E9Q2Z1 · CECR2_MOUSE

  • Protein
    Chromatin remodeling regulator CECR2
  • Gene
    Cecr2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular ComponentCERF complex
Cellular Componenteuchromatin
Cellular ComponentISWI-type complex
Molecular FunctionATP-dependent chromatin remodeler activity
Biological Processchromatin remodeling
Biological Processcochlea development
Biological Processexecution phase of apoptosis
Biological Processinner ear receptor cell stereocilium organization
Biological Processneural fold formation
Biological Processneural tube closure
Biological Processneural tube development
Biological Processsingle fertilization

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Chromatin remodeling regulator CECR2
  • Alternative names
    • Cat eye syndrome critical region protein 2 homolog

Gene names

    • Name
      Cecr2
    • Synonyms
      Kiaa1740

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    E9Q2Z1
  • Secondary accessions
    • E9QA25
    • F6VR46
    • F7B218
    • Q6PAQ2
    • Q6ZPI9

Proteomes

Organism-specific databases

Subcellular Location

Keywords

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).

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.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004417751-1453Chromatin remodeling regulator CECR2
Modified residue402Phosphoserine
Modified residue526Phosphothreonine
Modified residue551Phosphoserine
Modified residue983Phosphoserine
Modified residue1166Asymmetric dimethylarginine
Modified residue1172Asymmetric dimethylarginine
Modified residue1280Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Developmental stage

In embryos, predominantly expressed in neural tissues (PubMed:15640247).
Expressed throughout inner ear development: expressed in the neuroepithelium, head mesenchyme and the cochlear floor (PubMed:21246654).

Gene expression 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).
View interactors in UniProtKB
View CPX-454 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region170-237Disordered
Compositional bias220-237Polar residues
Domain431-501Bromo
Region536-667Disordered
Compositional bias586-603Polar residues
Region767-796Disordered
Region827-868Disordered
Compositional bias837-851Pro residues
Region884-1020Disordered
Compositional bias889-905Pro residues
Compositional bias933-948Basic and acidic residues
Compositional bias998-1020Polar residues
Region1046-1072Disordered
Compositional bias1131-1150Polar residues
Region1131-1308Disordered
Compositional bias1172-1211Polar residues
Compositional bias1224-1251Polar residues
Compositional bias1262-1290Basic and acidic residues
Compositional bias1291-1308Polar residues
Compositional bias1331-1348Polar residues
Region1331-1368Disordered
Compositional bias1353-1368Pro residues
Region1396-1453Disordered

Domain

The Bromo domain recognizes and binds acetylated histones. Also recognizes and binds histones that are butyrylated.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

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.

  • Length
    1,453
  • Mass (Da)
    161,530
  • Last updated
    2011-04-05 v1
  • Checksum
    BCD9BA085DC40814
MCPEEGGAAGLGELRSWWEVPAIAHFCSLFRTAFRLPDFEIEELEAALHRDDVEFISDLIACLLQGCYQRRDITPQTFHSYLEDIINYRWELEEGKPNPLREASFQDLPLRTRVEILHRLCDYRLDADDVFDLLKGLDADSLRVEPLGEDNSGALYWYFYGTRMYKEDPVQGRSNGELSLCRESERQKNVSNVPGKTGKRRGRPPKRKKLQEEIISSEKQEENSLTSDLQTRNGSRGPGQGTWWLLCQTEEEWRQVTESFRERTSLRERQLYKLLSEDFLPEICNMIAQKGKRPQRTKPELQHRFMSDHLSIKSIKLEETPMLTKIEKQKRREEEEERQLLLAVQKKEQEQMLKEERKREMEEKVKAVEDRAKRRKLREERAWLLAQGKELPPELSHLDLNSPMREGKKTKDLFELDDDFTAMYKVLDVVKAHKDSWPFLEPVDESYAPNYYQIIKIPMDISSMEKKLNGGLYCNKEEFVNDMKTMFRNCRKYNGDSSEYTKMSDNLERCFHRAMTKHFPGEDGDTDEEFWIKEDEKREKRRSRSGRSSGSHVWTRSRDTEGSSRKQPPVENGGKSLPPARRAASSGDDQSRSSIQLPPEVGTSHGQGFSRPLHCGRVPSHAPPLNQMRPAAPGTFGSLQGSDPTNLHGSSRIPEAPPGEPLQHPPFAIQAPVGISNHRGSLLSAPDLSNMGSHVPSLQLGQMNCPSQDGNMYPPAPFQAGFIPSRHGGTPARPPDFPESSEIPPGHIYHSYKYLNRAHPAVWNGNHGTTNPGRLGPDEKPHLGPGPSHHPHTLGHMMDGRVMRQPIPPNQWTKQSSFLPHGVPSSGYMQPPCKSAGHRLQPPPTPAPSPRFRGPSQALRGAQGGESMMDSPEMIAMQQLSSRVCPPGVPYHPRQPTPPQLPGPFPQVAHSASVCVSAPKPALDNPGSTQEMTETHEPEEDPAEPLPGHEEKAASICSSEGVYLKQLPHPAPPLQASCTRQSSPQERETEDSQLKSDASDSADTYKTSKNKNTWPLDNSYSSPAVQGCLRDLSIVAETGNLPENGVVGEASPCRSEGKGLDGSGSEKPLCPRGKTLQEAVPCTGPNATTPPCTDPSLMAATVNQFSPLYMPGIEYSNSATQYPMSPSLQGLASMMGGKSSGSQPQSFPPRGFQANGPHPGLFPRYRPQQGMRYSYQPPSQPSYHPYQRTPYYTCPQGFSDWQRSLPSQRSPSGPPGSHPPRSLFSEKNVLSSLQGCETLNTALTSPTQMDVVTAKVVPPDGHNSGPEEEKMDESVERPESPKEFLDLDNHNAATKRQNSLSTSDYLYGTPPPSLSSGMTFGSSAFPPHSVMLQTGSPYTPQRSASHFQPRAYPSPVPAHPPPHPVATQPNGLSPEDSLYCCQEEGLGHFQASMMEQTGTGSGLRGSFQEVHRPPGLQMHPVQSQSLFPKTPAPAASPEQLPPHKTPTLPLDQS

E9Q2Z1-2

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A5H1ZRM0A0A5H1ZRM0_MOUSECecr2234
A0A5H1ZRM3A0A5H1ZRM3_MOUSECecr2357

Features

Showing features for compositional bias, alternative sequence.

TypeIDPosition(s)Description
Compositional bias220-237Polar residues
Compositional bias586-603Polar residues
Alternative sequenceVSP_059110601-628in isoform 2
Compositional bias837-851Pro residues
Compositional bias889-905Pro residues
Compositional bias933-948Basic and acidic residues
Compositional bias998-1020Polar residues
Compositional bias1131-1150Polar residues
Compositional bias1172-1211Polar residues
Compositional bias1224-1251Polar residues
Compositional bias1262-1290Basic and acidic residues
Compositional bias1291-1308Polar residues
Compositional bias1331-1348Polar residues
Compositional bias1353-1368Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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