ID TE2IP_HUMAN Reviewed; 399 AA. AC Q9NYB0; B4DQN4; Q4W4Y2; Q8WYZ3; Q9NWR2; DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 28-JUN-2023, entry version 207. DE RecName: Full=Telomeric repeat-binding factor 2-interacting protein 1; DE Short=TERF2-interacting telomeric protein 1; DE Short=TRF2-interacting telomeric protein 1; DE AltName: Full=Dopamine receptor-interacting protein 5; DE AltName: Full=Repressor/activator protein 1 homolog; DE Short=RAP1 homolog; DE Short=hRap1; GN Name=TERF2IP; Synonyms=DRIP5, RAP1; ORFNames=PP8000; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Cervix carcinoma; RX PubMed=10850490; DOI=10.1016/s0092-8674(00)80858-2; RA Li B., Oestreich S., de Lange T.; RT "Identification of human RAP1: implications for telomere evolution."; RL Cell 101:471-483(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Lafuente M.J., Nasir J.; RT "Cloning and characterization of DRIP5, a new protein that specifically RT interacts with the D1 dopamine receptor."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15498874; DOI=10.1073/pnas.0404089101; RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X., RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.; RT "Large-scale cDNA transfection screening for genes related to cancer RT development and progression."; RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Ileal mucosa, and Teratocarcinoma; 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon, Lung, and Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP BIDIRECTIONAL PROMOTER WITH KARS1. RX PubMed=14659874; DOI=10.1016/j.gene.2003.08.026; RA Tan M., Wei C., Price C.M.; RT "The telomeric protein Rap1 is conserved in vertebrates and is expressed RT from a bidirectional promoter positioned between the Rap1 and KARS genes."; RL Gene 323:1-10(2003). RN [9] RP IDENTIFICATION IN THE SHELTERIN COMPLEX. RX PubMed=15316005; DOI=10.1074/jbc.m409047200; RA Ye J.Z.-S., Donigian J.R., van Overbeek M., Loayza D., Luo Y., RA Krutchinsky A.N., Chait B.T., de Lange T.; RT "TIN2 binds TRF1 and TRF2 simultaneously and stabilizes the TRF2 complex on RT telomeres."; RL J. Biol. Chem. 279:47264-47271(2004). RN [10] RP IDENTIFICATION IN THE SHELTERIN COMPLEX. RX PubMed=15383534; DOI=10.1074/jbc.m409293200; RA Liu D., O'Connor M.S., Qin J., Songyang Z.; RT "Telosome, a mammalian telomere-associated complex formed by multiple RT telomeric proteins."; RL J. Biol. Chem. 279:51338-51342(2004). RN [11] RP FUNCTION OF THE SHELTERIN COMPLEX. RX PubMed=16166375; DOI=10.1101/gad.1346005; RA de Lange T.; RT "Shelterin: the protein complex that shapes and safeguards human RT telomeres."; RL Genes Dev. 19:2100-2110(2005). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156 AND SER-203, 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 phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-154 AND SER-203, AND RP IDENTIFICATION BY MASS 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 [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [16] RP INTERACTION WITH SLX4. RX PubMed=19596235; DOI=10.1016/j.cell.2009.06.030; RA Svendsen J.M., Smogorzewska A., Sowa M.E., O'Connell B.C., Gygi S.P., RA Elledge S.J., Harper J.W.; RT "Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is RT required for DNA repair."; RL Cell 138:63-77(2009). RN [17] RP FUNCTION. RX PubMed=19763083; DOI=10.1038/emboj.2009.275; RA Sarthy J., Bae N.S., Scrafford J., Baumann P.; RT "Human RAP1 inhibits non-homologous end joining at telomeres."; RL EMBO J. 28:3390-3399(2009). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154 AND SER-203, 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-154 AND SER-203, AND RP IDENTIFICATION BY MASS 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., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [20] 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., Buerckstuemmer T., RA 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-43; SER-154; SER-203 RP AND SER-206, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND IDENTIFICATION BY RP 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., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [24] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-240, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [25] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-114; LYS-212 AND LYS-240, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [26] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-114; LYS-194; LYS-208; LYS-212; RP LYS-240 AND LYS-372, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [27] RP STRUCTURE BY NMR OF 132-190. RX PubMed=11545594; DOI=10.1006/jmbi.2001.4924; RA Hanaoka S., Nagadoi A., Yoshimura S., Aimoto S., Li B., de Lange T., RA Nishimura Y.; RT "NMR structure of the hRap1 Myb motif reveals a canonical three-helix RT bundle lacking the positive surface charge typical of Myb DNA-binding RT domains."; RL J. Mol. Biol. 312:167-175(2001). CC -!- FUNCTION: Acts both as a regulator of telomere function and as a CC transcription regulator. Involved in the regulation of telomere length CC and protection as a component of the shelterin complex (telosome). In CC contrast to other components of the shelterin complex, it is CC dispensible for telomere capping and does not participate in the CC protection of telomeres against non-homologous end-joining (NHEJ)- CC mediated repair. Instead, it is required to negatively regulate CC telomere recombination and is essential for repressing homology- CC directed repair (HDR), which can affect telomere length. Does not bind CC DNA directly: recruited to telomeric double-stranded 5'-TTAGGG-3' CC repeats via its interaction with TERF2. Independently of its function CC in telomeres, also acts as a transcription regulator: recruited to CC extratelomeric 5'-TTAGGG-3' sites via its association with TERF2 or CC other factors, and regulates gene expression. When cytoplasmic, CC associates with the I-kappa-B-kinase (IKK) complex and acts as a CC regulator of the NF-kappa-B signaling by promoting IKK-mediated CC phosphorylation of RELA/p65, leading to activate expression of NF- CC kappa-B target genes. {ECO:0000269|PubMed:16166375, CC ECO:0000269|PubMed:19763083}. CC -!- SUBUNIT: Associates with the I-kappa-B-kinase (IKK) core complex, CC composed of CHUK, IKBKB and IKBKG (By similarity). Homodimer. Component CC of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, CC TERF2IP ACD and POT1. Interacts with TERF2; the interaction is direct. CC Does not interact with TERF1. Interacts with SLX4/BTBD12. {ECO:0000250, CC ECO:0000269|PubMed:15316005, ECO:0000269|PubMed:15383534, CC ECO:0000269|PubMed:19596235}. CC -!- INTERACTION: CC Q9NYB0; Q13155: AIMP2; NbExp=2; IntAct=EBI-750109, EBI-745226; CC Q9NYB0; P14550: AKR1A1; NbExp=2; IntAct=EBI-750109, EBI-372388; CC Q9NYB0; O60218: AKR1B10; NbExp=2; IntAct=EBI-750109, EBI-1572139; CC Q9NYB0; O95154: AKR7A3; NbExp=2; IntAct=EBI-750109, EBI-748869; CC Q9NYB0; P31749: AKT1; NbExp=2; IntAct=EBI-750109, EBI-296087; CC Q9NYB0; Q9NWV8: BABAM1; NbExp=2; IntAct=EBI-750109, EBI-745725; CC Q9NYB0; Q9BQE9: BCL7B; NbExp=2; IntAct=EBI-750109, EBI-2560588; CC Q9NYB0; Q8IYL3: C1orf174; NbExp=2; IntAct=EBI-750109, EBI-715898; CC Q9NYB0; Q9NZ63: C9orf78; NbExp=2; IntAct=EBI-750109, EBI-2557577; CC Q9NYB0; P27482: CALML3; NbExp=2; IntAct=EBI-750109, EBI-747537; CC Q9NYB0; Q9UQN3: CHMP2B; NbExp=2; IntAct=EBI-750109, EBI-718324; CC Q9NYB0; Q14019: COTL1; NbExp=2; IntAct=EBI-750109, EBI-79926; CC Q9NYB0; Q96FN4: CPNE2; NbExp=2; IntAct=EBI-750109, EBI-7097057; CC Q9NYB0; P46108: CRK; NbExp=2; IntAct=EBI-750109, EBI-886; CC Q9NYB0; Q13363: CTBP1; NbExp=2; IntAct=EBI-750109, EBI-908846; CC Q9NYB0; Q92620: DHX38; NbExp=2; IntAct=EBI-750109, EBI-1043041; CC Q9NYB0; Q8N8S7: ENAH; NbExp=2; IntAct=EBI-750109, EBI-2834410; CC Q9NYB0; Q8TE68: EPS8L1; NbExp=2; IntAct=EBI-750109, EBI-7487998; CC Q9NYB0; P12104: FABP2; NbExp=2; IntAct=EBI-750109, EBI-3905109; CC Q9NYB0; Q13069: GAGE5; NbExp=2; IntAct=EBI-750109, EBI-745702; CC Q9NYB0; Q92917: GPKOW; NbExp=2; IntAct=EBI-750109, EBI-746309; CC Q9NYB0; Q16775: HAGH; NbExp=2; IntAct=EBI-750109, EBI-3905342; CC Q9NYB0; O15347: HMGB3; NbExp=2; IntAct=EBI-750109, EBI-2214136; CC Q9NYB0; O00479: HMGN4; NbExp=2; IntAct=EBI-750109, EBI-2867693; CC Q9NYB0; P61978: HNRNPK; NbExp=2; IntAct=EBI-750109, EBI-304185; CC Q9NYB0; P18510: IL1RN; NbExp=2; IntAct=EBI-750109, EBI-1026330; CC Q9NYB0; Q9NS86: LANCL2; NbExp=2; IntAct=EBI-750109, EBI-2510837; CC Q9NYB0; Q96A72: MAGOHB; NbExp=2; IntAct=EBI-750109, EBI-746778; CC Q9NYB0; P49736: MCM2; NbExp=2; IntAct=EBI-750109, EBI-374819; CC Q9NYB0; Q9UKD2: MRTO4; NbExp=2; IntAct=EBI-750109, EBI-1046493; CC Q9NYB0; P80297: MT1X; NbExp=2; IntAct=EBI-750109, EBI-11308402; CC Q9NYB0; P25713: MT3; NbExp=2; IntAct=EBI-750109, EBI-8084264; CC Q9NYB0; P49321: NASP; NbExp=2; IntAct=EBI-750109, EBI-716205; CC Q9NYB0; O95848: NUDT14; NbExp=2; IntAct=EBI-750109, EBI-536866; CC Q9NYB0; Q6ZVK8: NUDT18; NbExp=2; IntAct=EBI-750109, EBI-740486; CC Q9NYB0; Q14980: NUMA1; NbExp=2; IntAct=EBI-750109, EBI-521611; CC Q9NYB0; Q9NZT2: OGFR; NbExp=2; IntAct=EBI-750109, EBI-1044212; CC Q9NYB0; Q96E09: PABIR1; NbExp=2; IntAct=EBI-750109, EBI-9355758; CC Q9NYB0; Q8WW12: PCNP; NbExp=2; IntAct=EBI-750109, EBI-10972020; CC Q9NYB0; P48539: PCP4; NbExp=2; IntAct=EBI-750109, EBI-4287270; CC Q9NYB0; Q15121: PEA15; NbExp=2; IntAct=EBI-750109, EBI-714410; CC Q9NYB0; O95336: PGLS; NbExp=2; IntAct=EBI-750109, EBI-11307753; CC Q9NYB0; P28340: POLD1; NbExp=2; IntAct=EBI-750109, EBI-716569; CC Q9NYB0; Q5H9R7: PPP6R3; NbExp=2; IntAct=EBI-750109, EBI-355498; CC Q9NYB0; Q9BXM0: PRX; NbExp=2; IntAct=EBI-750109, EBI-1753064; CC Q9NYB0; P06454: PTMA; NbExp=2; IntAct=EBI-750109, EBI-2682091; CC Q9NYB0; P47224: RABIF; NbExp=2; IntAct=EBI-750109, EBI-713992; CC Q9NYB0; O75884: RBBP9; NbExp=2; IntAct=EBI-750109, EBI-11310604; CC Q9NYB0; Q96B86: RGMA; NbExp=2; IntAct=EBI-750109, EBI-722102; CC Q9NYB0; Q9BUL9: RPP25; NbExp=2; IntAct=EBI-750109, EBI-366570; CC Q9NYB0; P25815: S100P; NbExp=2; IntAct=EBI-750109, EBI-743700; CC Q9NYB0; Q96I15: SCLY; NbExp=2; IntAct=EBI-750109, EBI-2823066; CC Q9NYB0; Q8IY92: SLX4; NbExp=4; IntAct=EBI-750109, EBI-2370740; CC Q9NYB0; Q8TAQ2: SMARCC2; NbExp=2; IntAct=EBI-750109, EBI-357418; CC Q9NYB0; P37837: TALDO1; NbExp=2; IntAct=EBI-750109, EBI-1056712; CC Q9NYB0; O75347: TBCA; NbExp=2; IntAct=EBI-750109, EBI-2686341; CC Q9NYB0; Q15554: TERF2; NbExp=36; IntAct=EBI-750109, EBI-706637; CC Q9NYB0; Q9BSI4-3: TINF2; NbExp=3; IntAct=EBI-750109, EBI-717418; CC Q9NYB0; O14604: TMSB4Y; NbExp=2; IntAct=EBI-750109, EBI-751196; CC Q9NYB0; Q5JTV8: TOR1AIP1; NbExp=2; IntAct=EBI-750109, EBI-2559665; CC Q9NYB0; Q9Y5U2: TSSC4; NbExp=2; IntAct=EBI-750109, EBI-717229; CC Q9NYB0; Q6IBS0: TWF2; NbExp=2; IntAct=EBI-750109, EBI-722204; CC Q9NYB0; P09936: UCHL1; NbExp=2; IntAct=EBI-750109, EBI-714860; CC Q9NYB0; Q14135: VGLL4; NbExp=2; IntAct=EBI-750109, EBI-5278589; CC Q9NYB0; P61964: WDR5; NbExp=2; IntAct=EBI-750109, EBI-540834; CC Q9NYB0; Q96GT9: XAGE2; NbExp=2; IntAct=EBI-750109, EBI-750167; CC Q9NYB0; P12956: XRCC6; NbExp=3; IntAct=EBI-750109, EBI-353208; CC Q9NYB0; Q96IQ9: ZNF414; NbExp=2; IntAct=EBI-750109, EBI-744257; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q91VL8}. Cytoplasm CC {ECO:0000250|UniProtKB:Q91VL8}. Chromosome CC {ECO:0000250|UniProtKB:Q91VL8}. Chromosome, telomere CC {ECO:0000250|UniProtKB:Q91VL8}. Note=Associates with chromosomes, both CC at telomeres and in extratelomeric sites. Also exists as a cytoplasmic CC form, where it associates with the IKK complex. CC {ECO:0000250|UniProtKB:Q91VL8}. CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed. CC -!- MISCELLANEOUS: Shares a bidirectional promoter with KARS1. CC {ECO:0000305|PubMed:14659874}. CC -!- SIMILARITY: Belongs to the RAP1 family. {ECO:0000305}. CC -!- CAUTION: Was reported to participate in the protection of telomeres CC against non-homologous end-joining (NHEJ)-mediated repair in the CC absence of TERF2 (PubMed:19763083). However, this probably does not CC corresponds to its primary function and experiments in mouse showed CC that it is dispensible for such process and is required for repression CC of homology-directed repair (HDR). {ECO:0000305|PubMed:19763083}. CC -!- SEQUENCE CAUTION: CC Sequence=AAL55783.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAA91317.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305}; CC Sequence=BAG60996.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AF262988; AAF72711.1; -; mRNA. DR EMBL; AF250393; AAQ14259.1; -; mRNA. DR EMBL; AF289599; AAL55783.1; ALT_FRAME; mRNA. DR EMBL; AK000669; BAA91317.1; ALT_SEQ; mRNA. DR EMBL; AK298880; BAG60996.1; ALT_INIT; mRNA. DR EMBL; AC025287; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471114; EAW95616.1; -; Genomic_DNA. DR EMBL; CH471114; EAW95618.1; -; Genomic_DNA. DR EMBL; BC004465; AAH04465.1; -; mRNA. DR EMBL; BC005841; AAH05841.1; -; mRNA. DR EMBL; BC022428; AAH22428.1; -; mRNA. DR EMBL; BC078171; AAH78171.1; -; mRNA. DR CCDS; CCDS32491.1; -. DR RefSeq; NP_061848.2; NM_018975.3. DR PDB; 1FEX; NMR; -; A=132-190. DR PDB; 3K6G; X-ray; 1.95 A; A/B/C=303-399. DR PDB; 4RQI; X-ray; 2.44 A; E/F/G/H=89-106. DR PDB; 7OZ0; NMR; -; A=1-114. DR PDBsum; 1FEX; -. DR PDBsum; 3K6G; -. DR PDBsum; 4RQI; -. DR PDBsum; 7OZ0; -. DR AlphaFoldDB; Q9NYB0; -. DR BMRB; Q9NYB0; -. DR SMR; Q9NYB0; -. DR BioGRID; 119942; 614. DR ComplexPortal; CPX-152; Shelterin complex. DR CORUM; Q9NYB0; -. DR DIP; DIP-34868N; -. DR IntAct; Q9NYB0; 161. DR MINT; Q9NYB0; -. DR STRING; 9606.ENSP00000300086; -. DR BindingDB; Q9NYB0; -. DR ChEMBL; CHEMBL3751647; -. DR GlyCosmos; Q9NYB0; 1 site, 1 glycan. DR GlyGen; Q9NYB0; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q9NYB0; -. DR PhosphoSitePlus; Q9NYB0; -. DR BioMuta; TERF2IP; -. DR DMDM; 21542267; -. DR EPD; Q9NYB0; -. DR jPOST; Q9NYB0; -. DR MassIVE; Q9NYB0; -. DR MaxQB; Q9NYB0; -. DR PaxDb; Q9NYB0; -. DR PeptideAtlas; Q9NYB0; -. DR ProteomicsDB; 83206; -. DR Antibodypedia; 1877; 566 antibodies from 42 providers. DR DNASU; 54386; -. DR Ensembl; ENST00000300086.5; ENSP00000300086.4; ENSG00000166848.7. DR GeneID; 54386; -. DR KEGG; hsa:54386; -. DR MANE-Select; ENST00000300086.5; ENSP00000300086.4; NM_018975.4; NP_061848.2. DR UCSC; uc002fet.3; human. DR AGR; HGNC:19246; -. DR CTD; 54386; -. DR DisGeNET; 54386; -. DR GeneCards; TERF2IP; -. DR HGNC; HGNC:19246; TERF2IP. DR HPA; ENSG00000166848; Low tissue specificity. DR MalaCards; TERF2IP; -. DR MIM; 605061; gene. DR neXtProt; NX_Q9NYB0; -. DR OpenTargets; ENSG00000166848; -. DR Orphanet; 618; Familial melanoma. DR PharmGKB; PA134976325; -. DR VEuPathDB; HostDB:ENSG00000166848; -. DR eggNOG; ENOG502RPXS; Eukaryota. DR GeneTree; ENSGT00390000005351; -. DR HOGENOM; CLU_028192_0_0_1; -. DR InParanoid; Q9NYB0; -. DR OMA; MEKFAVD; -. DR OrthoDB; 2920206at2759; -. DR PhylomeDB; Q9NYB0; -. DR TreeFam; TF332348; -. DR PathwayCommons; Q9NYB0; -. DR Reactome; R-HSA-110328; Recognition and association of DNA glycosylase with site containing an affected pyrimidine. DR Reactome; R-HSA-110329; Cleavage of the damaged pyrimidine. DR Reactome; R-HSA-110330; Recognition and association of DNA glycosylase with site containing an affected purine. DR Reactome; R-HSA-110331; Cleavage of the damaged purine. DR Reactome; R-HSA-1221632; Meiotic synapsis. DR Reactome; R-HSA-171306; Packaging Of Telomere Ends. DR Reactome; R-HSA-171319; Telomere Extension By Telomerase. DR Reactome; R-HSA-174411; Polymerase switching on the C-strand of the telomere. DR Reactome; R-HSA-174414; Processive synthesis on the C-strand of the telomere. DR Reactome; R-HSA-174417; Telomere C-strand (Lagging Strand) Synthesis. DR Reactome; R-HSA-174430; Telomere C-strand synthesis initiation. DR Reactome; R-HSA-174437; Removal of the Flap Intermediate from the C-strand. DR Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence. DR Reactome; R-HSA-9670095; Inhibition of DNA recombination at telomere. DR SignaLink; Q9NYB0; -. DR SIGNOR; Q9NYB0; -. DR BioGRID-ORCS; 54386; 23 hits in 1161 CRISPR screens. DR ChiTaRS; TERF2IP; human. DR EvolutionaryTrace; Q9NYB0; -. DR GeneWiki; TERF2IP; -. DR GenomeRNAi; 54386; -. DR Pharos; Q9NYB0; Tchem. DR PRO; PR:Q9NYB0; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q9NYB0; protein. DR Bgee; ENSG00000166848; Expressed in middle temporal gyrus and 209 other tissues. DR ExpressionAtlas; Q9NYB0; baseline and differential. DR Genevisible; Q9NYB0; HS. DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:CAFA. DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0000228; C:nuclear chromosome; TAS:ProtInc. DR GO; GO:0000783; C:nuclear telomere cap complex; IDA:BHF-UCL. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0070187; C:shelterin complex; IDA:BHF-UCL. DR GO; GO:0098505; F:G-rich strand telomeric DNA binding; IDA:BHF-UCL. DR GO; GO:0019902; F:phosphatase binding; IPI:CAFA. DR GO; GO:0042162; F:telomeric DNA binding; IDA:BHF-UCL. DR GO; GO:0048239; P:negative regulation of DNA recombination at telomere; ISS:UniProtKB. DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:CAFA. DR GO; GO:0032205; P:negative regulation of telomere maintenance; IDA:UniProtKB. DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB. DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB. DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IMP:CAFA. DR GO; GO:0032206; P:positive regulation of telomere maintenance; NAS:ComplexPortal. DR GO; GO:0031848; P:protection from non-homologous end joining at telomere; IMP:BHF-UCL. DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; IMP:BHF-UCL. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:CAFA. DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISS:UniProtKB. DR GO; GO:0032204; P:regulation of telomere maintenance; IMP:BHF-UCL. DR GO; GO:0016233; P:telomere capping; IDA:ComplexPortal. DR GO; GO:0000723; P:telomere maintenance; IDA:BHF-UCL. DR GO; GO:0007004; P:telomere maintenance via telomerase; TAS:ProtInc. DR GO; GO:0010833; P:telomere maintenance via telomere lengthening; ISS:UniProtKB. DR CDD; cd11655; rap1_myb-like; 1. DR CDD; cd11653; rap1_RCT; 1. DR Gene3D; 1.10.10.2170; -; 1. DR Gene3D; 3.40.50.10190; BRCT domain; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. DR InterPro; IPR001357; BRCT_dom. DR InterPro; IPR036420; BRCT_dom_sf. DR InterPro; IPR009057; Homeobox-like_sf. DR InterPro; IPR021661; Rap1_C. DR InterPro; IPR038104; Rap1_C_sf. DR InterPro; IPR015010; Rap1_Myb_dom. DR InterPro; IPR039595; TE2IP/Rap1. DR PANTHER; PTHR16466; TELOMERE REPEAT-BINDING FACTOR 2-INTERACTING PROTEIN 1; 1. DR PANTHER; PTHR16466:SF6; TELOMERIC REPEAT-BINDING FACTOR 2-INTERACTING PROTEIN 1; 1. DR Pfam; PF16589; BRCT_2; 1. DR Pfam; PF08914; Myb_DNA-bind_2; 1. DR Pfam; PF11626; Rap1_C; 1. DR SUPFAM; SSF46689; Homeodomain-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Chromosome; Cytoplasm; KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Telomere; KW Transcription; Transcription regulation; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330" FT CHAIN 2..399 FT /note="Telomeric repeat-binding factor 2-interacting FT protein 1" FT /id="PRO_0000197126" FT DOMAIN 78..101 FT /note="BRCT" FT DOMAIN 128..188 FT /note="Myb-like" FT REGION 104..132 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 196..244 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 264..311 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 383..399 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 208..237 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 264..283 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 284..306 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 36 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 43 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 154 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 156 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243" FT MOD_RES 203 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 206 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 114 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 194 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 208 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 212 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 240 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733" FT CROSSLNK 372 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 324 FT /note="K -> E (in dbSNP:rs4888444)" FT /id="VAR_050195" FT CONFLICT 83 FT /note="Y -> H (in Ref. 4; BAA91317)" FT /evidence="ECO:0000305" FT HELIX 93..97 FT /evidence="ECO:0007829|PDB:4RQI" FT HELIX 138..150 FT /evidence="ECO:0007829|PDB:1FEX" FT TURN 155..159 FT /evidence="ECO:0007829|PDB:1FEX" FT HELIX 162..169 FT /evidence="ECO:0007829|PDB:1FEX" FT STRAND 172..174 FT /evidence="ECO:0007829|PDB:1FEX" FT HELIX 178..187 FT /evidence="ECO:0007829|PDB:1FEX" FT HELIX 308..324 FT /evidence="ECO:0007829|PDB:3K6G" FT HELIX 329..338 FT /evidence="ECO:0007829|PDB:3K6G" FT TURN 339..341 FT /evidence="ECO:0007829|PDB:3K6G" FT HELIX 343..352 FT /evidence="ECO:0007829|PDB:3K6G" FT HELIX 364..370 FT /evidence="ECO:0007829|PDB:3K6G" FT HELIX 375..385 FT /evidence="ECO:0007829|PDB:3K6G" FT HELIX 387..397 FT /evidence="ECO:0007829|PDB:3K6G" SQ SEQUENCE 399 AA; 44260 MW; EAA615777F9D3D3D CRC64; MAEAMDLGKD PNGPTHSSTL FVRDDGSSMS FYVRPSPAKR RLSTLILHGG GTVCRVQEPG AVLLAQPGEA LAEASGDFIS TQYILDCVER NERLELEAYR LGPASAADTG SEAKPGALAE GAAEPEPQRH AGRIAFTDAD DVAILTYVKE NARSPSSVTG NALWKAMEKS SLTQHSWQSL KDRYLKHLRG QEHKYLLGDA PVSPSSQKLK RKAEEDPEAA DSGEPQNKRT PDLPEEEYVK EEIQENEEAV KKMLVEATRE FEEVVVDESP PDFEIHITMC DDDPPTPEED SETQPDEEEE EEEEKVSQPE VGAAIKIIRQ LMEKFNLDLS TVTQAFLKNS GELEATSAFL ASGQRADGYP IWSRQDDIDL QKDDEDTREA LVKKFGAQNV ARRIEFRKK //