Genome3D
Mus musculus

Tp53bp1 Tumor suppressor p53-binding protein 1

UniProt Data

Accession P70399 [ UniProt ]
Name TP53B_MOUSE
Description Tumor suppressor p53-binding protein 1
Species Mus musculus
Sequence Length1969

Enzyme Annotations (0)

    GO Annotations

    Cellular component (11)

    • GO:0000776 Kinetochore
      A multisubunit complex that is located at the centromeric region of DNA and provides an attachment point for the spindle microtubules.
    • GO:0000784 Nuclear chromosome, telomeric region
      The terminal region of a linear nuclear chromosome that includes the telomeric DNA repeats and associated proteins.
    • GO:0005634 Nucleus
      A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
    • GO:0005634 Nucleus
      A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
    • GO:0005654 Nucleoplasm
      That part of the nuclear content other than the chromosomes or the nucleolus.
    • GO:0005657 Replication fork
      The Y-shaped region of a replicating DNA molecule, resulting from the separation of the DNA strands and in which the synthesis of new strands takes place. Also includes associated protein complexes.
    • GO:0005737 Cytoplasm
      All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
    • GO:0016604 Nuclear body
      Extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins.
    • GO:0035861 Site of double-strand break
      A region of a chromosome at which a DNA double-strand break has occurred. DNA damage signaling and repair proteins accumulate at the lesion to respond to the damage and repair the DNA to form a continuous DNA helix.
    • GO:0035861 Site of double-strand break
      A region of a chromosome at which a DNA double-strand break has occurred. DNA damage signaling and repair proteins accumulate at the lesion to respond to the damage and repair the DNA to form a continuous DNA helix.
    • GO:1990391 DNA repair complex
      A protein complex involved in DNA repair processes including direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.

    Molecular function (13)

    • GO:0001102 RNA polymerase II activating transcription factor binding
      Interacting selectively and non-covalently with an RNA polymerase II transcription activating factor, a protein involved in positive regulation of transcription.
    • GO:0001104 RNA polymerase II transcription cofactor activity
      Interacting selectively and non-covalently with an RNA polymerase II (RNAP II) regulatory transcription factor and also with the RNAP II basal transcription machinery in order to modulate transcription. Cofactors generally do not bind DNA, but rather mediate protein-protein interactions between regulatory transcription factors and the basal RNAP II transcription machinery.
    • GO:0002039 P53 binding
      Interacting selectively and non-covalently with one of the p53 family of proteins.
    • GO:0003684 Damaged DNA binding
      Interacting selectively and non-covalently with damaged DNA.
    • GO:0005515 Protein binding
      Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
    • GO:0008134 Transcription factor binding
      Interacting selectively and non-covalently with a transcription factor, any protein required to initiate or regulate transcription.
    • GO:0035064 Methylated histone binding
      Interacting selectively and non-covalently with a histone protein in which a residue has been modified by methylation. Histones are any of a group of water-soluble proteins found in association with the DNA of plant and animal chromosomes.
    • GO:0035064 Methylated histone binding
      Interacting selectively and non-covalently with a histone protein in which a residue has been modified by methylation. Histones are any of a group of water-soluble proteins found in association with the DNA of plant and animal chromosomes.
    • GO:0035064 Methylated histone binding
      Interacting selectively and non-covalently with a histone protein in which a residue has been modified by methylation. Histones are any of a group of water-soluble proteins found in association with the DNA of plant and animal chromosomes.
    • GO:0042162 Telomeric DNA binding
      Interacting selectively and non-covalently with a telomere, a specific structure at the end of a linear chromosome required for the integrity and maintenance of the end.
    • GO:0043565 Sequence-specific DNA binding
      Interacting selectively and non-covalently with DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding.
    • GO:0061649 Ubiquitinated histone binding
      Interacting selectively and non-covalently with a histone protein in which a residue has been modified by ubiquitination. Histones are any of a group of water-soluble proteins found in association with the DNA of plant and animal chromosomes.
    • GO:0061649 Ubiquitinated histone binding
      Interacting selectively and non-covalently with a histone protein in which a residue has been modified by ubiquitination. Histones are any of a group of water-soluble proteins found in association with the DNA of plant and animal chromosomes.

    Biological process (14)

    • GO:0006281 DNA repair
      The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
    • GO:0006303 Double-strand break repair via nonhomologous end joining
      The repair of a double-strand break in DNA in which the two broken ends are rejoined with little or no sequence complementarity. Information at the DNA ends may be lost due to the modification of broken DNA ends. This term covers instances of separate pathways, called classical (or canonical) and alternative nonhomologous end joining (C-NHEJ and A-NHEJ). These in turn may further branch into sub-pathways, but evidence is still unclear.
    • GO:0006303 Double-strand break repair via nonhomologous end joining
      The repair of a double-strand break in DNA in which the two broken ends are rejoined with little or no sequence complementarity. Information at the DNA ends may be lost due to the modification of broken DNA ends. This term covers instances of separate pathways, called classical (or canonical) and alternative nonhomologous end joining (C-NHEJ and A-NHEJ). These in turn may further branch into sub-pathways, but evidence is still unclear.
    • GO:0006303 Double-strand break repair via nonhomologous end joining
      The repair of a double-strand break in DNA in which the two broken ends are rejoined with little or no sequence complementarity. Information at the DNA ends may be lost due to the modification of broken DNA ends. This term covers instances of separate pathways, called classical (or canonical) and alternative nonhomologous end joining (C-NHEJ and A-NHEJ). These in turn may further branch into sub-pathways, but evidence is still unclear.
    • GO:0006355 Regulation of transcription, DNA-templated
      Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
    • GO:0006974 Cellular response to DNA damage stimulus
      Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.
    • GO:0045830 Positive regulation of isotype switching
      Any process that activates or increases the frequency, rate or extent of isotype switching.
    • GO:0045830 Positive regulation of isotype switching
      Any process that activates or increases the frequency, rate or extent of isotype switching.
    • GO:0045944 Positive regulation of transcription from RNA polymerase II promoter
      Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter.
    • GO:0051260 Protein homooligomerization
      The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.
    • GO:0051260 Protein homooligomerization
      The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.
    • GO:2000042 Negative regulation of double-strand break repair via homologous recombination
      Any process that stops, prevents, or reduces the frequency, rate or extent of double-strand break repair via homologous recombination.
    • GO:2000042 Negative regulation of double-strand break repair via homologous recombination
      Any process that stops, prevents, or reduces the frequency, rate or extent of double-strand break repair via homologous recombination.
    • GO:2000042 Negative regulation of double-strand break repair via homologous recombination
      Any process that stops, prevents, or reduces the frequency, rate or extent of double-strand break repair via homologous recombination.

    Protein Sequence

    >P70399
MPGEQMDPTGSQLDSDFSQQDTPCLIIEDSQPESQVLEEDAGSHFSVLSRHLPNLQMHKENPVLDIVSNPEQSAVEQGDS
NSSFNEHLKEKKASDPVESSHLGTSGSISQVIERLPQPNRTSSALAVTVEAASLPEEEKEEEELEEEKEGVGANAPGADS
LAAEDSASSQLGFGVLELSQSQDVEEHTVPYDVNQEHLQLVTTNSGSSPLSDVDASTAIKCEEQPTEDIAMIEQPSKDIP
VTVQPGKGIHVVEEQNLPLVRSEDRPSSPQVSVAAVETKEQVPARELLEEGPQVQPSSEPEVSSTQEDLFDQSSKTASDG
CSTPSREEGGCSPVSTPATTLQLLQLSGQKPLVQESLSTNSSDLVAPSPDAFRSTPFIVPSSPTEQGGRKDEPMDMSVIP
VGGEPFQKLHDDEAMETEKPLLPSQPAVSPQASTPVSRSTPVFTPGSLPIPSQPEFSHDIFIPSPSLEEPSDDVKKGGGL
HSSSLTVECSKTSESEPKNFTDDLGLSMTGDSCKLMLSTSEYSQSSKMESLGSPRTEEDRENTQIDDTEPLSPVSNSKLP
ADSENVLVTPSQDDQVEMSQNVDKAKEDETEDRGDCKGREDAVAEDVCIDLTCDSGSQAVPSPATRSEALSSVLDQEEAM
DTKEHHPEEGFSGSEVEEVPETPCGSHREEPKEEPMESIPLHLSLTETQSEALCLQKEAPKEECPEAMEVETSVISIDSP
QKLQVLDQELEHKDPDTWEEATSEDSSVVIVDVKEPSPRADVSCEPLEEVEKCSDSQSWEGVAPEEEPCAENRLDTPEEK
RIECDGDSKAETTEKDAVTEDSPQPPLPSVRDEPVRPDQETQQPQVQEKESPVTVDAEVADDKQLGPEGACQQLEKAPAC
ASQSFCESSSETPFHFTLPKEGDIIPPLTGATPPLIGHLKLEPKRHSTPIGISNYPESTIATSDVTSESMVEINDPLLGN
EKGDSESAPEMDGKLSLKMKLVSPETEASEESLQFSLEKPTTAERKNGSTAIAEPVASLQKPVPVFGCIYEAQQEKEAQS
EAPPSAPDRANLLHFPSAQEEDKERPDVTPKLRQSEQPVKPVGPVMDDAAPEDSASPVSQQRASQEQRASQEPFSPAEDV
METDLLEGLAANQDRPSKMLMDRPTQSNIGIQTVDHSLCAPETVSAATQTVKSVCEQGTSTAEQNSGKQDATVQTERGSG
EKPASAPVDDTESLHSQGEEEFEMPQPPHGHVLHRHMRTIREVRTLVTRVITDVYYVDGTEVERKVTEETEEPIVECQEC
ETEVSPSQTGGSSGDLGDISSFSSKASSSHHTSSGTSLSAIHSSGSSGRGAGPLKGKASGTEAADFALPSSRGGPGKLSP
RKGISQTGAPVCEEDGDAGLGIRQGGKAPVTPRGRGRRGRPPSRTTGTRETVVSGPLGVEDISPSMSPDDKSFTRIMPRV
PDSTKRTDASSSTLRRSDSPEIPFQAATGSSDGLDSSSSGNSFVGLRVVAKWSSNGYFYSGKITRDVGAGKYKLLFDDGY
ECDVLGKDILLCDPIPLDTEVTALSEDEYFSAGVVKGHRKESGELYYSIEKEGQRKWYKRMAVILSLEQGNRLREQYGLG
PYEAVTPLTKAADISLDNLVEGKRKRRSNISSPVTPTAASSSSTTPTRKATESPRASTGVPSGKRKLPTSEEERSPAKRG
RKSATVKPGTVGAAEFVSPCETGDNIGEPSVLEEPRGPLPLNKTLFLGYAFLLTMATTSDKLASRSKLLDGPTGSSEEEE
EFLEIPPFNKQYTECQLRAGAGYILEDFNEAQCNTAYQCLLIADQHCRTRKYFLCLASGIPCVSHVWVHDSCHANQLQNY
RNYLLPAGYSLEEQRILDWQPRENPFQNLKVLLVSDQQQNFLELWSEILMTGGAASVKQHHSSAHNKDIALGVFDVVVTD
PSCPASVLKCAEALQLPVVSQEWVIQCLIVGERIGFKQHPKYKHDYVSH