ID TE2IP_HUMAN Reviewed; 399 AA. AC Q9NYB0; Q8WYZ3; Q9NWR2; DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 21-AUG-2007, entry version 70. DE Telomeric repeat-binding factor 2-interacting protein 1 (TRF2- DE interacting telomeric protein Rap1) (hRap1). GN Name=TERF2IP; Synonyms=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 MEDLINE=20306663; 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 [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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Ileal mucosa; 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 [4] 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND MASS RP SPECTROMETRY. RC TISSUE=Epithelium; RX PubMed=15302935; DOI=10.1073/pnas.0404720101; RA Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., RA Li J., Cohn M.A., Cantley L.C., Gygi S.P.; RT "Large-scale characterization of HeLa cell nuclear phosphoproteins."; RL Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-156 AND RP SER-203, AND MASS SPECTROMETRY. RC TISSUE=Epithelium; 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASS RP SPECTROMETRY. RX PubMed=17287340; DOI=10.1073/pnas.0611217104; RA Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; RT "Global proteomic profiling of phosphopeptides using electron transfer RT dissociation tandem mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND SER-206, AND RP MASS SPECTROMETRY. 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 [9] RP STRUCTURE BY NMR OF 132-190. RX MEDLINE=21431821; 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: May play a role in telomere length regulation. CC -!- SUBUNIT: Homodimer. Binds to TRF2 (but not TRF1) with its C- CC terminus. CC -!- INTERACTION: CC Q9BSI4-3:TINF2; NbExp=1; IntAct=EBI-750109, EBI-717418; CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Colocalizes with telomeric DNA CC in interphase and metaphase cells. CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed. CC -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. CC -!- MISCELLANEOUS: Recruited to telomeres by TRF2; seemingly it does CC not directly bind to DNA itself. CC -!- SIMILARITY: Contains 1 BRCT domain. CC -!- SIMILARITY: Contains 1 Myb-like domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAL55783.1; Type=Frameshift; Positions=151; CC Sequence=BAA91317.1; Type=Erroneous termination; Positions=299; Note=Translated as Glu; 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; AF289599; AAL55783.1; ALT_FRAME; mRNA. DR EMBL; AK000669; BAA91317.1; ALT_SEQ; mRNA. 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 UniGene; Hs.301419; -. DR PDB; 1FEX; NMR; A=132-190. DR IntAct; Q9NYB0; -. DR PeptideAtlas; Q9NYB0; -. DR Ensembl; ENSG00000166848; Homo sapiens. DR KEGG; hsa:54386; -. DR H-InvDB; HIX0013251; -. DR HGNC; HGNC:19246; TERF2IP. DR MIM; 605061; gene. DR PharmGKB; PA134976325; -. DR Reactome; REACT_7970.1; Maintenance of Telomeres. DR LinkHub; Q9NYB0; -. DR ArrayExpress; Q9NYB0; -. DR GermOnline; ENSG00000166848; Homo sapiens. DR GO; GO:0000228; C:nuclear chromosome; TAS:ProtInc. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IMP:UniProtKB. DR GO; GO:0007004; P:telomere maintenance via telomerase; TAS:ProtInc. DR InterPro; IPR001357; BRCT. DR InterPro; IPR012287; Homeodomain-rel. DR InterPro; IPR015010; Myb_DNA-bd_2. DR InterPro; IPR001005; SANT_DNA-bd. DR Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1. DR Pfam; PF08914; Myb_DNA-bind_2; 1. DR PROSITE; PS50172; BRCT; FALSE_NEG. DR PROSITE; PS50090; MYB_LIKE; FALSE_NEG. PE 1: Evidence at protein level; KW 3D-structure; Chromosomal protein; Nucleus; Phosphorylation; Telomere. FT CHAIN 1 399 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 (Potential). FT COMPBIAS 214 304 Asp/Glu-rich (acidic). FT MOD_RES 154 154 Phosphoserine. FT MOD_RES 156 156 Phosphoserine. FT MOD_RES 203 203 Phosphoserine. FT MOD_RES 206 206 Phosphoserine. FT CONFLICT 83 83 Y -> H (in Ref. 3). FT HELIX 138 150 FT TURN 155 159 FT HELIX 162 169 FT STRAND 172 174 FT HELIX 178 187 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 //