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 27-MAR-2024, entry version 188. 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; 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=6; 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. 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; 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; 140. DR ComplexPortal; CPX-152; Shelterin complex. DR CORUM; Q9BSI4; -. DR DIP; DIP-29413N; -. DR ELM; Q9BSI4; -. DR IntAct; Q9BSI4; 118. 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; 9606-ENSP00000267415; -. DR PeptideAtlas; Q9BSI4; -. DR ProteomicsDB; 78895; -. [Q9BSI4-1] DR ProteomicsDB; 78896; -. [Q9BSI4-2] DR ProteomicsDB; 78897; -. [Q9BSI4-3] DR Pumba; Q9BSI4; -. DR Antibodypedia; 22798; 270 antibodies from 31 providers. DR DNASU; 26277; -. DR Ensembl; ENST00000267415.12; ENSP00000267415.7; ENSG00000092330.19. [Q9BSI4-1] DR Ensembl; ENST00000399423.8; ENSP00000382350.4; ENSG00000092330.19. [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 AGR; HGNC:11824; -. DR CTD; 26277; -. DR DisGeNET; 26277; -. DR GeneCards; TINF2; -. DR GeneReviews; TINF2; -. DR HGNC; HGNC:11824; TINF2. DR HPA; ENSG00000092330; Tissue enriched (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; KERPMVM; -. DR OrthoDB; 4328643at2759; -. 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; 742 hits in 1168 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 100 other cell types or tissues. DR ExpressionAtlas; Q9BSI4; baseline and differential. 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; NAS: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 CDD; cd11741; TIN2_TBM; 1. DR IDEAL; IID00180; -. DR InterPro; IPR039098; TINF2. DR InterPro; IPR029400; TINF2_N. DR PANTHER; PTHR15512; TERF1-INTERACTING NUCLEAR FACTOR 2; 1. DR PANTHER; PTHR15512:SF0; TERF1-INTERACTING NUCLEAR FACTOR 2; 1. DR Pfam; PF14973; TINF2_N; 1. DR Genevisible; Q9BSI4; HS. 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 //