Mus musculus Protein: Rad21 | |||||||||||||||||||||||
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Summary | |||||||||||||||||||||||
InnateDB Protein | IDBP-140000.6 | ||||||||||||||||||||||
Last Modified | 2014-10-13 [Report errors or provide feedback] | ||||||||||||||||||||||
Gene Symbol | Rad21 | ||||||||||||||||||||||
Protein Name | RAD21 homolog (S. pombe) | ||||||||||||||||||||||
Synonyms | mKIAA0078; SCC1; | ||||||||||||||||||||||
Species | Mus musculus | ||||||||||||||||||||||
Ensembl Protein | ENSMUSP00000022927 | ||||||||||||||||||||||
InnateDB Gene | IDBG-139998 (Rad21) | ||||||||||||||||||||||
Protein Structure |
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UniProt Annotation | |||||||||||||||||||||||
Function | Cleavable component of the cohesin complex, involved in chromosome cohesion during cell cycle, in DNA repair, and in apoptosis. Plays a role in apoptosis, via its cleavage by caspase- 3/CASP3 or caspase-7/CASP7 during early steps of apoptosis: the C- terminal 64 kDa cleavage product may act as a nuclear signal to initiate cytoplasmic events involved in the apoptotic pathway (By similarity). The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At metaphase-anaphase transition, this protein is cleaved by separase/ESPL1 and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. {ECO:0000250}. | ||||||||||||||||||||||
Subcellular Localization | Nucleus. Chromosome. Chromosome, centromere. Note=Associates with chromatin. Once cleaved by caspase-3, the C- terminal 64 kDa cleavage product translocates to the cytoplasm, where it may trigger apoptosis (By similarity). Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK, except at centromeres, where cohesin complexes remain. At anaphase, it is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation. {ECO:0000250}. | ||||||||||||||||||||||
Disease Associations | |||||||||||||||||||||||
Tissue Specificity | Widely expressed with highest levels in testis, brain, kidney, heart and thymus. Lowest levels in skeletal muscle. {ECO:0000269PubMed:8812457}. | ||||||||||||||||||||||
Comments | |||||||||||||||||||||||
Interactions | |||||||||||||||||||||||
Number of Interactions |
This gene and/or its encoded proteins are associated with 29 experimentally validated interaction(s) in this database.
They are also associated with 218 interaction(s) predicted by orthology.
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Gene Ontology | |||||||||||||||||||||||
Molecular Function |
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Biological Process |
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Cellular Component |
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Protein Structure and Domains | |||||||||||||||||||||||
PDB ID | MGI:108016 | ||||||||||||||||||||||
InterPro |
IPR003768
Prokaryotic chromosome segregation/condensation protein ScpA IPR006909 Rad21/Rec8-like protein, C-terminal, eukaryotic IPR006910 Rad21/Rec8-like protein, N-terminal |
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PFAM |
PF02616
PF04824 PF04825 |
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PRINTS | |||||||||||||||||||||||
PIRSF | |||||||||||||||||||||||
SMART | |||||||||||||||||||||||
TIGRFAMs | |||||||||||||||||||||||
Post-translational Modifications | |||||||||||||||||||||||
Modification | |||||||||||||||||||||||
Cross-References | |||||||||||||||||||||||
SwissProt | Q61550 | ||||||||||||||||||||||
PhosphoSite | PhosphoSite-Q61550 | ||||||||||||||||||||||
TrEMBL | Q3UTE4 | ||||||||||||||||||||||
UniProt Splice Variant | |||||||||||||||||||||||
Entrez Gene | 19357 | ||||||||||||||||||||||
UniGene | Mm.470496 | ||||||||||||||||||||||
RefSeq | NP_033035 | ||||||||||||||||||||||
MGI ID | |||||||||||||||||||||||
MGI Symbol | Rad21 | ||||||||||||||||||||||
OMIM | |||||||||||||||||||||||
CCDS | CCDS27463 | ||||||||||||||||||||||
HPRD | |||||||||||||||||||||||
IMGT | |||||||||||||||||||||||
EMBL | AF332085 AF332086 AK004746 AK139492 AK163992 BC043032 D49429 X98293 | ||||||||||||||||||||||
GenPept | AAH43032 AAK56113 AAK56114 BAA08408 BAB23527 BAE24036 BAE37576 CAA66939 | ||||||||||||||||||||||