E9Q2Z1 · CECR2_MOUSE
- ProteinChromatin remodeling regulator CECR2
- GeneCecr2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1453 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Regulatory subunit of the ATP-dependent CERF-1 and CERF-5 ISWI chromatin remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (By similarity).
The complexes do not have the ability to slide mononucleosomes to the center of a DNA template (By similarity).
The CERF-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the CERF-5 ISWI chromatin remodeling complex (By similarity).
Plays a role in various processes during development: required during embryogenesis for neural tube closure and inner ear development (PubMed:15640247, PubMed:20589882, PubMed:21246654).
In adults, required for spermatogenesis, via the formation of ISWI-type chromatin complexes (PubMed:22154806).
In histone-modifying complexes, CECR2 recognizes and binds acylated histones: binds histones that are acetylated and/or butyrylated (By similarity).
May also be involved through its interaction with LRPPRC in the integration of cytoskeletal network with vesicular trafficking, nucleocytosolic shuttling, transcription, chromosome remodeling and cytokinesis (By similarity).
The complexes do not have the ability to slide mononucleosomes to the center of a DNA template (By similarity).
The CERF-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the CERF-5 ISWI chromatin remodeling complex (By similarity).
Plays a role in various processes during development: required during embryogenesis for neural tube closure and inner ear development (PubMed:15640247, PubMed:20589882, PubMed:21246654).
In adults, required for spermatogenesis, via the formation of ISWI-type chromatin complexes (PubMed:22154806).
In histone-modifying complexes, CECR2 recognizes and binds acylated histones: binds histones that are acetylated and/or butyrylated (By similarity).
May also be involved through its interaction with LRPPRC in the integration of cytoskeletal network with vesicular trafficking, nucleocytosolic shuttling, transcription, chromosome remodeling and cytokinesis (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | CERF complex | |
Cellular Component | euchromatin | |
Cellular Component | ISWI-type complex | |
Molecular Function | ATP-dependent chromatin remodeler activity | |
Biological Process | chromatin remodeling | |
Biological Process | cochlea development | |
Biological Process | execution phase of apoptosis | |
Biological Process | inner ear receptor cell stereocilium organization | |
Biological Process | neural fold formation | |
Biological Process | neural tube closure | |
Biological Process | neural tube development | |
Biological Process | single fertilization |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameChromatin remodeling regulator CECR2
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionE9Q2Z1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Perinatal death with high penetrance due to cranial neural tube defects (PubMed:15640247, PubMed:20589882).
Exencephaly is frequently associated by open eyelids (PubMed:20589882).
Defects may be due to misregulation of mesenchymal/ectodermal transcription factors (PubMed:20589882).
Fetuses also show specific inner ear defects, such as smaller cochleae as well as rotational defects of sensory cells and extra cell rows in the inner ear reminiscent of planar cell polarity (PCP) mutants (PubMed:21246654).
Mutant males non-penetrant for neural tube defects produce smaller litters: mutants have normal seminiferous epithelium morphology, sperm count, motility and morphology, but the mutant spermatozoa are compromised in their ability to fertilize oocytes (PubMed:22154806).
Exencephaly is frequently associated by open eyelids (PubMed:20589882).
Defects may be due to misregulation of mesenchymal/ectodermal transcription factors (PubMed:20589882).
Fetuses also show specific inner ear defects, such as smaller cochleae as well as rotational defects of sensory cells and extra cell rows in the inner ear reminiscent of planar cell polarity (PCP) mutants (PubMed:21246654).
Mutant males non-penetrant for neural tube defects produce smaller litters: mutants have normal seminiferous epithelium morphology, sperm count, motility and morphology, but the mutant spermatozoa are compromised in their ability to fertilize oocytes (PubMed:22154806).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 90 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000441775 | 1-1453 | Chromatin remodeling regulator CECR2 | |||
Sequence: MCPEEGGAAGLGELRSWWEVPAIAHFCSLFRTAFRLPDFEIEELEAALHRDDVEFISDLIACLLQGCYQRRDITPQTFHSYLEDIINYRWELEEGKPNPLREASFQDLPLRTRVEILHRLCDYRLDADDVFDLLKGLDADSLRVEPLGEDNSGALYWYFYGTRMYKEDPVQGRSNGELSLCRESERQKNVSNVPGKTGKRRGRPPKRKKLQEEIISSEKQEENSLTSDLQTRNGSRGPGQGTWWLLCQTEEEWRQVTESFRERTSLRERQLYKLLSEDFLPEICNMIAQKGKRPQRTKPELQHRFMSDHLSIKSIKLEETPMLTKIEKQKRREEEEERQLLLAVQKKEQEQMLKEERKREMEEKVKAVEDRAKRRKLREERAWLLAQGKELPPELSHLDLNSPMREGKKTKDLFELDDDFTAMYKVLDVVKAHKDSWPFLEPVDESYAPNYYQIIKIPMDISSMEKKLNGGLYCNKEEFVNDMKTMFRNCRKYNGDSSEYTKMSDNLERCFHRAMTKHFPGEDGDTDEEFWIKEDEKREKRRSRSGRSSGSHVWTRSRDTEGSSRKQPPVENGGKSLPPARRAASSGDDQSRSSIQLPPEVGTSHGQGFSRPLHCGRVPSHAPPLNQMRPAAPGTFGSLQGSDPTNLHGSSRIPEAPPGEPLQHPPFAIQAPVGISNHRGSLLSAPDLSNMGSHVPSLQLGQMNCPSQDGNMYPPAPFQAGFIPSRHGGTPARPPDFPESSEIPPGHIYHSYKYLNRAHPAVWNGNHGTTNPGRLGPDEKPHLGPGPSHHPHTLGHMMDGRVMRQPIPPNQWTKQSSFLPHGVPSSGYMQPPCKSAGHRLQPPPTPAPSPRFRGPSQALRGAQGGESMMDSPEMIAMQQLSSRVCPPGVPYHPRQPTPPQLPGPFPQVAHSASVCVSAPKPALDNPGSTQEMTETHEPEEDPAEPLPGHEEKAASICSSEGVYLKQLPHPAPPLQASCTRQSSPQERETEDSQLKSDASDSADTYKTSKNKNTWPLDNSYSSPAVQGCLRDLSIVAETGNLPENGVVGEASPCRSEGKGLDGSGSEKPLCPRGKTLQEAVPCTGPNATTPPCTDPSLMAATVNQFSPLYMPGIEYSNSATQYPMSPSLQGLASMMGGKSSGSQPQSFPPRGFQANGPHPGLFPRYRPQQGMRYSYQPPSQPSYHPYQRTPYYTCPQGFSDWQRSLPSQRSPSGPPGSHPPRSLFSEKNVLSSLQGCETLNTALTSPTQMDVVTAKVVPPDGHNSGPEEEKMDESVERPESPKEFLDLDNHNAATKRQNSLSTSDYLYGTPPPSLSSGMTFGSSAFPPHSVMLQTGSPYTPQRSASHFQPRAYPSPVPAHPPPHPVATQPNGLSPEDSLYCCQEEGLGHFQASMMEQTGTGSGLRGSFQEVHRPPGLQMHPVQSQSLFPKTPAPAASPEQLPPHKTPTLPLDQS | ||||||
Modified residue | 402 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 526 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 551 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 983 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1166 | Asymmetric dimethylarginine | ||||
Sequence: R | ||||||
Modified residue | 1172 | Asymmetric dimethylarginine | ||||
Sequence: R | ||||||
Modified residue | 1280 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Component of the CERF-1 ISWI chromatin remodeling complex (also called the CECR2-containing remodeling factor (CERF) complex) at least composed of CECR2 and SMARCA1 (By similarity).
Component of the CERF-5 ISWI chromatin remodeling complex at least composed of SMARCA5/SNF2H and CECR2 (By similarity).
Within the CERF-1 and CERF-5 ISWI chromatin remodeling complexes interacts with SMARCA1 and SMARCA5/SNF2H, respectively (By similarity).
Interacts with acetylated lysine residues on histone H2A and H3 (in vitro) (By similarity).
Interacts with LRPPRC (By similarity).
Component of the CERF-5 ISWI chromatin remodeling complex at least composed of SMARCA5/SNF2H and CECR2 (By similarity).
Within the CERF-1 and CERF-5 ISWI chromatin remodeling complexes interacts with SMARCA1 and SMARCA5/SNF2H, respectively (By similarity).
Interacts with acetylated lysine residues on histone H2A and H3 (in vitro) (By similarity).
Interacts with LRPPRC (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 170-237 | Disordered | ||||
Sequence: VQGRSNGELSLCRESERQKNVSNVPGKTGKRRGRPPKRKKLQEEIISSEKQEENSLTSDLQTRNGSRG | ||||||
Compositional bias | 220-237 | Polar residues | ||||
Sequence: QEENSLTSDLQTRNGSRG | ||||||
Domain | 431-501 | Bromo | ||||
Sequence: KAHKDSWPFLEPVDESYAPNYYQIIKIPMDISSMEKKLNGGLYCNKEEFVNDMKTMFRNCRKYNGDSSEYT | ||||||
Region | 536-667 | Disordered | ||||
Sequence: EKREKRRSRSGRSSGSHVWTRSRDTEGSSRKQPPVENGGKSLPPARRAASSGDDQSRSSIQLPPEVGTSHGQGFSRPLHCGRVPSHAPPLNQMRPAAPGTFGSLQGSDPTNLHGSSRIPEAPPGEPLQHPPF | ||||||
Compositional bias | 586-603 | Polar residues | ||||
Sequence: SGDDQSRSSIQLPPEVGT | ||||||
Region | 767-796 | Disordered | ||||
Sequence: HGTTNPGRLGPDEKPHLGPGPSHHPHTLGH | ||||||
Region | 827-868 | Disordered | ||||
Sequence: GYMQPPCKSAGHRLQPPPTPAPSPRFRGPSQALRGAQGGESM | ||||||
Compositional bias | 837-851 | Pro residues | ||||
Sequence: GHRLQPPPTPAPSPR | ||||||
Region | 884-1020 | Disordered | ||||
Sequence: VCPPGVPYHPRQPTPPQLPGPFPQVAHSASVCVSAPKPALDNPGSTQEMTETHEPEEDPAEPLPGHEEKAASICSSEGVYLKQLPHPAPPLQASCTRQSSPQERETEDSQLKSDASDSADTYKTSKNKNTWPLDNSY | ||||||
Compositional bias | 889-905 | Pro residues | ||||
Sequence: VPYHPRQPTPPQLPGPF | ||||||
Compositional bias | 933-948 | Basic and acidic residues | ||||
Sequence: TETHEPEEDPAEPLPG | ||||||
Compositional bias | 998-1020 | Polar residues | ||||
Sequence: ASDSADTYKTSKNKNTWPLDNSY | ||||||
Region | 1046-1072 | Disordered | ||||
Sequence: VVGEASPCRSEGKGLDGSGSEKPLCPR | ||||||
Compositional bias | 1131-1150 | Polar residues | ||||
Sequence: LASMMGGKSSGSQPQSFPPR | ||||||
Region | 1131-1308 | Disordered | ||||
Sequence: LASMMGGKSSGSQPQSFPPRGFQANGPHPGLFPRYRPQQGMRYSYQPPSQPSYHPYQRTPYYTCPQGFSDWQRSLPSQRSPSGPPGSHPPRSLFSEKNVLSSLQGCETLNTALTSPTQMDVVTAKVVPPDGHNSGPEEEKMDESVERPESPKEFLDLDNHNAATKRQNSLSTSDYLYG | ||||||
Compositional bias | 1172-1211 | Polar residues | ||||
Sequence: RYSYQPPSQPSYHPYQRTPYYTCPQGFSDWQRSLPSQRSP | ||||||
Compositional bias | 1224-1251 | Polar residues | ||||
Sequence: FSEKNVLSSLQGCETLNTALTSPTQMDV | ||||||
Compositional bias | 1262-1290 | Basic and acidic residues | ||||
Sequence: HNSGPEEEKMDESVERPESPKEFLDLDNH | ||||||
Compositional bias | 1291-1308 | Polar residues | ||||
Sequence: NAATKRQNSLSTSDYLYG | ||||||
Compositional bias | 1331-1348 | Polar residues | ||||
Sequence: MLQTGSPYTPQRSASHFQ | ||||||
Region | 1331-1368 | Disordered | ||||
Sequence: MLQTGSPYTPQRSASHFQPRAYPSPVPAHPPPHPVATQ | ||||||
Compositional bias | 1353-1368 | Pro residues | ||||
Sequence: PSPVPAHPPPHPVATQ | ||||||
Region | 1396-1453 | Disordered | ||||
Sequence: QTGTGSGLRGSFQEVHRPPGLQMHPVQSQSLFPKTPAPAASPEQLPPHKTPTLPLDQS |
Domain
The Bromo domain recognizes and binds acetylated histones. Also recognizes and binds histones that are butyrylated.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
E9Q2Z1-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length1,453
- Mass (Da)161,530
- Last updated2011-04-05 v1
- ChecksumBCD9BA085DC40814
E9Q2Z1-2
- Name2
- Differences from canonical
- 601-628: Missing
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A5H1ZRM0 | A0A5H1ZRM0_MOUSE | Cecr2 | 234 | ||
A0A5H1ZRM3 | A0A5H1ZRM3_MOUSE | Cecr2 | 357 |
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 220-237 | Polar residues | ||||
Sequence: QEENSLTSDLQTRNGSRG | ||||||
Compositional bias | 586-603 | Polar residues | ||||
Sequence: SGDDQSRSSIQLPPEVGT | ||||||
Alternative sequence | VSP_059110 | 601-628 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 837-851 | Pro residues | ||||
Sequence: GHRLQPPPTPAPSPR | ||||||
Compositional bias | 889-905 | Pro residues | ||||
Sequence: VPYHPRQPTPPQLPGPF | ||||||
Compositional bias | 933-948 | Basic and acidic residues | ||||
Sequence: TETHEPEEDPAEPLPG | ||||||
Compositional bias | 998-1020 | Polar residues | ||||
Sequence: ASDSADTYKTSKNKNTWPLDNSY | ||||||
Compositional bias | 1131-1150 | Polar residues | ||||
Sequence: LASMMGGKSSGSQPQSFPPR | ||||||
Compositional bias | 1172-1211 | Polar residues | ||||
Sequence: RYSYQPPSQPSYHPYQRTPYYTCPQGFSDWQRSLPSQRSP | ||||||
Compositional bias | 1224-1251 | Polar residues | ||||
Sequence: FSEKNVLSSLQGCETLNTALTSPTQMDV | ||||||
Compositional bias | 1262-1290 | Basic and acidic residues | ||||
Sequence: HNSGPEEEKMDESVERPESPKEFLDLDNH | ||||||
Compositional bias | 1291-1308 | Polar residues | ||||
Sequence: NAATKRQNSLSTSDYLYG | ||||||
Compositional bias | 1331-1348 | Polar residues | ||||
Sequence: MLQTGSPYTPQRSASHFQ | ||||||
Compositional bias | 1353-1368 | Pro residues | ||||
Sequence: PSPVPAHPPPHPVATQ |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC084273 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC135105 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AK129435 EMBL· GenBank· DDBJ | BAC98245.1 EMBL· GenBank· DDBJ | mRNA | ||
BC060152 EMBL· GenBank· DDBJ | AAH60152.1 EMBL· GenBank· DDBJ | mRNA |