Q5H9I0 (TFDP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	405 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Ligand	DNA-binding
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G1/S transition of mitotic cell cycle Inferred from direct assay Ref.5. Source: UniProtKB response to DNA damage stimulus Inferred from direct assay Ref.6. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay Ref.5. Source: UniProtKB transcription factor complex Inferred from electronic annotation. Source: InterPro
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein heterodimerization activity Inferred from direct assay Ref.5. Source: UniProtKB sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 405	405	Transcription factor Dp family member 3		PRO_0000305940
Regions
	DNA binding	108 – 190	83	Potential
	Region	175 – 306	132	Involved in negatively regulating E2F activity
	Region	209 – 241	33	DCB1 By similarity
	Region	254 – 310	57	DCB2 By similarity
	Motif	156 – 190	35	DEF box By similarity
	Compositional bias	386 – 402	17	Asp/Glu-rich (acidic; NCB domain)
Sites
	Site	121	1	Critical for repression of E2F activity
	Site	130	1	Critical for repression of E2F activity
	Site	131	1	Critical for repression of E2F activity
	Site	140	1	Critical for repression of E2F activity
Experimental info
	Mutagenesis	112	1	C → R: No effect on down-regulation of E2F transcriptional activity; when associated with or without R-161 or with V-164.
	Mutagenesis	121	1	T → K: Restores enhanced E2F-mediated transcriptional activity; when associated with Y-130; N-131 and E-145. Ref.5
	Mutagenesis	130	1	C → Y: Restores enhanced E2F-mediated transcriptional activity; when associated with K-121; N-131 and E-145. Ref.5
	Mutagenesis	131	1	Q → N: Restores enhanced E2F-mediated transcriptional activity; when associated with K-121; Y-130 and E-145. Ref.5
	Mutagenesis	140	1	K → E: Restores enhanced E2F-mediated transcriptional activity; when associated with K-121; Y-130 and N-131. Ref.5
	Mutagenesis	161	1	K → R: No effect on down-regulation of E2F transcriptional activity; when associated with or without R-112.
	Mutagenesis	164	1	T → V: No effect on down-regulation of E2F transcriptional activity; when associated R-112.

Sequences

	Sequence		Length	Mass (Da)
	Q5H9I0 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: AE6F5709FE7E4C03	FASTA	405	44,967
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00176406.
RefSeq	NP_057605.3. NM_016521.2.
UniGene	Hs.142908.
3D structure databases
ProteinModelPortal	Q5H9I0.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q5H9I0. 1 interaction.
STRING	9606.ENSP00000385461.
PTM databases
PhosphoSite	Q5H9I0.
Polymorphism databases
DMDM	74762180.
Proteomic databases
PaxDb	Q5H9I0.
PRIDE	Q5H9I0.
Protocols and materials databases
DNASU	51270.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000310125; ENSP00000385461; ENSG00000183434.
GeneID	51270.
KEGG	hsa:51270.
UCSC	uc004exb.1. human.
Organism-specific databases
CTD	51270.
GeneCards	GC0XM132350.
HGNC	HGNC:24603. TFDP3.
MIM	300772. gene.
neXtProt	NX_Q5H9I0.
PharmGKB	PA134898258.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG282881.
HOGENOM	HOG000030696.
HOVERGEN	HBG009894.
InParanoid	Q5H9I0.
KO	K09393.
OMA	NIKRRTY.
OrthoDB	EOG4DFPNS.
Gene expression databases
Bgee	Q5H9I0.
CleanEx	HS_TFDP3.
Genevestigator	Q5H9I0.
Family and domain databases
Gene3D	1.10.10.10. 1 hit.
InterPro	IPR003316. E2F_TDP. IPR014889. Transc_factor_DP_C. IPR016556. Transcription_factor_DP_subgr. IPR015648. Transcrpt_fac_DP. IPR011991. WHTH_DNA-bd_dom. [Graphical view]
PANTHER	PTHR12548. PTHR12548. 1 hit.
Pfam	PF08781. DP. 1 hit. PF02319. E2F_TDP. 1 hit. [Graphical view]
PIRSF	PIRSF009404. Transcription_factor_DP. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	51270.
NextBio	54467.
SOURCE	Search...

Entry information

Entry name

TFDP3_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.