TINF2_HUMAN
ID TINF2_HUMAN Reviewed; 451 AA.
AC Q9BSI4; B3W5Q7; Q9H904; Q9UHC2;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=TERF1-interacting nuclear factor 2;
DE AltName: Full=TRF1-interacting nuclear protein 2;
GN Name=TINF2; Synonyms=TIN2;
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] (ISOFORM 2).
RC TISSUE=Fibroblast;
RX PubMed=10581025; DOI=10.1038/70508;
RA Kim S.-H., Kaminker P., Campisi J.;
RT "TIN2, a new regulator of telomere length in human cells.";
RL Nat. Genet. 23:405-412(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta, and Uterus;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 163-451 (ISOFORM 1).
RA Kaminker P.G., Kim S.-H., Desprez P.Y., Campisi J.;
RT "A novel form of telomere-associated TIN2 localizes to the nuclear
RT matrix.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION IN A COMPLEX WITH POT1; TERF1 AND TNKS1.
RX PubMed=12768206; DOI=10.1038/nature01688;
RA Loayza D., De Lange T.;
RT "POT1 as a terminal transducer of TRF1 telomere length control.";
RL Nature 423:1013-1018(2003).
RN [6]
RP INTERACTION WITH ACD.
RX PubMed=15231715; DOI=10.1101/gad.1215404;
RA Ye J.Z.-S., Hockemeyer D., Krutchinsky A.N., Loayza D., Hooper S.M.,
RA Chait B.T., de Lange T.;
RT "POT1-interacting protein PIP1: a telomere length regulator that recruits
RT POT1 to the TIN2/TRF1 complex.";
RL Genes Dev. 18:1649-1654(2004).
RN [7]
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 [8]
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 [9]
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 [10]
RP FUNCTION IN SHELTERIN COMPLEX ASSEMBLY.
RX PubMed=16880378; DOI=10.1073/pnas.0605303103;
RA O'Connor M.S., Safari A., Xin H., Liu D., Songyang Z.;
RT "A critical role for TPP1 and TIN2 interaction in high-order telomeric
RT complex assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11874-11879(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND IDENTIFICATION BY
RP 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 [12]
RP ALTERNATIVE SPLICING (ISOFORM 2), AND SUBCELLULAR LOCATION.
RX PubMed=19279399; DOI=10.4161/cc.8.6.8337;
RA Smith S.;
RT "The long and short of it: a new isoform of TIN2 in the nuclear matrix.";
RL Cell Cycle 8:797-798(2009).
RN [13]
RP FUNCTION (ISOFORM 1), AND SUBCELLULAR LOCATION (ISOFORM 1).
RX PubMed=19229133; DOI=10.4161/cc.8.6.7941;
RA Kaminker P.G., Kim S.H., Desprez P.Y., Campisi J.;
RT "A novel form of the telomere-associated protein TIN2 localizes to the
RT nuclear matrix.";
RL Cell Cycle 8:931-939(2009).
RN [14]
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 [15]
RP IDENTIFICATION 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., 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 [16]
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=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE 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 [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-302; LYS-306; LYS-341 AND
RP LYS-353, AND IDENTIFICATION BY MASS SPECTROMETRY [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-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 258-275 IN COMPLEX WITH TERF1 OR
RP TERF2, DOMAIN TBM, AND MUTAGENESIS OF PHE-258 AND PRO-262.
RX PubMed=18202258; DOI=10.1126/science.1151804;
RA Chen Y., Yang Y., van Overbeek M., Donigian J.R., Baciu P., de Lange T.,
RA Lei M.;
RT "A shared docking motif in TRF1 and TRF2 used for differential recruitment
RT of telomeric proteins.";
RL Science 319:1092-1096(2008).
RN [20]
RP VARIANTS DKCA3 GLU-280; HIS-282 AND SER-282, AND VARIANT DKCA5 HIS-282.
RX PubMed=18252230; DOI=10.1016/j.ajhg.2007.10.004;
RA Savage S.A., Giri N., Baerlocher G.M., Orr N., Lansdorp P.M., Alter B.P.;
RT "TINF2, a component of the shelterin telomere protection complex, is
RT mutated in dyskeratosis congenita.";
RL Am. J. Hum. Genet. 82:501-509(2008).
CC -!- FUNCTION: Component of the shelterin complex (telosome) that is
CC involved in the regulation of telomere length and protection. Shelterin
CC associates with arrays of double-stranded TTAGGG repeats added by
CC telomerase and protects chromosome ends; without its protective
CC activity, telomeres are no longer hidden from the DNA damage
CC surveillance and chromosome ends are inappropriately processed by DNA
CC repair pathways. Plays a role in shelterin complex assembly. Isoform 1
CC may have additional role in tethering telomeres to the nuclear matrix.
CC {ECO:0000269|PubMed:16166375, ECO:0000269|PubMed:16880378}.
CC -!- SUBUNIT: Monomer. Found in a complex with POT1; TERF1 and TNKS1.
CC Component of the shelterin complex (telosome) composed of TERF1, TERF2,
CC TINF2, TERF2IP ACD and POT1. Interacts with TERF1, TERF2 and ACD.
CC {ECO:0000269|PubMed:12768206, ECO:0000269|PubMed:15231715,
CC ECO:0000269|PubMed:15316005, ECO:0000269|PubMed:15383534,
CC ECO:0000269|PubMed:18202258}.
CC -!- INTERACTION:
CC Q9BSI4; A0A590TQL1: ACD; NbExp=5; IntAct=EBI-717399, EBI-23197871;
CC Q9BSI4; Q96AP0: ACD; NbExp=15; IntAct=EBI-717399, EBI-717666;
CC Q9BSI4; P60709: ACTB; NbExp=2; IntAct=EBI-717399, EBI-353944;
CC Q9BSI4; Q9NZN9: AIPL1; NbExp=2; IntAct=EBI-717399, EBI-6557414;
CC Q9BSI4; Q8IV38: ANKMY2; NbExp=2; IntAct=EBI-717399, EBI-9393876;
CC Q9BSI4; P09525: ANXA4; NbExp=2; IntAct=EBI-717399, EBI-2556852;
CC Q9BSI4; P08758: ANXA5; NbExp=2; IntAct=EBI-717399, EBI-296601;
CC Q9BSI4; P52565: ARHGDIA; NbExp=2; IntAct=EBI-717399, EBI-712693;
CC Q9BSI4; Q8IVW6: ARID3B; NbExp=2; IntAct=EBI-717399, EBI-5458329;
CC Q9BSI4; O95817: BAG3; NbExp=2; IntAct=EBI-717399, EBI-747185;
CC Q9BSI4; Q05682: CALD1; NbExp=2; IntAct=EBI-717399, EBI-1642116;
CC Q9BSI4; Q96MW1: CCDC43; NbExp=2; IntAct=EBI-717399, EBI-9247198;
CC Q9BSI4; Q9Y3X0: CCDC9; NbExp=2; IntAct=EBI-717399, EBI-2557532;
CC Q9BSI4; P49761: CLK3; NbExp=2; IntAct=EBI-717399, EBI-745579;
CC Q9BSI4; O75131: CPNE3; NbExp=2; IntAct=EBI-717399, EBI-718988;
CC Q9BSI4; Q16643: DBN1; NbExp=2; IntAct=EBI-717399, EBI-351394;
CC Q9BSI4; O43602: DCX; NbExp=2; IntAct=EBI-717399, EBI-8646694;
CC Q9BSI4; P23588: EIF4B; NbExp=2; IntAct=EBI-717399, EBI-970310;
CC Q9BSI4; P09104: ENO2; NbExp=2; IntAct=EBI-717399, EBI-713154;
CC Q9BSI4; Q86XD5: FAM131B; NbExp=2; IntAct=EBI-717399, EBI-11308812;
CC Q9BSI4; P04406: GAPDH; NbExp=2; IntAct=EBI-717399, EBI-354056;
CC Q9BSI4; Q8N5Z5: KCTD17; NbExp=2; IntAct=EBI-717399, EBI-743960;
CC Q9BSI4; Q3ZCW2: LGALSL; NbExp=2; IntAct=EBI-717399, EBI-10241423;
CC Q9BSI4; P09960: LTA4H; NbExp=2; IntAct=EBI-717399, EBI-721089;
CC Q9BSI4; P46734: MAP2K3; NbExp=2; IntAct=EBI-717399, EBI-602462;
CC Q9BSI4; Q9UBB6: NCDN; NbExp=2; IntAct=EBI-717399, EBI-1053490;
CC Q9BSI4; O60936: NOL3; NbExp=2; IntAct=EBI-717399, EBI-740992;
CC Q9BSI4; Q7Z2X7: PAGE2; NbExp=2; IntAct=EBI-717399, EBI-10256818;
CC Q9BSI4; P50542: PEX5; NbExp=2; IntAct=EBI-717399, EBI-597835;
CC Q9BSI4; P36871: PGM1; NbExp=2; IntAct=EBI-717399, EBI-2861475;
CC Q9BSI4; Q96G03: PGM2; NbExp=2; IntAct=EBI-717399, EBI-4399372;
CC Q9BSI4; P14618: PKM; NbExp=2; IntAct=EBI-717399, EBI-353408;
CC Q9BSI4; Q9NUX5: POT1; NbExp=3; IntAct=EBI-717399, EBI-752420;
CC Q9BSI4; P41236: PPP1R2; NbExp=2; IntAct=EBI-717399, EBI-1056517;
CC Q9BSI4; P05771: PRKCB; NbExp=2; IntAct=EBI-717399, EBI-706216;
CC Q9BSI4; O43566: RGS14; NbExp=2; IntAct=EBI-717399, EBI-750603;
CC Q9BSI4; P08865: RPSA; NbExp=2; IntAct=EBI-717399, EBI-354112;
CC Q9BSI4; Q96FV2: SCRN2; NbExp=2; IntAct=EBI-717399, EBI-11306862;
CC Q9BSI4; O00338: SULT1C2; NbExp=2; IntAct=EBI-717399, EBI-3913419;
CC Q9BSI4; Q01995: TAGLN; NbExp=2; IntAct=EBI-717399, EBI-1054248;
CC Q9BSI4; O60907: TBL1X; NbExp=2; IntAct=EBI-717399, EBI-3505105;
CC Q9BSI4; P54274: TERF1; NbExp=11; IntAct=EBI-717399, EBI-710997;
CC Q9BSI4; Q15554: TERF2; NbExp=11; IntAct=EBI-717399, EBI-706637;
CC Q9BSI4; Q15785: TOMM34; NbExp=2; IntAct=EBI-717399, EBI-1054499;
CC Q9BSI4; O95361: TRIM16; NbExp=2; IntAct=EBI-717399, EBI-727384;
CC Q9BSI4; Q15642: TRIP10; NbExp=2; IntAct=EBI-717399, EBI-739936;
CC Q9BSI4; P07437: TUBB; NbExp=2; IntAct=EBI-717399, EBI-350864;
CC Q9BSI4; Q9BRA2: TXNDC17; NbExp=2; IntAct=EBI-717399, EBI-1055906;
CC Q9BSI4; P61981: YWHAG; NbExp=2; IntAct=EBI-717399, EBI-359832;
CC Q9BSI4-3; Q96AP0: ACD; NbExp=5; IntAct=EBI-717418, EBI-717666;
CC Q9BSI4-3; P54274: TERF1; NbExp=2; IntAct=EBI-717418, EBI-710997;
CC Q9BSI4-3; Q15554: TERF2; NbExp=4; IntAct=EBI-717418, EBI-706637;
CC Q9BSI4-3; Q9NYB0: TERF2IP; NbExp=3; IntAct=EBI-717418, EBI-750109;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19279399}.
CC Chromosome, telomere {ECO:0000269|PubMed:19279399}. Note=Associated
CC with telomeres.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus matrix
CC {ECO:0000269|PubMed:19229133}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1; Synonyms=TIN2L;
CC IsoId=Q9BSI4-1; Sequence=Displayed;
CC Name=2; Synonyms=TIN2S;
CC IsoId=Q9BSI4-2; Sequence=VSP_003989;
CC Name=3;
CC IsoId=Q9BSI4-3; Sequence=VSP_003987, VSP_003988;
CC -!- TISSUE SPECIFICITY: Detected in heart, brain, placenta, lung, liver,
CC skeletal muscle, kidney and pancreas.
CC -!- DOMAIN: The TBM domain mediates interaction with TERF1.
CC {ECO:0000269|PubMed:18202258}.
CC -!- DISEASE: Dyskeratosis congenita, autosomal dominant, 3 (DKCA3)
CC [MIM:613990]: A rare multisystem disorder caused by defective telomere
CC maintenance. It is characterized by progressive bone marrow failure,
CC and the clinical triad of reticulated skin hyperpigmentation, nail
CC dystrophy, and mucosal leukoplakia. Common but variable features
CC include premature graying, aplastic anemia, low platelets,
CC osteoporosis, pulmonary fibrosis, and liver fibrosis among others.
CC Early mortality is often associated with bone marrow failure,
CC infections, fatal pulmonary complications, or malignancy.
CC {ECO:0000269|PubMed:18252230}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Dyskeratosis congenita, autosomal dominant, 5 (DKCA5)
CC [MIM:268130]: A disease characterized by bone marrow hypoplasia, nail
CC dystrophy, fine sparse hair, fine reticulate skin pigmentation, oral
CC leukoplakia, bilateral exudative retinopathy, cerebellar hypoplasia,
CC and growth retardation. {ECO:0000269|PubMed:18252230}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
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DR EMBL; AF195512; AAF18439.1; -; mRNA.
DR EMBL; AK023166; BAB14440.1; -; mRNA.
DR EMBL; BC005030; AAH05030.1; -; mRNA.
DR EMBL; BC019343; AAH19343.1; -; mRNA.
DR EMBL; EU851975; ACF17559.1; -; mRNA.
DR CCDS; CCDS41936.1; -. [Q9BSI4-1]
DR CCDS; CCDS41937.1; -. [Q9BSI4-2]
DR RefSeq; NP_001092744.1; NM_001099274.1. [Q9BSI4-1]
DR RefSeq; NP_036593.2; NM_012461.2. [Q9BSI4-2]
DR PDB; 3BQO; X-ray; 2.00 A; B=257-276.
DR PDB; 3BU8; X-ray; 2.15 A; C/D=258-275.
DR PDB; 5XYF; X-ray; 2.20 A; A=2-202.
DR PDBsum; 3BQO; -.
DR PDBsum; 3BU8; -.
DR PDBsum; 5XYF; -.
DR AlphaFoldDB; Q9BSI4; -.
DR SMR; Q9BSI4; -.
DR BioGRID; 117660; 133.
DR ComplexPortal; CPX-152; Shelterin complex.
DR CORUM; Q9BSI4; -.
DR DIP; DIP-29413N; -.
DR ELM; Q9BSI4; -.
DR IntAct; Q9BSI4; 119.
DR MINT; Q9BSI4; -.
DR STRING; 9606.ENSP00000267415; -.
DR MoonDB; Q9BSI4; Predicted.
DR iPTMnet; Q9BSI4; -.
DR PhosphoSitePlus; Q9BSI4; -.
DR BioMuta; TINF2; -.
DR DMDM; 21542262; -.
DR EPD; Q9BSI4; -.
DR jPOST; Q9BSI4; -.
DR MassIVE; Q9BSI4; -.
DR MaxQB; Q9BSI4; -.
DR PaxDb; Q9BSI4; -.
DR PeptideAtlas; Q9BSI4; -.
DR PRIDE; Q9BSI4; -.
DR ProteomicsDB; 78895; -. [Q9BSI4-1]
DR ProteomicsDB; 78896; -. [Q9BSI4-2]
DR ProteomicsDB; 78897; -. [Q9BSI4-3]
DR Antibodypedia; 22798; 249 antibodies from 31 providers.
DR DNASU; 26277; -.
DR Ensembl; ENST00000267415.12; ENSP00000267415.7; ENSG00000092330.18. [Q9BSI4-1]
DR Ensembl; ENST00000399423.8; ENSP00000382350.4; ENSG00000092330.18. [Q9BSI4-2]
DR Ensembl; ENST00000642983.1; ENSP00000494089.1; ENSG00000284915.3. [Q9BSI4-2]
DR Ensembl; ENST00000646576.2; ENSP00000495019.1; ENSG00000284915.3. [Q9BSI4-1]
DR GeneID; 26277; -.
DR KEGG; hsa:26277; -.
DR MANE-Select; ENST00000267415.12; ENSP00000267415.7; NM_001099274.3; NP_001092744.1.
DR UCSC; uc001woa.5; human. [Q9BSI4-1]
DR CTD; 26277; -.
DR DisGeNET; 26277; -.
DR GeneCards; TINF2; -.
DR GeneReviews; TINF2; -.
DR HGNC; HGNC:11824; TINF2.
DR HPA; ENSG00000092330; Tissue enhanced (parathyroid).
DR MalaCards; TINF2; -.
DR MIM; 268130; phenotype.
DR MIM; 604319; gene.
DR MIM; 613990; phenotype.
DR neXtProt; NX_Q9BSI4; -.
DR OpenTargets; ENSG00000092330; -.
DR Orphanet; 1775; Dyskeratosis congenita.
DR Orphanet; 3322; Hoyeraal-Hreidarsson syndrome.
DR Orphanet; 3088; Revesz syndrome.
DR PharmGKB; PA36530; -.
DR VEuPathDB; HostDB:ENSG00000092330; -.
DR eggNOG; ENOG502S5UZ; Eukaryota.
DR GeneTree; ENSGT00400000022326; -.
DR InParanoid; Q9BSI4; -.
DR OMA; HGAMPVP; -.
DR OrthoDB; 1445874at2759; -.
DR PhylomeDB; Q9BSI4; -.
DR TreeFam; TF334731; -.
DR PathwayCommons; Q9BSI4; -.
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; Q9BSI4; -.
DR SIGNOR; Q9BSI4; -.
DR BioGRID-ORCS; 26277; 706 hits in 1087 CRISPR screens.
DR ChiTaRS; TINF2; human.
DR EvolutionaryTrace; Q9BSI4; -.
DR GeneWiki; TINF2; -.
DR GenomeRNAi; 26277; -.
DR Pharos; Q9BSI4; Tbio.
DR PRO; PR:Q9BSI4; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9BSI4; protein.
DR Bgee; ENSG00000092330; Expressed in granulocyte and 98 other tissues.
DR ExpressionAtlas; Q9BSI4; baseline and differential.
DR Genevisible; Q9BSI4; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0000783; C:nuclear telomere cap complex; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0010370; C:perinucleolar chromocenter; IDA:BHF-UCL.
DR GO; GO:0070187; C:shelterin complex; IDA:BHF-UCL.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:UniProtKB.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:BHF-UCL.
DR GO; GO:0010836; P:negative regulation of protein ADP-ribosylation; IDA:BHF-UCL.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IMP:BHF-UCL.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; IC:ComplexPortal.
DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; IDA:CACAO.
DR GO; GO:1904356; P:regulation of telomere maintenance via telomere lengthening; IMP:BHF-UCL.
DR GO; GO:0032202; P:telomere assembly; IMP:BHF-UCL.
DR GO; GO:0016233; P:telomere capping; IDA:ComplexPortal.
DR CDD; cd11657; TIN2_N; 1.
DR IDEAL; IID00180; -.
DR InterPro; IPR039098; TINF2.
DR InterPro; IPR029400; TINF2_N.
DR PANTHER; PTHR15512; PTHR15512; 1.
DR Pfam; PF14973; TINF2_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromosome;
KW Disease variant; Dyskeratosis congenita; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Telomere; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..451
FT /note="TERF1-interacting nuclear factor 2"
FT /id="PRO_0000072541"
FT REGION 229..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 256..278
FT /note="TBM"
FT MOTIF 262..268
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 302
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 306
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 341
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 353
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 134..137
FT /note="ELEQ -> VRLV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_003987"
FT VAR_SEQ 138..451
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_003988"
FT VAR_SEQ 355..451
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10581025"
FT /id="VSP_003989"
FT VARIANT 43
FT /note="A -> T (in dbSNP:rs35653076)"
FT /id="VAR_051423"
FT VARIANT 237
FT /note="G -> D (in dbSNP:rs17102313)"
FT /id="VAR_051424"
FT VARIANT 241
FT /note="P -> S (in dbSNP:rs17102311)"
FT /id="VAR_051425"
FT VARIANT 280
FT /note="K -> E (in DKCA3; dbSNP:rs121918543)"
FT /evidence="ECO:0000269|PubMed:18252230"
FT /id="VAR_043914"
FT VARIANT 282
FT /note="R -> H (in DKCA3 and DKCA5; dbSNP:rs121918544)"
FT /evidence="ECO:0000269|PubMed:18252230"
FT /id="VAR_043915"
FT VARIANT 282
FT /note="R -> S (in DKCA3; dbSNP:rs121918545)"
FT /evidence="ECO:0000269|PubMed:18252230"
FT /id="VAR_043916"
FT MUTAGEN 258
FT /note="F->A: Abolishes interaction with TERF1."
FT /evidence="ECO:0000269|PubMed:18202258"
FT MUTAGEN 262
FT /note="P->A: Does not effect interaction with TERF1."
FT /evidence="ECO:0000269|PubMed:18202258"
FT CONFLICT 44
FT /note="V -> I (in Ref. 2; BAB14440)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="Missing (in Ref. 2; BAB14440)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="K -> N (in Ref. 1; AAF18439)"
FT /evidence="ECO:0000305"
FT CONFLICT 323..332
FT /note="ASTGKSKSPC -> PSNGKYKGPY (in Ref. 1; AAF18439)"
FT /evidence="ECO:0000305"
FT HELIX 8..24
FT /evidence="ECO:0007829|PDB:5XYF"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:5XYF"
FT HELIX 31..44
FT /evidence="ECO:0007829|PDB:5XYF"
FT HELIX 51..71
FT /evidence="ECO:0007829|PDB:5XYF"
FT HELIX 76..86
FT /evidence="ECO:0007829|PDB:5XYF"
FT HELIX 101..122
FT /evidence="ECO:0007829|PDB:5XYF"
FT HELIX 128..138
FT /evidence="ECO:0007829|PDB:5XYF"
FT HELIX 141..160
FT /evidence="ECO:0007829|PDB:5XYF"
FT HELIX 169..177
FT /evidence="ECO:0007829|PDB:5XYF"
FT HELIX 187..195
FT /evidence="ECO:0007829|PDB:5XYF"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:3BQO"
SQ SEQUENCE 451 AA; 50023 MW; E5A7FD11CE523979 CRC64;
MATPLVAGPA ALRFAAAASW QVVRGRCVEH FPRVLEFLRS LRAVAPGLVR YRHHERLCMG
LKAKVVVELI LQGRPWAQVL KALNHHFPES GPIVRDPKAT KQDLRKILEA QETFYQQVKQ
LSEAPVDLAS KLQELEQEYG EPFLAAMEKL LFEYLCQLEK ALPTPQAQQL QDVLSWMQPG
VSITSSLAWR QYGVDMGWLL PECSVTDSVN LAEPMEQNPP QQQRLALHNP LPKAKPGTHL
PQGPSSRTHP EPLAGRHFNL APLGRRRVQS QWASTRGGHK ERPTVMLFPF RNLGSPTQVI
SKPESKEEHA IYTADLAMGT RAASTGKSKS PCQTLGGRAL KENPVDLPAT EQKENCLDCY
MDPLRLSLLP PRARKPVCPP SLCSSVITIG DLVLDSDEEE NGQGEGKESL ENYQKTKFDT
LIPTLCEYLP PSGHGAIPVS SCDCRDSSRP L
