Full text data of RIF1
RIF1
[Confidence: low (only semi-automatic identification from reviews)]
Telomere-associated protein RIF1 (Rap1-interacting factor 1 homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Telomere-associated protein RIF1 (Rap1-interacting factor 1 homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q5UIP0
ID RIF1_HUMAN Reviewed; 2472 AA.
AC Q5UIP0; A6NC27; C9JBR1; Q5H9R3; Q5UIP2; Q66YK6; Q6PRU2; Q8TE94;
read moreAC Q99772; Q9H830; Q9H9B9; Q9NVP5; Q9Y4R4;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 22-JAN-2014, entry version 94.
DE RecName: Full=Telomere-associated protein RIF1;
DE AltName: Full=Rap1-interacting factor 1 homolog;
GN Name=RIF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP LOCATION, AND VARIANTS TYR-2021 AND VAL-2418.
RX PubMed=15342490; DOI=10.1101/gad.1216004;
RA Silverman J., Takai H., Buonomo S.B.C., Eisenhaber F., De Lange T.;
RT "Human Rif1, ortholog of a yeast telomeric protein, is regulated by
RT ATM and 53BP1 and functions in the S-phase checkpoint.";
RL Genes Dev. 18:2108-2119(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND VARIANTS SER-836;
RP MET-1362; TYR-2021 AND VAL-2418.
RX PubMed=15583028; DOI=10.1083/jcb.200408181;
RA Xu L., Blackburn E.H.;
RT "Human Rif1 protein binds aberrant telomeres and aligns along anaphase
RT midzone microtubules.";
RL J. Cell Biol. 167:819-830(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Simonsson T.;
RT "Identification and characterization of human Rif1.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-853 AND 1728-2472
RP (ISOFORM 1), AND VARIANTS TYR-2021 AND VAL-2418.
RC TISSUE=Testis, and Testis carcinoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-1499 AND 2217-2472
RP (ISOFORM 1), AND VARIANTS SER-836; MET-1362 AND VAL-2418.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2108-2472 (ISOFORM 2), AND
RP VARIANT VAL-2418.
RC TISSUE=Brain;
RX PubMed=9110174;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1454 AND SER-1688, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-409 AND SER-1579, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1513; THR-1518 AND
RP SER-1542, AND MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402; THR-409; SER-1162;
RP SER-1236; SER-1238; SER-1422; SER-1554; SER-1616; SER-1688; SER-1693;
RP SER-1810; SER-2144; SER-2172; SER-2196; SER-2205; SER-2260; SER-2339;
RP SER-2391; SER-2393; SER-2465 AND SER-2471, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-979; THR-1047; SER-1552;
RP SER-1554; SER-1579; SER-1688; THR-1806; SER-1971 AND SER-2196, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1238; SER-1454;
RP SER-1579; SER-1688; SER-1810; SER-1873; SER-1876; SER-2161; SER-2172;
RP SER-2176; SER-2196; SER-2205 AND SER-2393, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-782; SER-1422; SER-1454;
RP SER-1542; SER-1554; SER-1576; SER-1579; SER-1688; SER-1873; SER-2144;
RP SER-2161; THR-2167 AND SER-2393, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP VARIANTS [LARGE SCALE ANALYSIS] LYS-1784 AND HIS-1955.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Required for checkpoint mediated arrest of cell cycle
CC progression in response to DNA damage during S-phase (the intra-S-
CC phase checkpoint). This checkpoint requires activation of at least
CC 2 parallel pathways by the ATM kinase: one involves the MRN
CC (MRE11A-RAD50-NBS1) complex, while the second requires CHEK2. RIF1
CC seems to act independently of both these pathways. Seems to play
CC no role in either the G1/S or G2/M DNA damage checkpoints.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere. Cytoplasm,
CC cytoskeleton, spindle. Note=Exhibits ATM- and TP53BP1-dependent
CC localization to uncapped or aberrant telomeres and to DNA double
CC strand breaks (DSBs). Does not associate with normal telomere
CC structures. Localizes to microtubules of the midzone of the
CC mitotic spindle during anaphase, and to condensed chromosomes in
CC telophase.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5UIP0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5UIP0-2; Sequence=VSP_014431;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis.
CC -!- DEVELOPMENTAL STAGE: Expression peaks in late G2/S phase of the
CC cell cycle.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91705.1; Type=Erroneous initiation;
CC Sequence=BAB14313.1; Type=Erroneous initiation;
CC Sequence=BAB14792.1; Type=Erroneous initiation;
CC Sequence=BAB85058.1; Type=Erroneous initiation;
CC Sequence=CAI45961.1; Type=Frameshift; Positions=470;
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DR EMBL; AY585745; AAT40745.1; -; mRNA.
DR EMBL; AY727910; AAV51401.1; -; mRNA.
DR EMBL; AY727911; AAV51402.1; -; mRNA.
DR EMBL; AY727912; AAV51403.1; -; mRNA.
DR EMBL; AY727913; AAV51404.1; -; mRNA.
DR EMBL; AY584066; AAS94233.1; -; mRNA.
DR EMBL; AC009311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC009497; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL080129; CAB45727.1; -; mRNA.
DR EMBL; CR933663; CAI45961.1; ALT_SEQ; mRNA.
DR EMBL; AK001461; BAA91705.1; ALT_INIT; mRNA.
DR EMBL; AK022932; BAB14313.1; ALT_INIT; mRNA.
DR EMBL; AK024033; BAB14792.1; ALT_INIT; mRNA.
DR EMBL; AK074349; BAB85058.1; ALT_INIT; mRNA.
DR EMBL; U79263; AAB50209.1; -; mRNA.
DR PIR; T12518; T12518.
DR RefSeq; NP_001171134.1; NM_001177663.1.
DR RefSeq; NP_001171135.1; NM_001177664.1.
DR RefSeq; NP_001171136.1; NM_001177665.1.
DR RefSeq; NP_060621.3; NM_018151.4.
DR RefSeq; XP_005246722.1; XM_005246665.1.
DR UniGene; Hs.655671; -.
DR UniGene; Hs.735592; -.
DR ProteinModelPortal; Q5UIP0; -.
DR IntAct; Q5UIP0; 117.
DR MINT; MINT-3974483; -.
DR PhosphoSite; Q5UIP0; -.
DR DMDM; 68565701; -.
DR PaxDb; Q5UIP0; -.
DR PRIDE; Q5UIP0; -.
DR Ensembl; ENST00000243326; ENSP00000243326; ENSG00000080345.
DR Ensembl; ENST00000428287; ENSP00000415691; ENSG00000080345.
DR Ensembl; ENST00000430328; ENSP00000416123; ENSG00000080345.
DR Ensembl; ENST00000444746; ENSP00000390181; ENSG00000080345.
DR Ensembl; ENST00000453091; ENSP00000414615; ENSG00000080345.
DR GeneID; 55183; -.
DR KEGG; hsa:55183; -.
DR UCSC; uc002txm.3; human.
DR CTD; 55183; -.
DR GeneCards; GC02P152266; -.
DR HGNC; HGNC:23207; RIF1.
DR HPA; HPA036887; -.
DR HPA; HPA036888; -.
DR MIM; 608952; gene.
DR neXtProt; NX_Q5UIP0; -.
DR PharmGKB; PA134933858; -.
DR eggNOG; NOG87885; -.
DR HOVERGEN; HBG080431; -.
DR InParanoid; Q5UIP0; -.
DR KO; K11138; -.
DR OMA; PTESVYP; -.
DR OrthoDB; EOG70GMDW; -.
DR PhylomeDB; Q5UIP0; -.
DR ChiTaRS; RIF1; human.
DR GeneWiki; RIF1; -.
DR GenomeRNAi; 55183; -.
DR NextBio; 59015; -.
DR PRO; PR:Q5UIP0; -.
DR ArrayExpress; Q5UIP0; -.
DR Bgee; Q5UIP0; -.
DR CleanEx; HS_RIF1; -.
DR Genevestigator; Q5UIP0; -.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0001939; C:female pronucleus; IEA:Ensembl.
DR GO; GO:0001940; C:male pronucleus; IEA:Ensembl.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0019827; P:stem cell maintenance; IEA:Ensembl.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR028566; Rif1.
DR InterPro; IPR028567; Rif1_metazoan.
DR InterPro; IPR022031; Rif1_N.
DR PANTHER; PTHR22928; PTHR22928; 1.
DR PANTHER; PTHR22928:SF0; PTHR22928:SF0; 1.
DR Pfam; PF12231; Rif1_N; 1.
DR SUPFAM; SSF48371; SSF48371; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Chromosome; Complete proteome;
KW Cytoplasm; Cytoskeleton; DNA damage; Nucleus; Phosphoprotein;
KW Polymorphism; Reference proteome; Telomere.
FT CHAIN 1 2472 Telomere-associated protein RIF1.
FT /FTId=PRO_0000097333.
FT REGION 1924 2472 Interaction with condensed chromosomes in
FT telophase.
FT MOD_RES 402 402 Phosphoserine.
FT MOD_RES 409 409 Phosphothreonine.
FT MOD_RES 782 782 Phosphoserine.
FT MOD_RES 979 979 Phosphoserine.
FT MOD_RES 1047 1047 Phosphothreonine.
FT MOD_RES 1162 1162 Phosphoserine.
FT MOD_RES 1236 1236 Phosphoserine.
FT MOD_RES 1238 1238 Phosphoserine.
FT MOD_RES 1422 1422 Phosphoserine.
FT MOD_RES 1454 1454 Phosphoserine.
FT MOD_RES 1513 1513 Phosphoserine.
FT MOD_RES 1518 1518 Phosphothreonine.
FT MOD_RES 1542 1542 Phosphoserine.
FT MOD_RES 1552 1552 Phosphoserine.
FT MOD_RES 1554 1554 Phosphoserine.
FT MOD_RES 1576 1576 Phosphoserine.
FT MOD_RES 1579 1579 Phosphoserine.
FT MOD_RES 1616 1616 Phosphoserine.
FT MOD_RES 1688 1688 Phosphoserine.
FT MOD_RES 1693 1693 Phosphoserine.
FT MOD_RES 1806 1806 Phosphothreonine.
FT MOD_RES 1810 1810 Phosphoserine.
FT MOD_RES 1873 1873 Phosphoserine.
FT MOD_RES 1876 1876 Phosphoserine.
FT MOD_RES 1971 1971 Phosphoserine.
FT MOD_RES 2144 2144 Phosphoserine.
FT MOD_RES 2161 2161 Phosphoserine.
FT MOD_RES 2167 2167 Phosphothreonine.
FT MOD_RES 2172 2172 Phosphoserine.
FT MOD_RES 2176 2176 Phosphoserine.
FT MOD_RES 2196 2196 Phosphoserine.
FT MOD_RES 2205 2205 Phosphoserine.
FT MOD_RES 2260 2260 Phosphoserine.
FT MOD_RES 2339 2339 Phosphoserine.
FT MOD_RES 2391 2391 Phosphoserine.
FT MOD_RES 2393 2393 Phosphoserine.
FT MOD_RES 2465 2465 Phosphoserine.
FT MOD_RES 2471 2471 Phosphoserine.
FT VAR_SEQ 2250 2275 Missing (in isoform 2).
FT /FTId=VSP_014431.
FT VARIANT 836 836 G -> S (in dbSNP:rs2444263).
FT /FTId=VAR_022788.
FT VARIANT 1362 1362 V -> M (in dbSNP:rs2123465).
FT /FTId=VAR_022789.
FT VARIANT 1686 1686 R -> G (in dbSNP:rs3732305).
FT /FTId=VAR_022790.
FT VARIANT 1784 1784 E -> K (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_035983.
FT VARIANT 1862 1862 V -> I (in dbSNP:rs2444258).
FT /FTId=VAR_022791.
FT VARIANT 1955 1955 D -> H (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_035984.
FT VARIANT 2021 2021 N -> Y (in dbSNP:rs2444257).
FT /FTId=VAR_022792.
FT VARIANT 2165 2165 M -> R (in dbSNP:rs16830057).
FT /FTId=VAR_022793.
FT VARIANT 2418 2418 L -> V (in dbSNP:rs1065177).
FT /FTId=VAR_022794.
FT CONFLICT 96 96 N -> D (in Ref. 1; AAT40745).
FT CONFLICT 699 699 A -> P (in Ref. 6; BAA91705).
FT CONFLICT 1256 1256 M -> V (in Ref. 6; BAA91705).
FT CONFLICT 2316 2316 R -> G (in Ref. 6; BAB85058).
FT CONFLICT 2392 2392 L -> F (in Ref. 6; BAB85058).
FT CONFLICT 2445 2446 HE -> RV (in Ref. 6; BAB85058).
FT CONFLICT 2464 2464 R -> G (in Ref. 6; BAB85058).
SQ SEQUENCE 2472 AA; 274466 MW; A45DCE3C5F9E052D CRC64;
MTARGQSPLA PLLETLEDPS ASHGGQTDAY LTLTSRMTGE EGKEVITEIE KKLPRLYKVL
KTHISSQNSE LSSAALQALG FCLYNPKITS ELSEANALEL LSKLNDTIKN SDKNVRTRAL
WVISKQTFPS EVVGKMVSSI IDSLEILFNK GETHSAVVDF EALNVIVRLI EQAPIQMGEE
AVRWAKLVIP LVVHSAQKVH LRGATALEMG MPLLLQKQQE IASITEQLMT TKLISELQKL
FMSKNETYVL KLWPLFVKLL GRTLHRSGSF INSLLQLEEL GFRSGAPMIK KIAFIAWKSL
IDNFALNPDI LCSAKRLKLL MQPLSSIHVR TETLALTKLE VWWYLLMRLG PHLPANFEQV
CVPLIQSTIS IDSNASPQGN SCHVATSPGL NPMTPVHKGA SSPYGAPGTP RMNLSSNLGG
MATIPSIQLL GLEMLLHFLL GPEALSFAKQ NKLVLSLEPL EHPLISSPSF FSKHANTLIT
AVHDSFVAVG KDAPDVVVSA IWKELISLVK SVTESGNKKE KPGSEVLTLL LKSLESIVKS
EVFPVSKTLV LMEITIKGLP QKVLGSPAYQ VANMDILNGT PALFLIQLIF NNFLECGVSD
ERFFLSLESL VGCVLSGPTS PLAFSDSVLN VINQNAKQLE NKEHLWKMWS VIVTPLTELI
NQTNEVNQGD ALEHNFSAIY GALTLPVNHI FSEQRFPVAT MKTLLRTWSE LYRAFARCAA
LVATAEENLC CEELSSKIMS SLEDEGFSNL LFVDRIIYII TVMVDCIDFS PYNIKYQPKV
KSPQRPSDWS KKKNEPLGKL TSLFKLIVKV IYSFHTLSFK EAHSDTLFTI GNSITGIISS
VLGHISLPSM IRKIFATLTR PLALFYENSK LDEVPKVYSC LNNKLEKLLG EIIACLQFSY
TGTYDSELLE QLSPLLCIIF LHKNKQIRKQ SAQFWNATFA KVMMLVYPEE LKPVLTQAKQ
KFLLLLPGLE TVEMMEESSG PYSDGTENSQ LNVKISGMER KSNGKRDSFL AQTKNKKENM
KPAAKLKLES SSLKVKGEIL LEEEKSTDFV FIPPEGKDAK ERILTDHQKE VLKTKRCDIP
AMYNNLDVSQ DTLFTQYSQE EPMEIPTLTR KPKEDSKMMI TEEQMDSDIV IPQDVTEDCG
MAEHLEKSSL SNNECGSLDK TSPEMSNSNN DERKKALISS RKTSTECASS TENSFVVSSS
SVSNTTVAGT PPYPTSRRQT FITLEKFDGS ENRPFSPSPL NNISSTVTVK NNQETMIKTD
FLPKAKQREG TFSKSDSEKI VNGTKRSSRR AGKAEQTGNK RSKPLMRSEP EKNTEESVEG
IVVLENNPPG LLNQTECVSD NQVHLSESTM EHDNTKLKAA TVENAVLLET NTVEEKNVEI
NLESKENTPP VVISADQMVN EDSQVQITPN QKTLRRSSRR RSEVVESTTE SQDKENSHQK
KERRKEEEKP LQKSPLHIKD DVLPKQKLIA EQTLQENLIE KGSNLHEKTL GETSANAETE
QNKKKADPEN IKSEGDGTQD IVDKSSEKLV RGRTRYQTRR ASQGLLSSIE NSESDSSEAK
EEGSRKKRSG KWKNKSNESV DIQDQEEKVV KQECIKAENQ SHDYKATSEE DVSIKSPICE
KQDESNTVIC QDSTVTSDLL QVPDDLPNVC EEKNETSKYA EYSFTSLPVP ESNLRTRNAI
KRLHKRDSFD NCSLGESSKI GISDISSLSE KTFQTLECQH KRSRRVRRSK GCDCCGEKSQ
PQEKSLIGLK NTENNDVEIS ETKKADVQAP VSPSETSQAN PYSEGQFLDE HHSVNFHLGL
KEDNDTINDS LIVSETKSKE NTMQESLPSG IVNFREEICD MDSSEAMSLE SQESPNENFK
TVGPCLGDSK NVSQESLETK EEKPEETPKM ELSLENVTVE GNACKVTESN LEKAKTMELN
VGNEASFHGQ ERTKTGISEE AAIEENKRND DSEADTAKLN AKEVATEEFN SDISLSDNTT
PVKLNAQTEI SEQTAAGELD GGNDVSDLHS SEETNTKMKN NEEMMIGEAM AETGHDGETE
NEGITTKTSK PDEAETNMLT AEMDNFVCDT VEMSTEEGII DANKTETNTE YSKSEEKLDN
NQMVMESDIL QEDHHTSQKV EEPSQCLASG TAISELIIED NNASPQKLRE LDPSLVSAND
SPSGMQTRCV WSPLASPSTS ILKRGLKRSQ EDEISSPVNK VRRVSFADPI YQAGLADDID
RRCSIVRSHS SNSSPIGKSV KTSPTTQSKH NTTSAKGFLS PGSRSPKFKS SKKCLISEMA
KESIPCPTES VYPPLVNCVA PVDIILPQIT SNMWARGLGQ LIRAKNIKTI GDLSTLTASE
IKTLPIRSPK VSNVKKALRI YHEQQVKTRG LEEIPVFDIS EKTVNGIENK SLSPDEERLV
SDIIDPVALE IPLSKNLLAQ ISALALQLDS EDLHNYSGSQ LFEMHEKLSC MANSVIKNLQ
SRWRSPSHEN SI
//
ID RIF1_HUMAN Reviewed; 2472 AA.
AC Q5UIP0; A6NC27; C9JBR1; Q5H9R3; Q5UIP2; Q66YK6; Q6PRU2; Q8TE94;
read moreAC Q99772; Q9H830; Q9H9B9; Q9NVP5; Q9Y4R4;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 22-JAN-2014, entry version 94.
DE RecName: Full=Telomere-associated protein RIF1;
DE AltName: Full=Rap1-interacting factor 1 homolog;
GN Name=RIF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP LOCATION, AND VARIANTS TYR-2021 AND VAL-2418.
RX PubMed=15342490; DOI=10.1101/gad.1216004;
RA Silverman J., Takai H., Buonomo S.B.C., Eisenhaber F., De Lange T.;
RT "Human Rif1, ortholog of a yeast telomeric protein, is regulated by
RT ATM and 53BP1 and functions in the S-phase checkpoint.";
RL Genes Dev. 18:2108-2119(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND VARIANTS SER-836;
RP MET-1362; TYR-2021 AND VAL-2418.
RX PubMed=15583028; DOI=10.1083/jcb.200408181;
RA Xu L., Blackburn E.H.;
RT "Human Rif1 protein binds aberrant telomeres and aligns along anaphase
RT midzone microtubules.";
RL J. Cell Biol. 167:819-830(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Simonsson T.;
RT "Identification and characterization of human Rif1.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-853 AND 1728-2472
RP (ISOFORM 1), AND VARIANTS TYR-2021 AND VAL-2418.
RC TISSUE=Testis, and Testis carcinoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-1499 AND 2217-2472
RP (ISOFORM 1), AND VARIANTS SER-836; MET-1362 AND VAL-2418.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2108-2472 (ISOFORM 2), AND
RP VARIANT VAL-2418.
RC TISSUE=Brain;
RX PubMed=9110174;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1454 AND SER-1688, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-409 AND SER-1579, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1513; THR-1518 AND
RP SER-1542, AND MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402; THR-409; SER-1162;
RP SER-1236; SER-1238; SER-1422; SER-1554; SER-1616; SER-1688; SER-1693;
RP SER-1810; SER-2144; SER-2172; SER-2196; SER-2205; SER-2260; SER-2339;
RP SER-2391; SER-2393; SER-2465 AND SER-2471, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-979; THR-1047; SER-1552;
RP SER-1554; SER-1579; SER-1688; THR-1806; SER-1971 AND SER-2196, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1238; SER-1454;
RP SER-1579; SER-1688; SER-1810; SER-1873; SER-1876; SER-2161; SER-2172;
RP SER-2176; SER-2196; SER-2205 AND SER-2393, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-782; SER-1422; SER-1454;
RP SER-1542; SER-1554; SER-1576; SER-1579; SER-1688; SER-1873; SER-2144;
RP SER-2161; THR-2167 AND SER-2393, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP VARIANTS [LARGE SCALE ANALYSIS] LYS-1784 AND HIS-1955.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Required for checkpoint mediated arrest of cell cycle
CC progression in response to DNA damage during S-phase (the intra-S-
CC phase checkpoint). This checkpoint requires activation of at least
CC 2 parallel pathways by the ATM kinase: one involves the MRN
CC (MRE11A-RAD50-NBS1) complex, while the second requires CHEK2. RIF1
CC seems to act independently of both these pathways. Seems to play
CC no role in either the G1/S or G2/M DNA damage checkpoints.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere. Cytoplasm,
CC cytoskeleton, spindle. Note=Exhibits ATM- and TP53BP1-dependent
CC localization to uncapped or aberrant telomeres and to DNA double
CC strand breaks (DSBs). Does not associate with normal telomere
CC structures. Localizes to microtubules of the midzone of the
CC mitotic spindle during anaphase, and to condensed chromosomes in
CC telophase.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5UIP0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5UIP0-2; Sequence=VSP_014431;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis.
CC -!- DEVELOPMENTAL STAGE: Expression peaks in late G2/S phase of the
CC cell cycle.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91705.1; Type=Erroneous initiation;
CC Sequence=BAB14313.1; Type=Erroneous initiation;
CC Sequence=BAB14792.1; Type=Erroneous initiation;
CC Sequence=BAB85058.1; Type=Erroneous initiation;
CC Sequence=CAI45961.1; Type=Frameshift; Positions=470;
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DR EMBL; AY585745; AAT40745.1; -; mRNA.
DR EMBL; AY727910; AAV51401.1; -; mRNA.
DR EMBL; AY727911; AAV51402.1; -; mRNA.
DR EMBL; AY727912; AAV51403.1; -; mRNA.
DR EMBL; AY727913; AAV51404.1; -; mRNA.
DR EMBL; AY584066; AAS94233.1; -; mRNA.
DR EMBL; AC009311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC009497; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL080129; CAB45727.1; -; mRNA.
DR EMBL; CR933663; CAI45961.1; ALT_SEQ; mRNA.
DR EMBL; AK001461; BAA91705.1; ALT_INIT; mRNA.
DR EMBL; AK022932; BAB14313.1; ALT_INIT; mRNA.
DR EMBL; AK024033; BAB14792.1; ALT_INIT; mRNA.
DR EMBL; AK074349; BAB85058.1; ALT_INIT; mRNA.
DR EMBL; U79263; AAB50209.1; -; mRNA.
DR PIR; T12518; T12518.
DR RefSeq; NP_001171134.1; NM_001177663.1.
DR RefSeq; NP_001171135.1; NM_001177664.1.
DR RefSeq; NP_001171136.1; NM_001177665.1.
DR RefSeq; NP_060621.3; NM_018151.4.
DR RefSeq; XP_005246722.1; XM_005246665.1.
DR UniGene; Hs.655671; -.
DR UniGene; Hs.735592; -.
DR ProteinModelPortal; Q5UIP0; -.
DR IntAct; Q5UIP0; 117.
DR MINT; MINT-3974483; -.
DR PhosphoSite; Q5UIP0; -.
DR DMDM; 68565701; -.
DR PaxDb; Q5UIP0; -.
DR PRIDE; Q5UIP0; -.
DR Ensembl; ENST00000243326; ENSP00000243326; ENSG00000080345.
DR Ensembl; ENST00000428287; ENSP00000415691; ENSG00000080345.
DR Ensembl; ENST00000430328; ENSP00000416123; ENSG00000080345.
DR Ensembl; ENST00000444746; ENSP00000390181; ENSG00000080345.
DR Ensembl; ENST00000453091; ENSP00000414615; ENSG00000080345.
DR GeneID; 55183; -.
DR KEGG; hsa:55183; -.
DR UCSC; uc002txm.3; human.
DR CTD; 55183; -.
DR GeneCards; GC02P152266; -.
DR HGNC; HGNC:23207; RIF1.
DR HPA; HPA036887; -.
DR HPA; HPA036888; -.
DR MIM; 608952; gene.
DR neXtProt; NX_Q5UIP0; -.
DR PharmGKB; PA134933858; -.
DR eggNOG; NOG87885; -.
DR HOVERGEN; HBG080431; -.
DR InParanoid; Q5UIP0; -.
DR KO; K11138; -.
DR OMA; PTESVYP; -.
DR OrthoDB; EOG70GMDW; -.
DR PhylomeDB; Q5UIP0; -.
DR ChiTaRS; RIF1; human.
DR GeneWiki; RIF1; -.
DR GenomeRNAi; 55183; -.
DR NextBio; 59015; -.
DR PRO; PR:Q5UIP0; -.
DR ArrayExpress; Q5UIP0; -.
DR Bgee; Q5UIP0; -.
DR CleanEx; HS_RIF1; -.
DR Genevestigator; Q5UIP0; -.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0001939; C:female pronucleus; IEA:Ensembl.
DR GO; GO:0001940; C:male pronucleus; IEA:Ensembl.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0019827; P:stem cell maintenance; IEA:Ensembl.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR028566; Rif1.
DR InterPro; IPR028567; Rif1_metazoan.
DR InterPro; IPR022031; Rif1_N.
DR PANTHER; PTHR22928; PTHR22928; 1.
DR PANTHER; PTHR22928:SF0; PTHR22928:SF0; 1.
DR Pfam; PF12231; Rif1_N; 1.
DR SUPFAM; SSF48371; SSF48371; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Chromosome; Complete proteome;
KW Cytoplasm; Cytoskeleton; DNA damage; Nucleus; Phosphoprotein;
KW Polymorphism; Reference proteome; Telomere.
FT CHAIN 1 2472 Telomere-associated protein RIF1.
FT /FTId=PRO_0000097333.
FT REGION 1924 2472 Interaction with condensed chromosomes in
FT telophase.
FT MOD_RES 402 402 Phosphoserine.
FT MOD_RES 409 409 Phosphothreonine.
FT MOD_RES 782 782 Phosphoserine.
FT MOD_RES 979 979 Phosphoserine.
FT MOD_RES 1047 1047 Phosphothreonine.
FT MOD_RES 1162 1162 Phosphoserine.
FT MOD_RES 1236 1236 Phosphoserine.
FT MOD_RES 1238 1238 Phosphoserine.
FT MOD_RES 1422 1422 Phosphoserine.
FT MOD_RES 1454 1454 Phosphoserine.
FT MOD_RES 1513 1513 Phosphoserine.
FT MOD_RES 1518 1518 Phosphothreonine.
FT MOD_RES 1542 1542 Phosphoserine.
FT MOD_RES 1552 1552 Phosphoserine.
FT MOD_RES 1554 1554 Phosphoserine.
FT MOD_RES 1576 1576 Phosphoserine.
FT MOD_RES 1579 1579 Phosphoserine.
FT MOD_RES 1616 1616 Phosphoserine.
FT MOD_RES 1688 1688 Phosphoserine.
FT MOD_RES 1693 1693 Phosphoserine.
FT MOD_RES 1806 1806 Phosphothreonine.
FT MOD_RES 1810 1810 Phosphoserine.
FT MOD_RES 1873 1873 Phosphoserine.
FT MOD_RES 1876 1876 Phosphoserine.
FT MOD_RES 1971 1971 Phosphoserine.
FT MOD_RES 2144 2144 Phosphoserine.
FT MOD_RES 2161 2161 Phosphoserine.
FT MOD_RES 2167 2167 Phosphothreonine.
FT MOD_RES 2172 2172 Phosphoserine.
FT MOD_RES 2176 2176 Phosphoserine.
FT MOD_RES 2196 2196 Phosphoserine.
FT MOD_RES 2205 2205 Phosphoserine.
FT MOD_RES 2260 2260 Phosphoserine.
FT MOD_RES 2339 2339 Phosphoserine.
FT MOD_RES 2391 2391 Phosphoserine.
FT MOD_RES 2393 2393 Phosphoserine.
FT MOD_RES 2465 2465 Phosphoserine.
FT MOD_RES 2471 2471 Phosphoserine.
FT VAR_SEQ 2250 2275 Missing (in isoform 2).
FT /FTId=VSP_014431.
FT VARIANT 836 836 G -> S (in dbSNP:rs2444263).
FT /FTId=VAR_022788.
FT VARIANT 1362 1362 V -> M (in dbSNP:rs2123465).
FT /FTId=VAR_022789.
FT VARIANT 1686 1686 R -> G (in dbSNP:rs3732305).
FT /FTId=VAR_022790.
FT VARIANT 1784 1784 E -> K (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_035983.
FT VARIANT 1862 1862 V -> I (in dbSNP:rs2444258).
FT /FTId=VAR_022791.
FT VARIANT 1955 1955 D -> H (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_035984.
FT VARIANT 2021 2021 N -> Y (in dbSNP:rs2444257).
FT /FTId=VAR_022792.
FT VARIANT 2165 2165 M -> R (in dbSNP:rs16830057).
FT /FTId=VAR_022793.
FT VARIANT 2418 2418 L -> V (in dbSNP:rs1065177).
FT /FTId=VAR_022794.
FT CONFLICT 96 96 N -> D (in Ref. 1; AAT40745).
FT CONFLICT 699 699 A -> P (in Ref. 6; BAA91705).
FT CONFLICT 1256 1256 M -> V (in Ref. 6; BAA91705).
FT CONFLICT 2316 2316 R -> G (in Ref. 6; BAB85058).
FT CONFLICT 2392 2392 L -> F (in Ref. 6; BAB85058).
FT CONFLICT 2445 2446 HE -> RV (in Ref. 6; BAB85058).
FT CONFLICT 2464 2464 R -> G (in Ref. 6; BAB85058).
SQ SEQUENCE 2472 AA; 274466 MW; A45DCE3C5F9E052D CRC64;
MTARGQSPLA PLLETLEDPS ASHGGQTDAY LTLTSRMTGE EGKEVITEIE KKLPRLYKVL
KTHISSQNSE LSSAALQALG FCLYNPKITS ELSEANALEL LSKLNDTIKN SDKNVRTRAL
WVISKQTFPS EVVGKMVSSI IDSLEILFNK GETHSAVVDF EALNVIVRLI EQAPIQMGEE
AVRWAKLVIP LVVHSAQKVH LRGATALEMG MPLLLQKQQE IASITEQLMT TKLISELQKL
FMSKNETYVL KLWPLFVKLL GRTLHRSGSF INSLLQLEEL GFRSGAPMIK KIAFIAWKSL
IDNFALNPDI LCSAKRLKLL MQPLSSIHVR TETLALTKLE VWWYLLMRLG PHLPANFEQV
CVPLIQSTIS IDSNASPQGN SCHVATSPGL NPMTPVHKGA SSPYGAPGTP RMNLSSNLGG
MATIPSIQLL GLEMLLHFLL GPEALSFAKQ NKLVLSLEPL EHPLISSPSF FSKHANTLIT
AVHDSFVAVG KDAPDVVVSA IWKELISLVK SVTESGNKKE KPGSEVLTLL LKSLESIVKS
EVFPVSKTLV LMEITIKGLP QKVLGSPAYQ VANMDILNGT PALFLIQLIF NNFLECGVSD
ERFFLSLESL VGCVLSGPTS PLAFSDSVLN VINQNAKQLE NKEHLWKMWS VIVTPLTELI
NQTNEVNQGD ALEHNFSAIY GALTLPVNHI FSEQRFPVAT MKTLLRTWSE LYRAFARCAA
LVATAEENLC CEELSSKIMS SLEDEGFSNL LFVDRIIYII TVMVDCIDFS PYNIKYQPKV
KSPQRPSDWS KKKNEPLGKL TSLFKLIVKV IYSFHTLSFK EAHSDTLFTI GNSITGIISS
VLGHISLPSM IRKIFATLTR PLALFYENSK LDEVPKVYSC LNNKLEKLLG EIIACLQFSY
TGTYDSELLE QLSPLLCIIF LHKNKQIRKQ SAQFWNATFA KVMMLVYPEE LKPVLTQAKQ
KFLLLLPGLE TVEMMEESSG PYSDGTENSQ LNVKISGMER KSNGKRDSFL AQTKNKKENM
KPAAKLKLES SSLKVKGEIL LEEEKSTDFV FIPPEGKDAK ERILTDHQKE VLKTKRCDIP
AMYNNLDVSQ DTLFTQYSQE EPMEIPTLTR KPKEDSKMMI TEEQMDSDIV IPQDVTEDCG
MAEHLEKSSL SNNECGSLDK TSPEMSNSNN DERKKALISS RKTSTECASS TENSFVVSSS
SVSNTTVAGT PPYPTSRRQT FITLEKFDGS ENRPFSPSPL NNISSTVTVK NNQETMIKTD
FLPKAKQREG TFSKSDSEKI VNGTKRSSRR AGKAEQTGNK RSKPLMRSEP EKNTEESVEG
IVVLENNPPG LLNQTECVSD NQVHLSESTM EHDNTKLKAA TVENAVLLET NTVEEKNVEI
NLESKENTPP VVISADQMVN EDSQVQITPN QKTLRRSSRR RSEVVESTTE SQDKENSHQK
KERRKEEEKP LQKSPLHIKD DVLPKQKLIA EQTLQENLIE KGSNLHEKTL GETSANAETE
QNKKKADPEN IKSEGDGTQD IVDKSSEKLV RGRTRYQTRR ASQGLLSSIE NSESDSSEAK
EEGSRKKRSG KWKNKSNESV DIQDQEEKVV KQECIKAENQ SHDYKATSEE DVSIKSPICE
KQDESNTVIC QDSTVTSDLL QVPDDLPNVC EEKNETSKYA EYSFTSLPVP ESNLRTRNAI
KRLHKRDSFD NCSLGESSKI GISDISSLSE KTFQTLECQH KRSRRVRRSK GCDCCGEKSQ
PQEKSLIGLK NTENNDVEIS ETKKADVQAP VSPSETSQAN PYSEGQFLDE HHSVNFHLGL
KEDNDTINDS LIVSETKSKE NTMQESLPSG IVNFREEICD MDSSEAMSLE SQESPNENFK
TVGPCLGDSK NVSQESLETK EEKPEETPKM ELSLENVTVE GNACKVTESN LEKAKTMELN
VGNEASFHGQ ERTKTGISEE AAIEENKRND DSEADTAKLN AKEVATEEFN SDISLSDNTT
PVKLNAQTEI SEQTAAGELD GGNDVSDLHS SEETNTKMKN NEEMMIGEAM AETGHDGETE
NEGITTKTSK PDEAETNMLT AEMDNFVCDT VEMSTEEGII DANKTETNTE YSKSEEKLDN
NQMVMESDIL QEDHHTSQKV EEPSQCLASG TAISELIIED NNASPQKLRE LDPSLVSAND
SPSGMQTRCV WSPLASPSTS ILKRGLKRSQ EDEISSPVNK VRRVSFADPI YQAGLADDID
RRCSIVRSHS SNSSPIGKSV KTSPTTQSKH NTTSAKGFLS PGSRSPKFKS SKKCLISEMA
KESIPCPTES VYPPLVNCVA PVDIILPQIT SNMWARGLGQ LIRAKNIKTI GDLSTLTASE
IKTLPIRSPK VSNVKKALRI YHEQQVKTRG LEEIPVFDIS EKTVNGIENK SLSPDEERLV
SDIIDPVALE IPLSKNLLAQ ISALALQLDS EDLHNYSGSQ LFEMHEKLSC MANSVIKNLQ
SRWRSPSHEN SI
//
MIM
608952
*RECORD*
*FIELD* NO
608952
*FIELD* TI
*608952 RAP1-INTERACTING FACTOR 1, YEAST, HOMOLOG OF; RIF1
*FIELD* TX
CLONING
By searching a database for sequences similar to S. pombe and S.
read morecerevisiae Rif1, Silverman et al. (2004) identified human RIF1. The
deduced protein contains 2,472 amino acids. Alignment of the human,
mouse, and fugu proteins revealed 2 conserved N-terminal regions and a
conserved C-terminal region. The first 340 amino acids contain 8
armadillo-type repeats, which are helical folds that typically occur in
long arrays, creating an extended curved protein or RNA interaction
surface. RIF1 also contains a central serine-rich region and a bipartite
nuclear localization signal within the C-terminal conserved region.
GENE FUNCTION
Yeast Rif1 associates with telomeres and regulates their length. In
contrast, Silverman et al. (2004) found that human RIF1 did not
accumulate at functional telomeres, but localized to dysfunctional
telomeres and to telomeric DNA clusters in human ALT (alternative
lengthening of telomeres) cell lines, which maintain telomeric DNA in
the absence of telomerase. They noted that this pattern of telomere
association is typical of DNA damage response factors. After induction
of double-strand breaks in ALT cells, RIF1 formed foci that colocalized
with other DNA damage response factors. This response was strictly
dependent on ATM (607585) and 53BP1 (605230), but was not affected by
diminished function of ATR (601215), BRCA1 (113705), CHK2 (604373), NBS1
(602667), or MRE11 (600814). RIF1 inhibition resulted in
radiosensitivity and a defect in the intra-S-phase checkpoint. Silverman
et al. (2004) concluded that RIF1 contributes to ATM-mediated protection
against DNA damage.
53BP1 (605230) is critical for the control of double-strand break (DSB)
repair, promoting nonhomologous end-joining (NHEJ) and inhibiting the
5-prime end resection needed for homology-directed repair (HDR). Using
dysfunctional telomeres and genomewide DSBs, Zimmermann et al. (2013)
identified RIF1 as the main factor used by 53BP1 to impair 5-prime end
resection. RIF1 inhibits resection involving CTIP (604124), BLM
(604610), and EXO1 (606063), limits accumulation of BRCA1/BARD1 (601593)
complexes at sites of DNA damage, and defines one of the mechanisms by
which 53BP1 causes chromosomal abnormalities in BRCA1-deficient cells.
Zimmermann et al. (2013) concluded that their data established RIF1 as
an important contributor to the control of DSB repair by 53BP1.
Di Virgilio et al. (2013) identified RIF1 as an ATM
phosphorylation-dependent interactor of 53BP1 and showed that absence of
RIF1 results in 5-prime/3-prime DNA-end resection in mice. Consistent
with enhanced DNA resection, RIF1 deficiency impairs DNA repair in the
G1 and S phases of the cell cycle, interferes with class switch
recombination in B lymphocytes, and leads to accumulation of chromosome
DSBs.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the RIF1
gene to chromosome 2 (TMAP SHGC-56421).
*FIELD* RF
1. Di Virgilio, M.; Callen, E.; Yamane, A.; Zhang, W.; Jankovic, M.;
Gitlin, A. D.; Feldhahn, N.; Resch, W.; Oliveria, T. Y.; Chait, B.
T.; Nussenzweig, A.; Casellas, R.; Robbiani, D. F.; Nussenzweig, M.
C.: Rif1 prevents resection of DNA breaks and promotes immunoglobulin
class switching. Science 339: 711-715, 2013.
2. Silverman, J.; Takai, H.; Buonomo, S. B. C.; Eisenhaber, F.; de
Lange, T.: Human Rif1, ortholog of a yeast telomeric protein, is
regulated by ATM and 53BP1 and functions in the S-phase checkpoint. Genes
Dev. 18: 2108-2119, 2004.
3. Zimmermann, M.; Lottersberger, F.; Buonomo, S. B.; Sfeir, A.; de
Lange, T.: 53BP1 regulates DSB repair using Rif1 to control 5-prime
end resection. Science 339: 700-704, 2013.
*FIELD* CN
Ada Hamosh - updated: 3/8/2013
*FIELD* CD
Patricia A. Hartz: 9/28/2004
*FIELD* ED
alopez: 03/11/2013
terry: 3/8/2013
mgross: 9/28/2004
*RECORD*
*FIELD* NO
608952
*FIELD* TI
*608952 RAP1-INTERACTING FACTOR 1, YEAST, HOMOLOG OF; RIF1
*FIELD* TX
CLONING
By searching a database for sequences similar to S. pombe and S.
read morecerevisiae Rif1, Silverman et al. (2004) identified human RIF1. The
deduced protein contains 2,472 amino acids. Alignment of the human,
mouse, and fugu proteins revealed 2 conserved N-terminal regions and a
conserved C-terminal region. The first 340 amino acids contain 8
armadillo-type repeats, which are helical folds that typically occur in
long arrays, creating an extended curved protein or RNA interaction
surface. RIF1 also contains a central serine-rich region and a bipartite
nuclear localization signal within the C-terminal conserved region.
GENE FUNCTION
Yeast Rif1 associates with telomeres and regulates their length. In
contrast, Silverman et al. (2004) found that human RIF1 did not
accumulate at functional telomeres, but localized to dysfunctional
telomeres and to telomeric DNA clusters in human ALT (alternative
lengthening of telomeres) cell lines, which maintain telomeric DNA in
the absence of telomerase. They noted that this pattern of telomere
association is typical of DNA damage response factors. After induction
of double-strand breaks in ALT cells, RIF1 formed foci that colocalized
with other DNA damage response factors. This response was strictly
dependent on ATM (607585) and 53BP1 (605230), but was not affected by
diminished function of ATR (601215), BRCA1 (113705), CHK2 (604373), NBS1
(602667), or MRE11 (600814). RIF1 inhibition resulted in
radiosensitivity and a defect in the intra-S-phase checkpoint. Silverman
et al. (2004) concluded that RIF1 contributes to ATM-mediated protection
against DNA damage.
53BP1 (605230) is critical for the control of double-strand break (DSB)
repair, promoting nonhomologous end-joining (NHEJ) and inhibiting the
5-prime end resection needed for homology-directed repair (HDR). Using
dysfunctional telomeres and genomewide DSBs, Zimmermann et al. (2013)
identified RIF1 as the main factor used by 53BP1 to impair 5-prime end
resection. RIF1 inhibits resection involving CTIP (604124), BLM
(604610), and EXO1 (606063), limits accumulation of BRCA1/BARD1 (601593)
complexes at sites of DNA damage, and defines one of the mechanisms by
which 53BP1 causes chromosomal abnormalities in BRCA1-deficient cells.
Zimmermann et al. (2013) concluded that their data established RIF1 as
an important contributor to the control of DSB repair by 53BP1.
Di Virgilio et al. (2013) identified RIF1 as an ATM
phosphorylation-dependent interactor of 53BP1 and showed that absence of
RIF1 results in 5-prime/3-prime DNA-end resection in mice. Consistent
with enhanced DNA resection, RIF1 deficiency impairs DNA repair in the
G1 and S phases of the cell cycle, interferes with class switch
recombination in B lymphocytes, and leads to accumulation of chromosome
DSBs.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the RIF1
gene to chromosome 2 (TMAP SHGC-56421).
*FIELD* RF
1. Di Virgilio, M.; Callen, E.; Yamane, A.; Zhang, W.; Jankovic, M.;
Gitlin, A. D.; Feldhahn, N.; Resch, W.; Oliveria, T. Y.; Chait, B.
T.; Nussenzweig, A.; Casellas, R.; Robbiani, D. F.; Nussenzweig, M.
C.: Rif1 prevents resection of DNA breaks and promotes immunoglobulin
class switching. Science 339: 711-715, 2013.
2. Silverman, J.; Takai, H.; Buonomo, S. B. C.; Eisenhaber, F.; de
Lange, T.: Human Rif1, ortholog of a yeast telomeric protein, is
regulated by ATM and 53BP1 and functions in the S-phase checkpoint. Genes
Dev. 18: 2108-2119, 2004.
3. Zimmermann, M.; Lottersberger, F.; Buonomo, S. B.; Sfeir, A.; de
Lange, T.: 53BP1 regulates DSB repair using Rif1 to control 5-prime
end resection. Science 339: 700-704, 2013.
*FIELD* CN
Ada Hamosh - updated: 3/8/2013
*FIELD* CD
Patricia A. Hartz: 9/28/2004
*FIELD* ED
alopez: 03/11/2013
terry: 3/8/2013
mgross: 9/28/2004