TE2IP_HUMAN
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 03-AUG-2022, entry version 202.
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};
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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 PDBsum; 1FEX; -.
DR PDBsum; 3K6G; -.
DR PDBsum; 4RQI; -.
DR AlphaFoldDB; Q9NYB0; -.
DR BMRB; Q9NYB0; -.
DR SMR; Q9NYB0; -.
DR BioGRID; 119942; 597.
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 GlyGen; Q9NYB0; 1 site, 1 O-linked glycan (1 site).
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 PRIDE; Q9NYB0; -.
DR ProteomicsDB; 83206; -.
DR Antibodypedia; 1877; 529 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 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; TQHSWQA; -.
DR OrthoDB; 602157at2759; -.
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; 22 hits in 1084 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:0005829; C:cytosol; IDA:HPA.
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: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:0032206; P:positive regulation of telomere maintenance; IC: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: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; 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 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 InterPro; IPR039595; TE2IP/Rap1.
DR PANTHER; PTHR16466; PTHR16466; 2.
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; 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
