Protein:CECR2 |
Protein Summary |
 Gene summary |
| Gene name: CECR2 | ASpdb.0 ID: 27443 | Gene | Gene symbol | CECR2 | Gene ID | 27443 |
| Gene name | CECR2 histone acetyl-lysine reader |
| Synonyms | - |
| Cytomap | 22q11.1-q11.21 |
| Type of gene | protein-coding |
| Description | chromatin remodeling regulator CECR2cat eye syndrome chromosome region, candidate 2cat eye syndrome critical region protein 2 |
| Modification date | 20240403 |
| UniProtAcc | Q9BXF3 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | CECR2 | GO:0005634 | nucleus | 12762840|25593309 |
| Gene | CECR2 | GO:0006338 | chromatin remodeling | 15640247 |
| Gene | CECR2 | GO:0090537 | CERF complex | 15640247 |
| Gene | CECR2 | GO:0097194 | execution phase of apoptosis | 12762840 |
| Gene | CECR2 | GO:0140658 | ATP-dependent chromatin remodeler activity | 15640247 |
AS Summary |
| Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| Q9BXF3-1 | Q9BXF3-1_5v84_A.pdb | 5V84 | X-ray | 2.7 | A | 437 | 538 |
| ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| Q9BXF3 | CECR2 | Q9BXF3-1 | Q9BXF3-2 | 1484 | 498 | 291 | 318 | Deletion | none | none | 290 | 290 |
| Q9BXF3 | CECR2 | Q9BXF3-1 | Q9BXF3-2 | 1484 | 498 | 519 | 526 | Substitution | EYTKMSDN | GKQGRSLC | 491 | 498 |
| Q9BXF3 | CECR2 | Q9BXF3-1 | Q9BXF3-2 | 1484 | 498 | 527 | 1484 | Deletion | none | none | 498 | 498 |
| Multiple sequence alignment of our canonical and alternatively spliced CECR2 |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of CECR2 |
| UniProt-id | ENSG | ENST | ENSP |
| Q9BXF3-1 | ENSG00000099954.19 | ENST00000342247.10 | ENSP00000341219.6 |
| UniProt-id | NM ID | NP ID |
| Amino acid sequences of our canonical and alternatively spliced CECR2 |
| accession_id | Protein sequence |
| Q9BXF3-1 | MCPEEGGAAGLGELRSWWEVPAIAHFCSLFRTAFRLPDFEIEELEAALHRDDVEFISDLIACLLQGCYQRRDITPQTFHSYLEDIINYRW ELEEGKPNPLREASFQDLPLRTRVEILHRLCDYRLDADDVFDLLKGLDADSLRVEPLGEDNSGALYWYFYGTRMYKEDPVQGKSNGELSL SRESEGQKNVSSIPGKTGKRRGRPPKRKKLQEEILLSEKQEENSLASEPQTRHGSQGPGQGTWWLLCQTEEEWRQVTESFRERTSLRERQ LYKLLSEDFLPEICNMIAQKGKRPQRTKAELHPRWMSDHLSIKPVKQEETPVLTRIEKQKRKEEEEERQILLAVQKKEQEQMLKEERKRE LEEKVKAVEGMCSVRVVWRGACLSTSRPVDRAKRRKLREERAWLLAQGKELPPELSHLDPNSPMREEKKTKDLFELDDDFTAMYKVLDVV KAHKDSWPFLEPVDESYAPNYYQIIKAPMDISSMEKKLNGGLYCTKEEFVNDMKTMFRNCRKYNGESSEYTKMSDNLERCFHRAMMKHFP GEDGDTDEEFWIREDEKREKRRSRAGRSGGSHVWTRSRDPEGSSRKQQPMENGGKSLPPTRRAPSSGDDQSSSSTQPPREVGTSNGRGFS HPLHCGGTPSQAPFLNQMRPAVPGTFGPLRGSDPATLYGSSGVPEPHPGEPVQQRQPFTMQPPVGINSLRGPRLGTPEEKQMCGGLTHLS NMGPHPGSLQLGQISGPSQDGSMYAPAQFQPGFIPPRHGGAPARPPDFPESSEIPPSHMYRSYKYLNRVHSAVWNGNHGATNQGPLGPDE KPHLGPGPSHQPRTLGHVMDSRVMRPPVPPNQWTEQSGFLPHGVPSSGYMRPPCKSAGHRLQPPPVPAPSSLFGAPAQALRGVQGGDSMM DSPEMIAMQQLSSRVCPPGVPYHPHQPAHPRLPGPFPQVAHPMSVTVSAPKPALGNPGRAPENSEAQEPENDQAEPLPGLEEKPPGVGTS EGVYLTQLPHPTPPLQTDCTRQSSPQERETVGPELKSSSSESADNCKAMKGKNPWPSDSSYPGPAAQGCVRDLSTVADRGALSENGVIGE ASPCGSEGKGLGSSGSEKLLCPRGRTLQETMPCTGQNAATPPSTDPGLTGGTVSQFPPLYMPGLEYPNSAAHYHISPGLQGVGPVMGGKS PASHPQHFPPRGFQSNHPHSGGFPRYRPPQGMRYSYHPPPQPSYHHYQRTPYYACPQSFSDWQRPLHPQGSPSGPPASQPPPPRSLFSDK NAMASLQGCETLNAALTSPTRMDAVAAKVPNDGQNPGPEEEKLDESMERPESPKEFLDLDNHNAATKRQSSLSASEYLYGTPPPLSSGMG FGSSAFPPHSVMLQTGPPYTPQRPASHFQPRAYSSPVAALPPHHPGATQPNGLSQEGPIYRCQEEGLGHFQAVMMEQIGTRSGIRGPFQE |
| Q9BXF3-2 | MCPEEGGAAGLGELRSWWEVPAIAHFCSLFRTAFRLPDFEIEELEAALHRDDVEFISDLIACLLQGCYQRRDITPQTFHSYLEDIINYRW ELEEGKPNPLREASFQDLPLRTRVEILHRLCDYRLDADDVFDLLKGLDADSLRVEPLGEDNSGALYWYFYGTRMYKEDPVQGKSNGELSL SRESEGQKNVSSIPGKTGKRRGRPPKRKKLQEEILLSEKQEENSLASEPQTRHGSQGPGQGTWWLLCQTEEEWRQVTESFRERTSLRERQ LYKLLSEDFLPEICNMIAQKETPVLTRIEKQKRKEEEEERQILLAVQKKEQEQMLKEERKRELEEKVKAVEGMCSVRVVWRGACLSTSRP VDRAKRRKLREERAWLLAQGKELPPELSHLDPNSPMREEKKTKDLFELDDDFTAMYKVLDVVKAHKDSWPFLEPVDESYAPNYYQIIKAP |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| CECR2 (go to UniProt):Q9BXF3 |
| Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Q9BXF3 | Domain | 451 | 521 | Note=Bromo;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035 | Type=Substitution;Start=519;End=526 |
| Q9BXF3 | Region | 556 | 704 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=527;End=1484 |
| Q9BXF3 | Region | 796 | 825 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=527;End=1484 |
| Q9BXF3 | Region | 919 | 1053 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=527;End=1484 |
| Q9BXF3 | Region | 1165 | 1259 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=527;End=1484 |
| Q9BXF3 | Region | 1287 | 1320 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=527;End=1484 |
| Q9BXF3 | Region | 1442 | 1484 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=527;End=1484 |
| Q9BXF3 | Compositional bias | 603 | 623 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=527;End=1484 |
| Q9BXF3 | Compositional bias | 920 | 937 | Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=527;End=1484 |
| Q9BXF3 | Compositional bias | 1000 | 1036 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=527;End=1484 |
| Q9BXF3 | Compositional bias | 1223 | 1237 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=527;End=1484 |
| Q9BXF3 | Compositional bias | 1239 | 1253 | Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=527;End=1484 |
| Q9BXF3 | Compositional bias | 1295 | 1320 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=527;End=1484 |
| Q9BXF3 | Compositional bias | 1448 | 1468 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=527;End=1484 |
Gene Isoform Structures and Expression Levels for CECR2 |
| Gene structures of our canonical and alternative spliced genes of CECR2 * Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
| Expression levels of gene isoforms across GTEx. |
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| Expression levels of gene isoforms across TCGA. |
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Protein Structures |
| PDB and CIF files of the predicted protein structures * Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format. |
| 3D view using mol* of Q9BXF3-1 |
| 3D view using mol* of Q9BXF3-2 |
pLDDT Score Distribution |
| pLDDT score distribution of the predicted protein structures from AlphaFold2 * AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
| pLDDT distribution across the protein length of Q9BXF3-1 |
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| pLDDT distribution across the protein length of Q9BXF3-2 |
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Ramachandran Plot of Protein Structures |
| Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide. |
| Ramachandran plot of Q9BXF3-1 |
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| Ramachandran plot of Q9BXF3-2 |
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Potential Active Site Information |
| The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| Q9BXF3-1 | 1.069 | 126 | 1.088 | 266.854 | 0.455 | 0.788 | 1.128 | 1.171 | 0.997 | 1.174 | 0.96 | 27,28,31,37,38,39,40,41,42,158,160,161,162,279,282 ,283,286,289,290,292,293,296,902,903,904,905,907,9 08,911 |
| Q9BXF3-2 | 1.084 | 108 | 1.137 | 238.728 | 0.4 | 0.744 | 1.02 | 1.286 | 0.766 | 1.678 | 0.572 | 429,430,431,432,433,434,435,436,439,440,443,444,45 0,451,452,478,481,482,485,486,497 |
Protein Structure and Feature Comparision |
| Protein Structure Comparision Using Template Modeling Scores (TM-score). |
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| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green) |
| 3D view using mol* of Q9BXF3-1_Q9BXF3-1_5v84_A.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q9BXF3-1_5v84_A_Q9BXF3-2.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q9BXF3-1_Q9BXF3-2.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/Q9BXF3-1_vs_Q9BXF3-2.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/Q9BXF3-1_vs_Q9BXF3-2.png |
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Protein-Protein Interaction |
| Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to CECR2 |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
Related Diseases to CECR2 |
| Previous studies relating to the alternative splicing of CECR2 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| CECR2 | 15640247 | CECR2, a protein involved in neurulation, forms a novel chromatin remodeling complex with SNF2L. | Chromatin remodeling complexes play critical roles in development. Here we describe a transcription factor, CECR2, which is involved in neurulation and chromatin remodeling. CECR2 shows complex alternative splicing, but all variants contain DDT and bromodomain motifs. A mutant mouse line was generated from an embryonic stem cell line containing a genetrap within Cecr2. Reporter gene expression demonstrated Cecr2 expression to be predominantly neural in the embryo. Mice homozygous for the Cecr2 genetrap-induced mutation show a high penetrance of the neural tube defect exencephaly, the human equivalent of anencephaly, in a strain-dependent fashion. Biochemical isolation of CECR2 revealed the presence of this protein as a component of a novel heterodimeric complex termed CECR2-containing remodeling factor (CERF). CERF comprises CECR2 and the ATP-dependent chromatin remodeler SNF2L, a mammalian ISWI ortholog expressed predominantly in the central nervous system. CERF is capable of remodeling chromatin in vitro and displays an ATP hydrolyzing activity that is stimulated by nucleosomes. Together, these data identify a novel chromatin remodeling complex with a critical role in neurulation. | D009436 | Neural Tube Defects |
Clinically important variants in CECR2 |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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