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   27-MAR-2024, entry version 144.
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; 34.
DR   STRING; 10090.ENSMUSP00000022528; -.
DR   iPTMnet; Q9CZX5; -.
DR   PhosphoSitePlus; Q9CZX5; -.
DR   EPD; Q9CZX5; -.
DR   jPOST; Q9CZX5; -.
DR   MaxQB; Q9CZX5; -.
DR   PaxDb; 10090-ENSMUSP00000022528; -.
DR   PeptideAtlas; Q9CZX5; -.
DR   ProteomicsDB; 289577; -.
DR   Pumba; Q9CZX5; -.
DR   Antibodypedia; 54507; 291 antibodies from 31 providers.
DR   DNASU; 72400; -.
DR   Ensembl; ENSMUST00000022528.6; ENSMUSP00000022528.5; ENSMUSG00000021958.6.
DR   GeneID; 72400; -.
DR   KEGG; mmu:72400; -.
DR   UCSC; uc007uhx.2; mouse.
DR   AGR; MGI:1919650; -.
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; PCWDQSS; -.
DR   OrthoDB; 2919396at2759; -.
DR   PhylomeDB; Q9CZX5; -.
DR   TreeFam; TF321918; -.
DR   BioGRID-ORCS; 72400; 17 hits in 82 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 248 other cell types or tissues.
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 chromosome alignment; 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: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: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:0007004; P:telomere maintenance via telomerase; ISO:MGI.
DR   InterPro; IPR000467; G_patch_dom.
DR   PANTHER; PTHR23149; G PATCH DOMAIN CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR23149:SF27; PIN2_TERF1-INTERACTING TELOMERASE INHIBITOR 1; 1.
DR   Pfam; PF01585; G-patch; 1.
DR   SMART; SM00443; G_patch; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
DR   Genevisible; Q9CZX5; MM.
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
//