PTTG_HUMAN
ID PTTG_HUMAN Reviewed; 180 AA.
AC P53801; B2RDP7; D3DSL9; Q9NS09;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 176.
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; Synonyms=C21orf1, C21orf3;
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].
RC TISSUE=Thymus;
RX PubMed=9570958; DOI=10.1006/geno.1998.5217;
RA Yaspo M.-L., Aaltonen J., Horelli-Kuitunen N., Peltonen L., Lehrach H.;
RT "Cloning of a novel human putative type Ia integral membrane protein
RT mapping to 21q22.3.";
RL Genomics 49:133-136(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH PTTG1.
RX PubMed=10781616; DOI=10.1074/jbc.m910105199;
RA Chien W., Pei L.;
RT "A novel binding factor facilitates nuclear translocation and
RT transcriptional activation function of the pituitary tumor-transforming
RT gene product.";
RL J. Biol. Chem. 275:19422-19427(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, Lung, Muscle, and Ovary;
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 [7]
RP INDUCTION.
RX PubMed=15190888; DOI=10.1359/jbmr.2004.19.6.959;
RA Stock M., Schafer H., Fliegauf M., Otto F.;
RT "Identification of novel genes of the bone-specific transcription factor
RT Runx2.";
RL J. Bone Miner. Res. 19:959-972(2004).
CC -!- FUNCTION: May facilitate PTTG1 nuclear translocation.
CC -!- SUBUNIT: Interacts with PTTG1. {ECO:0000269|PubMed:10781616}.
CC -!- INTERACTION:
CC P53801; Q86WK6: AMIGO1; NbExp=3; IntAct=EBI-3906138, EBI-19125216;
CC P53801; Q86V38: ATN1; NbExp=3; IntAct=EBI-3906138, EBI-11954292;
CC P53801; O75787: ATP6AP2; NbExp=3; IntAct=EBI-3906138, EBI-2512037;
CC P53801; Q9BXN2: CLEC7A; NbExp=3; IntAct=EBI-3906138, EBI-3939278;
CC P53801; Q9BXN2-6: CLEC7A; NbExp=3; IntAct=EBI-3906138, EBI-11989440;
CC P53801; P02489: CRYAA; NbExp=3; IntAct=EBI-3906138, EBI-6875961;
CC P53801; Q92876: KLK6; NbExp=3; IntAct=EBI-3906138, EBI-2432309;
CC P53801; Q5T700: LDLRAD1; NbExp=3; IntAct=EBI-3906138, EBI-10173166;
CC P53801; P23219: PTGS1; NbExp=3; IntAct=EBI-3906138, EBI-6655935;
CC P53801; Q16585: SGCB; NbExp=3; IntAct=EBI-3906138, EBI-5663627;
CC P53801; A1A5C7-2: SLC22A23; NbExp=3; IntAct=EBI-3906138, EBI-12081840;
CC P53801; Q9BVX2: TMEM106C; NbExp=3; IntAct=EBI-3906138, EBI-2821497;
CC P53801; O15393-2: TMPRSS2; NbExp=3; IntAct=EBI-3906138, EBI-12345267;
CC P53801; O43557: TNFSF14; NbExp=3; IntAct=EBI-3906138, EBI-524131;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Cytoplasm
CC {ECO:0000269|PubMed:10781616}. Nucleus {ECO:0000269|PubMed:10781616}.
CC Note=According to PubMed:10781616, it is found in the cytoplasm and the
CC nucleus.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- INDUCTION: By transcription factor RUNX2.
CC {ECO:0000269|PubMed:15190888}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PTTG1IPID41944ch21q22.html";
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DR EMBL; Z50022; CAA90325.1; -; mRNA.
DR EMBL; AF149785; AAF73770.1; -; mRNA.
DR EMBL; AK315626; BAG37994.1; -; mRNA.
DR EMBL; AL163300; CAB90552.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09386.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09388.1; -; Genomic_DNA.
DR EMBL; BC000415; AAH00415.1; -; mRNA.
DR EMBL; BC012858; AAH12858.1; -; mRNA.
DR EMBL; BC019295; AAH19295.1; -; mRNA.
DR EMBL; BC020983; AAH20983.1; -; mRNA.
DR EMBL; BC031097; AAH31097.1; -; mRNA.
DR EMBL; BC034250; AAH34250.1; -; mRNA.
DR CCDS; CCDS13715.1; -.
DR RefSeq; NP_001273751.1; NM_001286822.1.
DR RefSeq; NP_004330.1; NM_004339.3.
DR AlphaFoldDB; P53801; -.
DR SMR; P53801; -.
DR BioGRID; 107210; 28.
DR IntAct; P53801; 26.
DR MINT; P53801; -.
DR STRING; 9606.ENSP00000328325; -.
DR GlyConnect; 1607; 5 N-Linked glycans (1 site).
DR GlyGen; P53801; 3 sites, 5 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; P53801; -.
DR PhosphoSitePlus; P53801; -.
DR SwissPalm; P53801; -.
DR BioMuta; PTTG1IP; -.
DR DMDM; 1711387; -.
DR EPD; P53801; -.
DR jPOST; P53801; -.
DR MassIVE; P53801; -.
DR MaxQB; P53801; -.
DR PaxDb; P53801; -.
DR PeptideAtlas; P53801; -.
DR PRIDE; P53801; -.
DR ProteomicsDB; 56621; -.
DR Antibodypedia; 24351; 172 antibodies from 30 providers.
DR DNASU; 754; -.
DR Ensembl; ENST00000330938.8; ENSP00000328325.3; ENSG00000183255.12.
DR GeneID; 754; -.
DR KEGG; hsa:754; -.
DR MANE-Select; ENST00000330938.8; ENSP00000328325.3; NM_004339.4; NP_004330.1.
DR UCSC; uc002zgb.3; human.
DR CTD; 754; -.
DR DisGeNET; 754; -.
DR GeneCards; PTTG1IP; -.
DR HGNC; HGNC:13524; PTTG1IP.
DR HPA; ENSG00000183255; Low tissue specificity.
DR MIM; 603784; gene.
DR neXtProt; NX_P53801; -.
DR OpenTargets; ENSG00000183255; -.
DR PharmGKB; PA34034; -.
DR VEuPathDB; HostDB:ENSG00000183255; -.
DR eggNOG; ENOG502RYM1; Eukaryota.
DR GeneTree; ENSGT00390000004977; -.
DR HOGENOM; CLU_109415_0_0_1; -.
DR InParanoid; P53801; -.
DR OMA; QNVACLW; -.
DR OrthoDB; 1458076at2759; -.
DR PhylomeDB; P53801; -.
DR TreeFam; TF329310; -.
DR PathwayCommons; P53801; -.
DR SignaLink; P53801; -.
DR BioGRID-ORCS; 754; 11 hits in 1087 CRISPR screens.
DR ChiTaRS; PTTG1IP; human.
DR GeneWiki; PTTG1IP; -.
DR GenomeRNAi; 754; -.
DR Pharos; P53801; Tbio.
DR PRO; PR:P53801; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P53801; protein.
DR Bgee; ENSG00000183255; Expressed in visceral pleura and 207 other tissues.
DR ExpressionAtlas; P53801; baseline and differential.
DR Genevisible; P53801; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0002039; F:p53 binding; IPI:MGI.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IMP:MGI.
DR GO; GO:1902254; P:negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IMP:MGI.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:MGI.
DR GO; GO:0006606; P:protein import into nucleus; IDA:UniProtKB.
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 Coiled coil; Cytoplasm; Glycoprotein; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..180
FT /note="Pituitary tumor-transforming gene 1 protein-
FT interacting protein"
FT /id="PRO_0000022184"
FT TOPO_DOM 33..96
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 39..92
FT /note="PSI"
FT REGION 131..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 130..165
FT /evidence="ECO:0000255"
FT MOD_RES 174
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8R143"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 9..19
FT /note="PTPYWRLRLGG -> ARRTGGCASV (in Ref. 2; AAF73770)"
FT /evidence="ECO:0000305"
FT CONFLICT 108..114
FT /note="TLLLGIA -> NPPPGHC (in Ref. 2; AAF73770)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 180 AA; 20324 MW; F1E66014D49EC1DE CRC64;
MAPGVARGPT PYWRLRLGGA ALLLLLIPVA AAQEPPGAAC SQNTNKTCEE CLKNVSCLWC
NTNKACLDYP VTSVLPPASL CKLSSARWGV CWVNFEALII TMSVVGGTLL LGIAICCCCC
CRRKRSRKPD RSEEKAMRER EERRIRQEER RAEMKTRHDE IRKKYGLFKE ENPYARFENN