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Protein

Transcription factor Dp family member 3

Gene

TFDP3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Competitive inhibitor of E2F-mediated transactivation activity. Impairs E2F-mediated cell-cycle progression from G1 to S phase.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei121 – 1211Critical for repression of E2F activity
Sitei130 – 1301Critical for repression of E2F activity
Sitei131 – 1311Critical for repression of E2F activity
Sitei140 – 1401Critical for repression of E2F activity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi108 – 19083Sequence AnalysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor Dp family member 3
Alternative name(s):
Cancer/testis antigen 30
Short name:
CT30
Hepatocellular carcinoma-associated antigen 661
Gene namesi
Name:TFDP3
Synonyms:DP4, HCA661
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:24603. TFDP3.

Subcellular locationi

  • Nucleus
  • Cytoplasm

  • Note: Translocates to the nucleus on heterodimerization with E2F family members.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleus Source: GO_Central
  • transcription factor complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi112 – 1121C → R: No effect on down-regulation of E2F transcriptional activity; when associated with or without R-161 or with V-164.
Mutagenesisi121 – 1211T → K: Restores enhanced E2F-mediated transcriptional activity; when associated with Y-130; N-131 and E-145. 1 Publication
Mutagenesisi130 – 1301C → Y: Restores enhanced E2F-mediated transcriptional activity; when associated with K-121; N-131 and E-145. 1 Publication
Mutagenesisi131 – 1311Q → N: Restores enhanced E2F-mediated transcriptional activity; when associated with K-121; Y-130 and E-145. 1 Publication
Mutagenesisi140 – 1401K → E: Restores enhanced E2F-mediated transcriptional activity; when associated with K-121; Y-130 and N-131. 1 Publication
Mutagenesisi161 – 1611K → R: No effect on down-regulation of E2F transcriptional activity; when associated with or without R-112.
Mutagenesisi164 – 1641T → V: No effect on down-regulation of E2F transcriptional activity; when associated R-112.

Organism-specific databases

PharmGKBiPA134898258.

Polymorphism and mutation databases

BioMutaiTFDP3.
DMDMi74762180.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 405405Transcription factor Dp family member 3PRO_0000305940Add
BLAST

Proteomic databases

PaxDbiQ5H9I0.
PRIDEiQ5H9I0.

PTM databases

PhosphoSiteiQ5H9I0.

Expressioni

Tissue specificityi

Predominantly expressed in testis. Low level of expression in pancreas. Highly expressed in ovarian and colon cancer cell lines.2 Publications

Inductioni

In response to DNA damage.1 Publication

Gene expression databases

BgeeiQ5H9I0.
CleanExiHS_TFDP3.
GenevisibleiQ5H9I0. HS.

Interactioni

Subunit structurei

Heterodimer: with E2F family members. TFDP3/E2F heterodimers do not bind DNA and repress E2F-dependent transcriptional activity.2 Publications

Protein-protein interaction databases

BioGridi119423. 21 interactions.
IntActiQ5H9I0. 11 interactions.
STRINGi9606.ENSP00000385461.

Structurei

3D structure databases

ProteinModelPortaliQ5H9I0.
SMRiQ5H9I0. Positions 108-189, 194-341.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni175 – 306132Involved in negatively regulating E2F activityAdd
BLAST
Regioni209 – 24133DCB1By similarityAdd
BLAST
Regioni254 – 31057DCB2By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi156 – 19035DEF boxBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi386 – 40217Asp/Glu-rich (acidic; NCB domain)Add
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the E2F/DP family.Curated

Phylogenomic databases

eggNOGiNOG282881.
GeneTreeiENSGT00390000018222.
HOGENOMiHOG000030696.
HOVERGENiHBG009894.
InParanoidiQ5H9I0.
KOiK09393.
OMAiNIKRRTY.
OrthoDBiEOG7C2R27.
PhylomeDBiQ5H9I0.
TreeFamiTF314396.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR003316. E2F_WHTH_DNA-bd_dom.
IPR028315. TFDP3.
IPR014889. Transc_factor_DP_C.
IPR015648. Transcrpt_fac_DP.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12548. PTHR12548. 1 hit.
PTHR12548:SF13. PTHR12548:SF13. 1 hit.
PfamiPF08781. DP. 1 hit.
PF02319. E2F_TDP. 1 hit.
[Graphical view]
PIRSFiPIRSF009404. Transcription_factor_DP. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5H9I0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKYVSLTEA NEELKVLMDE NQTSRPVAVH TSTVNPLGKQ LLPKTFGQSS
60 70 80 90 100
VNIDQQVVIG MPQRPAASNI PVVGSPNPPS THFASQNQHS YSSPPWAGQH
110 120 130 140 150
NRKGEKNGMG LCRLSMKVWE TVQRKGTTSC QEVVGELVAK FRAASNHASP
160 170 180 190 200
NESAYDVKNI KRRTYDALNV LMAMNIISRE KKKIKWIGLT TNSAQNCQNL
210 220 230 240 250
RVERQKRLER IKQKQSELQQ LILQQIAFKN LVLRNQYVEE QVSQRPLPNS
260 270 280 290 300
VIHVPFIIIS SSKKTVINCS ISDDKSEYLF KFNSSFEIHD DTEVLMWMGM
310 320 330 340 350
TFGLESGSCS AEDLKMARNL VPKALEPYVT EMAQGTFGGV FTTAGSRSNG
360 370 380 390 400
TWLSASDLTN IAIGMLATSS GGSQYSGSRV ETPAVEEEEE EDNNDDDLSE

NDEDD
Length:405
Mass (Da):44,967
Last modified:February 15, 2005 - v1
Checksum:iAE6F5709FE7E4C03
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF219119 mRNA. Translation: AAF37562.2. Different initiation.
Z77249 Genomic DNA. Translation: CAI42694.1.
CH471107 Genomic DNA. Translation: EAX11773.1.
CCDSiCCDS14636.2.
RefSeqiNP_057605.3. NM_016521.2.
UniGeneiHs.142908.

Genome annotation databases

EnsembliENST00000310125; ENSP00000385461; ENSG00000183434.
GeneIDi51270.
KEGGihsa:51270.
UCSCiuc004exb.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF219119 mRNA. Translation: AAF37562.2. Different initiation.
Z77249 Genomic DNA. Translation: CAI42694.1.
CH471107 Genomic DNA. Translation: EAX11773.1.
CCDSiCCDS14636.2.
RefSeqiNP_057605.3. NM_016521.2.
UniGeneiHs.142908.

3D structure databases

ProteinModelPortaliQ5H9I0.
SMRiQ5H9I0. Positions 108-189, 194-341.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119423. 21 interactions.
IntActiQ5H9I0. 11 interactions.
STRINGi9606.ENSP00000385461.

PTM databases

PhosphoSiteiQ5H9I0.

Polymorphism and mutation databases

BioMutaiTFDP3.
DMDMi74762180.

Proteomic databases

PaxDbiQ5H9I0.
PRIDEiQ5H9I0.

Protocols and materials databases

DNASUi51270.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000310125; ENSP00000385461; ENSG00000183434.
GeneIDi51270.
KEGGihsa:51270.
UCSCiuc004exb.1. human.

Organism-specific databases

CTDi51270.
GeneCardsiGC0XM132350.
HGNCiHGNC:24603. TFDP3.
MIMi300772. gene.
neXtProtiNX_Q5H9I0.
PharmGKBiPA134898258.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG282881.
GeneTreeiENSGT00390000018222.
HOGENOMiHOG000030696.
HOVERGENiHBG009894.
InParanoidiQ5H9I0.
KOiK09393.
OMAiNIKRRTY.
OrthoDBiEOG7C2R27.
PhylomeDBiQ5H9I0.
TreeFamiTF314396.

Miscellaneous databases

GenomeRNAii51270.
NextBioi54467.
PROiQ5H9I0.
SOURCEiSearch...

Gene expression databases

BgeeiQ5H9I0.
CleanExiHS_TFDP3.
GenevisibleiQ5H9I0. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR003316. E2F_WHTH_DNA-bd_dom.
IPR028315. TFDP3.
IPR014889. Transc_factor_DP_C.
IPR015648. Transcrpt_fac_DP.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12548. PTHR12548. 1 hit.
PTHR12548:SF13. PTHR12548:SF13. 1 hit.
PfamiPF08781. DP. 1 hit.
PF02319. E2F_TDP. 1 hit.
[Graphical view]
PIRSFiPIRSF009404. Transcription_factor_DP. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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.

Entry informationi

Entry nameiTFDP3_HUMAN
AccessioniPrimary (citable) accession number: Q5H9I0
Secondary accession number(s): Q6DK49, Q9NZ54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: February 15, 2005
Last modified: June 24, 2015
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.