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Q5H9I0 (TFDP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor Dp family member 3
Alternative name(s):
Cancer/testis antigen 30
Short name=CT30
Hepatocellular carcinoma-associated antigen 661
Gene names
Name:TFDP3
Synonyms:DP4, HCA661
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length405 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Competitive inhibitor of E2F-mediated transactivation activity. Impairs E2F-mediated cell-cycle progression from G1 to S phase. Ref.4 Ref.5 Ref.6

Subunit structure

Heterodimer: with E2F family members. TFDP3/E2F heterodimers do not bind DNA and repress E2F-dependent transcriptional activity. Ref.5 Ref.6

Subcellular location

Nucleus. Cytoplasm. Note: Translocates to the nucleus on heterodimerization with E2F family members. Ref.4 Ref.5

Tissue specificity

Predominantly expressed in testis. Low level of expression in pancreas. Highly expressed in ovarian and colon cancer cell lines. Ref.1 Ref.4

Induction

In response to DNA damage. Ref.6

Domain

The potential DNA-binding domain differs in sequence from that of other DP family members and can not bind DNA.

Sequence similarities

Belongs to the E2F/DP family.

Sequence caution

The sequence AAF37562.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 405405Transcription factor Dp family member 3
PRO_0000305940

Regions

DNA binding108 – 19083 Potential
Region175 – 306132Involved in negatively regulating E2F activity
Region209 – 24133DCB1 By similarity
Region254 – 31057DCB2 By similarity
Motif156 – 19035DEF box By similarity
Compositional bias386 – 40217Asp/Glu-rich (acidic; NCB domain)

Sites

Site1211Critical for repression of E2F activity
Site1301Critical for repression of E2F activity
Site1311Critical for repression of E2F activity
Site1401Critical for repression of E2F activity

Experimental info

Mutagenesis1121C → R: No effect on down-regulation of E2F transcriptional activity; when associated with or without R-161 or with V-164.
Mutagenesis1211T → K: Restores enhanced E2F-mediated transcriptional activity; when associated with Y-130; N-131 and E-145. Ref.5
Mutagenesis1301C → Y: Restores enhanced E2F-mediated transcriptional activity; when associated with K-121; N-131 and E-145. Ref.5
Mutagenesis1311Q → N: Restores enhanced E2F-mediated transcriptional activity; when associated with K-121; Y-130 and E-145. Ref.5
Mutagenesis1401K → E: Restores enhanced E2F-mediated transcriptional activity; when associated with K-121; Y-130 and N-131. Ref.5
Mutagenesis1611K → R: No effect on down-regulation of E2F transcriptional activity; when associated with or without R-112.
Mutagenesis1641T → V: No effect on down-regulation of E2F transcriptional activity; when associated R-112.

Sequences

Sequence LengthMass (Da)Tools
Q5H9I0 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: AE6F5709FE7E4C03

FASTA40544,967
        10         20         30         40         50         60 
MAKYVSLTEA NEELKVLMDE NQTSRPVAVH TSTVNPLGKQ LLPKTFGQSS VNIDQQVVIG 

        70         80         90        100        110        120 
MPQRPAASNI PVVGSPNPPS THFASQNQHS YSSPPWAGQH NRKGEKNGMG LCRLSMKVWE 

       130        140        150        160        170        180 
TVQRKGTTSC QEVVGELVAK FRAASNHASP NESAYDVKNI KRRTYDALNV LMAMNIISRE 

       190        200        210        220        230        240 
KKKIKWIGLT TNSAQNCQNL RVERQKRLER IKQKQSELQQ LILQQIAFKN LVLRNQYVEE 

       250        260        270        280        290        300 
QVSQRPLPNS VIHVPFIIIS SSKKTVINCS ISDDKSEYLF KFNSSFEIHD DTEVLMWMGM 

       310        320        330        340        350        360 
TFGLESGSCS AEDLKMARNL VPKALEPYVT EMAQGTFGGV FTTAGSRSNG TWLSASDLTN 

       370        380        390        400 
IAIGMLATSS GGSQYSGSRV ETPAVEEEEE EDNNDDDLSE NDEDD 

« Hide

References

« Hide 'large scale' references
[1]"Large scale identification of human hepatocellular carcinoma-associated antigens by autoantibodies."
Wang Y., Han K.-J., Pang X.-W., Vaughan H.A., Qu W., Dong X.-Y., Peng J.-R., Zhao H.-T., Rui J.-A., Leng X.-S., Cebon J., Burgess A.W., Chen W.-F.
J. Immunol. 169:1102-1109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, IDENTIFICATION AS A CANCER/TESTIS ANTIGEN.
Tissue: Hepatoma.
[2]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"A functionally distinct member of the DP family of E2F subunits."
Milton A., Luoto K., Ingram L., Munro S., Logan N., Graham A.L., Brummelkamp T.R., Hijmans E.M., Bernards R., La Thangue N.B.
Oncogene 25:3212-3218(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[5]"Human TFDP3, a novel DP protein, inhibits DNA binding and transactivation by E2F."
Qiao H., Di Stefano L., Tian C., Li Y.Y., Yin Y.H., Qian X.P., Pang X.W., Li Y., McNutt M.A., Helin K., Zhang Y., Chen W.F.
J. Biol. Chem. 282:454-466(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF THR-121; CYS-130; GLN-131 AND LYS-140.
[6]"E2F-1 regulation by an unusual DNA damage-responsive DP partner subunit."
Ingram L., Munro S., Coutts A.S., La Thangue N.B.
Cell Death Differ. 18:122-132(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF219119 mRNA. Translation: AAF37562.2. Different initiation.
Z77249 Genomic DNA. Translation: CAI42694.1.
CH471107 Genomic DNA. Translation: EAX11773.1.
CCDSCCDS14636.2.
RefSeqNP_057605.3. NM_016521.2.
UniGeneHs.142908.

3D structure databases

ProteinModelPortalQ5H9I0.
SMRQ5H9I0. Positions 108-189, 194-341.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119423. 2 interactions.
IntActQ5H9I0. 1 interaction.
STRING9606.ENSP00000385461.

PTM databases

PhosphoSiteQ5H9I0.

Polymorphism databases

DMDM74762180.

Proteomic databases

PaxDbQ5H9I0.
PRIDEQ5H9I0.

Protocols and materials databases

DNASU51270.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000310125; ENSP00000385461; ENSG00000183434.
GeneID51270.
KEGGhsa:51270.
UCSCuc004exb.1. human.

Organism-specific databases

CTD51270.
GeneCardsGC0XM132350.
HGNCHGNC:24603. TFDP3.
MIM300772. gene.
neXtProtNX_Q5H9I0.
PharmGKBPA134898258.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG282881.
HOGENOMHOG000030696.
HOVERGENHBG009894.
InParanoidQ5H9I0.
KOK09393.
OMANIKRRTY.
OrthoDBEOG7C2R27.
PhylomeDBQ5H9I0.
TreeFamTF314396.

Gene expression databases

BgeeQ5H9I0.
CleanExHS_TFDP3.
GenevestigatorQ5H9I0.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR003316. E2F_TDP.
IPR028315. TFDP3.
IPR014889. Transc_factor_DP_C.
IPR015648. Transcrpt_fac_DP.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERPTHR12548. PTHR12548. 1 hit.
PTHR12548:SF13. PTHR12548:SF13. 1 hit.
PfamPF08781. DP. 1 hit.
PF02319. E2F_TDP. 1 hit.
[Graphical view]
PIRSFPIRSF009404. Transcription_factor_DP. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi51270.
NextBio54467.
PROQ5H9I0.
SOURCESearch...

Entry information

Entry nameTFDP3_HUMAN
AccessionPrimary (citable) accession number: Q5H9I0
Secondary accession number(s): Q6DK49, Q9NZ54
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: February 15, 2005
Last modified: July 9, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM