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DNA endonuclease RBBP8 (EC 3.1.-.-) (CtBP-interacting protein) (CtIP) (Retinoblastoma-binding protein 8) (RBBP-8) (Retinoblastoma-interacting protein and myosin-like) (RIM) (Sporulation in the absence of SPO11 protein 2 homolog) (SAE2)

 CTIP_HUMAN              Reviewed;         897 AA.
Q99708; A6NKN2; A8K8W6; E7ETY1; O75371; Q8NHQ3;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
22-NOV-2017, entry version 167.
RecName: Full=DNA endonuclease RBBP8;
EC=3.1.-.-;
AltName: Full=CtBP-interacting protein;
Short=CtIP;
AltName: Full=Retinoblastoma-binding protein 8;
Short=RBBP-8;
AltName: Full=Retinoblastoma-interacting protein and myosin-like;
Short=RIM;
AltName: Full=Sporulation in the absence of SPO11 protein 2 homolog;
Short=SAE2;
Name=RBBP8; Synonyms=CTIP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH RB1.
PubMed=9721205; DOI=10.1006/geno.1998.5368;
Fusco C., Reymond A., Zervos A.S.;
"Molecular cloning and characterization of a novel retinoblastoma-
binding protein.";
Genomics 51:351-358(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH CTBP1.
PubMed=9535825; DOI=10.1074/jbc.273.15.8549;
Schaeper U., Subramanian T., Lim L., Boyd J.M., Chinnadurai G.;
"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.";
J. Biol. Chem. 273:8549-8552(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Endometrial cancer;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16177791; DOI=10.1038/nature03983;
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BRCA1.
PubMed=10764811; DOI=10.1074/jbc.M909494199;
Yu X., Baer R.;
"Nuclear localization and cell cycle-specific expression of CtIP, a
protein that associates with the BRCA1 tumor suppressor.";
J. Biol. Chem. 275:18541-18549(2000).
[9]
FUNCTION, PHOSPHORYLATION AT SER-664 AND SER-745, AND MUTAGENESIS OF
SER-664 AND SER-745.
PubMed=10910365; DOI=10.1038/35018134;
Li S., Ting N.S.Y., Zheng L., Chen P.-L., Ziv Y., Shiloh Y.,
Lee E.Y.-H.P., Lee W.-H.;
"Functional link of BRCA1 and ataxia telangiectasia gene product in
DNA damage response.";
Nature 406:210-215(2000).
[10]
INTERACTION WITH LMO4.
PubMed=11751867; DOI=10.1074/jbc.M110603200;
Sum E.Y., Peng B., Yu X., Chen J., Byrne J., Lindeman G.J.,
Visvader J.E.;
"The LIM domain protein LMO4 interacts with the cofactor CtIP and the
tumor suppressor BRCA1 and inhibits BRCA1 activity.";
J. Biol. Chem. 277:7849-7856(2002).
[11]
INTERACTION WITH SIAH1, AND UBIQUITINATION.
PubMed=14654780; DOI=10.1038/sj.onc.1206994;
Germani A., Prabel A., Mourah S., Podgorniak M.-P., Di Carlo A.,
Ehrlich R., Gisselbrecht S., Varin-Blank N., Calvo F.,
Bruzzoni-Giovanelli H.;
"SIAH-1 interacts with CtIP and promotes its degradation by the
proteasome pathway.";
Oncogene 22:8845-8851(2003).
[12]
SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15084581; DOI=10.1074/jbc.M313974200;
Dubin M.J., Stokes P.H., Sum E.Y., Williams R.S., Valova V.A.,
Robinson P.J., Lindeman G.J., Glover J.N., Visvader J.E.,
Matthews J.M.;
"Dimerization of CtIP, a BRCA1- and CtBP-interacting protein, is
mediated by an N-terminal coiled-coil motif.";
J. Biol. Chem. 279:26932-26938(2004).
[13]
FUNCTION, PHOSPHORYLATION AT SER-327, INTERACTION WITH BRCA1, AND
MUTAGENESIS OF SER-327.
PubMed=15485915; DOI=10.1128/MCB.24.21.9478-9486.2004;
Yu X., Chen J.;
"DNA damage-induced cell cycle checkpoint control requires CtIP, a
phosphorylation-dependent binding partner of BRCA1 C-terminal
domains.";
Mol. Cell. Biol. 24:9478-9486(2004).
[14]
INTERACTION WITH BRCA1, FUNCTION, SUBCELLULAR LOCATION,
UBIQUITINATION, AND MUTAGENESIS OF SER-327.
PubMed=16818604; DOI=10.1101/gad.1431006;
Yu X., Fu S., Lai M., Baer R., Chen J.;
"BRCA1 ubiquitinates its phosphorylation-dependent binding partner
CtIP.";
Genes Dev. 20:1721-1726(2006).
[15]
FUNCTION.
PubMed=16581787; DOI=10.1128/MCB.26.8.3124-3134.2006;
Liu F., Lee W.H.;
"CtIP activates its own and cyclin D1 promoters via the E2F/RB pathway
during G1/S progression.";
Mol. Cell. Biol. 26:3124-3134(2006).
[16]
DISEASE, AND TISSUE SPECIFICITY.
PubMed=18171986; DOI=10.1158/1541-7786.MCR-07-0126;
Wu M., Soler D.R., Abba M.C., Nunez M.I., Baer R., Hatzis C.,
Llombart-Cussac A., Llombart-Bosch A., Aldaz C.M.;
"CtIP silencing as a novel mechanism of tamoxifen resistance in breast
cancer.";
Mol. Cancer Res. 5:1285-1295(2007).
[17]
FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND INTERACTION WITH
BRCA1; MRE11 AND RAD50.
PubMed=17965729; DOI=10.1038/nature06337;
Sartori A.A., Lukas C., Coates J., Mistrik M., Fu S., Bartek J.,
Baer R., Lukas J., Jackson S.P.;
"Human CtIP promotes DNA end resection.";
Nature 450:509-514(2007).
[18]
ASSOCIATION WITH OVARIAN CANCER SURVIVAL.
PubMed=19270026; DOI=10.1093/hmg/ddp107;
Quaye L., Dafou D., Ramus S.J., Song H., Gentry-Maharaj A.,
Notaridou M., Hogdall E., Kjaer S.K., Christensen L., Hogdall C.,
Easton D.F., Jacobs I., Menon U., Pharoah P.D., Gayther S.A.;
"Functional complementation studies identify candidate genes and
common genetic variants associated with ovarian cancer survival.";
Hum. Mol. Genet. 18:1869-1878(2009).
[19]
FUNCTION, DNA-BINDING, PHOSPHORYLATION AT THR-847, AND MUTAGENESIS OF
THR-847.
PubMed=19202191; DOI=10.1074/jbc.M808906200;
Huertas P., Jackson S.P.;
"Human CtIP mediates cell cycle control of DNA end resection and
double strand break repair.";
J. Biol. Chem. 284:9558-9565(2009).
[20]
FUNCTION, INTERACTION WITH MRE11; RAD50 AND NBN, AND MUTAGENESIS OF
HIS-31; VAL-35; LYS-41 AND LEU-45.
PubMed=19759395; DOI=10.1074/jbc.M109.023424;
Yuan J., Chen J.;
"N terminus of CtIP is critical for homologous recombination-mediated
double-strand break repair.";
J. Biol. Chem. 284:31746-31752(2009).
[21]
FUNCTION, AND MUTAGENESIS OF LYS-513 AND LYS-515.
PubMed=20064462; DOI=10.1016/j.molcel.2009.12.002;
You Z., Shi L.Z., Zhu Q., Wu P., Zhang Y.W., Basilio A., Tonnu N.,
Verma I.M., Berns M.W., Hunter T.;
"CtIP links DNA double-strand break sensing to resection.";
Mol. Cell 36:954-969(2009).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[24]
FUNCTION, ACETYLATION AT LYS-432; LYS-526 AND LYS-604, INTERACTION
WITH SIRT6, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF
LYS-432; LYS-526 AND LYS-604.
PubMed=20829486; DOI=10.1126/science.1192049;
Kaidi A., Weinert B.T., Choudhary C., Jackson S.P.;
"Human SIRT6 promotes DNA end resection through CtIP deacetylation.";
Science 329:1348-1353(2010).
[25]
ASSOCIATION WITH BREAST CANCER.
PubMed=21799032; DOI=10.1158/0008-5472.CAN-11-0773;
Rebbeck T.R., Mitra N., Domchek S.M., Wan F., Friebel T.M., Tran T.V.,
Singer C.F., Tea M.K., Blum J.L., Tung N., Olopade O.I., Weitzel J.N.,
Lynch H.T., Snyder C.L., Garber J.E., Antoniou A.C., Peock S.,
Evans D.G., Paterson J., Kennedy M.J., Donaldson A., Dorkins H.,
Easton D.F., Rubinstein W.S., Daly M.B., Isaacs C., Nevanlinna H.,
Couch F.J., Andrulis I.L., Freidman E., Laitman Y., Ganz P.A.,
Tomlinson G.E., Neuhausen S.L., Narod S.A., Phelan C.M., Greenberg R.,
Nathanson K.L.;
"Modification of BRCA1-associated breast and ovarian cancer risk by
BRCA1-interacting genes.";
Cancer Res. 71:5792-5805(2011).
[26]
INVOLVEMENT IN JWDS, AND INVOLVEMENT IN SCKL2.
PubMed=21998596; DOI=10.1371/journal.pgen.1002310;
Jackson S.P., Borglum A.D.;
"CtIP mutations cause Seckel and Jawad syndromes.";
PLoS Genet. 7:E1002310-E1002310(2011).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; THR-315; SER-327;
SER-379 AND SER-723, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[28]
INTERACTION WITH BRCA1; MRE11 AND PIN1, SUBCELLULAR LOCATION,
MUTAGENESIS OF SER-276 AND THR-315, AND PHOSPHORYLATION AT SER-276 AND
THR-315.
PubMed=23623683; DOI=10.1016/j.molcel.2013.03.023;
Steger M., Murina O., Huehn D., Ferretti L.P., Walser R., Haenggi K.,
Lafranchi L., Neugebauer C., Paliwal S., Janscak P., Gerrits B.,
Del Sal G., Zerbe O., Sartori A.A.;
"Prolyl isomerase PIN1 regulates DNA double-strand break repair by
counteracting DNA end resection.";
Mol. Cell 50:333-343(2013).
[29]
INTERACTION WITH FZR1, SUBCELLULAR LOCATION, INDUCTION DURING THE CELL
CYCLE, AND MUTAGENESIS OF LYS-179 AND LYS-467.
PubMed=25349192; DOI=10.15252/embj.201489017;
Lafranchi L., de Boer H.R., de Vries E.G., Ong S.E., Sartori A.A.,
van Vugt M.A.;
"APC/C(Cdh1) controls CtIP stability during the cell cycle and in
response to DNA damage.";
EMBO J. 33:2860-2879(2014).
[30]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-869, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[31]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-193; LYS-378; LYS-604;
LYS-613 AND LYS-869, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[32]
INTERACTION WITH CUL3 AND KLHL15, UBIQUITINATION, AND MUTAGENESIS OF
SER-276; THR-315; LYS-467; ARG-839; PHE-840 AND TYR-842.
PubMed=27561354; DOI=10.1038/ncomms12628;
Ferretti L.P., Himmels S.F., Trenner A., Walker C., von Aesch C.,
Eggenschwiler A., Murina O., Enchev R.I., Peter M., Freire R.,
Porro A., Sartori A.A.;
"Cullin3-KLHL15 ubiquitin ligase mediates CtIP protein turnover to
fine-tune DNA-end resection.";
Nat. Commun. 7:12628-12628(2016).
[33]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-62; LYS-115; LYS-193;
LYS-360; LYS-378; LYS-396; LYS-404; LYS-410; LYS-438; LYS-449;
LYS-526; LYS-530; LYS-572; LYS-578; LYS-604; LYS-613; LYS-638;
LYS-640; LYS-676; LYS-719; LYS-782 AND LYS-869, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[34]
VARIANT SCKL2 TRP-100.
PubMed=24389050; DOI=10.1101/gr.160572.113;
Shaheen R., Faqeih E., Ansari S., Abdel-Salam G., Al-Hassnan Z.N.,
Al-Shidi T., Alomar R., Sogaty S., Alkuraya F.S.;
"Genomic analysis of primordial dwarfism reveals novel disease
genes.";
Genome Res. 24:291-299(2014).
[35]
UBIQUITINATION, INTERACTION WITH RNF138, AND MUTAGENESIS OF LYS-62;
LYS-78; LYS-115; LYS-132; LYS-133; LYS-404; LYS-572; LYS-578; LYS-640;
LYS-759; LYS-760 AND LYS-782.
PubMed=26502057; DOI=10.1038/ncb3260;
Schmidt C.K., Galanty Y., Sczaniecka-Clift M., Coates J., Jhujh S.,
Demir M., Cornwell M., Beli P., Jackson S.P.;
"Systematic E2 screening reveals a UBE2D-RNF138-CtIP axis promoting
DNA repair.";
Nat. Cell Biol. 17:1458-1470(2015).
[36]
INTERACTION WITH EXD2.
PubMed=26807646; DOI=10.1038/ncb3303;
Broderick R., Nieminuszczy J., Baddock H.T., Deshpande R.A.,
Gileadi O., Paull T.T., McHugh P.J., Niedzwiedz W.;
"EXD2 promotes homologous recombination by facilitating DNA end
resection.";
Nat. Cell Biol. 18:271-280(2016).
-!- FUNCTION: Endonuclease that cooperates with the MRE11-RAD50-NBN
(MRN) complex in DNA-end resection, the first step of double-
strand break (DSB) repair through the homologous recombination
(HR) pathway. HR is restricted to S and G2 phases of the cell
cycle and preferentially repairs DSBs resulting from replication
fork collapse. Key determinant of DSB repair pathway choice, as it
commits cells to HR by preventing classical non-homologous end-
joining (NHEJ). 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 (PubMed:10764811,
PubMed:10910365, PubMed:15485915, PubMed:16581787,
PubMed:16818604, PubMed:17965729, PubMed:19202191,
PubMed:19759395, PubMed:20064462, PubMed:20829486). During
immunoglobulin heavy chain class-switch recombination, promotes
microhomology-mediated alternative end joining (A-NHEJ) and plays
an essential role in chromosomal translocations (By similarity).
{ECO:0000250|UniProtKB:Q80YR6, ECO:0000269|PubMed:10764811,
ECO:0000269|PubMed:10910365, ECO:0000269|PubMed:15485915,
ECO:0000269|PubMed:16581787, ECO:0000269|PubMed:16818604,
ECO:0000269|PubMed:17965729, ECO:0000269|PubMed:19202191,
ECO:0000269|PubMed:19759395, ECO:0000269|PubMed:20064462,
ECO:0000269|PubMed:20829486}.
-!- SUBUNIT: Homodimer; dimerizes via the coiled coil domain
(PubMed:15084581). Interacts (via the PXDLS motif) with CTBP1; the
interaction is disrupted via binding of the adenovirus E1A to
CTBP1 (PubMed:9535825). Component of the BRCA1-RBBP8 complex.
Interacts (the Ser-327 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 (PubMed:10764811,
PubMed:15485915, PubMed:16818604, PubMed:17965729,
PubMed:23623683). Interacts with RB1 (PubMed:9721205). Interacts
with the MRN complex. Interacts directly with MRE11; the
interaction is required for efficient homologous recombination
(HR) and regulation of the MRN complex (PubMed:19759395,
PubMed:23623683). Interacts directly with RAD50 (PubMed:19759395).
Interacts directly with NBN (PubMed:19759395). Interacts with
SIRT6; the interaction deacetylates RBBP8 upon DNA damage
(PubMed:20829486). Interacts with LM04 (via the LIM zinc-binding 1
domain) (PubMed:11751867). Interacts with SIAH1 (PubMed:14654780).
Interacts with RNF138 (PubMed:26502057). Interacts with EXD2
(PubMed:26807646). Interacts with CUL3 and KLHL15; this
interaction leads to RBBP8 proteasomal degradation
(PubMed:27561354). Directly interacts with PIN1; this interaction
depends upon RBBP8 phosphorylation, predominantly at Thr-315
(PubMed:23623683). Interacts with FZR1; this interaction leads to
APC/C-mediated RBBP8 proteasomal degradation (PubMed:25349192).
{ECO:0000269|PubMed:10764811, ECO:0000269|PubMed:11751867,
ECO:0000269|PubMed:14654780, ECO:0000269|PubMed:15084581,
ECO:0000269|PubMed:15485915, ECO:0000269|PubMed:16818604,
ECO:0000269|PubMed:17965729, ECO:0000269|PubMed:19759395,
ECO:0000269|PubMed:20829486, ECO:0000269|PubMed:23623683,
ECO:0000269|PubMed:25349192, ECO:0000269|PubMed:26502057,
ECO:0000269|PubMed:26807646, ECO:0000269|PubMed:27561354,
ECO:0000269|PubMed:9535825, ECO:0000269|PubMed:9721205}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-745715, EBI-745715;
P38398:BRCA1; NbExp=10; IntAct=EBI-745715, EBI-349905;
Q9NVH0:EXD2; NbExp=3; IntAct=EBI-745715, EBI-11324738;
Q9UQ84:EXO1; NbExp=4; IntAct=EBI-745715, EBI-944667;
P25800:LMO1; NbExp=3; IntAct=EBI-10203615, EBI-8639312;
P61968:LMO4; NbExp=3; IntAct=EBI-10203615, EBI-2798728;
P49959:MRE11; NbExp=3; IntAct=EBI-745715, EBI-396513;
O60934:NBN; NbExp=2; IntAct=EBI-745715, EBI-494844;
Q13526:PIN1; NbExp=3; IntAct=EBI-10203615, EBI-714158;
O75475:PSIP1; NbExp=4; IntAct=EBI-745715, EBI-1801773;
P06400:RB1; NbExp=2; IntAct=EBI-745715, EBI-491274;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10764811,
ECO:0000269|PubMed:17965729, ECO:0000269|PubMed:23623683}.
Chromosome {ECO:0000269|PubMed:10764811,
ECO:0000269|PubMed:16818604}. Note=Associates with sites of DNA
damage in S/G2 phase (PubMed:10764811, Ref.29). Ubiquitinated
RBBP8 binds to chromatin following DNA damage (PubMed:16818604).
{ECO:0000269|PubMed:10764811, ECO:0000269|PubMed:16818604,
ECO:0000269|PubMed:25349192}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q99708-1; Sequence=Displayed;
Name=2;
IsoId=Q99708-2; Sequence=VSP_043220;
Name=3;
IsoId=Q99708-3; Sequence=VSP_045247, VSP_045248;
Note=No experimental confirmation available. Ref.4 (BX648221)
sequence is in conflict in position: 862:S->G. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in ER-positive breast cancer lines,
but tends to be down-regulated ER-negative cells (at protein
level). {ECO:0000269|PubMed:18171986}.
-!- INDUCTION: Expression is cell-cycle regulated. Levels increase as
dividing cells traverse the G1/S boundary (PubMed:18171986). The
protein is degraded by the proteasome pathway during mitotic exit.
Also degraded in response to DNA damage in G2 cells; this
degradation is mediated by the E3 FZR1/APC/C complex
(PubMed:25349192). {ECO:0000269|PubMed:18171986,
ECO:0000269|PubMed:25349192}.
-!- DOMAIN: The PXDLS motif binds to a cleft in CtBP proteins.
-!- DOMAIN: The damage-recruitment motif is required for DNA binding
and translocation to sites of DNA damage.
-!- PTM: Acetylated. Deacetylation by SIRT6 upon DNA damage promotes
DNA end resection. {ECO:0000269|PubMed:20829486}.
-!- PTM: Hyperphosphorylation upon ionizing radiation results in
dissociation from BRCA1. Phosphorylation at Thr-847 by CDK1 is
essential for the recruitment to DNA and the DNA repair function.
Phosphorylated on Ser-327 as cells enter G2 phase. This
phosphorylation is required for binding BRCA1 and for the G2/M DNA
damage transition checkpoint control. Phosphorylation at Thr-315,
probably catalyzed by CDK2, is required for PIN1-binding, while
phosphorylation at Ser-276 serves as a PIN1 isomerization site.
Phosphorylation at Thr-315 is cell-cycle dependent. It steadily
increases during S phase, peaks at late S/G2 phase, and drops at
G1 (PubMed:23623683). {ECO:0000269|PubMed:10910365,
ECO:0000269|PubMed:15485915, ECO:0000269|PubMed:17965729,
ECO:0000269|PubMed:19202191, ECO:0000269|PubMed:23623683}.
-!- PTM: Ubiquitinated (PubMed:14654780, PubMed:16818604,
PubMed:27561354). 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 (PubMed:16818604). Ubiquitinated by RNF138 at its N-
terminus (PubMed:26502057). Ubiquitinated through 'Lys-48' by the
E3 CUL3-KLHL15 complex; this modification leads to proteasomal
degradation (PubMed:27561354). Ubiquitinated by the E3 FZR1/APC/C
complex; this modification leads to proteasomal degradation
(PubMed:25349192). {ECO:0000269|PubMed:14654780,
ECO:0000269|PubMed:16818604, ECO:0000269|PubMed:25349192,
ECO:0000269|PubMed:26502057, ECO:0000269|PubMed:27561354}.
-!- DISEASE: Seckel syndrome 2 (SCKL2) [MIM:606744]: A rare autosomal
recessive disorder characterized by proportionate dwarfism of
prenatal onset associated with low birth weight, growth
retardation, severe microcephaly with a bird-headed like
appearance, and mental retardation. {ECO:0000269|PubMed:21998596,
ECO:0000269|PubMed:24389050}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Jawad syndrome (JWDS) [MIM:251255]: A syndrome
characterized by congenital microcephaly, moderately severe mental
retardation, and symmetrical digital anomalies. Digital
malformations of variable degree include hallux valgus, syndactyly
of toes 4 and 5, short fifth fingers, single flexion crease of
fifth fingers, polydactyly and synpolydactyly.
{ECO:0000269|PubMed:21998596}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=Genetic variability in RBBP8 is noted as a factor in
BRCA1-associated breast cancer risk (PubMed:21799032). Associated
with sensitivity to tamoxifen in certain breast cancer cell lines
(PubMed:18171986). {ECO:0000269|PubMed:18171986,
ECO:0000269|PubMed:21799032}.
-!- SIMILARITY: Belongs to the COM1/SAE2/CtIP family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RBBP8ID42066ch18q11.html";
-----------------------------------------------------------------------
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EMBL; AF043431; AAC34368.1; -; mRNA.
EMBL; U72066; AAC14371.1; -; mRNA.
EMBL; AK292481; BAF85170.1; -; mRNA.
EMBL; BX648221; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC091147; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC106033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471088; EAX01144.1; -; Genomic_DNA.
EMBL; BC030590; AAH30590.1; -; mRNA.
CCDS; CCDS11874.1; -. [Q99708-3]
CCDS; CCDS11875.1; -. [Q99708-1]
RefSeq; NP_002885.1; NM_002894.2. [Q99708-1]
RefSeq; NP_976036.1; NM_203291.1. [Q99708-1]
RefSeq; NP_976037.1; NM_203292.1. [Q99708-3]
RefSeq; XP_006722582.1; XM_006722519.2. [Q99708-1]
RefSeq; XP_006722583.1; XM_006722520.2. [Q99708-1]
RefSeq; XP_006722584.1; XM_006722521.2. [Q99708-1]
RefSeq; XP_011524434.1; XM_011526132.2. [Q99708-1]
UniGene; Hs.546282; -.
PDB; 2L4Z; NMR; -; A=641-685.
PDB; 4D2H; X-ray; 1.90 A; A/B/C/D/E/F/G/H=18-52.
PDBsum; 2L4Z; -.
PDBsum; 4D2H; -.
ProteinModelPortal; Q99708; -.
SMR; Q99708; -.
BioGrid; 111867; 61.
CORUM; Q99708; -.
DIP; DIP-24244N; -.
ELM; Q99708; -.
IntAct; Q99708; 42.
MINT; MINT-102295; -.
STRING; 9606.ENSP00000323050; -.
iPTMnet; Q99708; -.
PhosphoSitePlus; Q99708; -.
BioMuta; RBBP8; -.
DMDM; 116242745; -.
EPD; Q99708; -.
MaxQB; Q99708; -.
PaxDb; Q99708; -.
PeptideAtlas; Q99708; -.
PRIDE; Q99708; -.
DNASU; 5932; -.
Ensembl; ENST00000327155; ENSP00000323050; ENSG00000101773. [Q99708-1]
Ensembl; ENST00000399722; ENSP00000382628; ENSG00000101773. [Q99708-1]
Ensembl; ENST00000399725; ENSP00000382630; ENSG00000101773. [Q99708-3]
GeneID; 5932; -.
KEGG; hsa:5932; -.
UCSC; uc002ktw.4; human. [Q99708-1]
CTD; 5932; -.
DisGeNET; 5932; -.
EuPathDB; HostDB:ENSG00000101773.16; -.
GeneCards; RBBP8; -.
GeneReviews; RBBP8; -.
HGNC; HGNC:9891; RBBP8.
HPA; HPA039890; -.
HPA; HPA052946; -.
MalaCards; RBBP8; -.
MIM; 251255; phenotype.
MIM; 604124; gene.
MIM; 606744; phenotype.
neXtProt; NX_Q99708; -.
OpenTargets; ENSG00000101773; -.
Orphanet; 313795; Jawad syndrome.
Orphanet; 808; Seckel syndrome.
PharmGKB; PA34255; -.
eggNOG; ENOG410IJ39; Eukaryota.
eggNOG; ENOG410ZSBE; LUCA.
GeneTree; ENSGT00530000063835; -.
HOGENOM; HOG000293331; -.
HOVERGEN; HBG057046; -.
InParanoid; Q99708; -.
KO; K20773; -.
PhylomeDB; Q99708; -.
TreeFam; TF106469; -.
Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
Reactome; R-HSA-5685939; HDR through MMEJ (alt-NHEJ).
Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-HSA-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
Reactome; R-HSA-5693579; Homologous DNA Pairing and Strand Exchange.
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
Reactome; R-HSA-912446; Meiotic recombination.
SIGNOR; Q99708; -.
ChiTaRS; RBBP8; human.
EvolutionaryTrace; Q99708; -.
GeneWiki; RBBP8; -.
GenomeRNAi; 5932; -.
PRO; PR:Q99708; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000101773; -.
CleanEx; HS_RBBP8; -.
ExpressionAtlas; Q99708; baseline and differential.
Genevisible; Q99708; HS.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0017053; C:transcriptional repressor complex; IDA:BHF-UCL.
GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IPI:BHF-UCL.
GO; GO:0001106; F:RNA polymerase II transcription corepressor activity; IDA:BHF-UCL.
GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IMP:UniProtKB.
GO; GO:0001835; P:blastocyst hatching; IEA:Ensembl.
GO; GO:0000075; P:cell cycle checkpoint; TAS:ProtInc.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0000729; P:DNA double-strand break processing; TAS:Reactome.
GO; GO:0010792; P:DNA double-strand break processing involved in repair via single-strand annealing; IMP:UniProtKB.
GO; GO:0006281; P:DNA repair; TAS:ProtInc.
GO; GO:0006260; P:DNA replication; TAS:Reactome.
GO; GO:0000731; P:DNA synthesis involved in DNA repair; TAS:Reactome.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:UniProtKB.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0031572; P:G2 DNA damage checkpoint; IDA:UniProtKB.
GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
GO; GO:0006289; P:nucleotide-excision repair; IMP:CACAO.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0000732; P:strand displacement; TAS:Reactome.
InterPro; IPR019518; CtIP_N.
InterPro; IPR013882; Ctp1_C.
InterPro; IPR033594; RBBP8.
InterPro; IPR033316; RBBP8-like.
PANTHER; PTHR15107; PTHR15107; 1.
PANTHER; PTHR15107:SF4; PTHR15107:SF4; 1.
Pfam; PF10482; CtIP_N; 1.
Pfam; PF08573; SAE2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell cycle;
Cell division; Chromosome; Coiled coil; Complete proteome;
Disease mutation; DNA damage; DNA repair; DNA-binding; Dwarfism;
Endonuclease; Hydrolase; Isopeptide bond; Meiosis; Mental retardation;
Mitosis; Nuclease; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Ubl conjugation.
CHAIN 1 897 DNA endonuclease RBBP8.
/FTId=PRO_0000097179.
REGION 22 45 Essential for binding to the MRN complex
and for RPA focus formation on DNA
damage.
REGION 509 557 Damage-recruitment motif.
COILED 28 157 {ECO:0000255}.
MOTIF 490 494 PXDLS motif.
MOTIF 840 842 KLHL15-binding.
{ECO:0000269|PubMed:27561354}.
MOD_RES 233 233 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 276 276 Phosphoserine.
{ECO:0000269|PubMed:23623683}.
MOD_RES 315 315 Phosphothreonine; by CDK2.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:23623683}.
MOD_RES 326 326 Phosphoserine.
{ECO:0000269|PubMed:17965729}.
MOD_RES 327 327 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15485915}.
MOD_RES 349 349 Phosphoserine.
{ECO:0000269|PubMed:17965729}.
MOD_RES 379 379 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 432 432 N6-acetyllysine.
{ECO:0000269|PubMed:20829486}.
MOD_RES 526 526 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:20829486}.
MOD_RES 604 604 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:20829486}.
MOD_RES 664 664 Phosphoserine; by ATM.
{ECO:0000269|PubMed:10910365}.
MOD_RES 679 679 Phosphoserine.
{ECO:0000269|PubMed:17965729}.
MOD_RES 723 723 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 745 745 Phosphoserine; by ATM.
{ECO:0000269|PubMed:10910365}.
MOD_RES 847 847 Phosphothreonine; by CDK1.
{ECO:0000269|PubMed:19202191}.
CROSSLNK 62 62 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 115 115 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 193 193 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 360 360 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 378 378 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 396 396 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 404 404 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 410 410 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 438 438 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 449 449 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 526 526 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 530 530 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 572 572 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 578 578 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 604 604 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 613 613 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 638 638 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 640 640 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 676 676 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 719 719 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 782 782 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 869 869 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 714 714 S -> SMLFYI (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043220.
VAR_SEQ 786 867 RETSLQNFPHIEVVRKKEERRKLLGHTCKECEIYYADMPAE
EREKKLASCSRHRFRYIPPNTPENFWEVGFPSTQTCMERGY
-> SIMQICQQKKEKRNWLPAQDTDSATFHPTHQRIFGKLV
FLPLRLVWKEVILRKILILVLVQKDVSLTTQYFLQKARSRR
HRR (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_045247.
VAR_SEQ 868 897 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_045248.
VARIANT 100 100 R -> W (in SCKL2; dbSNP:rs373804633).
{ECO:0000269|PubMed:24389050}.
/FTId=VAR_075824.
VARIANT 357 357 K -> N (in dbSNP:rs34678569).
/FTId=VAR_051308.
VARIANT 387 387 H -> Y (in dbSNP:rs1804732).
/FTId=VAR_028308.
MUTAGEN 31 31 H->A: No effect on RPA focus formation on
DNA damage.
{ECO:0000269|PubMed:19759395}.
MUTAGEN 35 35 V->A: No effect on RPA focus formation on
DNA damage.
{ECO:0000269|PubMed:19759395}.
MUTAGEN 41 41 K->A: No effect on RPA focus formation on
DNA damage.
{ECO:0000269|PubMed:19759395}.
MUTAGEN 45 45 L->A: No effect on RPA focus formation on
DNA damage.
{ECO:0000269|PubMed:19759395}.
MUTAGEN 62 62 K->R: In K12R; defects in ability to
promoting DNA resection and homologous
recombination; when associated with R-78;
R-115; R-132; R-133; R-404; R-572; R-578;
R-640; R-759; R-760 and R-782. In K5R;
defects in ability to promoting DNA
resection and homologous recombination;
when associated with R-78; R-115; R-132
and R-133. {ECO:0000269|PubMed:26502057}.
MUTAGEN 78 78 K->R: In K12R; defects in ability to
promoting DNA resection and homologous
recombination; when associated with R-62;
R-115; R-132; R-133; R-404; R-572; R-578;
R-640; R-759; R-760 and R-782. In K5R;
defects in ability to promoting DNA
resection and homologous recombination;
when associated with R-62; R-115; R-132
and R-133. {ECO:0000269|PubMed:26502057}.
MUTAGEN 115 115 K->R: In K12R; defects in ability to
promoting DNA resection and homologous
recombination; when associated with R-62;
R-78; R-132; R-133; R-404; R-572; R-578;
R-640; R-759; R-760 and R-782. In K5R;
defects in ability to promoting DNA
resection and homologous recombination;
when associated with R-62; R-78; R-132
and R-133. {ECO:0000269|PubMed:26502057}.
MUTAGEN 132 132 K->R: In K12R; defects in ability to
promoting DNA resection and homologous
recombination; when associated with R-62;
R-78; R-115; R-133; R-404; R-572; R-578;
R-640; R-759; R-760 and R-782. In K5R;
defects in ability to promoting DNA
resection and homologous recombination;
when associated with R-62; R-78; R-115
and R-133. {ECO:0000269|PubMed:26502057}.
MUTAGEN 133 133 K->R: In K12R; defects in ability to
promoting DNA resection and homologous
recombination; when associated with R-62;
R-78; R-115; R-133; R-404; R-572; R-578;
R-640; R-759; R-760 and R-782. In K5R;
defects in ability to promoting DNA
resection and homologous recombination;
when associated with R-62; R-78; R-115
and R-132. {ECO:0000269|PubMed:26502057}.
MUTAGEN 179 179 K->A: No effect on FZR1-binding.
{ECO:0000269|PubMed:25349192}.
MUTAGEN 276 276 S->A: No effect on PIN1-binding. Impaired
PIN1-binding, partially decreased
CUL3/KLHL15-mediated proteasomal
degradation, no effect on BRCA1-, MRE11-,
nor on KLHL15-binding; when associated
with A-315. {ECO:0000269|PubMed:23623683,
ECO:0000269|PubMed:27561354}.
MUTAGEN 315 315 T->A: Decreased PIN1-binding. Impaired
PIN1-binding, partially decreased
CUL3/KLHL15-mediated proteasomal
degradation, no effect on BRCA1-, MRE11-,
nor on KLHL15-binding; when associated
with A-276. {ECO:0000269|PubMed:23623683,
ECO:0000269|PubMed:27561354}.
MUTAGEN 327 327 S->A: Abolishes BRCA1 interaction and
ubiquitination. No activation of CHEK1
after DNA damage.
{ECO:0000269|PubMed:15485915,
ECO:0000269|PubMed:16818604}.
MUTAGEN 404 404 K->R: In K12R; defects in ability to
promoting DNA resection and homologous
recombination; when associated with R-62;
R-78; R-115; R-132; R-133; R-572; R-578;
R-640; R-759; R-760 and R-782.
{ECO:0000269|PubMed:26502057}.
MUTAGEN 432 432 K->R: Greatly reduced acetylation.
Alleviates resection defects caused by
depletion of SIRT6; when associated with
R-526 and R-604.
{ECO:0000269|PubMed:20829486}.
MUTAGEN 467 467 K->A: Impaired FZR1-binding and APC/C-
mediated polyubiquitination. Increased
stability. No effect on MRE11-binding,
nor on CUL3/KLHL15-mediated proteasomal
degradation. No effect on DNA-en
resection activity.
{ECO:0000269|PubMed:25349192,
ECO:0000269|PubMed:27561354}.
MUTAGEN 513 513 K->A: Abolishes damage recruitment
capability.
{ECO:0000269|PubMed:20064462}.
MUTAGEN 515 515 K->A: Abolishes damage recruitment
capability.
{ECO:0000269|PubMed:20064462}.
MUTAGEN 526 526 K->R: Greatly reduced acetylation.
Alleviates resection defects caused by
depletion of SIRT6; when associated with
R-432 and R-604.
{ECO:0000269|PubMed:20829486}.
MUTAGEN 572 572 K->R: In K12R; defects in ability to
promoting DNA resection and homologous
recombination; when associated with R-62;
R-78; R-115; R-132; R-133; R-404; R-578;
R-640; R-759; R-760 and R-782.
{ECO:0000269|PubMed:26502057}.
MUTAGEN 578 578 K->R: In K12R; defects in ability to
promoting DNA resection and homologous
recombination; when associated with R-62;
R-78; R-115; R-132; R-133; R-404; R-572;
R-640; R-759; R-760 and R-782.
{ECO:0000269|PubMed:26502057}.
MUTAGEN 604 604 K->R: Greatly reduced acetylation.
Alleviates resection defects caused by
depletion of SIRT6; when associated with
R-432 and R-526.
{ECO:0000269|PubMed:20829486}.
MUTAGEN 640 640 K->R: In K12R; defects in ability to
promoting DNA resection and homologous
recombination; when associated with R-62;
R-78; R-115; R-132; R-133; R-404; R-572;
R-578; R-759; R-760 and R-782.
{ECO:0000269|PubMed:26502057}.
MUTAGEN 664 664 S->A: Abrogates dissociation of BRCA1.
{ECO:0000269|PubMed:10910365}.
MUTAGEN 745 745 S->A: Abrogates dissociation of BRCA1.
{ECO:0000269|PubMed:10910365}.
MUTAGEN 759 759 K->R: In K12R; defects in ability to
promoting DNA resection and homologous
recombination; when associated with R-62;
R-78; R-115; R-132; R-133; R-404; R-572;
R-578; R-640; R-760 and R-782.
{ECO:0000269|PubMed:26502057}.
MUTAGEN 760 760 K->R: In K12R; defects in ability to
promoting DNA resection and homologous
recombination; when associated with R-62;
R-78; R-115; R-132; R-133; R-404; R-572;
R-578; R-640; R-759 and R-782.
{ECO:0000269|PubMed:26502057}.
MUTAGEN 782 782 K->R: In K12R; defects in ability to
promoting DNA resection and homologous
recombination; when associated with R-62;
R-78; R-115; R-132; R-133; R-404; R-572;
R-578; R-640; R-759 and R-760.
{ECO:0000269|PubMed:26502057}.
MUTAGEN 839 839 R->A: No effect on CUL3/KLHL15-mediated
proteasomal degradation.
{ECO:0000269|PubMed:27561354}.
MUTAGEN 840 840 F->A: Decreased CUL3/KLHL15-mediated
proteasomal degradation.
{ECO:0000269|PubMed:27561354}.
MUTAGEN 842 842 Y->A: Decreased interaction with KLHL15,
decreased polyubiquitination and
CUL3/KLHL15-mediated proteasomal
degradation. No effect on DNA-end
resection activity.
{ECO:0000269|PubMed:27561354}.
MUTAGEN 842 842 Y->F: No effect on KLHL15-binding, nor on
CUL3/KLHL15-mediated proteasomal
degradation.
{ECO:0000269|PubMed:27561354}.
MUTAGEN 847 847 T->A: Impairs DNA resection.
{ECO:0000269|PubMed:19202191}.
MUTAGEN 847 847 T->E: Mimics constitutive
phosphorylation.
{ECO:0000269|PubMed:19202191}.
CONFLICT 4 4 S -> L (in Ref. 1; AAC14371).
{ECO:0000305}.
CONFLICT 74 74 H -> Q (in Ref. 4; BX648221).
{ECO:0000305}.
CONFLICT 92 92 C -> Y (in Ref. 3; BAF85170).
{ECO:0000305}.
CONFLICT 123 123 E -> G (in Ref. 3; BAF85170).
{ECO:0000305}.
CONFLICT 341 341 D -> G (in Ref. 4; BX648221).
{ECO:0000305}.
CONFLICT 515 515 K -> R (in Ref. 4; BX648221).
{ECO:0000305}.
CONFLICT 521 521 L -> P (in Ref. 3; BAF85170).
{ECO:0000305}.
CONFLICT 642 642 L -> P (in Ref. 4; BX648221).
{ECO:0000305}.
HELIX 18 50 {ECO:0000244|PDB:4D2H}.
STRAND 648 650 {ECO:0000244|PDB:2L4Z}.
HELIX 651 653 {ECO:0000244|PDB:2L4Z}.
TURN 662 666 {ECO:0000244|PDB:2L4Z}.
STRAND 677 679 {ECO:0000244|PDB:2L4Z}.
SEQUENCE 897 AA; 101942 MW; E028DE56DE55C0F2 CRC64;
MNISGSSCGS PNSADTSSDF KDLWTKLKEC HDREVQGLQV KVTKLKQERI LDAQRLEEFF
TKNQQLREQQ KVLHETIKVL EDRLRAGLCD RCAVTEEHMR KKQQEFENIR QQNLKLITEL
MNERNTLQEE NKKLSEQLQQ KIENDQQHQA AELECEEDVI PDSPITAFSF SGVNRLRRKE
NPHVRYIEQT HTKLEHSVCA NEMRKVSKSS THPQHNPNEN EILVADTYDQ SQSPMAKAHG
TSSYTPDKSS FNLATVVAET LGLGVQEESE TQGPMSPLGD ELYHCLEGNH KKQPFEESTR
NTEDSLRFSD STSKTPPQEE LPTRVSSPVF GATSSIKSGL DLNTSLSPSL LQPGKKKHLK
TLPFSNTCIS RLEKTRSKSE DSALFTHHSL GSEVNKIIIQ SSNKQILINK NISESLGEQN
RTEYGKDSNT DKHLEPLKSL GGRTSKRKKT EEESEHEVSC PQASFDKENA FPFPMDNQFS
MNGDCVMDKP LDLSDRFSAI QRQEKSQGSE TSKNKFRQVT LYEALKTIPK GFSSSRKASD
GNCTLPKDSP GEPCSQECII LQPLNKCSPD NKPSLQIKEE NAVFKIPLRP RESLETENVL
DDIKSAGSHE PIKIQTRSDH GGCELASVLQ LNPCRTGKIK SLQNNQDVSF ENIQWSIDPG
ADLSQYKMDV TVIDTKDGSQ SKLGGETVDM DCTLVSETVL LKMKKQEQKG EKSSNEERKM
NDSLEDMFDR TTHEEYESCL ADSFSQAADE EEELSTATKK LHTHGDKQDK VKQKAFVEPY
FKGDERETSL QNFPHIEVVR KKEERRKLLG HTCKECEIYY ADMPAEEREK KLASCSRHRF
RYIPPNTPEN FWEVGFPSTQ TCMERGYIKE DLDPCPRPKR RQPYNAIFSP KGKEQKT


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