PTOV1_HUMAN
ID PTOV1_HUMAN Reviewed; 416 AA.
AC Q86YD1; Q6UXX7; Q96BU3; Q9HBN4; Q9NYL1;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Prostate tumor-overexpressed gene 1 protein;
DE Short=PTOV-1;
DE AltName: Full=Activator interaction domain-containing protein 2;
GN Name=PTOV1; Synonyms=ACID2; ORFNames=PP642, UNQ6127/PRO20092;
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 [GENOMIC DNA], SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11313889; DOI=10.1038/sj.onc.1204233;
RA Benedit P., Paciucci R., Thomson T.M., Valeri M., Nadal M., Caceres C.,
RA de Torres I., Estivill X., Lozano J.J., Morote J., Reventos J.;
RT "PTOV1, a novel protein overexpressed in prostate cancer containing a new
RT class of protein homology blocks.";
RL Oncogene 20:1455-1464(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [MRNA] OF
RP 260-416 (ISOFORMS 1/3).
RC TISSUE=Colon adenocarcinoma;
RX PubMed=14657022; DOI=10.1093/emboj/cdg619;
RA Mittler G., Stuehler T., Santolin L., Uhlmann T., Kremmer E.,
RA Lottspeich F., Berti L., Meisterernst M.;
RT "A novel docking site on Mediator is critical for activation by VP16 in
RT mammalian cells.";
RL EMBO J. 22:6494-6504(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Pancreas;
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12598323; DOI=10.1016/s0002-9440(10)63885-0;
RA Santamaria A., Fernandez P.L., Farre X., Benedit P., Reventos J.,
RA Morote J., Paciucci R., Thomson T.M.;
RT "PTOV-1, a novel protein overexpressed in prostate cancer, shuttles between
RT the cytoplasm and the nucleus and promotes entry into the S phase of the
RT cell division cycle.";
RL Am. J. Pathol. 162:897-905(2003).
RN [8]
RP FUNCTION, INTERACTION WITH FLOT1, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15713644; DOI=10.1128/mcb.25.5.1900-1911.2005;
RA Santamaria A., Castellanos E., Gomez V., Benedit P., Renau-Piqueras J.,
RA Morote J., Reventos J., Thomson T.M., Paciucci R.;
RT "PTOV1 enables the nuclear translocation and mitogenic activity of
RT flotillin-1, a major protein of lipid rafts.";
RL Mol. Cell. Biol. 25:1900-1911(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15778465; DOI=10.1074/mcp.m500021-mcp200;
RA Benzinger A., Muster N., Koch H.B., Yates J.R. III, Hermeking H.;
RT "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly
RT silenced in cancer.";
RL Mol. Cell. Proteomics 4:785-795(2005).
RN [10]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=16639697; DOI=10.1002/path.1993;
RA Nakamura Y., Suzuki T., Igarashi K., Kanno J., Furukawa T., Tazawa C.,
RA Fujishima F., Miura I., Ando T., Moriyama N., Moriya T., Saito H.,
RA Yamada S., Sasano H.;
RT "PTOV1: a novel testosterone-induced atherogenic gene in human aorta.";
RL J. Pathol. 209:522-531(2006).
RN [11]
RP FUNCTION, AND INTERACTION WITH CREBBP.
RX PubMed=17641689; DOI=10.1038/sj.emboj.7601797;
RA Lee H.-K., Park U.-H., Kim E.-J., Um S.-J.;
RT "MED25 is distinct from TRAP220/MED1 in cooperating with CBP for retinoid
RT receptor activation.";
RL EMBO J. 26:3545-3557(2007).
RN [12]
RP UBIQUITINATION.
RX PubMed=29779948; DOI=10.1016/j.cell.2018.04.028;
RA Koren I., Timms R.T., Kula T., Xu Q., Li M.Z., Elledge S.J.;
RT "The eukaryotic proteome is shaped by E3 ubiquitin ligases targeting C-
RT terminal degrons.";
RL Cell 173:1622-1635(2018).
CC -!- FUNCTION: May activate transcription. Required for nuclear
CC translocation of FLOT1. Promotes cell proliferation.
CC {ECO:0000269|PubMed:12598323, ECO:0000269|PubMed:15713644,
CC ECO:0000269|PubMed:17641689}.
CC -!- SUBUNIT: May interact with CREBBP. Interacts with FLOT1.
CC {ECO:0000269|PubMed:15713644, ECO:0000269|PubMed:17641689}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12598323,
CC ECO:0000269|PubMed:16639697}. Nucleus {ECO:0000269|PubMed:12598323,
CC ECO:0000269|PubMed:15713644}. Cell membrane
CC {ECO:0000269|PubMed:15713644}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:11313889}. Note=Translocates from the cytoplasm to
CC the nucleus at the onset of S-phase (PubMed:12598323). Also localizes
CC to lipid rafts (PubMed:15713644). {ECO:0000269|PubMed:12598323,
CC ECO:0000269|PubMed:15713644}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86YD1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86YD1-2; Sequence=VSP_028154, VSP_028155, VSP_028156;
CC Name=3;
CC IsoId=Q86YD1-3; Sequence=VSP_028153;
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, placenta,
CC skeletal muscle and small intestine. {ECO:0000269|PubMed:11313889}.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels in quiescent cells.
CC Expression rises upon entry into S-phase.
CC {ECO:0000269|PubMed:15713644}.
CC -!- INDUCTION: By testosterone. {ECO:0000269|PubMed:16639697}.
CC -!- PTM: Ubiquitinated by the CRL2(KLHDC2) complex, which recognizes the
CC diglycine (Gly-Gly) at the C-terminus, leading to its degradation
CC (PubMed:29779948). Ubiquitinated by the CRL2(APPBP2) complex, which
CC recognizes the Arg-Xaa-Xaa-Gly sequence at the C-terminus, leading to
CC its degradation (PubMed:29779948). {ECO:0000269|PubMed:29779948}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 25 family. PTOV1
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Despite sequence similarity to MED25, to date this protein has
CC not been identified as a component of the Mediator complex.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF70635.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF238381; AAF70635.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ617480; CAE84582.1; -; mRNA.
DR EMBL; AF218026; AAG17268.1; -; mRNA.
DR EMBL; AY358168; AAQ88535.1; -; mRNA.
DR EMBL; CH471177; EAW52558.1; -; Genomic_DNA.
DR EMBL; BC015172; AAH15172.1; -; mRNA.
DR EMBL; BC042921; AAH42921.1; -; mRNA.
DR CCDS; CCDS12782.1; -. [Q86YD1-1]
DR RefSeq; NP_001292034.1; NM_001305105.1. [Q86YD1-1]
DR RefSeq; NP_001292037.1; NM_001305108.1.
DR RefSeq; NP_059128.2; NM_017432.4. [Q86YD1-1]
DR AlphaFoldDB; Q86YD1; -.
DR SMR; Q86YD1; -.
DR BioGRID; 119792; 99.
DR IntAct; Q86YD1; 19.
DR MINT; Q86YD1; -.
DR STRING; 9606.ENSP00000375717; -.
DR iPTMnet; Q86YD1; -.
DR PhosphoSitePlus; Q86YD1; -.
DR BioMuta; PTOV1; -.
DR DMDM; 74762466; -.
DR EPD; Q86YD1; -.
DR jPOST; Q86YD1; -.
DR MassIVE; Q86YD1; -.
DR MaxQB; Q86YD1; -.
DR PaxDb; Q86YD1; -.
DR PeptideAtlas; Q86YD1; -.
DR PRIDE; Q86YD1; -.
DR ProteomicsDB; 70397; -. [Q86YD1-1]
DR ProteomicsDB; 70398; -. [Q86YD1-2]
DR ProteomicsDB; 70399; -. [Q86YD1-3]
DR Antibodypedia; 18733; 133 antibodies from 24 providers.
DR DNASU; 53635; -.
DR Ensembl; ENST00000391842.5; ENSP00000375717.1; ENSG00000104960.15. [Q86YD1-1]
DR Ensembl; ENST00000599732.5; ENSP00000469128.1; ENSG00000104960.15. [Q86YD1-1]
DR Ensembl; ENST00000601675.5; ENSP00000472816.1; ENSG00000104960.15. [Q86YD1-1]
DR GeneID; 53635; -.
DR KEGG; hsa:53635; -.
DR UCSC; uc002pqb.5; human. [Q86YD1-1]
DR CTD; 53635; -.
DR DisGeNET; 53635; -.
DR GeneCards; PTOV1; -.
DR HGNC; HGNC:9632; PTOV1.
DR HPA; ENSG00000104960; Low tissue specificity.
DR MIM; 610195; gene.
DR neXtProt; NX_Q86YD1; -.
DR OpenTargets; ENSG00000104960; -.
DR PharmGKB; PA33976; -.
DR VEuPathDB; HostDB:ENSG00000104960; -.
DR eggNOG; ENOG502SS25; Eukaryota.
DR GeneTree; ENSGT00940000161923; -.
DR HOGENOM; CLU_045342_0_0_1; -.
DR InParanoid; Q86YD1; -.
DR OMA; ELDCLTH; -.
DR OrthoDB; 340324at2759; -.
DR PhylomeDB; Q86YD1; -.
DR TreeFam; TF329598; -.
DR PathwayCommons; Q86YD1; -.
DR SignaLink; Q86YD1; -.
DR BioGRID-ORCS; 53635; 8 hits in 1022 CRISPR screens.
DR ChiTaRS; PTOV1; human.
DR GeneWiki; PTOV1; -.
DR GenomeRNAi; 53635; -.
DR Pharos; Q86YD1; Tbio.
DR PRO; PR:Q86YD1; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q86YD1; protein.
DR Bgee; ENSG00000104960; Expressed in ganglionic eminence and 202 other tissues.
DR ExpressionAtlas; Q86YD1; baseline and differential.
DR Genevisible; Q86YD1; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 2.40.290.30; -; 2.
DR InterPro; IPR045105; Med25/PTOV1.
DR InterPro; IPR021394; Med25_PTOV.
DR InterPro; IPR038196; Med25_PTOV_sf.
DR PANTHER; PTHR12433; PTHR12433; 2.
DR Pfam; PF11232; Med25; 2.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cell membrane; Cytoplasm; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..416
FT /note="Prostate tumor-overexpressed gene 1 protein"
FT /id="PRO_0000304965"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..416
FT /note="Interaction with FLOT1"
FT /evidence="ECO:0000269|PubMed:15713644"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91VU8"
FT VAR_SEQ 1..189
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15498874"
FT /id="VSP_028153"
FT VAR_SEQ 1..32
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_028154"
FT VAR_SEQ 33..57
FT /note="RSRSWPASPRGPQPPRIRARSAPPM -> MRSPAVPTPARGQLGVAFVLLPP
FT HS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_028155"
FT VAR_SEQ 348..397
FT /note="AGCVHFSYKASCEIRVLMLLYSSEKKIFIGLIPHDQGNFVNGIRRVIANQ
FT -> RRKSSLASSPMTRATLSTASGVSLPTSSRSCSGTWSRSNSNEGWGGSGYP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_028156"
SQ SEQUENCE 416 AA; 46869 MW; 888573E714E75180 CRC64;
MVRPRRAPYR SGAGGPLGGR GRPPRPLVVR AVRSRSWPAS PRGPQPPRIR ARSAPPMEGA
RVFGALGPIG PSSPGLTLGG LAVSEHRLSN KLLAWSGVLE WQEKRRPYSD STAKLKRTLP
CQAYVNQGEN LETDQWPQKL IMQLIPQQLL TTLGPLFRNS QLAQFHFTNR DCDSLKGLCR
IMGNGFAGCM LFPHISPCEV RVLMLLYSSK KKIFMGLIPY DQSGFVSAIR QVITTRKQAV
GPGGVNSGPV QIVNNKFLAW SGVMEWQEPR PEPNSRSKRW LPSHVYVNQG EILRTEQWPR
KLYMQLIPQQ LLTTLVPLFR NSRLVQFHFT KDLETLKSLC RIMDNGFAGC VHFSYKASCE
IRVLMLLYSS EKKIFIGLIP HDQGNFVNGI RRVIANQQQV LQRNLEQEQQ QRGMGG
