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 18-JUL-2018, entry version 179. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT specifically 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., RA Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., RA Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., RA 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., 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 [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., RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., RA 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., RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., RA 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP BIDIRECTIONAL PROMOTER WITH KARS. 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 RT expressed from a bidirectional promoter positioned between the Rap1 RT 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 RT complex on 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 RT phosphorylation 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, 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-154 AND SER-203, RP AND 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 RP 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 [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, RP AND 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation 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., 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND IDENTIFICATION RP BY MASS 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 [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-43; SER-154; RP SER-203 AND SER-206, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP 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 [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND IDENTIFICATION RP 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 [24] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-240, AND IDENTIFICATION BY RP MASS 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, RP AND 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 RT replication stress reveals novel small ubiquitin-like modified target RT proteins and 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; RP LYS-212; LYS-240 AND LYS-372, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE 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- RT modification 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 CC length and protection as a component of the shelterin complex CC (telosome). In contrast to other components of the shelterin CC complex, it is dispensible for telomere capping and does not CC participate in the protection of telomeres against non-homologous CC end-joining (NHEJ)-mediated repair. Instead, it is required to CC negatively regulate telomere recombination and is essential for CC repressing homology-directed repair (HDR), which can affect CC telomere length. Does not bind DNA directly: recruited to CC telomeric double-stranded 5'-TTAGGG-3' repeats via its interaction CC with TERF2. Independently of its function in telomeres, also acts CC as a transcription regulator: recruited to extratelomeric 5'- CC TTAGGG-3' sites via its association with TERF2 or other factors, CC and regulates gene expression. When cytoplasmic, associates with CC the I-kappa-B-kinase (IKK) complex and acts as a regulator of the CC NF-kappa-B signaling by promoting IKK-mediated phosphorylation of CC RELA/p65, leading to activate expression of NF-kappa-B target CC genes. {ECO:0000269|PubMed:16166375, 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. CC Component of the shelterin complex (telosome) composed of TERF1, CC TERF2, TINF2, TERF2IP ACD and POT1. Interacts with TERF2; the CC interaction is direct. Does not interact with TERF1. Interacts CC with SLX4/BTBD12. {ECO:0000250, ECO:0000269|PubMed:15316005, CC ECO:0000269|PubMed:15383534, ECO:0000269|PubMed:19596235}. CC -!- INTERACTION: CC Q13155:AIMP2; NbExp=2; IntAct=EBI-750109, EBI-745226; CC P14550:AKR1A1; NbExp=2; IntAct=EBI-750109, EBI-372388; CC O60218:AKR1B10; NbExp=2; IntAct=EBI-750109, EBI-1572139; CC O95154:AKR7A3; NbExp=2; IntAct=EBI-750109, EBI-748869; CC P31749:AKT1; NbExp=2; IntAct=EBI-750109, EBI-296087; CC Q9NWV8:BABAM1; NbExp=2; IntAct=EBI-750109, EBI-745725; CC Q9BQE9:BCL7B; NbExp=2; IntAct=EBI-750109, EBI-2560588; CC Q8IYL3:C1orf174; NbExp=2; IntAct=EBI-750109, EBI-715898; CC Q9NZ63:C9orf78; NbExp=2; IntAct=EBI-750109, EBI-2557577; CC P27482:CALML3; NbExp=2; IntAct=EBI-750109, EBI-747537; CC Q9UQN3:CHMP2B; NbExp=2; IntAct=EBI-750109, EBI-718324; CC Q14019:COTL1; NbExp=2; IntAct=EBI-750109, EBI-79926; CC Q96FN4:CPNE2; NbExp=2; IntAct=EBI-750109, EBI-7097057; CC P46108:CRK; NbExp=2; IntAct=EBI-750109, EBI-886; CC Q13363:CTBP1; NbExp=2; IntAct=EBI-750109, EBI-908846; CC Q92620:DHX38; NbExp=2; IntAct=EBI-750109, EBI-1043041; CC Q8N8S7:ENAH; NbExp=2; IntAct=EBI-750109, EBI-2834410; CC Q8TE68:EPS8L1; NbExp=2; IntAct=EBI-750109, EBI-7487998; CC P12104:FABP2; NbExp=2; IntAct=EBI-750109, EBI-3905109; CC Q96E09:FAM122A; NbExp=2; IntAct=EBI-750109, EBI-9355758; CC Q13069:GAGE5; NbExp=2; IntAct=EBI-750109, EBI-745702; CC Q92917:GPKOW; NbExp=2; IntAct=EBI-750109, EBI-746309; CC Q16775:HAGH; NbExp=2; IntAct=EBI-750109, EBI-3905342; CC O15347:HMGB3; NbExp=2; IntAct=EBI-750109, EBI-2214136; CC O00479:HMGN4; NbExp=2; IntAct=EBI-750109, EBI-2867693; CC P61978:HNRNPK; NbExp=2; IntAct=EBI-750109, EBI-304185; CC P18510:IL1RN; NbExp=2; IntAct=EBI-750109, EBI-1026330; CC Q9NS86:LANCL2; NbExp=2; IntAct=EBI-750109, EBI-2510837; CC Q96A72:MAGOHB; NbExp=2; IntAct=EBI-750109, EBI-746778; CC P49736:MCM2; NbExp=2; IntAct=EBI-750109, EBI-374819; CC Q9UKD2:MRTO4; NbExp=2; IntAct=EBI-750109, EBI-1046493; CC P80297:MT1X; NbExp=2; IntAct=EBI-750109, EBI-11308402; CC P25713:MT3; NbExp=2; IntAct=EBI-750109, EBI-8084264; CC P49321:NASP; NbExp=2; IntAct=EBI-750109, EBI-716205; CC O95848:NUDT14; NbExp=2; IntAct=EBI-750109, EBI-536866; CC Q6ZVK8:NUDT18; NbExp=2; IntAct=EBI-750109, EBI-740486; CC Q14980:NUMA1; NbExp=2; IntAct=EBI-750109, EBI-521611; CC Q9NZT2:OGFR; NbExp=2; IntAct=EBI-750109, EBI-1044212; CC Q8WW12:PCNP; NbExp=2; IntAct=EBI-750109, EBI-10972020; CC P48539:PCP4; NbExp=2; IntAct=EBI-750109, EBI-4287270; CC Q15121:PEA15; NbExp=2; IntAct=EBI-750109, EBI-714410; CC O95336:PGLS; NbExp=2; IntAct=EBI-750109, EBI-11307753; CC P28340:POLD1; NbExp=2; IntAct=EBI-750109, EBI-716569; CC Q5H9R7:PPP6R3; NbExp=2; IntAct=EBI-750109, EBI-355498; CC Q9BXM0:PRX; NbExp=2; IntAct=EBI-750109, EBI-1753064; CC P06454:PTMA; NbExp=2; IntAct=EBI-750109, EBI-2682091; CC P47224:RABIF; NbExp=2; IntAct=EBI-750109, EBI-713992; CC O75884:RBBP9; NbExp=2; IntAct=EBI-750109, EBI-11310604; CC Q96B86:RGMA; NbExp=2; IntAct=EBI-750109, EBI-722102; CC Q9BUL9:RPP25; NbExp=2; IntAct=EBI-750109, EBI-366570; CC P25815:S100P; NbExp=2; IntAct=EBI-750109, EBI-743700; CC Q96I15:SCLY; NbExp=2; IntAct=EBI-750109, EBI-2823066; CC Q8IY92:SLX4; NbExp=4; IntAct=EBI-750109, EBI-2370740; CC Q8TAQ2:SMARCC2; NbExp=2; IntAct=EBI-750109, EBI-357418; CC P37837:TALDO1; NbExp=2; IntAct=EBI-750109, EBI-1056712; CC O75347:TBCA; NbExp=2; IntAct=EBI-750109, EBI-2686341; CC Q15554:TERF2; NbExp=36; IntAct=EBI-750109, EBI-706637; CC Q9BSI4-3:TINF2; NbExp=3; IntAct=EBI-750109, EBI-717418; CC O14604:TMSB4Y; NbExp=2; IntAct=EBI-750109, EBI-751196; CC Q5JTV8:TOR1AIP1; NbExp=2; IntAct=EBI-750109, EBI-2559665; CC Q9Y5U2:TSSC4; NbExp=2; IntAct=EBI-750109, EBI-717229; CC Q6IBS0:TWF2; NbExp=2; IntAct=EBI-750109, EBI-722204; CC P09936:UCHL1; NbExp=2; IntAct=EBI-750109, EBI-714860; CC Q14135:VGLL4; NbExp=2; IntAct=EBI-750109, EBI-5278589; CC P61964:WDR5; NbExp=2; IntAct=EBI-750109, EBI-540834; CC Q96GT9:XAGE2; NbExp=2; IntAct=EBI-750109, EBI-750167; CC P12956:XRCC6; NbExp=3; IntAct=EBI-750109, EBI-353208; CC Q96IQ9:ZNF414; NbExp=2; IntAct=EBI-750109, EBI-744257; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q91VL8}. CC Cytoplasm {ECO:0000250|UniProtKB:Q91VL8}. Chromosome CC {ECO:0000250|UniProtKB:Q91VL8}. Chromosome, telomere CC {ECO:0000250|UniProtKB:Q91VL8}. Note=Associates with chromosomes, CC both at telomeres and in extratelomeric sites. Also exists as a CC cytoplasmic 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 KARS. CC {ECO:0000305|PubMed:14659874}. CC -!- SIMILARITY: Belongs to the RAP1 family. {ECO:0000305}. CC -!- CAUTION: Was reported to participate in the protection of CC telomeres against non-homologous end-joining (NHEJ)-mediated CC repair in the absence of TERF2 (PubMed:19763083). However, this CC probably does not corresponds to its primary function and CC experiments in mouse showed that it is dispensible for such CC process and is required for repressiion of homology-directed CC repair (HDR). {ECO:0000305|PubMed:19763083}. CC -!- SEQUENCE CAUTION: CC Sequence=AAL55783.1; Type=Frameshift; Positions=151; Evidence={ECO:0000305}; CC Sequence=BAA91317.1; Type=Erroneous termination; Positions=299; Note=Translated as Glu.; Evidence={ECO:0000305}; CC Sequence=BAG60996.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; 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 UniGene; Hs.301419; -. 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 PDBsum; 1FEX; -. DR PDBsum; 3K6G; -. DR PDBsum; 4RQI; -. DR ProteinModelPortal; Q9NYB0; -. DR SMR; Q9NYB0; -. DR BioGrid; 119942; 160. DR ComplexPortal; CPX-152; Shelterin complex. DR CORUM; Q9NYB0; -. DR DIP; DIP-34868N; -. DR IntAct; Q9NYB0; 149. DR MINT; Q9NYB0; -. DR STRING; 9606.ENSP00000300086; -. DR BindingDB; Q9NYB0; -. DR ChEMBL; CHEMBL3751647; -. DR iPTMnet; Q9NYB0; -. DR PhosphoSitePlus; Q9NYB0; -. DR BioMuta; TERF2IP; -. DR DMDM; 21542267; -. DR EPD; Q9NYB0; -. DR MaxQB; Q9NYB0; -. DR PaxDb; Q9NYB0; -. DR PeptideAtlas; Q9NYB0; -. DR PRIDE; Q9NYB0; -. DR ProteomicsDB; 83206; -. DR DNASU; 54386; -. DR Ensembl; ENST00000300086; ENSP00000300086; ENSG00000166848. DR GeneID; 54386; -. DR KEGG; hsa:54386; -. DR UCSC; uc002fet.3; human. DR CTD; 54386; -. DR DisGeNET; 54386; -. DR EuPathDB; HostDB:ENSG00000166848.5; -. DR GeneCards; TERF2IP; -. DR HGNC; HGNC:19246; TERF2IP. DR HPA; CAB018660; -. DR HPA; CAB018749; -. DR HPA; HPA006719; -. DR MalaCards; TERF2IP; -. DR MIM; 605061; gene. DR neXtProt; NX_Q9NYB0; -. DR OpenTargets; ENSG00000166848; -. DR PharmGKB; PA134976325; -. DR eggNOG; ENOG410IJNC; Eukaryota. DR eggNOG; ENOG4111QPC; LUCA. DR GeneTree; ENSGT00390000005351; -. DR HOGENOM; HOG000120115; -. DR HOVERGEN; HBG054209; -. DR InParanoid; Q9NYB0; -. DR KO; K11113; -. DR OMA; GFEIHIT; -. DR OrthoDB; EOG091G0NZ2; -. DR PhylomeDB; Q9NYB0; -. DR TreeFam; TF332348; -. DR Reactome; R-HSA-1221632; Meiotic synapsis. DR Reactome; R-HSA-171306; Packaging Of Telomere Ends. DR Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence. DR ChiTaRS; TERF2IP; human. DR EvolutionaryTrace; Q9NYB0; -. DR GeneWiki; TERF2IP; -. DR GenomeRNAi; 54386; -. DR PRO; PR:Q9NYB0; -. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000166848; -. DR CleanEx; HS_TERF2IP; -. 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:0005829; C:cytosol; IDA:HPA. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0000228; C:nuclear chromosome; TAS:ProtInc. DR GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL. DR GO; GO:0005635; C:nuclear envelope; IEA:Ensembl. 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:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:UniProtKB. DR GO; GO:1901985; P:positive regulation of protein acetylation; IMP:UniProtKB. 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: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:0006355; P:regulation of transcription, DNA-templated; IMP:CAFA. DR GO; GO:0016233; P:telomere capping; TAS:Reactome. 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 GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.2170; -; 1. DR Gene3D; 3.40.50.10190; -; 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 Pfam; PF16589; BRCT_2; 1. DR Pfam; PF08914; Myb_DNA-bind_2; 1. DR Pfam; PF11626; Rap1_C; 1. DR SUPFAM; SSF46689; SSF46689; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Chromosome; Complete proteome; KW Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism; KW Reference proteome; Telomere; Transcription; Transcription regulation; KW Ubl conjugation. FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}. FT CHAIN 2 399 Telomeric repeat-binding factor 2- FT interacting protein 1. FT /FTId=PRO_0000197126. FT DOMAIN 78 101 BRCT. FT DOMAIN 128 188 Myb-like. FT MOTIF 383 399 Nuclear localization signal. FT {ECO:0000255}. FT COMPBIAS 214 304 Asp/Glu-rich (acidic). FT MOD_RES 2 2 N-acetylalanine. FT {ECO:0000244|PubMed:19413330}. FT MOD_RES 36 36 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 43 43 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 154 154 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 156 156 Phosphoserine. FT {ECO:0000244|PubMed:16964243}. FT MOD_RES 203 203 Phosphoserine. FT {ECO:0000244|PubMed:16964243, 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 ECO:0000244|PubMed:24275569}. FT MOD_RES 206 206 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT CROSSLNK 114 114 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25755297, FT ECO:0000244|PubMed:28112733}. FT CROSSLNK 194 194 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT CROSSLNK 208 208 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT CROSSLNK 212 212 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25755297, FT ECO:0000244|PubMed:28112733}. FT CROSSLNK 240 240 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447, FT ECO:0000244|PubMed:25755297, FT ECO:0000244|PubMed:28112733}. FT CROSSLNK 372 372 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT VARIANT 324 324 K -> E (in dbSNP:rs4888444). FT /FTId=VAR_050195. FT CONFLICT 83 83 Y -> H (in Ref. 4; BAA91317). FT {ECO:0000305}. FT HELIX 93 97 {ECO:0000244|PDB:4RQI}. FT HELIX 138 150 {ECO:0000244|PDB:1FEX}. FT TURN 155 159 {ECO:0000244|PDB:1FEX}. FT HELIX 162 169 {ECO:0000244|PDB:1FEX}. FT STRAND 172 174 {ECO:0000244|PDB:1FEX}. FT HELIX 178 187 {ECO:0000244|PDB:1FEX}. FT HELIX 308 324 {ECO:0000244|PDB:3K6G}. FT HELIX 329 338 {ECO:0000244|PDB:3K6G}. FT TURN 339 341 {ECO:0000244|PDB:3K6G}. FT HELIX 343 352 {ECO:0000244|PDB:3K6G}. FT HELIX 364 370 {ECO:0000244|PDB:3K6G}. FT HELIX 375 385 {ECO:0000244|PDB:3K6G}. FT HELIX 387 397 {ECO:0000244|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 //