TFDP3_HUMAN
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 03-AUG-2022, entry version 145.
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};
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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 AlphaFoldDB; Q5H9I0; -.
DR SMR; Q5H9I0; -.
DR BioGRID; 119423; 37.
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; 181 antibodies from 20 providers.
DR DNASU; 51270; -.
DR Ensembl; ENST00000310125.5; ENSP00000385461.1; ENSG00000183434.10.
DR GeneID; 51270; -.
DR KEGG; hsa:51270; -.
DR MANE-Select; ENST00000310125.5; ENSP00000385461.1; NM_016521.3; NP_057605.3.
DR UCSC; uc004exb.1; human.
DR CTD; 51270; -.
DR DisGeNET; 51270; -.
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 VEuPathDB; HostDB:ENSG00000183434; -.
DR eggNOG; KOG2829; Eukaryota.
DR GeneTree; ENSGT00940000167066; -.
DR HOGENOM; CLU_039874_3_1_1; -.
DR InParanoid; Q5H9I0; -.
DR OMA; NIKRRTY; -.
DR OrthoDB; 1046304at2759; -.
DR PhylomeDB; Q5H9I0; -.
DR TreeFam; TF314396; -.
DR PathwayCommons; Q5H9I0; -.
DR SignaLink; Q5H9I0; -.
DR BioGRID-ORCS; 51270; 4 hits in 724 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 5 other tissues.
DR Genevisible; Q5H9I0; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; IDA:ARUK-UCL.
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 68..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 REGION 369..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 156..190
FT /note="DEF box"
FT /evidence="ECO:0000250"
FT COMPBIAS 73..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..405
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
