PINX1_RAT
ID PINX1_RAT Reviewed; 331 AA.
AC A4L691;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=PIN2/TERF1-interacting telomerase inhibitor 1;
DE AltName: Full=Pin2-interacting protein X1;
GN Name=Pinx1 {ECO:0000312|EMBL:ABO28828.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND FUNCTION.
RC STRAIN=Fischer 344;
RX PubMed=17624691; DOI=10.1016/j.gene.2007.05.015;
RA Oh B.K., Yoon S.M., Lee C.H., Park Y.N.;
RT "Rat homolog of PinX1 is a nucleolar protein involved in the regulation of
RT telomere length.";
RL Gene 400:35-43(2007).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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, ECO:0000269|PubMed:17624691}.
CC -!- SUBUNIT: Interacts with MCRS1, TERT, TERF1, NCL/nucleolin, and the
CC telomerase RNA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96BK5}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:17624691}. Chromosome, telomere
CC {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The TID (telomerase inhibiting domain) domain is sufficient to
CC bind TERT and inhibits its activity. {ECO:0000250|UniProtKB:Q96BK5}.
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; EF446165; ABO28828.1; -; mRNA.
DR RefSeq; NP_001076806.1; NM_001083337.1.
DR AlphaFoldDB; A4L691; -.
DR STRING; 10116.ENSRNOP00000016027; -.
DR iPTMnet; A4L691; -.
DR PhosphoSitePlus; A4L691; -.
DR PaxDb; A4L691; -.
DR PeptideAtlas; A4L691; -.
DR PRIDE; A4L691; -.
DR Ensembl; ENSRNOT00000016027; ENSRNOP00000016027; ENSRNOG00000012012.
DR GeneID; 305963; -.
DR KEGG; rno:305963; -.
DR UCSC; RGD:1566025; rat.
DR CTD; 54984; -.
DR RGD; 1566025; Pinx1.
DR eggNOG; KOG2809; Eukaryota.
DR GeneTree; ENSGT00450000040279; -.
DR HOGENOM; CLU_047471_0_0_1; -.
DR InParanoid; A4L691; -.
DR OMA; WDQSSEA; -.
DR OrthoDB; 1577610at2759; -.
DR PhylomeDB; A4L691; -.
DR TreeFam; TF321918; -.
DR PRO; PR:A4L691; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000012012; Expressed in ovary and 19 other tissues.
DR ExpressionAtlas; A4L691; baseline and differential.
DR Genevisible; A4L691; RN.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:RGD.
DR GO; GO:0000776; C:kinetochore; ISO:RGD.
DR GO; GO:0000228; C:nuclear chromosome; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0005819; C:spindle; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0010521; F:telomerase inhibitor activity; ISO:RGD.
DR GO; GO:0070034; F:telomerase RNA binding; ISO:RGD.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISO:RGD.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:0051974; P:negative regulation of telomerase activity; ISO:RGD.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:RGD.
DR GO; GO:1904751; P:positive regulation of protein localization to nucleolus; ISO:RGD.
DR GO; GO:1904744; P:positive regulation of telomeric DNA binding; ISO:RGD.
DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; ISO:RGD.
DR GO; GO:1902570; P:protein localization to nucleolus; ISO:RGD.
DR GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
DR GO; GO:0090069; P:regulation of ribosome biogenesis; IBA:GO_Central.
DR GO; GO:0007004; P:telomere maintenance via telomerase; ISO:RGD.
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..331
FT /note="PIN2/TERF1-interacting telomerase inhibitor 1"
FT /id="PRO_0000294933"
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 156..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..328
FT /note="Telomerase inhibitory domain (TID)"
FT /evidence="ECO:0000250|UniProtKB:Q96BK5"
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 157..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..299
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:22673903"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZX5"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZX5"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZX5"
SQ SEQUENCE 331 AA; 36710 MW; B90C47DDB010F254 CRC64;
MSMLAERRRK QKWAVDPRNT AWSNDDSKFG QKMLEKMGWS KGKGLGAQEQ GATEHIKVKV
KNNHLGLGAT NNNEDNWIAH QDDFNQLLAA LNTCHGQETA DSSDNKEKKS FSLEEKSKIS
KNRVHYMKFT KGKDLSSRSE TDLDCIFGKR RNKKLAQDGC SNSTADEADT SLTTTTTTTS
AFTIQEYFAK RMAQLKSKSQ AAAPGSDLSE TPIEWKKGKK KTKEAAGTDI ENSPQHKAKR
HKKKKRVEAE RGPAAKKRDQ VELQPGGPSG DECSDASVEA AEDRVQTPDT QDDVPKPRKR
RAKKTLQRPG GVAVDTAPDS APVKKKKKVS R
