The following text describes a protein:
Function:
Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis. Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1. In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites. Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites. Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs. Participates in the repair and the orientation of the broken DNA ends during CSR. In contrast, it is not required for classic NHEJ and V(D)J recombination. Promotes NHEJ of dysfunctional telomeres (By similarity).
Subcellular Localization:
Nucleus. Chromosome. Chromosome, centromere, kinetochore. Note=Localizes to the nucleus in absence of DNA damage. Following DNA damage, recruited to sites of DNA damage, such as double stand breaks (DSBs). Recognizes and binds histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites. Associated with kinetochores during mitosis.
Domain:
The Tudor-like region mediates binding to histone H4 dimethylated at 'Lys-20' (H4K20me2). Interaction with NUDT16L1/TIRR masks the Tudor-like domain and prevents recruitment to chromatin (By similarity); The UDR (ubiquitin-dependent recruitment) motif specifically recognizes and binds histone H2A monoubiquitinated at 'Lys-15' (H2AK15ub). Phosphorylation of the UDR blocks interaction with H2AK15ub.
Sequence:
MPGEQMDPTGSQLDSDFSQQDTPCLIIEDSQPESQVLEEDAGSHFSVLSRHLPNLQMHKENPVLDIVSNPEQSAVEQGDSNSSFNEHLKEKKASDPVESSHLGTSGSISQVIERLPQPNRTSSALAVTVEAASLPEEEKEEEELEEEKEGVGANAPGADSLAAEDSASSQLGFGVLELSQSQDVEEHTVPYDVNQEHLQLVTTNSGSSPLSDVDASTAIKCEEQPTEDIAMIEQPSKDIPVTVQPGKGIHVVEEQNLPLVRSEDRPSSPQVSVAAVETKEQVPARELLEEGPQVQPSSEPEVSSTQEDLFDQSSKTASDGCSTPSREEGGCSPVSTPATTLQLLQLSGQKPLVQESLSTNSSDLVAPSPDAFRSTPFIVPSSPTEQGGRKDEPMDMSVIPVGGEPFQKLHDDEAMETEKPLLPSQPAVSPQASTPVSRSTPVFTPGSLPIPSQPEFSHDIFIPSPSLEEPSDDVKKGGGLHSSSLTVECSKTSESEPKNFTDDLGLSMTGDSCKLMLSTSEYSQSSKMESLGSPRTEEDRENTQIDDTEPLSPVSNSKLPADSENVLVTPSQDDQVEMSQNVDKAKEDETEDRGDCKGREDAVAEDVCIDLTCDSGSQAVPSPATRSEALSSVLDQEEAMDTKEHHPEEGFSGSEVEEVPETPCGSHREEPKEEPMESIPLHLSLTETQSEALCLQKEAPKEECPEAMEVETSVISIDSPQKLQVLDQELEHKDPDTWEEATSEDSSVVIVDVKEPSPRADVSCEPLEEVEKCSDSQSWEGVAPEEEPCAENRLDTPEEKRIECDGDSKAETTEKDAVTEDSPQPPLPSVRDEPVRPDQETQQPQVQEKESPVTVDAEVADDKQLGPEGACQQLEKAPACASQSFCESSSETPFHFTLPKEGDIIPPLTGATPPLIGHLKLEPKRHSTPIGISNYPESTIATSDVTSESMVEINDPLLGNEKGDSESAPEMDGKLSLKMKLVSPETEASEESLQFSLEKPTTAERKNGSTAIAEPVASLQKPVPVFGCIYEAQQEKEAQSEAPPSAPDRANLLHFPSAQEEDKERPDVTPKLRQSEQPVKPVGPVMDDAAPEDSASPVSQQRASQEQRASQEPFSPAEDVMETDLLEGLAANQDRPSKMLMDRPTQSNIGIQTVDHSLCAPETVSAATQTVKSVCEQGTSTAEQNSGKQDATVQTERGSGEKPASAPVDDTESLHSQGEEEFEMPQPPHGHVLHRHMRTIREVRTLVTRVITDVYYVDGTEVERKVTEETEEPIVECQECETEVSPSQTGGSSGDLGDISSFSSKASSSHHTSSGTSLSAIHSSGSSGRGAGPLKGKASGTEAADFALPSSRGGPGKLSPRKGISQTGAPVCEEDGDAGLGIRQGGKAPVTPRGRGRRGRPPSRTTGTRETVVSGPLGVEDISPSMSPDDKSFTRIMPRVPDSTKRTDASSSTLRRSDSPEIPFQAATGSSDGLDSSSSGNSFVGLRVVAKWSSNGYFYSGKITRDVGAGKYKLLFDDGYECDVLGKDILLCDPIPLDTEVTALSEDEYFSAGVVKGHRKESGELYYSIEKEGQRKWYKRMAVILSLEQGNRLREQYGLGPYEAVTPLTKAADISLDNLVEGKRKRRSNISSPVTPTAASSSSTTPTRKATESPRASTGVPSGKRKLPTSEEERSPAKRGRKSATVKPGTVGAAEFVSPCETGDNIGEPSVLEEPRGPLPLNKTLFLGYAFLLTMATTSDKLASRSKLLDGPTGSSEEEEEFLEIPPFNKQYTECQLRAGAGYILEDFNEAQCNTAYQCLLIADQHCRTRKYFLCLASGIPCVSHVWVHDSCHANQLQNYRNYLLPAGYSLEEQRILDWQPRENPFQNLKVLLVSDQQQNFLELWSEILMTGGAASVKQHHSSAHNKDIALGVFDVVVTDPSCPASVLKCAEALQLPVVSQEWVIQCLIVGERIGFKQHPKYKHDYVSH