Tp53bp1
entrez
27223
canonical
uniprot
P70399
canonical
ensembl
ENSMUSG00000043909
resolver
ensp
ENSMUSP00000106277
resolver
ensp
ENSMUSP00000106278
resolver
ensp
ENSMUSP00000114457
resolver
ensp
ENSMUSP00000324778
resolver
ensp
ENSMUSP00000324780
resolver
ensp
ENSMUSP00000324782
resolver
ensp
ENSMUSP00000324785
resolver
ensp
ENSMUSP00000325825
resolver
enst
ENSMUST00000110647
resolver
genesymbol
Tp53bp1
resolver
genesymbol
Trp53bp1
resolver
genesymbol_syn
Trp53bp1
resolver
uniprot
A0A5H1ZRL7
resolver
uniprot
A2AU89
resolver
uniprot
A2AU91
resolver
uniprot
Q3V1P7
resolver
uniprot
Q68FD0
resolver
uniprot
Q8BZ87
resolver
uniprot
Q8CI97
resolver
uniprot
Q91YC9
resolver
uniprot_entry
A0A5H1ZRL7_MOUSE
resolver
uniprot_entry
Q3V1P7_MOUSE
resolver
uniprot_entry
Q8BZ87_MOUSE
resolver
uniprot_entry
TP53B_MOUSE
resolver
uniprot_sec
A2AU89
resolver
uniprot_sec
A2AU91
resolver
uniprot_sec
Q68FD0
resolver
uniprot_sec
Q8CI97
resolver
uniprot_sec
Q91YC9
resolver
amino_acid_sequence
MPGEQMDPTGSQLDSDFSQQDTPCLIIEDSQPESQVLEEDAGSHFSVLSRHLPNLQMHKENPVLDIVSNPEQSAVEQGDSNSSFNEHLKEKKASDPVESSHLGTSGSISQVIERLPQPNRTSSALAVTVEAASLPEEEKEEEELEEEKEGVGANAPGADSLAAEDSASSQLGFGVLELSQSQDVEEHTVPYDVNQEHLQLVTTNSGSSPLSDVDASTAIKCEEQPTEDIAMIEQPSKDIPVTVQPGKGIHVVEEQNLPLVRSEDRPSSPQVSVAAVETKEQVPARELLEEGPQVQPSSEPEVSSTQEDLFDQSSKTASDGCSTPSREEGGCSPVSTPATTLQLLQLSGQKPLVQESLSTNSSDLVAPSPDAFRSTPFIVPSSPTEQGGRKDEPMDMSVIPVGGEPFQKLHDDEAMETEKPLLPSQPAVSPQASTPVSRSTPVFTPGSLPIPSQPEFSHDIFIPSPSLEEPSDDVKKGGGLHSSSLTVECSKTSESEPKNFTDDLGLSMTGDSCKLMLSTSEYSQSSKMESLGSPRTEEDRENTQIDDTEPLSPVSNSKLPADSENVLVTPSQDDQVEMSQNVDKAKEDETEDRGDCKGREDAVAEDVCIDLTCDSGSQAVPSPATRSEALSSVLDQEEAMDTKEHHPEEGFSGSEVEEVPETPCGSHREEPKEEPMESIPLHLSLTETQSEALCLQKEAPKEECPEAMEVETSVISIDSPQKLQVLDQELEHKDPDTWEEATSEDSSVVIVDVKEPSPRADVSCEPLEEVEKCSDSQSWEGVAPEEEPCAENRLDTPEEKRIECDGDSKAETTEKDAVTEDSPQPPLPSVRDEPVRPDQETQQPQVQEKESPVTVDAEVADDKQLGPEGACQQLEKAPACASQSFCESSSETPFHFTLPKEGDIIPPLTGATPPLIGHLKLEPKRHSTPIGISNYPESTIATSDVTSESMVEINDPLLGNEKGDSESAPEMDGKLSLKMKLVSPETEASEESLQFSLEKPTTAERKNGSTAIAEPVASLQKPVPVFGCIYEAQQEKEAQSEAPPSAPDRANLLHFPSAQEEDKERPDVTPKLRQSEQPVKPVGPVMDDAAPEDSASPVSQQRASQEQRASQEPFSPAEDVMETDLLEGLAANQDRPSKMLMDRPTQSNIGIQTVDHSLCAPETVSAATQTVKSVCEQGTSTAEQNSGKQDATVQTERGSGEKPASAPVDDTESLHSQGEEEFEMPQPPHGHVLHRHMRTIREVRTLVTRVITDVYYVDGTEVERKVTEETEEPIVECQECETEVSPSQTGGSSGDLGDISSFSSKASSSHHTSSGTSLSAIHSSGSSGRGAGPLKGKASGTEAADFALPSSRGGPGKLSPRKGISQTGAPVCEEDGDAGLGIRQGGKAPVTPRGRGRRGRPPSRTTGTRETVVSGPLGVEDISPSMSPDDKSFTRIMPRVPDSTKRTDASSSTLRRSDSPEIPFQAATGSSDGLDSSSSGNSFVGLRVVAKWSSNGYFYSGKITRDVGAGKYKLLFDDGYECDVLGKDILLCDPIPLDTEVTALSEDEYFSAGVVKGHRKESGELYYSIEKEGQRKWYKRMAVILSLEQGNRLREQYGLGPYEAVTPLTKAADISLDNLVEGKRKRRSNISSPVTPTAASSSSTTPTRKATESPRASTGVPSGKRKLPTSEEERSPAKRGRKSATVKPGTVGAAEFVSPCETGDNIGEPSVLEEPRGPLPLNKTLFLGYAFLLTMATTSDKLASRSKLLDGPTGSSEEEEEFLEIPPFNKQYTECQLRAGAGYILEDFNEAQCNTAYQCLLIADQHCRTRKYFLCLASGIPCVSHVWVHDSCHANQLQNYRNYLLPAGYSLEEQRILDWQPRENPFQNLKVLLVSDQQQNFLELWSEILMTGGAASVKQHHSSAHNKDIALGVFDVVVTDPSCPASVLKCAEALQLPVVSQEWVIQCLIVGERIGFKQHPKYKHDYVSH
uniprot
proteins
function
FUNCTION: Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:15077110, PubMed:15159415, PubMed:20362325, PubMed:20453858, PubMed:23333305, PubMed:26308889). 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 (PubMed:20362325, PubMed:23333305, PubMed:30297459). 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 (PubMed:15077110, PubMed:15159415). Participates in the repair and the orientation of the broken DNA ends during CSR (PubMed:26308889). In contrast, it is not required for classic NHEJ and V(D)J recombination (PubMed:15159415). Promotes NHEJ of dysfunctional telomeres (By similarity). {ECO:0000250|UniProtKB:Q12888, ECO:0000269|PubMed:15077110, ECO:0000269|PubMed:15159415, ECO:0000269|PubMed:20362325, ECO:0000269|PubMed:20453858, ECO:0000269|PubMed:23333305, ECO:0000269|PubMed:26308889, ECO:0000269|PubMed:30297459}.
uniprot
proteins
mass_dalton
212735
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at basal level in the absence of DNA damage (By similarity). Phosphorylated by ATM in response to DNA damage: phosphorylation at different sites promotes interaction with different set of proteins: phosphorylation at the N-terminus by ATM (residues from 11-181) promotes interaction with PAXIP1 and non-homologous end joining (NHEJ) of dysfunctional telomeres (By similarity). Phosphorylation by ATM at residues that are located more C-terminus (residues 300-650) leads to promote interaction with RIF1 (PubMed:23306439, PubMed:23333305). Interaction with RIF1 leads to disrupt interaction with NUDT16L1/TIRR (By similarity). Phosphorylation at Thr-1606 and Ser-1615 in the UDR motif blocks interaction with H2AK15ub (By similarity). Dephosphorylated by PPP4C (By similarity). Hyperphosphorylation during mitosis correlates with its exclusion from chromatin and DNA lesions (By similarity). Hyperphosphorylated in an ATR-dependent manner in response to DNA damage induced by UV irradiation (By similarity). Dephosphorylated by PPP5C (By similarity). Phosphorylation at Ser-368 and Thr-662 promotes interaction with TOPBP1 (By similarity). Phosphorylated by VRK1 (By similarity). {ECO:0000250|UniProtKB:Q12888, ECO:0000269|PubMed:23306439, ECO:0000269|PubMed:23333305}.; PTM: Asymmetrically dimethylated on Arg residues by PRMT1. Methylation is required for DNA binding. {ECO:0000250|UniProtKB:Q12888}.; PTM: Monoubiquitinated at Lys-1682 by MSL2 in response to DNA damage, leading to its stabilization. {ECO:0000250|UniProtKB:Q12888}.
uniprot
proteins
pubmed
11673449
uniprot
proteins
pubmed
11801725
uniprot
proteins
pubmed
12640136
uniprot
proteins
pubmed
15077110
uniprot
proteins
pubmed
15159415
uniprot
proteins
pubmed
15341721
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19131326
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20362325
uniprot
proteins
pubmed
20453858
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23209566
uniprot
proteins
pubmed
23306439
uniprot
proteins
pubmed
23333305
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
26308889
uniprot
proteins
pubmed
30297459
uniprot
proteins
pubmed
8910340
uniprot
proteins
sequence_length
1969
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11801725}. Chromosome {ECO:0000269|PubMed:11673449, ECO:0000269|PubMed:23209566, ECO:0000269|PubMed:23306439, ECO:0000269|PubMed:23333305, ECO:0000269|PubMed:30297459}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:11801725}. Note=Localizes to the nucleus in absence of DNA damage (PubMed:11801725). Following DNA damage, recruited to sites of DNA damage, such as double strand breaks (DSBs) (PubMed:11673449, PubMed:23209566, PubMed:23306439, PubMed:23333305). 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 (PubMed:23209566). Associated with kinetochores during mitosis (PubMed:11801725). {ECO:0000269|PubMed:11673449, ECO:0000269|PubMed:11801725, ECO:0000269|PubMed:23209566, ECO:0000269|PubMed:23306439, ECO:0000269|PubMed:23333305}.
uniprot
proteins