ID TFDP3_HUMAN Reviewed; 405 AA. AC Q5H9I0; Q6DK49; Q9NZ54; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 12-AUG-2020, entry version 137. DE RecName: Full=Transcription factor Dp family member 3; DE AltName: Full=Cancer/testis antigen 30; DE Short=CT30; DE AltName: Full=Hepatocellular carcinoma-associated antigen 661; GN Name=TFDP3; Synonyms=DP4, HCA661; 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], TISSUE SPECIFICITY, AND IDENTIFICATION AS A RP CANCER/TESTIS ANTIGEN. RC TISSUE=Hepatoma; RX PubMed=12097419; DOI=10.4049/jimmunol.169.2.1102; RA Wang Y., Han K.-J., Pang X.-W., Vaughan H.A., Qu W., Dong X.-Y., RA Peng J.-R., Zhao H.-T., Rui J.-A., Leng X.-S., Cebon J., Burgess A.W., RA Chen W.-F.; RT "Large scale identification of human hepatocellular carcinoma-associated RT antigens by autoantibodies."; RL J. Immunol. 169:1102-1109(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [3] 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 [4] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=16418725; DOI=10.1038/sj.onc.1209343; RA Milton A., Luoto K., Ingram L., Munro S., Logan N., Graham A.L., RA Brummelkamp T.R., Hijmans E.M., Bernards R., La Thangue N.B.; RT "A functionally distinct member of the DP family of E2F subunits."; RL Oncogene 25:3212-3218(2006). RN [5] RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF THR-121; RP CYS-130; GLN-131 AND LYS-140. RX PubMed=17062573; DOI=10.1074/jbc.m606169200; RA Qiao H., Di Stefano L., Tian C., Li Y.Y., Yin Y.H., Qian X.P., Pang X.W., RA Li Y., McNutt M.A., Helin K., Zhang Y., Chen W.F.; RT "Human TFDP3, a novel DP protein, inhibits DNA binding and transactivation RT by E2F."; RL J. Biol. Chem. 282:454-466(2007). RN [6] RP FUNCTION, SUBUNIT, AND INDUCTION. RX PubMed=20559320; DOI=10.1038/cdd.2010.70; RA Ingram L., Munro S., Coutts A.S., La Thangue N.B.; RT "E2F-1 regulation by an unusual DNA damage-responsive DP partner subunit."; RL Cell Death Differ. 18:122-132(2011). CC -!- FUNCTION: Competitive inhibitor of E2F-mediated transactivation CC activity. Impairs E2F-mediated cell-cycle progression from G(1) to S CC phase. {ECO:0000269|PubMed:16418725, ECO:0000269|PubMed:17062573, CC ECO:0000269|PubMed:20559320}. CC -!- SUBUNIT: Heterodimer: with E2F family members. TFDP3/E2F heterodimers CC do not bind DNA and repress E2F-dependent transcriptional activity. CC {ECO:0000269|PubMed:17062573, ECO:0000269|PubMed:20559320}. CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Translocates to the CC nucleus on heterodimerization with E2F family members. CC -!- TISSUE SPECIFICITY: Predominantly expressed in testis. Low level of CC expression in pancreas. Highly expressed in ovarian and colon cancer CC cell lines. {ECO:0000269|PubMed:12097419, ECO:0000269|PubMed:16418725}. CC -!- INDUCTION: In response to DNA damage. {ECO:0000269|PubMed:20559320}. CC -!- DOMAIN: The potential DNA-binding domain differs in sequence from that CC of other DP family members and cannot bind DNA. CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF37562.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF219119; AAF37562.2; ALT_INIT; mRNA. DR EMBL; Z77249; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471107; EAX11773.1; -; Genomic_DNA. DR CCDS; CCDS14636.2; -. DR RefSeq; NP_057605.3; NM_016521.2. DR SMR; Q5H9I0; -. DR BioGRID; 119423; 30. DR IntAct; Q5H9I0; 25. DR STRING; 9606.ENSP00000385461; -. DR iPTMnet; Q5H9I0; -. DR PhosphoSitePlus; Q5H9I0; -. DR BioMuta; TFDP3; -. DR DMDM; 74762180; -. DR jPOST; Q5H9I0; -. DR MassIVE; Q5H9I0; -. DR PaxDb; Q5H9I0; -. DR PeptideAtlas; Q5H9I0; -. DR PRIDE; Q5H9I0; -. DR ProteomicsDB; 62889; -. DR Antibodypedia; 30265; 168 antibodies. DR DNASU; 51270; -. DR Ensembl; ENST00000310125; ENSP00000385461; ENSG00000183434. DR GeneID; 51270; -. DR KEGG; hsa:51270; -. DR UCSC; uc004exb.1; human. DR CTD; 51270; -. DR DisGeNET; 51270; -. DR EuPathDB; HostDB:ENSG00000183434.9; -. DR GeneCards; TFDP3; -. DR HGNC; HGNC:24603; TFDP3. DR HPA; ENSG00000183434; Tissue enriched (testis). DR MIM; 300772; gene. DR neXtProt; NX_Q5H9I0; -. DR OpenTargets; ENSG00000183434; -. DR PharmGKB; PA134898258; -. DR eggNOG; KOG2829; Eukaryota. DR GeneTree; ENSGT00940000167066; -. DR HOGENOM; CLU_039874_3_1_1; -. DR InParanoid; Q5H9I0; -. DR KO; K09393; -. DR OMA; NIKRRTY; -. DR OrthoDB; 1046304at2759; -. DR PhylomeDB; Q5H9I0; -. DR TreeFam; TF314396; -. DR PathwayCommons; Q5H9I0; -. DR BioGRID-ORCS; 51270; 0 hits in 526 CRISPR screens. DR GenomeRNAi; 51270; -. DR Pharos; Q5H9I0; Tbio. DR PRO; PR:Q5H9I0; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q5H9I0; protein. DR Bgee; ENSG00000183434; Expressed in buccal mucosa cell and 14 other tissues. DR Genevisible; Q5H9I0; HS. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0000790; C:nuclear chromatin; ISA:NTNU_SB. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005667; C:transcription regulator complex; IEA:InterPro. DR GO; GO:0033613; F:activating transcription factor binding; IPI:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB. DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:InterPro. DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:UniProtKB. DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd14458; DP_DD; 1. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 1.20.140.80; -; 1. DR InterPro; IPR037241; E2F-DP_heterodim. DR InterPro; IPR003316; E2F_WHTH_DNA-bd_dom. DR InterPro; IPR038168; TF_DP_C_sf. DR InterPro; IPR028315; TFDP3. DR InterPro; IPR014889; Transc_factor_DP_C. DR InterPro; IPR015648; Transcrpt_fac_DP. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR12548; PTHR12548; 1. DR PANTHER; PTHR12548:SF13; PTHR12548:SF13; 1. DR Pfam; PF08781; DP; 1. DR Pfam; PF02319; E2F_TDP; 1. DR PIRSF; PIRSF009404; Transcription_factor_DP; 1. DR SMART; SM01138; DP; 1. DR SMART; SM01372; E2F_TDP; 1. DR SUPFAM; SSF144074; SSF144074; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 1: Evidence at protein level; KW Cytoplasm; DNA-binding; Nucleus; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1..405 FT /note="Transcription factor Dp family member 3" FT /id="PRO_0000305940" FT DNA_BIND 108..190 FT /evidence="ECO:0000255" FT REGION 175..306 FT /note="Involved in negatively regulating E2F activity" FT REGION 209..241 FT /note="DCB1" FT /evidence="ECO:0000250" FT REGION 254..310 FT /note="DCB2" FT /evidence="ECO:0000250" FT MOTIF 156..190 FT /note="DEF box" FT /evidence="ECO:0000250" FT COMPBIAS 386..402 FT /note="Asp/Glu-rich (acidic; NCB domain)" FT SITE 121 FT /note="Critical for repression of E2F activity" FT SITE 130 FT /note="Critical for repression of E2F activity" FT SITE 131 FT /note="Critical for repression of E2F activity" FT SITE 140 FT /note="Critical for repression of E2F activity" FT MUTAGEN 112 FT /note="C->R: No effect on down-regulation of E2F FT transcriptional activity; when associated with or without FT R-161 or with V-164." FT MUTAGEN 121 FT /note="T->K: Restores enhanced E2F-mediated transcriptional FT activity; when associated with Y-130; N-131 and E-145." FT /evidence="ECO:0000269|PubMed:17062573" FT MUTAGEN 130 FT /note="C->Y: Restores enhanced E2F-mediated transcriptional FT activity; when associated with K-121; N-131 and E-145." FT /evidence="ECO:0000269|PubMed:17062573" FT MUTAGEN 131 FT /note="Q->N: Restores enhanced E2F-mediated transcriptional FT activity; when associated with K-121; Y-130 and E-145." FT /evidence="ECO:0000269|PubMed:17062573" FT MUTAGEN 140 FT /note="K->E: Restores enhanced E2F-mediated transcriptional FT activity; when associated with K-121; Y-130 and N-131." FT /evidence="ECO:0000269|PubMed:17062573" FT MUTAGEN 161 FT /note="K->R: No effect on down-regulation of E2F FT transcriptional activity; when associated with or without FT R-112." FT MUTAGEN 164 FT /note="T->V: No effect on down-regulation of E2F FT transcriptional activity; when associated R-112." SQ SEQUENCE 405 AA; 44967 MW; AE6F5709FE7E4C03 CRC64; MAKYVSLTEA NEELKVLMDE NQTSRPVAVH TSTVNPLGKQ LLPKTFGQSS VNIDQQVVIG MPQRPAASNI PVVGSPNPPS THFASQNQHS YSSPPWAGQH NRKGEKNGMG LCRLSMKVWE TVQRKGTTSC QEVVGELVAK FRAASNHASP NESAYDVKNI KRRTYDALNV LMAMNIISRE KKKIKWIGLT TNSAQNCQNL RVERQKRLER IKQKQSELQQ LILQQIAFKN LVLRNQYVEE QVSQRPLPNS VIHVPFIIIS SSKKTVINCS ISDDKSEYLF KFNSSFEIHD DTEVLMWMGM TFGLESGSCS AEDLKMARNL VPKALEPYVT EMAQGTFGGV FTTAGSRSNG TWLSASDLTN IAIGMLATSS GGSQYSGSRV ETPAVEEEEE EDNNDDDLSE NDEDD //