Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA endonuclease RBBP8

Gene

Rbbp8

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in processing meiotic and mitotic double-strand breaks (DSBs) by ensuring both resection and intrachromosomal association of the broken ends. Functions downstream of the MRN complex and ATM, promotes ATR activation and its recruitment to DSBs in the S/G2 phase facilitating the generation of ssDNA. Component of the BRCA1-RBBP8 complex that regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage. Promotes microhomology-mediated alternative end joining (A-NHEJ) during class-switch recombination and plays an essential role in chromosomal translocations.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Cell cycle, Cell division, DNA damage, DNA repair, Meiosis, Mitosis

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-RNO-5685938. HDR through Single Strand Annealing (SSA).
R-RNO-5685939. HDR through MMEJ (alt-NHEJ).
R-RNO-5685942. HDR through Homologous Recombination (HRR).
R-RNO-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-RNO-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-RNO-5693579. Homologous DNA Pairing and Strand Exchange.
R-RNO-5693607. Processing of DNA double-strand break ends.
R-RNO-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-RNO-6804756. Regulation of TP53 Activity through Phosphorylation.
R-RNO-69473. G2/M DNA damage checkpoint.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA endonuclease RBBP8 (EC:3.1.-.-)
Alternative name(s):
CtBP-interacting protein
Short name:
CtIP
Retinoblastoma-binding protein 8
Short name:
RBBP-8
Retinoblastoma-interacting protein and myosin-like
Short name:
RIM
Sporulation in the absence of SPO11 protein 2 homolog
Short name:
SAE2
Gene namesi
Name:Rbbp8
Synonyms:Ctip
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 18

Organism-specific databases

RGDi1308872. Rbbp8.

Subcellular locationi

  • Nucleus By similarity
  • Chromosome By similarity

  • Note: Associates with sites of DNA damage in S/G2 phase. Ubiquitinated RBBP8 binds to chromatin following DNA damage.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004170371 – 893DNA endonuclease RBBP8Add BLAST893

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki193Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei233PhosphoserineBy similarity1
Modified residuei325PhosphoserineBy similarity1
Modified residuei326PhosphoserineBy similarity1
Modified residuei348PhosphoserineBy similarity1
Cross-linki377Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei378PhosphoserineBy similarity1
Modified residuei431N6-acetyllysineBy similarity1
Modified residuei525N6-acetyllysineBy similarity1
Modified residuei602N6-acetyllysine; alternateBy similarity1
Cross-linki602Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki611Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei662Phosphoserine; by ATMBy similarity1
Modified residuei677PhosphoserineBy similarity1
Modified residuei720PhosphoserineBy similarity1
Modified residuei742Phosphoserine; by ATMBy similarity1
Modified residuei843Phosphothreonine; by CDK1By similarity1
Cross-linki865Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Post-translational modificationi

Acetylated. Deacetylation by SIRT6 upon DNA damage promotes DNA end resection.By similarity
Hyperphosphorylation upon ionizing radiation results in dissociation from BRCA1. Phosphorylation at Thr-843 by CDK1 is essential for the recruitment to DNA and the DNA repair function. Phosphorylated on Ser-326 as cells enter G2 phase. This phosphorylation is required for binding BRCA1 and for the G2/M DNA damage transition checkpoint control (By similarity).By similarity
Ubiquitinated. Ubiquitination at multiple sites by BRCA1 (via its N-terminal RING domain) does not lead to its proteosomal degradation but instead the ubiquitinated RBBP8 binds to chromatin following DNA damage and may play a role in G2/M checkpoint control. Ubiquitinated by RNF138 at its N-terminus.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiB1WC58.
PRIDEiB1WC58.

Expressioni

Gene expression databases

BgeeiENSRNOG00000012899.
ExpressionAtlasiB1WC58. baseline and differential.
GenevisibleiB1WC58. RN.

Interactioni

Subunit structurei

Homodimer; dimerizes via the coiled coil domain. Interacts (via the PXDLS motif) with CTBP1. Component of the BRCA1-RBBP8 complex. Interacts (the Ser-326 phosphorylated form) with BRCA1 (via the C-terminal BRCA1 domains): the interaction occurs in the G2 phase, ubiquitinates RBBP8 and involves RBBP8 in BRCA1-dependent G2/M checkpoint control on DNA damage. Interacts with RB1. Interacts with the MRN complex. Interacts directly with MRE11A; the interaction is required for efficient homologous recombination (HR) and regulation of the MRN complex. Interacts directly with RAD50. Interacts directly with NBN. Interacts with SIRT6; the interaction deacetylates RBBP8 upon DNA damage. Interacts with LM04 (via the LIM zinc-binding 1 domain). Interacts with SIAH1. Interacts with RNF138. Interacts with EXD2 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000017291.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni22 – 45Essential for binding to the MRN complex and for RPA focus formation on DNA damageBy similarityAdd BLAST24
Regioni489 – 493PXDLS motif5
Regioni508 – 556Damage-recruitment motifBy similarityAdd BLAST49

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili54 – 147Sequence analysisAdd BLAST94

Domaini

The damage-recruitment motif is required for DNA binding and translocation to sites of DNA damage.By similarity
The PXDLS motif binds to a cleft in CtBP proteins.By similarity

Sequence similaritiesi

Belongs to the COM1/SAE2/CtIP family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IJ39. Eukaryota.
ENOG410ZSBE. LUCA.
GeneTreeiENSGT00530000063835.
HOGENOMiHOG000293331.
HOVERGENiHBG057046.
InParanoidiB1WC58.
KOiK20773.
OMAiETVDMDC.
OrthoDBiEOG091G0QP3.
PhylomeDBiB1WC58.
TreeFamiTF106469.

Family and domain databases

InterProiIPR019518. CtIP_N.
IPR013882. Ctp1_C.
IPR033594. RBBP8.
IPR033316. RBBP8-like.
[Graphical view]
PANTHERiPTHR15107. PTHR15107. 3 hits.
PTHR15107:SF4. PTHR15107:SF4. 3 hits.
PfamiPF10482. CtIP_N. 1 hit.
PF08573. SAE2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B1WC58-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSISGSSCGS PNSTDISSDF KELWTKLKEY HDKEVQGLQI KVTKLKKERI
60 70 80 90 100
LDAQRLEEFF TKNQQLRDQQ KVLQETIKIL EDRLRAGLCD RCAVTEEHMH
110 120 130 140 150
KKQQEFENIR QQNLRLITEL MNEKSALQEE NKKLSEQLQQ KMESGQQDQV
160 170 180 190 200
AELECEENII PDSPITSFSF SGINRLRRKE NLHVRYVEQT HTKLEHSACT
210 220 230 240 250
SELRKFSKGS TPAPVNSEEH EILVADTCDQ SHSPLSKICG TSSYPADKLS
260 270 280 290 300
SNLDAVVAET LGLDGQEESE PQGPVSPLGN ELYHCLKEDH KKQPFMESAI
310 320 330 340 350
RNEDNVRFSD SASKAPPREL TTRGSSPVFG PTSTVKTHLG LKTSFSPSLL
360 370 380 390 400
DSGKKNLLST APFSSISVSR SEKVRSKSED NALFTQQSAG SEVKVISQSF
410 420 430 440 450
PSKQILTSKN VSDSVDEQGG ADHMKDAVSD KHLVPLKSLG GKASKRKRTE
460 470 480 490 500
EEGEHAVHCP QTCFDKENAL PFPMENQFPV NGDHVMDKPL DLSDRFAANQ
510 520 530 540 550
RQEKNHGDET CKHKLKQVTI YEALKPVPKG SSSGRKALSG ACTLAQDSAE
560 570 580 590 600
TYCLQQRTLQ CSSKFSPDHN TQLQIKEENP VFKTPPRSQE SLETENLFGD
610 620 630 640 650
VKGIGSLVPI KVKGRSAHGG CELASVLQLN PCRVAKTKSL PSNHDMSFEN
660 670 680 690 700
IQWSVDPGAD LSQYKMDVTV IDTKDSSHSR LGGETVDMDC TLVSETMLLK
710 720 730 740 750
MKKQEQREKS PNGDIKMNDS LEDMFDRTTH EEYESCLADN FSQVPDEEEL
760 770 780 790 800
SDTTKKPNIH GDKQDGIKQK AFVEPYFKDK ERETSIQNFP HIEVVRKKEE
810 820 830 840 850
RRKLLGHTCK ECEIYYADLP AEEREKKLAS CSRHRFRYIP TNTPENFWEV
860 870 880 890
GFPSTQTCLE RGYIKEDLDP CPRPKRRQPY NAVFSPKGKE QRT
Length:893
Mass (Da):100,705
Last modified:May 20, 2008 - v1
Checksum:i57A4189635AA5F9B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC162012 mRNA. Translation: AAI62012.1.
RefSeqiNP_001127889.1. NM_001134417.1.
XP_008770161.2. XM_008771939.2.
UniGeneiRn.128724.

Genome annotation databases

EnsembliENSRNOT00000017291; ENSRNOP00000017291; ENSRNOG00000012899.
GeneIDi291787.
KEGGirno:291787.
UCSCiRGD:1308872. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC162012 mRNA. Translation: AAI62012.1.
RefSeqiNP_001127889.1. NM_001134417.1.
XP_008770161.2. XM_008771939.2.
UniGeneiRn.128724.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000017291.

Proteomic databases

PaxDbiB1WC58.
PRIDEiB1WC58.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000017291; ENSRNOP00000017291; ENSRNOG00000012899.
GeneIDi291787.
KEGGirno:291787.
UCSCiRGD:1308872. rat.

Organism-specific databases

CTDi5932.
RGDi1308872. Rbbp8.

Phylogenomic databases

eggNOGiENOG410IJ39. Eukaryota.
ENOG410ZSBE. LUCA.
GeneTreeiENSGT00530000063835.
HOGENOMiHOG000293331.
HOVERGENiHBG057046.
InParanoidiB1WC58.
KOiK20773.
OMAiETVDMDC.
OrthoDBiEOG091G0QP3.
PhylomeDBiB1WC58.
TreeFamiTF106469.

Enzyme and pathway databases

ReactomeiR-RNO-5685938. HDR through Single Strand Annealing (SSA).
R-RNO-5685939. HDR through MMEJ (alt-NHEJ).
R-RNO-5685942. HDR through Homologous Recombination (HRR).
R-RNO-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-RNO-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-RNO-5693579. Homologous DNA Pairing and Strand Exchange.
R-RNO-5693607. Processing of DNA double-strand break ends.
R-RNO-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-RNO-6804756. Regulation of TP53 Activity through Phosphorylation.
R-RNO-69473. G2/M DNA damage checkpoint.

Miscellaneous databases

PROiB1WC58.

Gene expression databases

BgeeiENSRNOG00000012899.
ExpressionAtlasiB1WC58. baseline and differential.
GenevisibleiB1WC58. RN.

Family and domain databases

InterProiIPR019518. CtIP_N.
IPR013882. Ctp1_C.
IPR033594. RBBP8.
IPR033316. RBBP8-like.
[Graphical view]
PANTHERiPTHR15107. PTHR15107. 3 hits.
PTHR15107:SF4. PTHR15107:SF4. 3 hits.
PfamiPF10482. CtIP_N. 1 hit.
PF08573. SAE2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCOM1_RAT
AccessioniPrimary (citable) accession number: B1WC58
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2012
Last sequence update: May 20, 2008
Last modified: November 30, 2016
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.