PINX1_HUMAN
ID PINX1_HUMAN Reviewed; 328 AA.
AC Q96BK5; B2R9B1; Q548A5; Q6QWG9; Q7Z7J8; Q96QD7; Q9HBU7; Q9NWW2;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=PIN2/TERF1-interacting telomerase inhibitor 1;
DE AltName: Full=Liver-related putative tumor suppressor;
DE AltName: Full=Pin2-interacting protein X1;
DE AltName: Full=Protein 67-11-3;
DE AltName: Full=TRF1-interacting protein 1;
GN Name=PINX1; Synonyms=LPTL, LPTS;
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=Liver;
RX PubMed=11003615; DOI=10.1053/jhep.2000.17967;
RA Liao C., Zhao M., Song H., Uchida K., Yokoyama K.K., Li T.P.;
RT "Identification of the gene for a novel liver-related putative tumor
RT suppressor at a high-frequency loss of heterozygosity region of chromosome
RT 8p23 in human hepatocellular carcinoma.";
RL Hepatology 32:721-727(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT CYS-254.
RC TISSUE=Cervix carcinoma;
RX PubMed=11701125; DOI=10.1016/s0092-8674(01)00538-4;
RA Zhou X.Z., Lu K.P.;
RT "The Pin2/TRF1-interacting protein PinX1 is a potent telomerase
RT inhibitor.";
RL Cell 107:347-359(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Schmidt T.;
RL Thesis (2001), University of Goettingen, Germany.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Liao C., Zhao M., Li T.P.;
RT "Identification of the gene LPTL, encoding for a new isoform of human
RT putative tumor suppressor LPTS.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Qiang F.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Fu Q., Cao Y., Zuo A., Liang D., Zhang Y., Wang B., Huang H., Wu Y.,
RA Zhu L., Wang P., Guo S., Guo G., Zhang J., Wang X.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-215.
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 [8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [10]
RP INTERACTION WITH MCRS1.
RX PubMed=15044100; DOI=10.1016/j.bbrc.2004.02.166;
RA Song H., Li Y., Chen G., Xing Z., Zhao J., Yokoyama K.K., Li T., Zhao M.;
RT "Human MCRS2, a cell-cycle-dependent protein, associates with LPTS/PinX1
RT and reduces the telomere length.";
RL Biochem. Biophys. Res. Commun. 316:1116-1123(2004).
RN [11]
RP FUNCTION, AND INTERACTION WITH TERT AND THE TELOMERASE RNA.
RX PubMed=15381700; DOI=10.1074/jbc.m408131200;
RA Banik S.S.R., Counter C.M.;
RT "Characterization of interactions between PinX1 and human telomerase
RT subunits hTERT and hTR.";
RL J. Biol. Chem. 279:51745-51748(2004).
RN [12]
RP FUNCTION.
RX PubMed=17198684; DOI=10.1016/j.bbrc.2006.12.123;
RA Lin J., Jin R., Zhang B., Yang P.X., Chen H., Bai Y.X., Xie Y., Huang C.,
RA Huang J.;
RT "Characterization of a novel effect of hPinX1 on hTERT nucleolar
RT localization.";
RL Biochem. Biophys. Res. Commun. 353:946-952(2007).
RN [13]
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 [14]
RP INTERACTION WITH TERF1, DOMAIN TBM, AND MUTAGENESIS OF LEU-291 AND PRO-293.
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 [15]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NCL/NUCLEOLIN.
RX PubMed=19393617; DOI=10.1016/j.bbrc.2009.04.077;
RA Li N., Yuan K., Yan F., Huo Y., Zhu T., Liu X., Guo Z., Yao X.;
RT "PinX1 is recruited to the mitotic chromosome periphery by nucleolin and
RT facilitates chromosome congression.";
RL Biochem. Biophys. Res. Commun. 384:76-81(2009).
RN [16]
RP FUNCTION.
RX PubMed=19117989; DOI=10.1158/0008-5472.can-08-1393;
RA Zhang B., Bai Y.X., Ma H.H., Feng F., Jin R., Wang Z.L., Lin J., Sun S.P.,
RA Yang P., Wang X.X., Huang P.T., Huang C.F., Peng Y., Chen Y.C., Kung H.F.,
RA Huang J.J.;
RT "Silencing PinX1 compromises telomere length maintenance as well as
RT tumorigenicity in telomerase-positive human cancer cells.";
RL Cancer Res. 69:75-83(2009).
RN [17]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=19553660; DOI=10.1074/jbc.m109.001990;
RA Yuan K., Li N., Jiang K., Zhu T., Huo Y., Wang C., Lu J., Shaw A.,
RA Thomas K., Zhang J., Mann D., Liao J., Jin C., Yao X.;
RT "PinX1 is a novel microtubule-binding protein essential for accurate
RT chromosome segregation.";
RL J. Biol. Chem. 284:23072-23082(2009).
RN [18]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=19265708; DOI=10.1016/j.jmb.2009.02.051;
RA Yoo J.E., Oh B.-K., Park Y.N.;
RT "Human PinX1 mediates TRF1 accumulation in nucleolus and enhances TRF1
RT binding to telomeres.";
RL J. Mol. Biol. 388:928-940(2009).
RN [19]
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 [20]
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 [21]
RP IDENTIFICATION BY 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 [22]
RP CLEAVAGE BY ENTEROVIRUS 71 PROTEASE 3C (MICROBIAL INFECTION), SUBCELLULAR
RP LOCATION, CLEAVAGE SITE, AND MUTAGENESIS OF GLN-50.
RX PubMed=27847364; DOI=10.1128/jvi.02016-16;
RA Li J., Yao Y., Chen Y., Xu X., Lin Y., Yang Z., Qiao W., Tan J.;
RT "Enterovirus 71 3C Promotes Apoptosis through Cleavage of PinX1, a Telomere
RT Binding Protein.";
RL J. Virol. 91:0-0(2017).
CC -!- FUNCTION: Microtubule-binding protein essential for faithful chromosome
CC segregation. Mediates TRF1 and TERT accumulation in nucleolus and
CC enhances TRF1 binding to telomeres. Inhibits telomerase activity. May
CC inhibit cell proliferation and act as tumor suppressor.
CC {ECO:0000269|PubMed:15381700, ECO:0000269|PubMed:17198684,
CC ECO:0000269|PubMed:19117989, ECO:0000269|PubMed:19265708,
CC ECO:0000269|PubMed:19393617, ECO:0000269|PubMed:19553660}.
CC -!- SUBUNIT: Interacts with MCRS1, TERT, TERF1, NCL/nucleolin, and the
CC telomerase RNA. {ECO:0000269|PubMed:15044100,
CC ECO:0000269|PubMed:15381700, ECO:0000269|PubMed:18202258,
CC ECO:0000269|PubMed:19393617}.
CC -!- INTERACTION:
CC Q96BK5; Q96BJ3: AIDA; NbExp=4; IntAct=EBI-721782, EBI-4401674;
CC Q96BK5; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-721782, EBI-725606;
CC Q96BK5; Q8N9N8: EIF1AD; NbExp=3; IntAct=EBI-721782, EBI-750700;
CC Q96BK5; P13807: GYS1; NbExp=3; IntAct=EBI-721782, EBI-740553;
CC Q96BK5; P55081: MFAP1; NbExp=3; IntAct=EBI-721782, EBI-1048159;
CC Q96BK5; P06748: NPM1; NbExp=11; IntAct=EBI-721782, EBI-78579;
CC Q96BK5; P54274: TERF1; NbExp=3; IntAct=EBI-721782, EBI-710997;
CC Q96BK5; O14746: TERT; NbExp=6; IntAct=EBI-721782, EBI-1772203;
CC Q96BK5; Q9UKI8: TLK1; NbExp=3; IntAct=EBI-721782, EBI-740492;
CC Q96BK5; O14787-2: TNPO2; NbExp=3; IntAct=EBI-721782, EBI-12076664;
CC Q96BK5; Q9BZL1: UBL5; NbExp=3; IntAct=EBI-721782, EBI-607755;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27847364}. Nucleus,
CC nucleolus. Chromosome, telomere. Chromosome, centromere, kinetochore.
CC Note=Localizes in nucleoli, at telomere speckles and to the outer plate
CC of kinetochores. Localization to the kinetochore is mediated by its
CC central region and depends on NDC80 and CENPE.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96BK5-1; Sequence=Displayed;
CC Name=2; Synonyms=PINY1;
CC IsoId=Q96BK5-2; Sequence=VSP_003945, VSP_003946;
CC -!- TISSUE SPECIFICITY: Ubiquitous; expressed at low levels. Not detectable
CC in a number of hepatocarcinoma cell lines.
CC -!- DOMAIN: The TID (telomerase inhibiting domain) domain is sufficient to
CC bind TERT and inhibit its activity. {ECO:0000269|PubMed:18202258}.
CC -!- DOMAIN: The TBM domain mediates interaction with TERF1.
CC {ECO:0000269|PubMed:18202258}.
CC -!- PTM: Cleaved by enterovirus protease 3C to promote apoptosis.
CC {ECO:0000269|PubMed:27847364}.
CC -!- SIMILARITY: Belongs to the PINX1 family. {ECO:0000305}.
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DR EMBL; AF205718; AAG18009.1; -; mRNA.
DR EMBL; AY029161; AAK31790.1; -; mRNA.
DR EMBL; AJ344104; CAC51436.1; -; mRNA.
DR EMBL; AF418553; AAN31333.1; -; mRNA.
DR EMBL; AY238941; AAP37006.1; -; mRNA.
DR EMBL; AY523566; AAS19507.1; -; mRNA.
DR EMBL; AK000572; BAA91263.1; -; mRNA.
DR EMBL; AK313715; BAG36458.1; -; mRNA.
DR EMBL; CH471157; EAW65596.1; -; Genomic_DNA.
DR EMBL; BC015479; AAH15479.1; -; mRNA.
DR EMBL; BC093762; AAH93762.1; -; mRNA.
DR CCDS; CCDS47801.1; -. [Q96BK5-1]
DR CCDS; CCDS64825.1; -. [Q96BK5-2]
DR RefSeq; NP_001271285.1; NM_001284356.1. [Q96BK5-2]
DR RefSeq; NP_060354.4; NM_017884.5. [Q96BK5-1]
DR AlphaFoldDB; Q96BK5; -.
DR BioGRID; 120319; 98.
DR ELM; Q96BK5; -.
DR IntAct; Q96BK5; 46.
DR MINT; Q96BK5; -.
DR STRING; 9606.ENSP00000318966; -.
DR iPTMnet; Q96BK5; -.
DR PhosphoSitePlus; Q96BK5; -.
DR BioMuta; PINX1; -.
DR DMDM; 21542178; -.
DR EPD; Q96BK5; -.
DR jPOST; Q96BK5; -.
DR MassIVE; Q96BK5; -.
DR MaxQB; Q96BK5; -.
DR PaxDb; Q96BK5; -.
DR PeptideAtlas; Q96BK5; -.
DR PRIDE; Q96BK5; -.
DR ProteomicsDB; 76086; -. [Q96BK5-1]
DR ProteomicsDB; 76087; -. [Q96BK5-2]
DR Antibodypedia; 54507; 250 antibodies from 31 providers.
DR DNASU; 54984; -.
DR Ensembl; ENST00000314787.8; ENSP00000318966.3; ENSG00000254093.9. [Q96BK5-1]
DR Ensembl; ENST00000519088.5; ENSP00000428853.1; ENSG00000254093.9. [Q96BK5-2]
DR GeneID; 54984; -.
DR KEGG; hsa:54984; -.
DR MANE-Select; ENST00000314787.8; ENSP00000318966.3; NM_017884.6; NP_060354.4.
DR UCSC; uc003wth.4; human. [Q96BK5-1]
DR CTD; 54984; -.
DR DisGeNET; 54984; -.
DR GeneCards; PINX1; -.
DR HGNC; HGNC:30046; PINX1.
DR HPA; ENSG00000254093; Low tissue specificity.
DR MIM; 606505; gene.
DR neXtProt; NX_Q96BK5; -.
DR OpenTargets; ENSG00000254093; -.
DR PharmGKB; PA165585852; -.
DR VEuPathDB; HostDB:ENSG00000254093; -.
DR eggNOG; KOG2809; Eukaryota.
DR GeneTree; ENSGT00450000040279; -.
DR HOGENOM; CLU_047471_0_0_1; -.
DR InParanoid; Q96BK5; -.
DR OMA; WDQSSEA; -.
DR OrthoDB; 1577610at2759; -.
DR PhylomeDB; Q96BK5; -.
DR TreeFam; TF321918; -.
DR PathwayCommons; Q96BK5; -.
DR SignaLink; Q96BK5; -.
DR SIGNOR; Q96BK5; -.
DR BioGRID-ORCS; 54984; 71 hits in 1032 CRISPR screens.
DR ChiTaRS; PINX1; human.
DR GeneWiki; PINX1; -.
DR GenomeRNAi; 54984; -.
DR Pharos; Q96BK5; Tbio.
DR PRO; PR:Q96BK5; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q96BK5; protein.
DR Bgee; ENSG00000254093; Expressed in oocyte and 180 other tissues.
DR ExpressionAtlas; Q96BK5; baseline and differential.
DR Genevisible; Q96BK5; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0000228; C:nuclear chromosome; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:BHF-UCL.
DR GO; GO:0010521; F:telomerase inhibitor activity; IDA:BHF-UCL.
DR GO; GO:0070034; F:telomerase RNA binding; IDA:UniProtKB.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; NAS:UniProtKB.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IDA:BHF-UCL.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:BHF-UCL.
DR GO; GO:0051974; P:negative regulation of telomerase activity; IDA:BHF-UCL.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IDA:BHF-UCL.
DR GO; GO:1904357; P:negative regulation of telomere maintenance via telomere lengthening; NAS:BHF-UCL.
DR GO; GO:1904751; P:positive regulation of protein localization to nucleolus; IDA:BHF-UCL.
DR GO; GO:1904744; P:positive regulation of telomeric DNA binding; IDA:BHF-UCL.
DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; IMP:BHF-UCL.
DR GO; GO:1902570; P:protein localization to nucleolus; IDA:BHF-UCL.
DR GO; GO:0031647; P:regulation of protein stability; IMP:BHF-UCL.
DR GO; GO:0090069; P:regulation of ribosome biogenesis; IBA:GO_Central.
DR GO; GO:0051972; P:regulation of telomerase activity; TAS:UniProtKB.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IDA:MGI.
DR InterPro; IPR000467; G_patch_dom.
DR Pfam; PF01585; G-patch; 1.
DR SMART; SM00443; G_patch; 1.
DR PROSITE; PS50174; G_PATCH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Centromere; Chromosome; Kinetochore; Nucleus;
KW Phosphoprotein; Reference proteome; Telomere; Tumor suppressor.
FT CHAIN 1..328
FT /note="PIN2/TERF1-interacting telomerase inhibitor 1"
FT /id="PRO_0000058443"
FT DOMAIN 26..72
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..328
FT /note="Telomerase inhibitory domain (TID)"
FT MOTIF 287..297
FT /note="TBM"
FT COMPBIAS 99..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 50..51
FT /note="(Microbial infection) Cleavage by enterovirus 71
FT protease 3C"
FT /evidence="ECO:0000269|PubMed:27847364"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZX5"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZX5"
FT VAR_SEQ 133..174
FT /note="KDLSSRSKTDLDCIFGKRQSKKTPEGDASPSTPEENETTTTS -> RCQSLH
FT SRGERNHDNQRLHHPGVLCQADGSTEEQAPGSSSRV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11003615, ECO:0000303|Ref.5"
FT /id="VSP_003945"
FT VAR_SEQ 175..328
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11003615, ECO:0000303|Ref.5"
FT /id="VSP_003946"
FT VARIANT 206
FT /note="Q -> H (in dbSNP:rs35530857)"
FT /id="VAR_054024"
FT VARIANT 215
FT /note="R -> I (in dbSNP:rs17855458)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_054025"
FT VARIANT 220
FT /note="T -> A (in dbSNP:rs17711777)"
FT /id="VAR_054026"
FT VARIANT 254
FT /note="S -> C (in dbSNP:rs1078543)"
FT /evidence="ECO:0000269|PubMed:11701125"
FT /id="VAR_054027"
FT VARIANT 315
FT /note="E -> A (in dbSNP:rs34656824)"
FT /id="VAR_054028"
FT MUTAGEN 50
FT /note="Q->A: Abolishes cleavage by enterovirus 71."
FT /evidence="ECO:0000269|PubMed:27847364"
FT MUTAGEN 291
FT /note="L->A: Abolishes interaction with TERF1."
FT /evidence="ECO:0000269|PubMed:18202258"
FT MUTAGEN 293
FT /note="P->A: Does not affect interaction with TERF1."
FT /evidence="ECO:0000269|PubMed:18202258"
FT CONFLICT 50
FT /note="Q -> H (in Ref. 9; AAH15479)"
FT /evidence="ECO:0000305"
FT CONFLICT 185..186
FT /note="RM -> PV (in Ref. 2; AAK31790)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="E -> V (in Ref. 3; CAC51436)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="T -> A (in Ref. 6; AAS19507)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="E -> K (in Ref. 2; AAK31790)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 328 AA; 37035 MW; A298B31AEA6D18E1 CRC64;
MSMLAERRRK QKWAVDPQNT AWSNDDSKFG QRMLEKMGWS KGKGLGAQEQ GATDHIKVQV
KNNHLGLGAT INNEDNWIAH QDDFNQLLAE LNTCHGQETT DSSDKKEKKS FSLEEKSKIS
KNRVHYMKFT KGKDLSSRSK TDLDCIFGKR QSKKTPEGDA SPSTPEENET TTTSAFTIQE
YFAKRMAALK NKPQVPVPGS DISETQVERK RGKKRNKEAT GKDVESYLQP KAKRHTEGKP
ERAEAQERVA KKKSAPAEEQ LRGPCWDQSS KASAQDAGDH VQPPEGRDFT LKPKKRRGKK
KLQKPVEIAE DATLEETLVK KKKKKDSK
