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Q14188 (TFDP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor Dp-2
Alternative name(s):
E2F dimerization partner 2
Gene names
Name:TFDP2
Synonyms:DP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length446 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Can stimulate E2F-dependent transcription. Binds DNA cooperatively with E2F family members through the E2 recognition site, 5'-TTTC[CG]CGC-3', found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DP2/E2F complex functions in the control of cell-cycle progression from G1 to S phase. The E2F1/DP complex appears to mediate both cell proliferation and apoptosis.

Subunit structure

Component of the DRTF1/E2F transcription factor complex. Forms heterodimers with E2F family members. The complex can interact with hypophosphorylated retinoblastoma protein RB1 and related proteins (RBL1 and RBL2) that inhibit the E2F transactivation domain. During the cell cycle, RB becomes phosphorylated in mid-to-late G1 phase, detaches from the DRTF1/E2F complex rendering E2F transcriptionally active. Viral oncoproteins, notably E1A, T-antigen and HPV E7, are capable of sequestering RB protein, thus releasing the active complex. Interacts with GMCL By similarity. Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2. Ref.12 Ref.13

Subcellular location

Nucleus.

Tissue specificity

High levels in heart and skeletal muscle. Also found in placenta, kidney, brain, lung and liver. The presence as well as the abundance of the different transcripts appear to vary significantly in different tissues and cell lines.

Post-translational modification

Ser-24 is probably phosphorylated by CDK2.

Sequence similarities

Belongs to the E2F/DP family.

Sequence caution

The sequence AAR89905.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB45775.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processCell cycle
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandDNA-binding
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNotch signaling pathway

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

heart development

Inferred from electronic annotation. Source: Ensembl

mitotic cell cycle

Traceable author statement. Source: Reactome

positive regulation of transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription, DNA-templated

Traceable author statement. Source: Reactome

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

transcription factor complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionDNA binding

Traceable author statement Ref.2. Source: ProtInc

protein domain specific binding

Inferred from physical interaction Ref.12. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Non-traceable author statement Ref.2. Source: ProtInc

transcription cofactor activity

Traceable author statement Ref.2. Source: ProtInc

transcription factor binding

Inferred from physical interaction Ref.12. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]
Isoform Alpha (identifier: Q14188-1)

Also known as: 49 kDa;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Beta (identifier: Q14188-2)

Also known as: 43 kDa;

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: Missing.
     103-118: Missing.
Note: Gene prediction based on similarity to mouse ortholog. No experimental confirmation available.
Isoform Gamma (identifier: Q14188-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: Missing.
     103-118: Missing.
     173-173: S → SQ
Note: Gene prediction based on similarity to mouse ortholog. No experimental confirmation available.
Isoform Delta (identifier: Q14188-4)

Also known as: 48 kDa;

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: Missing.
Isoform Epsilon (identifier: Q14188-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: Missing.
     173-173: S → SQ
Isoform 6 (identifier: Q14188-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MTAKNV → MLDPKC
     7-103: Missing.
Isoform 7 (identifier: Q14188-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-136: Missing.
Note: No experimental confirmation available.
Isoform 8 (identifier: Q14188-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-62: MTAKNVGLTS...PINVNVGPQM → MQPEGIIFEAENKPSPGTESAGTFILDLSATSRT
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.16
Chain2 – 446445Transcription factor Dp-2
PRO_0000219477

Regions

DNA binding129 – 21082 Potential
Region219 – 29274Dimerization Potential
Region229 – 26133DCB1
Region274 – 33057DCB2
Motif103 – 11816Nuclear localization signal By similarity
Motif176 – 21035DEF box
Compositional bias432 – 44615Asp/Glu-rich (acidic; NCB domain)

Amino acid modifications

Modified residue21N-acetylthreonine Ref.16

Natural variations

Alternative sequence1 – 136136Missing in isoform 7.
VSP_045455
Alternative sequence1 – 6262MTAKN…VGPQM → MQPEGIIFEAENKPSPGTES AGTFILDLSATSRT in isoform 8.
VSP_047415
Alternative sequence1 – 6161Missing in isoform Beta, isoform Gamma, isoform Delta and isoform Epsilon.
VSP_001352
Alternative sequence1 – 66MTAKNV → MLDPKC in isoform 6.
VSP_043140
Alternative sequence7 – 10397Missing in isoform 6.
VSP_043141
Alternative sequence103 – 11816Missing in isoform Beta and isoform Gamma.
VSP_001353
Alternative sequence1731S → SQ in isoform Gamma and isoform Epsilon.
VSP_001354
Natural variant641I → T.
VAR_002272
Natural variant811P → S. Ref.3
Corresponds to variant rs11569200 [ dbSNP | Ensembl ].
VAR_020567

Experimental info

Sequence conflict2691N → S in BAH13914. Ref.4

Secondary structure

............ 446
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha (49 kDa) [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 19A6C85BAD61DFF1

FASTA44649,236
        10         20         30         40         50         60 
MTAKNVGLTS TNAEVRGFID QNLSPTKGNI SFVAFPVSNT NSPTKILPKT LGPINVNVGP 

        70         80         90        100        110        120 
QMIISTPQRL TSSGSVLIGS PYTPAPAMVT QTHIAEATGW VPGDRKRARK FIDSDFSESK 

       130        140        150        160        170        180 
RSKKGDKNGK GLRHFSMKVC EKVQRKGTTS YNEVADELVS EFTNSNNHLA ADSAYDQKNI 

       190        200        210        220        230        240 
RRRVYDALNV LMAMNIISKE KKEIKWIGLP TNSAQECQNL EIEKQRRIER IKQKRAQLQE 

       250        260        270        280        290        300 
LLLQQIAFKN LVQRNRQNEQ QNQGPPALNS TIQLPFIIIN TSRKTVIDCS ISSDKFEYLF 

       310        320        330        340        350        360 
NFDNTFEIHD DIEVLKRMGM SFGLESGKCS LEDLKLAKSL VPKALEGYIT DISTGPSWLN 

       370        380        390        400        410        420 
QGLLLNSTQS VSNLDLTTGA TLPQSSVNQG LCLDAEVALA TGQFLAPNSH QSSSAASHCS 

       430        440 
ESRGETPCSF NDEDEEDDEE DSSSPE 

« Hide

Isoform Beta (43 kDa) [UniParc].

Checksum: 95F7F33EAFE93A9E
Show »

FASTA36940,948
Isoform Gamma [UniParc].

Checksum: 35ED26B84C6B4545
Show »

FASTA37041,076
Isoform Delta (48 kDa) [UniParc].

Checksum: CFB1E7BE8C9439B2
Show »

FASTA38542,857
Isoform Epsilon [UniParc].

Checksum: 08F760ACCC483846
Show »

FASTA38642,985
Isoform 6 [UniParc].

Checksum: 230EEB6A470CACA9
Show »

FASTA34939,238
Isoform 7 [UniParc].

Checksum: 47C7A015A2A79CB0
Show »

FASTA31034,686
Isoform 8 [UniParc].

Checksum: C15F9B7F7FCCB8FF
Show »

FASTA41846,304

References

« Hide 'large scale' references
[1]"In vivo association of E2F and DP family proteins."
Wu C.-L., Zukerberg L.R., Ngwu C., Harlow E., Lees J.A.
Mol. Cell. Biol. 15:2536-2546(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA), CHARACTERIZATION.
[2]"Cloning and characterization of human DP2, a novel dimerization partner of E2F."
Zhang Y., Chellappan S.P.
Oncogene 10:2085-2093(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EPSILON).
Tissue: Kidney.
[3]NIEHS SNPs program
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-81.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 7).
Tissue: Thymus.
[5]"Full-length cDNA libraries and normalization."
Li W.B., Gruber C., Jessee J., Polayes D.
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
Tissue: Neuroblastoma.
[6]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM EPSILON).
Tissue: Placenta.
[9]"Transcriptional activation and expression of DP transcription factors during cell cycle and TPA-induced U937 differentiation."
Zhang Y., Chellappan S.P.
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-102 (ISOFORM ALPHA).
[10]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-418 (ISOFORM 8).
Tissue: Testis.
[11]"DP-2, a heterodimeric partner of E2F: identification and characterization of DP-2 proteins expressed in vivo."
Rogers K.T., Higgins P.D.R., Milla M.M., Phillips R.S., Horowitz J.M.
Proc. Natl. Acad. Sci. U.S.A. 93:7594-7599(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 62-79 (ISOFORM DELTA), ALTERNATIVE SPLICING.
Tissue: Keratinocyte.
[12]"Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation-induced E2F release."
Rubin S.M., Gall A.-L., Zheng N., Pavletich N.P.
Cell 123:1093-1106(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WITH RB1 AND E2F4.
[13]"Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein complex represses human cell cycle-dependent genes in quiescence."
Litovchick L., Sadasivam S., Florens L., Zhu X., Swanson S.K., Velmurugan S., Chen R., Washburn M.P., Liu X.S., DeCaprio J.A.
Mol. Cell 26:539-551(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE DREAM COMPLEX.
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[17]"Structural basis of DNA recognition by the heterodimeric cell cycle transcription factor E2F-DP."
Zheng N., Fraenkel E., Pabo C.O., Pavletich N.P.
Genes Dev. 13:666-674(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 121-215.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L40386 mRNA. Translation: AAA69016.1.
U18422 mRNA. Translation: AAB60378.1.
AY509596 Genomic DNA. Translation: AAR89905.1. Sequence problems.
AK303181 mRNA. Translation: BAH13914.1.
AK303634 mRNA. Translation: BAH14001.1.
CR597951 mRNA. No translation available.
AC108679 Genomic DNA. No translation available.
AC112504 Genomic DNA. No translation available.
AC128648 Genomic DNA. No translation available.
AC133435 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78977.1.
CH471052 Genomic DNA. Translation: EAW78981.1.
BC021113 mRNA. Translation: AAH21113.1.
U75488 mRNA. Translation: AAB37321.1.
AL080206 mRNA. Translation: CAB45775.2. Different initiation.
U35117 mRNA. Translation: AAC50642.1.
RefSeqNP_001171609.1. NM_001178138.1.
NP_001171610.1. NM_001178139.1.
NP_001171611.1. NM_001178140.1.
NP_001171612.1. NM_001178141.1.
NP_001171613.1. NM_001178142.1.
NP_006277.1. NM_006286.4.
XP_005247792.1. XM_005247735.2.
UniGeneHs.379018.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CF7X-ray2.60B121-215[»]
ProteinModelPortalQ14188.
SMRQ14188. Positions 129-210, 214-355.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112887. 10 interactions.
DIPDIP-294N.
IntActQ14188. 9 interactions.
MINTMINT-88143.
STRING9606.ENSP00000309622.

PTM databases

PhosphoSiteQ14188.

Polymorphism databases

DMDM8039810.

Proteomic databases

PaxDbQ14188.
PRIDEQ14188.

Protocols and materials databases

DNASU7029.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000310282; ENSP00000309622; ENSG00000114126. [Q14188-5]
ENST00000397991; ENSP00000381078; ENSG00000114126. [Q14188-8]
ENST00000467072; ENSP00000418590; ENSG00000114126. [Q14188-5]
ENST00000477292; ENSP00000418971; ENSG00000114126. [Q14188-7]
ENST00000479040; ENSP00000417585; ENSG00000114126. [Q14188-4]
ENST00000486111; ENSP00000420599; ENSG00000114126. [Q14188-5]
ENST00000489671; ENSP00000420616; ENSG00000114126. [Q14188-1]
ENST00000495310; ENSP00000419036; ENSG00000114126. [Q14188-6]
ENST00000499676; ENSP00000439782; ENSG00000114126. [Q14188-5]
GeneID7029.
KEGGhsa:7029.
UCSCuc003eul.4. human. [Q14188-5]
uc003eun.4. human. [Q14188-1]
uc011bnf.2. human. [Q14188-6]

Organism-specific databases

CTD7029.
GeneCardsGC03M141665.
HGNCHGNC:11751. TFDP2.
HPACAB018396.
MIM602160. gene.
neXtProtNX_Q14188.
PharmGKBPA36466.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG271896.
HOGENOMHOG000030696.
HOVERGENHBG009894.
InParanoidQ14188.
KOK09392.
OMADSQAYDQ.
OrthoDBEOG7C2R27.
PhylomeDBQ14188.
TreeFamTF314396.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ14188.
BgeeQ14188.
CleanExHS_TFDP2.
GenevestigatorQ14188.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR028314. DP-2.
IPR003316. E2F_TDP.
IPR014889. Transc_factor_DP_C.
IPR015648. Transcrpt_fac_DP.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERPTHR12548. PTHR12548. 1 hit.
PTHR12548:SF5. PTHR12548:SF5. 1 hit.
PfamPF08781. DP. 1 hit.
PF02319. E2F_TDP. 1 hit.
[Graphical view]
PIRSFPIRSF009404. Transcription_factor_DP. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ14188.
GeneWikiTFDP2.
GenomeRNAi7029.
NextBio27461.
PROQ14188.
SOURCESearch...

Entry information

Entry nameTFDP2_HUMAN
AccessionPrimary (citable) accession number: Q14188
Secondary accession number(s): B7Z8C8 expand/collapse secondary AC list , B7Z8L5, D3DNG1, E9PFC3, F8WAI2, Q13331, Q14187, Q6R754, Q8WU88, Q9UG28
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 30, 2000
Last modified: April 16, 2014
This is version 138 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM