDHL SIKPVKQEET PVLTRIEKQK RKEEEEERQI LLAVQKKEQE QMLKEERKRE
LEEKVKAVEG MCSVRVVWRG ACLSTSRPVD RAKRRKLREE RAWLLAQGKE LPPELSHLDP
NSPMREEKKT KDLFELDDDF TAMYKVLDVV KAHKDSWPFL EPVDESYAPN YYQIIKAPMD
ISSMEKKLNG GLYCTKEEFV NDMKTMFRNC RKYNGESSEY TKMSDNLERC FHRAMMKHFP
GEDGDTDEEF WIREDEKREK RRSRAGRSGG SHVWTRSRDP EGSSRKQQPM ENGGKSLPPT
RRAPSSGDDQ SSSSTQPPRE VGTSNGRGFS HPLHCGGTPS QAPFLNQMRP AVPGTFGPLR
GSDPATLYGS SGVPEPHPGE PVQQRQPFTM QPPVGINSLR GPRLGTPEEK QMCGGLTHLS
NMGPHPGSLQ LGQISGPSQD GSMYAPAQFQ PGFIPPRHGG APARPPDFPE SSEIPPSHMY
RSYKYLNRVH SAVWNGNHGA TNQGPLGPDE KPHLGPGPSH QPRTLGHVMD SRVMRPPVPP
NQWTEQSGFL PHGVPSSGYM RPPCKSAGHR LQPPPVPAPS SLFGAPAQAL RGVQGGDSMM
DSPEMIAMQQ LSSRVCPPGV PYHPHQPAHP RLPGPFPQVA HPMSVTVSAP KPALGNPGRA
PENSEAQEPE NDQAEPLPGL EEKPPGVGTS EGVYLTQLPH PTPPLQTDCT RQSSPQERET
VGPELKSSSS ESADNCKAMK GKNPWPSDSS YPGPAAQGCV RDLSTVADRG ALSENGVIGE
ASPCGSEGKG LGSSGSEKLL CPRGRTLQET MPCTGQNAAT PPSTDPGLTG GTVSQFPPLY
MPGLEYPNSA AHYHISPGLQ GVGPVMGGKS PASHPQHFPP RGFQSNHPHS GGFPRYRPPQ
GMRYSYHPPP QPSYHHYQRT PYYACPQSFS DWQRPLHPQG SPSGPPASQP PPPRSLFSDK
NAMASLQGCE TLNAALTSPT RMDAVAAKVP NDGQNPGPEE EKLDESMERP ESPKEFLDLD
NHNAATKRQS SLSASEYLYG TPPPLSSGMG FGSSAFPPHS VMLQTGPPYT PQRPASHFQP
RAYSSPVAAL PPHHPGATQP NGLSQEGPIY RCQEEGLGHF QAVMMEQIGT RSGIRGPFQE
MYRPSGMQMH PVQSQASFPK TPTAATSQEE VPPHKPPTLP LDQS
