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-MAY-2013, entry version 87.
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;
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.
CC -!- SUBUNIT: Heterodimer: with E2F family members. TFDP3/E2F
CC heterodimers do not bind DNA and repress E2F-dependent
CC transcriptional activity.
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.
CC -!- INDUCTION: In response to DNA damage.
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.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF37562.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
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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 IPI; IPI00176406; -.
DR RefSeq; NP_057605.3; NM_016521.2.
DR UniGene; Hs.142908; -.
DR HSSP; Q14186; 2AZE.
DR ProteinModelPortal; Q5H9I0; -.
DR IntAct; Q5H9I0; 1.
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; EOG4DFPNS; -.
DR GenomeRNAi; 51270; -.
DR NextBio; 54467; -.
DR Bgee; Q5H9I0; -.
DR CleanEx; HS_TFDP3; -.
DR Genevestigator; Q5H9I0; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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:0000082; P:G1/S transition of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0006974; P:response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR003316; E2F_TDP.
DR InterPro; IPR014889; Transc_factor_DP_C.
DR InterPro; IPR016556; Transcription_factor_DP_subgr.
DR InterPro; IPR015648; Transcrpt_fac_DP.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR PANTHER; PTHR12548; PTHR12548; 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 Potential.
FT REGION 175 306 Involved in negatively regulating E2F
FT activity.
FT REGION 209 241 DCB1 (By similarity).
FT REGION 254 310 DCB2 (By similarity).
FT MOTIF 156 190 DEF box (By similarity).
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 MUTAGEN 130 130 C->Y: Restores enhanced E2F-mediated
FT transcriptional activity; when associated
FT with K-121; N-131 and E-145.
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 MUTAGEN 140 140 K->E: Restores enhanced E2F-mediated
FT transcriptional activity; when associated
FT with K-121; Y-130 and N-131.
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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