ID TE2IP_HUMAN STANDARD; PRT; 399 AA. AC Q9NYB0; Q8WYZ3; Q9NWR2; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 24-JAN-2006 (Rel. 49, Last annotation update) 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; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Cervical 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.-I., Saito K., Kawai Y., Isono Y., Nakamura Y., RA Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., RA Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., RA Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., RA Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., RA Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., RA Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., RA Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., RA Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., RA Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., RA Imose N., 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 MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [5] RP PHOSPHORYLATION SITE SER-154. 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 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 -!- SUBCELLULAR LOCATION: Nuclear. Colocalizes with telomeric DNA in CC interphase and metaphase cells. CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed. 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 DNA-binding domain. CC -!- CAUTION: Ref.2 sequence differs from that shown due to a CC frameshift in position 151. CC -!- CAUTION: Ref.3 sequence differs from that shown due to a stop CC codon in position 299 which was translated as Glu to extend the CC sequence. 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 PDB; 1FEX; NMR; A=132-190. DR Ensembl; ENSG00000166848; Homo sapiens. DR HGNC; HGNC:19246; TERF2IP. DR H-InvDB; HIX0013251; -. DR MIM; 605061; -. DR GO; GO:0000228; C:nuclear chromosome; TAS. DR GO; GO:0042162; F:telomeric DNA binding; TAS. DR GO; GO:0007004; P:telomerase-dependent telomere maintenance; TAS. DR InterPro; IPR001357; BRCT. DR InterPro; IPR012287; Homeodomain-rel. DR InterPro; IPR001005; Myb_DNA_bd. DR PROSITE; PS50172; BRCT; FALSE_NEG. DR PROSITE; PS50090; MYB_3; FALSE_NEG. KW 3D-structure; Chromosomal protein; Nuclear protein; Phosphorylation; KW Telomere. FT DOMAIN 78 101 BRCT. FT DNA_BIND 128 188 Myb. FT MOTIF 383 399 Nuclear localization signal (Potential). FT COMPBIAS 214 304 Asp/Glu-rich (acidic). FT MOD_RES 154 154 Phosphoserine. FT CONFLICT 83 83 Y -> H (in Ref. 3). FT HELIX 138 150 FT TURN 151 151 FT TURN 155 159 FT HELIX 162 169 FT HELIX 178 187 FT TURN 188 188 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 //