PINX1_MOUSE
ID PINX1_MOUSE Reviewed; 332 AA.
AC Q9CZX5; Q14BS4; Q3V450; Q8C6E5; Q91WZ9; Q9D0C2;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=PIN2/TERF1-interacting telomerase inhibitor 1;
DE AltName: Full=67-11-3 protein;
DE AltName: Full=LPTS1;
DE AltName: Full=Liver-related putative tumor suppressor;
DE AltName: Full=Pin2-interacting protein X1;
DE AltName: Full=TRF1-interacting protein 1;
GN Name=Pinx1; Synonyms=Lpts;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR;
RA Liao C., Zhao M., Li T.;
RT "The expression of mouse LPTS1, a homolog of human tumor suppressor LPTS,
RT in mouse liver.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 38-332.
RC TISSUE=Embryo;
RA Schmidt T.;
RL Thesis (2001), University of Goettingen, Germany.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; SER-269; SER-274 AND
RP SER-277, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MCRS1, TERT, TERF1, NCL/nucleolin, and the
CC telomerase RNA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus
CC {ECO:0000250}. Chromosome, telomere {ECO:0000250}. Chromosome,
CC centromere, kinetochore {ECO:0000250}. Note=Localizes in nucleoli, at
CC telomere speckles and to the outer plate of kinetochores. Localization
CC to the kinetochore is mediated by its central region and depends on
CC NDC80 and CENPE (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The TID (telomerase inhibiting domain) domain is sufficient to
CC bind TERT and inhibits its activity. {ECO:0000250}.
CC -!- DOMAIN: The TBM domain mediates interaction with TERF1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PINX1 family. {ECO:0000305}.
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DR EMBL; AF421879; AAL32445.1; -; mRNA.
DR EMBL; AF321817; AAL37221.1; -; mRNA.
DR EMBL; AK011578; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK012057; BAE43228.1; -; mRNA.
DR EMBL; AK075840; BAC35998.1; -; mRNA.
DR EMBL; BC115636; AAI15637.1; -; mRNA.
DR EMBL; AJ344106; CAC51439.1; -; mRNA.
DR CCDS; CCDS27205.1; -.
DR RefSeq; NP_082504.1; NM_028228.3.
DR AlphaFoldDB; Q9CZX5; -.
DR BioGRID; 215357; 33.
DR STRING; 10090.ENSMUSP00000022528; -.
DR iPTMnet; Q9CZX5; -.
DR PhosphoSitePlus; Q9CZX5; -.
DR EPD; Q9CZX5; -.
DR jPOST; Q9CZX5; -.
DR MaxQB; Q9CZX5; -.
DR PaxDb; Q9CZX5; -.
DR PeptideAtlas; Q9CZX5; -.
DR PRIDE; Q9CZX5; -.
DR ProteomicsDB; 289577; -.
DR Antibodypedia; 54507; 250 antibodies from 31 providers.
DR DNASU; 72400; -.
DR Ensembl; ENSMUST00000022528; ENSMUSP00000022528; ENSMUSG00000021958.
DR GeneID; 72400; -.
DR KEGG; mmu:72400; -.
DR UCSC; uc007uhx.2; mouse.
DR CTD; 54984; -.
DR MGI; MGI:1919650; Pinx1.
DR VEuPathDB; HostDB:ENSMUSG00000021958; -.
DR eggNOG; KOG2809; Eukaryota.
DR GeneTree; ENSGT00450000040279; -.
DR HOGENOM; CLU_047471_0_0_1; -.
DR InParanoid; Q9CZX5; -.
DR OMA; WDQSSEA; -.
DR OrthoDB; 1577610at2759; -.
DR PhylomeDB; Q9CZX5; -.
DR TreeFam; TF321918; -.
DR BioGRID-ORCS; 72400; 17 hits in 77 CRISPR screens.
DR ChiTaRS; Pinx1; mouse.
DR PRO; PR:Q9CZX5; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9CZX5; protein.
DR Bgee; ENSMUSG00000021958; Expressed in undifferentiated genital tubercle and 245 other tissues.
DR Genevisible; Q9CZX5; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0000228; C:nuclear chromosome; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005819; C:spindle; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0010521; F:telomerase inhibitor activity; ISO:MGI.
DR GO; GO:0070034; F:telomerase RNA binding; ISO:MGI.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISO:MGI.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:MGI.
DR GO; GO:0051974; P:negative regulation of telomerase activity; ISO:MGI.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:1904751; P:positive regulation of protein localization to nucleolus; ISO:MGI.
DR GO; GO:1904744; P:positive regulation of telomeric DNA binding; ISO:MGI.
DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; ISO:MGI.
DR GO; GO:1902570; P:protein localization to nucleolus; ISO:MGI.
DR GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
DR GO; GO:0090069; P:regulation of ribosome biogenesis; IBA:GO_Central.
DR GO; GO:0007004; P:telomere maintenance via telomerase; ISO: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 Centromere; Chromosome; Kinetochore; Nucleus; Phosphoprotein;
KW Reference proteome; Telomere; Tumor suppressor.
FT CHAIN 1..332
FT /note="PIN2/TERF1-interacting telomerase inhibitor 1"
FT /id="PRO_0000058444"
FT DOMAIN 26..72
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..328
FT /note="Telomerase inhibitory domain (TID)"
FT MOTIF 291..301
FT /note="TBM"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 40
FT /note="S -> A (in Ref. 3; BAC35998)"
FT /evidence="ECO:0000305"
FT CONFLICT 210..213
FT /note="ETPV -> HAPC (in Ref. 3; BAE43228)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 37221 MW; 6B7147CED58D991A CRC64;
MSMLAERRRK QKWTVDPRNT AWSNDDSKFG QKMLEKMGWS KGKGLGAQEQ GATEHIKVKV
KNNHLGLGAT NNNEDNWIAH QDDFNQLLAA LNTCHGQETA DSSDKKEKKS FSLEEKSKIS
KNRVHYMKFT KGKDLSSRSE TDLDCIFGKR RNKKLAQDGC SNSSADEVNT SLTTTTTTTS
AFTIQEYFAK RMAQLKNKPQ ASAPGSDLSE TPVERKKGKK KNKEAADTDV ENSPQHKAKR
HKKKKRVEAE RGPVAKKRDR AELQPGGPSE DECSDASVEA AEDCVQTPDI QDDVPKPKKR
KAKKKLQRPE GVEIDATLDR APVKKKKKKV SR
