LOCUS       NP_002885                897 aa            linear   PRI 27-APR-2025
DEFINITION  DNA endonuclease RBBP8 isoform a [Homo sapiens].
ACCESSION   NP_002885
VERSION     NP_002885.1
DBSOURCE    REFSEQ: accession NM_002894.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 897)
  AUTHORS   Zhang,Z., Samsa,W.E. and Gong,Z.
  TITLE     NUDT16 regulates CtIP PARylation to dictate homologous
            recombination repair
  JOURNAL   Nucleic Acids Res 52 (7), 3761-3777 (2024)
   PUBMED   38324469
  REMARK    GeneRIF: NUDT16 regulates CtIP PARylation to dictate homologous
            recombination repair.
REFERENCE   2  (residues 1 to 897)
  AUTHORS   Yan,J., Wu,J., Wang,Y., Di,X., Jiang,H., Wen,D., Li,D. and Zhang,S.
  TITLE     A novel RBBP8(p.E281*) germline mutation is a predisposing mutation
            in familial hereditary cancer syndrome
  JOURNAL   J Mol Med (Berl) 101 (10), 1255-1265 (2023)
   PUBMED   37615686
  REMARK    GeneRIF: A novel RBBP8(p.E281*) germline mutation is a predisposing
            mutation in familial hereditary cancer syndrome.
REFERENCE   3  (residues 1 to 897)
  AUTHORS   Jeong,S.Y., Hariharasudhan,G., Kim,M.J., Lim,J.Y., Jung,S.M.,
            Choi,E.J., Chang,I.Y., Kee,Y., You,H.J. and Lee,J.H.
  TITLE     SIAH2 regulates DNA end resection and replication fork recovery by
            promoting CtIP ubiquitination
  JOURNAL   Nucleic Acids Res 50 (18), 10469-10486 (2022)
   PUBMED   36155803
  REMARK    GeneRIF: SIAH2 regulates DNA end resection and replication fork
            recovery by promoting CtIP ubiquitination.
REFERENCE   4  (residues 1 to 897)
  AUTHORS   Averbeck,N.B., Barent,C., Jakob,B., Syzonenko,T., Durante,M. and
            Taucher-Scholz,G.
  TITLE     The Ubiquitin Ligase RNF138 Cooperates with CtIP to Stimulate
            Resection of Complex DNA Double-Strand Breaks in Human G1-Phase
            Cells
  JOURNAL   Cells 11 (16), 2561 (2022)
   PUBMED   36010636
  REMARK    GeneRIF: The Ubiquitin Ligase RNF138 Cooperates with CtIP to
            Stimulate Resection of Complex DNA Double-Strand Breaks in Human
            G1-Phase Cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 897)
  AUTHORS   Wang,J., Sheng,Z., Dong,Z., Wu,Q. and Cai,Y.
  TITLE     The mechanism of radiotherapy for lung adenocarcinoma in promoting
            protein SIRT6-mediated deacetylation of RBBP8 to enhance the
            sensitivity of targeted therapy
  JOURNAL   Int J Immunopathol Pharmacol 36, 3946320221130727 (2022)
   PUBMED   36172813
  REMARK    GeneRIF: The mechanism of radiotherapy for lung adenocarcinoma in
            promoting protein SIRT6-mediated deacetylation of RBBP8 to enhance
            the sensitivity of targeted therapy.
REFERENCE   6  (residues 1 to 897)
  AUTHORS   Yu,X., Wu,L.C., Bowcock,A.M., Aronheim,A. and Baer,R.
  TITLE     The C-terminal (BRCT) domains of BRCA1 interact in vivo with CtIP,
            a protein implicated in the CtBP pathway of transcriptional
            repression
  JOURNAL   J Biol Chem 273 (39), 25388-25392 (1998)
   PUBMED   9738006
REFERENCE   7  (residues 1 to 897)
  AUTHORS   Fusco,C., Reymond,A. and Zervos,A.S.
  TITLE     Molecular cloning and characterization of a novel
            retinoblastoma-binding protein
  JOURNAL   Genomics 51 (3), 351-358 (1998)
   PUBMED   9721205
REFERENCE   8  (residues 1 to 897)
  AUTHORS   Schaeper,U., Subramanian,T., Lim,L., Boyd,J.M. and Chinnadurai,G.
  TITLE     Interaction between a cellular protein that binds to the C-terminal
            region of adenovirus E1A (CtBP) and a novel cellular protein is
            disrupted by E1A through a conserved PLDLS motif
  JOURNAL   J Biol Chem 273 (15), 8549-8552 (1998)
   PUBMED   9535825
REFERENCE   9  (residues 1 to 897)
  AUTHORS   Matoba,R., Okubo,K., Hori,N., Fukushima,A. and Matsubara,K.
  TITLE     The addition of 5'-coding information to a 3'-directed cDNA library
            improves analysis of gene expression
  JOURNAL   Gene 146 (2), 199-207 (1994)
   PUBMED   8076819
REFERENCE   10 (residues 1 to 897)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091147.15, BG723261.1 and
            AF043431.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a ubiquitously
            expressed nuclear protein. It is found among several proteins that
            bind directly to retinoblastoma protein, which regulates cell
            proliferation. This protein complexes with transcriptional
            co-repressor CTBP. It is also associated with BRCA1 and is thought
            to modulate the functions of BRCA1 in transcriptional regulation,
            DNA repair, and/or cell cycle checkpoint control. It is suggested
            that this gene may itself be a tumor suppressor acting in the same
            pathway as BRCA1. Three transcript variants encoding two different
            isoforms have been found for this gene. More transcript variants
            exist, but their full-length natures have not been determined.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1 and 2 both encode isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U72066.1, SRR1803612.200164.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000327155.10/ ENSP00000323050.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..897
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q11.2"
     Protein         1..897
                     /product="DNA endonuclease RBBP8 isoform a"
                     /note="CTBP-interacting protein; DNA endonuclease RBBP8;
                     sporulation in the absence of SPO11 protein 2 homolog;
                     retinoblastoma binding protein 8"
                     /calculated_mol_wt=101811
     Region          20..139
                     /region_name="CtIP_N"
                     /note="Tumour-suppressor protein CtIP N-terminal domain;
                     pfam10482"
                     /db_xref="CDD:463107"
     Region          22..45
                     /region_name="Essential for binding to the MRN complex and
                     for RPA focus formation on DNA damage"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99708.2)"
     Region          45..160
                     /region_name="Required for interaction with LMO4, probably
                     by stabilizing the interaction through RPPB8 dimerization.
                     /evidence=ECO:0000269|PubMed:23353824"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99708.2)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99708.2)"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23623683; propagated from
                     UniProtKB/Swiss-Prot (Q99708.2)"
     Region          292..325
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99708.2)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK2.
                     /evidence=ECO:0000269|PubMed:23623683,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99708.2)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17965729; propagated from
                     UniProtKB/Swiss-Prot (Q99708.2)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15485915,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99708.2)"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17965729; propagated from
                     UniProtKB/Swiss-Prot (Q99708.2)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99708.2)"
     Region          419..464
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99708.2)"
     Region          490..494
                     /region_name="PXDLS motif.
                     /evidence=ECO:0000269|PubMed:9535825"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99708.2)"
     Region          509..557
                     /region_name="Damage-recruitment motif.
                     /evidence=ECO:0000269|PubMed:20064462"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99708.2)"
     Region          641..685
                     /region_name="Required for interaction with LMO4, probably
                     by making physical contact with LMO4.
                     /evidence=ECO:0000269|PubMed:23353824"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99708.2)"
     Site            664
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM.
                     /evidence=ECO:0000269|PubMed:10910365; propagated from
                     UniProtKB/Swiss-Prot (Q99708.2)"
     Site            679
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17965729; propagated from
                     UniProtKB/Swiss-Prot (Q99708.2)"
     Region          704..723
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99708.2)"
     Site            723
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99708.2)"
     Site            745
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM.
                     /evidence=ECO:0000269|PubMed:10910365; propagated from
                     UniProtKB/Swiss-Prot (Q99708.2)"
     Region          797..860
                     /region_name="SAE2"
                     /note="DNA endonuclease activator SAE2/CtIP C-terminus;
                     pfam08573"
                     /db_xref="CDD:462525"
     Region          840..842
                     /region_name="KLHL15-binding.
                     /evidence=ECO:0000269|PubMed:27561354"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99708.2)"
     Site            847
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000269|PubMed:27814491,
                     ECO:0000269|PubMed:33836577; propagated from
                     UniProtKB/Swiss-Prot (Q99708.2)"
     Site            859
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by ATR.
                     /evidence=ECO:0000269|PubMed:19202191,
                     ECO:0000269|PubMed:23273981, ECO:0000269|PubMed:27814491,
                     ECO:0000269|PubMed:27889449, ECO:0000269|PubMed:33836577;
                     propagated from UniProtKB/Swiss-Prot (Q99708.2)"
     Region          873..897
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99708.2)"
     CDS             1..897
                     /gene="RBBP8"
                     /gene_synonym="COM1; CTIP; JAWAD; JWDS; RIM; SAE2; SCKL2"
                     /coded_by="NM_002894.3:336..3029"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11875.1"
                     /db_xref="GeneID:5932"
                     /db_xref="HGNC:HGNC:9891"
                     /db_xref="MIM:604124"
ORIGIN      
        1 mnisgsscgs pnsadtssdf kdlwtklkec hdrevqglqv kvtklkqeri ldaqrleeff
       61 tknqqlreqq kvlhetikvl edrlraglcd rcavteehmr kkqqefenir qqnlklitel
      121 mnerntlqee nkklseqlqq kiendqqhqa aeleceedvi pdspitafsf sgvnrlrrke
      181 nphvryieqt htklehsvca nemrkvskss thpqhnpnen eilvadtydq sqspmakahg
      241 tssytpdkss fnlatvvaet lglgvqeese tqgpmsplgd elyhclegnh kkqpfeestr
      301 ntedslrfsd stsktppqee lptrvsspvf gatssiksgl dlntslspsl lqpgkkkhlk
      361 tlpfsntcis rlektrskse dsalfthhsl gsevnkiiiq ssnkqilink niseslgeqn
      421 rteygkdsnt dkhleplksl ggrtskrkkt eeesehevsc pqasfdkena fpfpmdnqfs
      481 mngdcvmdkp ldlsdrfsai qrqeksqgse tsknkfrqvt lyealktipk gfsssrkasd
      541 gnctlpkdsp gepcsqecii lqplnkcspd nkpslqikee navfkiplrp resletenvl
      601 ddiksagshe pikiqtrsdh ggcelasvlq lnpcrtgkik slqnnqdvsf eniqwsidpg
      661 adlsqykmdv tvidtkdgsq sklggetvdm dctlvsetvl lkmkkqeqkg ekssneerkm
      721 ndsledmfdr ttheeyescl adsfsqaade eeelstatkk lhthgdkqdk vkqkafvepy
      781 fkgderetsl qnfphievvr kkeerrkllg htckeceiyy admpaeerek klascsrhrf
      841 ryippntpen fwevgfpstq tcmergyike dldpcprpkr rqpynaifsp kgkeqkt
//
