PTTG_MOUSE
ID PTTG_MOUSE Reviewed; 174 AA.
AC Q8R143; Q3TVT1; Q8BJ96; Q8N7P0;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Pituitary tumor-transforming gene 1 protein-interacting protein;
DE AltName: Full=Pituitary tumor-transforming gene protein-binding factor;
DE Short=PBF;
DE Short=PTTG-binding factor;
DE Flags: Precursor;
GN Name=Pttg1ip;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, DBA/2J, and NOD;
RC TISSUE=Bone marrow, Pancreas, Thymus, and Urinary bladder;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver, and Mammary tumor;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-171, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
CC -!- FUNCTION: May facilitate PTTG1 nuclear translocation. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PTTG1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000250}. Note=May be cytoplasmic and nuclear. {ECO:0000250}.
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DR EMBL; AK035696; BAC29156.1; -; mRNA.
DR EMBL; AK075773; BAC35947.1; -; mRNA.
DR EMBL; AK088813; BAC40589.1; -; mRNA.
DR EMBL; AK089887; BAC40985.1; -; mRNA.
DR EMBL; AK098093; BAC05231.1; -; mRNA.
DR EMBL; AK152366; BAE31156.1; -; mRNA.
DR EMBL; AK159987; BAE35537.1; -; mRNA.
DR EMBL; AK167972; BAE39966.1; -; mRNA.
DR EMBL; AK168164; BAE40125.1; -; mRNA.
DR EMBL; AK170802; BAE42037.1; -; mRNA.
DR EMBL; AK170971; BAE42150.1; -; mRNA.
DR EMBL; AK170972; BAE42151.1; -; mRNA.
DR EMBL; AK171140; BAE42273.1; -; mRNA.
DR EMBL; BC025533; AAH25533.1; -; mRNA.
DR EMBL; BC023961; AAH23961.1; -; mRNA.
DR EMBL; BC029144; AAH29144.1; -; mRNA.
DR EMBL; BC032184; AAH32184.1; -; mRNA.
DR CCDS; CCDS23957.1; -.
DR RefSeq; NP_666037.1; NM_145925.2.
DR AlphaFoldDB; Q8R143; -.
DR SMR; Q8R143; -.
DR STRING; 10090.ENSMUSP00000009435; -.
DR GlyGen; Q8R143; 2 sites.
DR iPTMnet; Q8R143; -.
DR PhosphoSitePlus; Q8R143; -.
DR SwissPalm; Q8R143; -.
DR EPD; Q8R143; -.
DR jPOST; Q8R143; -.
DR MaxQB; Q8R143; -.
DR PaxDb; Q8R143; -.
DR PeptideAtlas; Q8R143; -.
DR PRIDE; Q8R143; -.
DR ProteomicsDB; 301888; -.
DR Antibodypedia; 24351; 172 antibodies from 30 providers.
DR DNASU; 108705; -.
DR Ensembl; ENSMUST00000009435; ENSMUSP00000009435; ENSMUSG00000009291.
DR GeneID; 108705; -.
DR KEGG; mmu:108705; -.
DR UCSC; uc007fvx.1; mouse.
DR CTD; 754; -.
DR MGI; MGI:2652132; Pttg1ip.
DR VEuPathDB; HostDB:ENSMUSG00000009291; -.
DR eggNOG; ENOG502RYM1; Eukaryota.
DR GeneTree; ENSGT00390000004977; -.
DR HOGENOM; CLU_109415_0_0_1; -.
DR InParanoid; Q8R143; -.
DR OMA; QNVACLW; -.
DR OrthoDB; 1458076at2759; -.
DR PhylomeDB; Q8R143; -.
DR TreeFam; TF329310; -.
DR BioGRID-ORCS; 108705; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Pttg1ip; mouse.
DR PRO; PR:Q8R143; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8R143; protein.
DR Bgee; ENSMUSG00000009291; Expressed in epithelium of stomach and 271 other tissues.
DR ExpressionAtlas; Q8R143; baseline and differential.
DR Genevisible; Q8R143; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002039; F:p53 binding; ISO:MGI.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; ISO:MGI.
DR GO; GO:1902254; P:negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator; ISO:MGI.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:MGI.
DR GO; GO:0006606; P:protein import into nucleus; ISO:MGI.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR042492; PTTG1IP.
DR PANTHER; PTHR15191:SF2; PTHR15191:SF2; 1.
DR SMART; SM00423; PSI; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Cytoplasm; Glycoprotein; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..174
FT /note="Pituitary tumor-transforming gene 1 protein-
FT interacting protein"
FT /id="PRO_0000022185"
FT TOPO_DOM 30..93
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..89
FT /note="PSI"
FT REGION 125..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 127..163
FT /evidence="ECO:0000255"
FT MOD_RES 171
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 8
FT /note="L -> R (in Ref. 1; BAC40985)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="R -> W (in Ref. 1; BAC40985)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 174 AA; 19965 MW; 78FC04B6D4752FA0 CRC64;
MAPANLGLTP HWVMLLGAVL LLLLSGASAQ EPPRVGCSEY TNRSCEECLR NVSCLWCNEN
KACMDYPVRK ILPPASLCKL SSARWGVCWV NFEALIITMS VLGGSVLLGI TVCCCYCCRR
KKSRKPDKSD ERAMREQEER RVRQEERRAE MKSRHDEIRK KYGLFKEQNP YEKF
