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   27-MAR-2024, entry version 185.
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="https://atlasgeneticsoncology.org/gene/41944/PTTG1IP";
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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; 55.
DR   IntAct; P53801; 26.
DR   MINT; P53801; -.
DR   STRING; 9606.ENSP00000328325; -.
DR   GlyConnect; 1607; 5 N-Linked glycans (1 site).
DR   GlyCosmos; P53801; 2 sites, 5 glycans.
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; 9606-ENSP00000328325; -.
DR   PeptideAtlas; P53801; -.
DR   ProteomicsDB; 56621; -.
DR   Pumba; P53801; -.
DR   Antibodypedia; 24351; 184 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   AGR; HGNC:13524; -.
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; 3092243at2759; -.
DR   PhylomeDB; P53801; -.
DR   TreeFam; TF329310; -.
DR   PathwayCommons; P53801; -.
DR   SignaLink; P53801; -.
DR   SIGNOR; P53801; -.
DR   BioGRID-ORCS; 754; 11 hits in 1165 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 209 other cell types or tissues.
DR   ExpressionAtlas; P53801; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
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   PANTHER; PTHR15191:SF13; PITUITARY TUMOR-TRANSFORMING GENE 1 PROTEIN-INTERACTING PROTEIN; 1.
DR   PANTHER; PTHR15191; PROTEIN CBG20567; 1.
DR   SMART; SM00423; PSI; 1.
DR   Genevisible; P53801; HS.
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
//