ID RIF1_HUMAN Reviewed; 2472 AA. AC Q5UIP0; A6NC27; C9JBR1; Q5H9R3; Q5UIP2; Q66YK6; Q6PRU2; Q8TE94; AC Q99772; Q9H830; Q9H9B9; Q9NVP5; Q9Y4R4; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 2. DT 31-JUL-2019, entry version 147. DE RecName: Full=Telomere-associated protein RIF1 {ECO:0000305}; DE AltName: Full=Rap1-interacting factor 1 homolog {ECO:0000305|PubMed:15342490}; GN Name=RIF1 {ECO:0000303|PubMed:15342490, ECO:0000312|HGNC:HGNC:23207}; 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. 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 IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402; SER-782; SER-1008; RP SER-1162; THR-1220; SER-1236; SER-1238; SER-1422; SER-1454; SER-1513; RP SER-1542; SER-1552; SER-1554; SER-1556; SER-1579; SER-1613; SER-1616; RP SER-1688; SER-1706; SER-1709; THR-1806; SER-1810; SER-1926; SER-2144; RP SER-2161; SER-2172; SER-2176; SER-2196; SER-2205 AND SER-2339, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [19] RP FUNCTION, AND INTERACTION WITH TP53BP1. RX PubMed=23333306; DOI=10.1016/j.molcel.2013.01.001; RA Escribano-Diaz C., Orthwein A., Fradet-Turcotte A., Xing M., RA Young J.T., Tkac J., Cook M.A., Rosebrock A.P., Munro M., Canny M.D., RA Xu D., Durocher D.; RT "A cell cycle-dependent regulatory circuit composed of 53BP1-RIF1 and RT BRCA1-CtIP controls DNA repair pathway choice."; RL Mol. Cell 49:872-883(2013). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [21] RP FUNCTION, AND INTERACTION WITH TP53BP1. RX PubMed=28241136; DOI=10.1038/nature21358; RA Drane P., Brault M.E., Cui G., Meghani K., Chaubey S., Detappe A., RA Parnandi N., He Y., Zheng X.F., Botuyan M.V., Kalousi A., RA Yewdell W.T., Muench C., Harper J.W., Chaudhuri J., Soutoglou E., RA Mer G., Chowdhury D.; RT "TIRR regulates 53BP1 by masking its histone methyl-lysine binding RT function."; RL Nature 543:211-216(2017). RN [22] RP INTERACTION WITH SHLD2, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=29789392; DOI=10.15252/embj.201899543; RA Tomida J., Takata K.I., Bhetawal S., Person M.D., Chao H.P., RA Tang D.G., Wood R.D.; RT "FAM35A associates with REV7 and modulates DNA damage responses of RT normal and BRCA1-defective cells."; RL EMBO J. 37:0-0(2018). RN [23] 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: Key regulator of TP53BP1 that plays a key role in the CC repair of double-strand DNA breaks (DSBs) in response to DNA CC damage: acts by promoting non-homologous end joining (NHEJ)- CC mediated repair of DSBs (PubMed:15342490, PubMed:28241136). In CC response to DNA damage, interacts with ATM-phosphorylated TP53BP1 CC (PubMed:23333306, PubMed:28241136). Interaction with TP53BP1 leads CC to dissociate the interaction between NUDT16L1/TIRR and TP53BP1, CC thereby unmasking the tandem Tudor-like domain of TP53BP1 and CC allowing recruitment to DNA DSBs (PubMed:28241136). Once recruited CC to DSBs, RIF1 and TP53BP1 act by promoting NHEJ-mediated repair of CC DSBs (PubMed:23333306). In the same time, RIF1 and TP53BP1 CC specifically counteract the function of BRCA1 by blocking DSBs CC resection via homologous recombination (HR) during G1 phase CC (PubMed:23333306). Also required for immunoglobulin class-switch CC recombination (CSR) during antibody genesis, a process that CC involves the generation of DNA DSBs (By similarity). Promotes NHEJ CC of dysfunctional telomeres (By similarity). CC {ECO:0000250|UniProtKB:Q6PR54, ECO:0000269|PubMed:15342490, CC ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:28241136}. CC -!- SUBUNIT: Interacts with TP53BP1 (when phosphorylated by ATM) CC (PubMed:23333306, PubMed:28241136). May interact with TRF2 (By CC similarity). Interacts with SHLD2 (PubMed:29789392). CC {ECO:0000250|UniProtKB:Q6PR54, ECO:0000269|PubMed:23333306, CC ECO:0000269|PubMed:28241136, ECO:0000269|PubMed:29789392}. CC -!- INTERACTION: CC P62136:PPP1CA; NbExp=4; IntAct=EBI-711331, EBI-357253; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15583028}. CC Chromosome {ECO:0000250|UniProtKB:Q6PR54}. Chromosome, telomere CC {ECO:0000269|PubMed:15342490, ECO:0000269|PubMed:15583028}. CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15583028}. CC Note=Following interaction with TP53BP1, recruited to sites of DNA CC damage, such as DSBs (By similarity). Exhibits ATM- and TP53BP1- CC dependent localization to uncapped or aberrant telomeres and to CC DNA double strand breaks (DSBs) (PubMed:15342490). Does not CC associate with normal telomere structures (PubMed:15342490, CC PubMed:15583028). Localizes to microtubules of the midzone of the CC mitotic spindle during anaphase, and to condensed chromosomes in CC telophase (PubMed:15583028). {ECO:0000250|UniProtKB:Q6PR54, CC ECO:0000269|PubMed:15342490, ECO:0000269|PubMed:15583028}. 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 {ECO:0000269|PubMed:15583028}. CC -!- DEVELOPMENTAL STAGE: Expression peaks in late G2/S phase of the CC cell cycle. {ECO:0000269|PubMed:15583028}. CC -!- SIMILARITY: Belongs to the RIF1 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA91705.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAB14313.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAB14792.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAB85058.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAI45961.1; Type=Frameshift; Positions=470; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 CCDS; CCDS2194.1; -. [Q5UIP0-1] DR CCDS; CCDS54406.1; -. [Q5UIP0-2] DR PIR; T12518; T12518. DR RefSeq; NP_001171134.1; NM_001177663.1. [Q5UIP0-2] DR RefSeq; NP_001171135.1; NM_001177664.1. [Q5UIP0-2] DR RefSeq; NP_001171136.1; NM_001177665.1. [Q5UIP0-2] DR RefSeq; NP_060621.3; NM_018151.4. [Q5UIP0-1] DR RefSeq; XP_005246722.1; XM_005246665.3. [Q5UIP0-1] DR BioGrid; 120482; 68. DR IntAct; Q5UIP0; 146. DR MINT; Q5UIP0; -. DR STRING; 9606.ENSP00000243326; -. DR GlyConnect; 1791; -. DR iPTMnet; Q5UIP0; -. DR PhosphoSitePlus; Q5UIP0; -. DR SwissPalm; Q5UIP0; -. DR BioMuta; RIF1; -. DR DMDM; 68565701; -. DR CPTAC; CPTAC-3254; -. DR EPD; Q5UIP0; -. DR jPOST; Q5UIP0; -. DR MaxQB; Q5UIP0; -. DR PaxDb; Q5UIP0; -. DR PeptideAtlas; Q5UIP0; -. DR PRIDE; Q5UIP0; -. DR ProteomicsDB; 65248; -. [Q5UIP0-1] DR ProteomicsDB; 65249; -. [Q5UIP0-2] DR Ensembl; ENST00000243326; ENSP00000243326; ENSG00000080345. [Q5UIP0-1] DR Ensembl; ENST00000428287; ENSP00000415691; ENSG00000080345. [Q5UIP0-2] DR Ensembl; ENST00000430328; ENSP00000416123; ENSG00000080345. [Q5UIP0-2] DR Ensembl; ENST00000444746; ENSP00000390181; ENSG00000080345. [Q5UIP0-1] DR Ensembl; ENST00000453091; ENSP00000414615; ENSG00000080345. [Q5UIP0-2] DR GeneID; 55183; -. DR KEGG; hsa:55183; -. DR UCSC; uc002txl.4; human. [Q5UIP0-1] DR CTD; 55183; -. DR DisGeNET; 55183; -. DR GeneCards; RIF1; -. DR HGNC; HGNC:23207; RIF1. DR HPA; HPA036887; -. DR HPA; HPA036888; -. DR MIM; 608952; gene. DR neXtProt; NX_Q5UIP0; -. DR OpenTargets; ENSG00000080345; -. DR PharmGKB; PA134933858; -. DR eggNOG; ENOG410IJ7R; Eukaryota. DR eggNOG; ENOG410YNMC; LUCA. DR GeneTree; ENSGT00390000012204; -. DR InParanoid; Q5UIP0; -. DR KO; K11138; -. DR OMA; GNNLHEK; -. DR OrthoDB; 10400at2759; -. DR PhylomeDB; Q5UIP0; -. DR TreeFam; TF323789; -. DR Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ). DR ChiTaRS; RIF1; human. DR GeneWiki; RIF1; -. DR GenomeRNAi; 55183; -. DR PRO; PR:Q5UIP0; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; ENSG00000080345; Expressed in 226 organ(s), highest expression level in gastrocnemius. DR ExpressionAtlas; Q5UIP0; baseline and differential. DR Genevisible; Q5UIP0; HS. DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell. DR GO; GO:0000793; C:condensed chromosome; IDA:BHF-UCL. 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:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0000790; C:nuclear chromatin; ISS:BHF-UCL. DR GO; GO:0031965; C:nuclear membrane; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB. DR GO; GO:0051233; C:spindle midzone; IDA:BHF-UCL. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB. DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl. DR GO; GO:0006348; P:chromatin silencing at telomere; ISS:BHF-UCL. DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; TAS:Reactome. DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IDA:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:BHF-UCL. DR GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; IDA:UniProtKB. DR GO; GO:0051574; P:positive regulation of histone H3-K9 methylation; ISS:BHF-UCL. DR GO; GO:0045830; P:positive regulation of isotype switching; ISS:UniProtKB. DR GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl. DR GO; GO:0000723; P:telomere maintenance; ISS:BHF-UCL. DR GO; GO:0043247; P:telomere maintenance in response to DNA damage; IDA:BHF-UCL. DR Gene3D; 1.25.10.10; -; 1. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR022031; Rif1_N. DR Pfam; PF12231; Rif1_N; 1. DR SUPFAM; SSF48371; SSF48371; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell cycle; Chromosome; Complete proteome; KW Cytoplasm; Cytoskeleton; DNA damage; DNA repair; Nucleus; KW Phosphoprotein; 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 {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 409 409 Phosphothreonine. FT {ECO:0000244|PubMed:16964243, FT ECO:0000244|PubMed:18669648}. FT MOD_RES 782 782 Phosphoserine. FT {ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 979 979 Phosphoserine. FT {ECO:0000244|PubMed:19690332}. FT MOD_RES 1008 1008 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 1047 1047 Phosphothreonine. FT {ECO:0000244|PubMed:19690332}. FT MOD_RES 1162 1162 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 1220 1220 Phosphothreonine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 1236 1236 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 1238 1238 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 1422 1422 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 1454 1454 Phosphoserine. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 1513 1513 Phosphoserine. FT {ECO:0000244|PubMed:17525332, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 1518 1518 Phosphothreonine. FT {ECO:0000244|PubMed:17525332}. FT MOD_RES 1542 1542 Phosphoserine. FT {ECO:0000244|PubMed:17525332, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 1552 1552 Phosphoserine. FT {ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 1554 1554 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 1556 1556 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 1564 1564 Phosphoserine. FT {ECO:0000250|UniProtKB:Q6PR54}. FT MOD_RES 1576 1576 Phosphoserine. FT {ECO:0000244|PubMed:21406692}. FT MOD_RES 1579 1579 Phosphoserine. FT {ECO:0000244|PubMed:16964243, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 1613 1613 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 1616 1616 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 1688 1688 Phosphoserine. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 1693 1693 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1706 1706 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 1709 1709 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 1806 1806 Phosphothreonine. FT {ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 1810 1810 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 1873 1873 Phosphoserine. FT {ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 1876 1876 Phosphoserine. FT {ECO:0000244|PubMed:20068231}. FT MOD_RES 1926 1926 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 1971 1971 Phosphoserine. FT {ECO:0000244|PubMed:19690332}. FT MOD_RES 2144 2144 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 2161 2161 Phosphoserine. FT {ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 2167 2167 Phosphothreonine. FT {ECO:0000244|PubMed:21406692}. FT MOD_RES 2172 2172 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 2176 2176 Phosphoserine. FT {ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 2195 2195 Phosphoserine. FT {ECO:0000250|UniProtKB:Q6PR54}. FT MOD_RES 2196 2196 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 2205 2205 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 2260 2260 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 2339 2339 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 2391 2391 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 2393 2393 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 2465 2465 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 2471 2471 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT VAR_SEQ 2250 2275 Missing (in isoform 2). FT {ECO:0000303|PubMed:15583028, FT ECO:0000303|PubMed:9110174}. FT /FTId=VSP_014431. FT VARIANT 836 836 G -> S (in dbSNP:rs2444263). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15583028}. FT /FTId=VAR_022788. FT VARIANT 1362 1362 V -> M (in dbSNP:rs2123465). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15583028}. 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 {ECO:0000269|PubMed:16959974}. 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 {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_035984. FT VARIANT 2021 2021 N -> Y (in dbSNP:rs2444257). FT {ECO:0000269|PubMed:15342490, FT ECO:0000269|PubMed:15583028, FT ECO:0000269|PubMed:17974005}. 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 {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15342490, FT ECO:0000269|PubMed:15583028, FT ECO:0000269|PubMed:17974005, FT ECO:0000269|PubMed:9110174}. FT /FTId=VAR_022794. FT CONFLICT 96 96 N -> D (in Ref. 1; AAT40745). FT {ECO:0000305}. FT CONFLICT 699 699 A -> P (in Ref. 6; BAA91705). FT {ECO:0000305}. FT CONFLICT 1256 1256 M -> V (in Ref. 6; BAA91705). FT {ECO:0000305}. FT CONFLICT 2316 2316 R -> G (in Ref. 6; BAB85058). FT {ECO:0000305}. FT CONFLICT 2392 2392 L -> F (in Ref. 6; BAB85058). FT {ECO:0000305}. FT CONFLICT 2445 2446 HE -> RV (in Ref. 6; BAB85058). FT {ECO:0000305}. FT CONFLICT 2464 2464 R -> G (in Ref. 6; BAB85058). FT {ECO:0000305}. 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 //