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Database: UniProt
Entry: TFDP3_HUMAN
LinkDB: TFDP3_HUMAN
Original site: 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   01-OCT-2014, entry version 96.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND IDENTIFICATION AS
RP   A 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-
RT   associated 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.,
RA   Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA   Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA   Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA   Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA   Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA   Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA   Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA   Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA   Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA   Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA   Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA   Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA   Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA   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.,
RA   Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA   Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA   Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA   Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA   Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA   Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA   Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA   Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA   Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA   de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA   Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA   Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA   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.,
RA   Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA   Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA   Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA   Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA   Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA   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.,
RA   Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA   Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA   Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA   Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA   Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA   Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA   Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA   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.,
RA   Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA   Gibbs R.A., Beck S., 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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.,
RA   Pang X.W., Li Y., McNutt M.A., Helin K., Zhang Y., Chen W.F.;
RT   "Human TFDP3, a novel DP protein, inhibits DNA binding and
RT   transactivation 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
RT   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
CC       S phase. {ECO:0000269|PubMed:16418725,
CC       ECO:0000269|PubMed:17062573, ECO:0000269|PubMed:20559320}.
CC   -!- SUBUNIT: Heterodimer: with E2F family members. TFDP3/E2F
CC       heterodimers do not bind DNA and repress E2F-dependent
CC       transcriptional activity. {ECO:0000269|PubMed:17062573,
CC       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
CC       of expression in pancreas. Highly expressed in ovarian and colon
CC       cancer cell lines. {ECO:0000269|PubMed:12097419,
CC       ECO:0000269|PubMed:16418725}.
CC   -!- INDUCTION: In response to DNA damage.
CC       {ECO:0000269|PubMed:20559320}.
CC   -!- DOMAIN: The potential DNA-binding domain differs in sequence from
CC       that of other DP family members and can not bind DNA.
CC   -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF37562.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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DR   EMBL; AF219119; AAF37562.2; ALT_INIT; mRNA.
DR   EMBL; Z77249; CAI42694.1; -; Genomic_DNA.
DR   EMBL; CH471107; EAX11773.1; -; Genomic_DNA.
DR   CCDS; CCDS14636.2; -.
DR   RefSeq; NP_057605.3; NM_016521.2.
DR   UniGene; Hs.142908; -.
DR   ProteinModelPortal; Q5H9I0; -.
DR   SMR; Q5H9I0; 108-189, 194-341.
DR   BioGrid; 119423; 2.
DR   IntAct; Q5H9I0; 11.
DR   STRING; 9606.ENSP00000385461; -.
DR   PhosphoSite; Q5H9I0; -.
DR   DMDM; 74762180; -.
DR   PaxDb; Q5H9I0; -.
DR   PRIDE; Q5H9I0; -.
DR   DNASU; 51270; -.
DR   Ensembl; ENST00000310125; ENSP00000385461; ENSG00000183434.
DR   GeneID; 51270; -.
DR   KEGG; hsa:51270; -.
DR   UCSC; uc004exb.1; human.
DR   CTD; 51270; -.
DR   GeneCards; GC0XM132350; -.
DR   HGNC; HGNC:24603; TFDP3.
DR   MIM; 300772; gene.
DR   neXtProt; NX_Q5H9I0; -.
DR   PharmGKB; PA134898258; -.
DR   eggNOG; NOG282881; -.
DR   HOGENOM; HOG000030696; -.
DR   HOVERGEN; HBG009894; -.
DR   InParanoid; Q5H9I0; -.
DR   KO; K09393; -.
DR   OMA; NIKRRTY; -.
DR   OrthoDB; EOG7C2R27; -.
DR   PhylomeDB; Q5H9I0; -.
DR   TreeFam; TF314396; -.
DR   GenomeRNAi; 51270; -.
DR   NextBio; 54467; -.
DR   PRO; PR:Q5H9I0; -.
DR   Bgee; Q5H9I0; -.
DR   CleanEx; HS_TFDP3; -.
DR   Genevestigator; Q5H9I0; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005667; C:transcription factor complex; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
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; IDA:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR003316; E2F_TDP.
DR   InterPro; IPR028315; TFDP3.
DR   InterPro; IPR014889; Transc_factor_DP_C.
DR   InterPro; IPR015648; Transcrpt_fac_DP.
DR   InterPro; IPR011991; WHTH_DNA-bd_dom.
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.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; DNA-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN         1    405       Transcription factor Dp family member 3.
FT                                /FTId=PRO_0000305940.
FT   DNA_BIND    108    190       {ECO:0000255}.
FT   REGION      175    306       Involved in negatively regulating E2F
FT                                activity.
FT   REGION      209    241       DCB1. {ECO:0000250}.
FT   REGION      254    310       DCB2. {ECO:0000250}.
FT   MOTIF       156    190       DEF box. {ECO:0000250}.
FT   COMPBIAS    386    402       Asp/Glu-rich (acidic; NCB domain).
FT   SITE        121    121       Critical for repression of E2F activity.
FT   SITE        130    130       Critical for repression of E2F activity.
FT   SITE        131    131       Critical for repression of E2F activity.
FT   SITE        140    140       Critical for repression of E2F activity.
FT   MUTAGEN     112    112       C->R: No effect on down-regulation of E2F
FT                                transcriptional activity; when associated
FT                                with or without R-161 or with V-164.
FT   MUTAGEN     121    121       T->K: Restores enhanced E2F-mediated
FT                                transcriptional activity; when associated
FT                                with Y-130; N-131 and E-145.
FT                                {ECO:0000269|PubMed:17062573}.
FT   MUTAGEN     130    130       C->Y: Restores enhanced E2F-mediated
FT                                transcriptional activity; when associated
FT                                with K-121; N-131 and E-145.
FT                                {ECO:0000269|PubMed:17062573}.
FT   MUTAGEN     131    131       Q->N: Restores enhanced E2F-mediated
FT                                transcriptional activity; when associated
FT                                with K-121; Y-130 and E-145.
FT                                {ECO:0000269|PubMed:17062573}.
FT   MUTAGEN     140    140       K->E: Restores enhanced E2F-mediated
FT                                transcriptional activity; when associated
FT                                with K-121; Y-130 and N-131.
FT                                {ECO:0000269|PubMed:17062573}.
FT   MUTAGEN     161    161       K->R: No effect on down-regulation of E2F
FT                                transcriptional activity; when associated
FT                                with or without R-112.
FT   MUTAGEN     164    164       T->V: No effect on down-regulation of E2F
FT                                transcriptional activity; when associated
FT                                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
//
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