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Q14188

- TFDP2_HUMAN

UniProt

Q14188 - TFDP2_HUMAN

Protein

Transcription factor Dp-2

Gene

TFDP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    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.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi129 – 21082Sequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: ProtInc
    2. protein domain specific binding Source: UniProtKB
    3. sequence-specific DNA binding transcription factor activity Source: ProtInc
    4. transcription cofactor activity Source: ProtInc
    5. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. heart development Source: Ensembl
    3. mitotic cell cycle Source: Reactome
    4. Notch signaling pathway Source: Reactome
    5. positive regulation of transcription from RNA polymerase II promoter Source: Reactome
    6. transcription, DNA-templated Source: Reactome
    7. transcription initiation from RNA polymerase II promoter Source: Reactome
    8. transforming growth factor beta receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Cell cycle, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_111214. G0 and Early G1.
    REACT_118568. Pre-NOTCH Transcription and Translation.
    REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    REACT_821. Cyclin D associated events in G1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor Dp-2
    Alternative name(s):
    E2F dimerization partner 2
    Gene namesi
    Name:TFDP2
    Synonyms:DP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:11751. TFDP2.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. transcription factor complex Source: InterPro

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36466.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 446445Transcription factor Dp-2PRO_0000219477Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine1 Publication

    Post-translational modificationi

    Ser-24 is probably phosphorylated by CDK2.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ14188.
    PaxDbiQ14188.
    PRIDEiQ14188.

    PTM databases

    PhosphoSiteiQ14188.

    Expressioni

    Tissue specificityi

    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.

    Gene expression databases

    ArrayExpressiQ14188.
    BgeeiQ14188.
    CleanExiHS_TFDP2.
    GenevestigatoriQ14188.

    Organism-specific databases

    HPAiCAB018396.

    Interactioni

    Subunit structurei

    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.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi112887. 10 interactions.
    DIPiDIP-294N.
    IntActiQ14188. 9 interactions.
    MINTiMINT-88143.
    STRINGi9606.ENSP00000309622.

    Structurei

    Secondary structure

    1
    446
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi131 – 14616
    Beta strandi147 – 1493
    Helixi151 – 16313
    Helixi170 – 1723
    Helixi174 – 19320
    Beta strandi204 – 2063

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CF7X-ray2.60B121-215[»]
    ProteinModelPortaliQ14188.
    SMRiQ14188. Positions 129-210, 214-355.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14188.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni219 – 29274DimerizationSequence AnalysisAdd
    BLAST
    Regioni229 – 26133DCB1Add
    BLAST
    Regioni274 – 33057DCB2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi103 – 11816Nuclear localization signalBy similarityAdd
    BLAST
    Motifi176 – 21035DEF boxAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi432 – 44615Asp/Glu-rich (acidic; NCB domain)Add
    BLAST

    Sequence similaritiesi

    Belongs to the E2F/DP family.Curated

    Phylogenomic databases

    eggNOGiNOG271896.
    HOGENOMiHOG000030696.
    HOVERGENiHBG009894.
    InParanoidiQ14188.
    KOiK09392.
    OMAiDSQAYDQ.
    OrthoDBiEOG7C2R27.
    PhylomeDBiQ14188.
    TreeFamiTF314396.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    InterProiIPR028314. DP-2.
    IPR003316. E2F_TDP.
    IPR014889. Transc_factor_DP_C.
    IPR015648. Transcrpt_fac_DP.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PANTHERiPTHR12548. PTHR12548. 1 hit.
    PTHR12548:SF5. PTHR12548:SF5. 1 hit.
    PfamiPF08781. DP. 1 hit.
    PF02319. E2F_TDP. 1 hit.
    [Graphical view]
    PIRSFiPIRSF009404. Transcription_factor_DP. 1 hit.

    Sequences (8)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 8 isoformsi produced by alternative splicing. Align

    Isoform Alpha (identifier: Q14188-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MTAKNVGLTS TNAEVRGFID QNLSPTKGNI SFVAFPVSNT NSPTKILPKT    50
    LGPINVNVGP QMIISTPQRL TSSGSVLIGS PYTPAPAMVT QTHIAEATGW 100
    VPGDRKRARK FIDSDFSESK RSKKGDKNGK GLRHFSMKVC EKVQRKGTTS 150
    YNEVADELVS EFTNSNNHLA ADSAYDQKNI RRRVYDALNV LMAMNIISKE 200
    KKEIKWIGLP TNSAQECQNL EIEKQRRIER IKQKRAQLQE LLLQQIAFKN 250
    LVQRNRQNEQ QNQGPPALNS TIQLPFIIIN TSRKTVIDCS ISSDKFEYLF 300
    NFDNTFEIHD DIEVLKRMGM SFGLESGKCS LEDLKLAKSL VPKALEGYIT 350
    DISTGPSWLN QGLLLNSTQS VSNLDLTTGA TLPQSSVNQG LCLDAEVALA 400
    TGQFLAPNSH QSSSAASHCS ESRGETPCSF NDEDEEDDEE DSSSPE 446
    Length:446
    Mass (Da):49,236
    Last modified:May 30, 2000 - v2
    Checksum:i19A6C85BAD61DFF1
    GO
    Isoform Beta (identifier: Q14188-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:369
    Mass (Da):40,948
    Checksum:i95F7F33EAFE93A9E
    GO
    Isoform Gamma (identifier: Q14188-3) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:370
    Mass (Da):41,076
    Checksum:i35ED26B84C6B4545
    GO
    Isoform Delta (identifier: Q14188-4) [UniParc]FASTAAdd to Basket

    Also known as: 48 kDa

    The sequence of this isoform differs from the canonical sequence as follows:
         1-61: Missing.

    Show »
    Length:385
    Mass (Da):42,857
    Checksum:iCFB1E7BE8C9439B2
    GO
    Isoform Epsilon (identifier: Q14188-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-61: Missing.
         173-173: S → SQ

    Show »
    Length:386
    Mass (Da):42,985
    Checksum:i08F760ACCC483846
    GO
    Isoform 6 (identifier: Q14188-6) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:349
    Mass (Da):39,238
    Checksum:i230EEB6A470CACA9
    GO
    Isoform 7 (identifier: Q14188-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-136: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:310
    Mass (Da):34,686
    Checksum:i47C7A015A2A79CB0
    GO
    Isoform 8 (identifier: Q14188-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-62: MTAKNVGLTS...PINVNVGPQM → MQPEGIIFEAENKPSPGTESAGTFILDLSATSRT

    Note: No experimental confirmation available.

    Show »
    Length:418
    Mass (Da):46,304
    Checksum:iC15F9B7F7FCCB8FF
    GO

    Sequence cautioni

    The sequence CAB45775.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAR89905.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti269 – 2691N → S in BAH13914. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti64 – 641I → T.
    VAR_002272
    Natural varianti81 – 811P → S.1 Publication
    Corresponds to variant rs11569200 [ dbSNP | Ensembl ].
    VAR_020567

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 136136Missing in isoform 7. 1 PublicationVSP_045455Add
    BLAST
    Alternative sequencei1 – 6262MTAKN…VGPQM → MQPEGIIFEAENKPSPGTES AGTFILDLSATSRT in isoform 8. 1 PublicationVSP_047415Add
    BLAST
    Alternative sequencei1 – 6161Missing in isoform Beta, isoform Gamma, isoform Delta and isoform Epsilon. 4 PublicationsVSP_001352Add
    BLAST
    Alternative sequencei1 – 66MTAKNV → MLDPKC in isoform 6. 1 PublicationVSP_043140
    Alternative sequencei7 – 10397Missing in isoform 6. 1 PublicationVSP_043141Add
    BLAST
    Alternative sequencei103 – 11816Missing in isoform Beta and isoform Gamma. CuratedVSP_001353Add
    BLAST
    Alternative sequencei173 – 1731S → SQ in isoform Gamma and isoform Epsilon. 2 PublicationsVSP_001354

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS43159.1. [Q14188-5]
    CCDS54647.1. [Q14188-7]
    CCDS54648.1. [Q14188-8]
    CCDS54649.1. [Q14188-6]
    CCDS54650.1. [Q14188-1]
    RefSeqiNP_001171609.1. NM_001178138.1. [Q14188-5]
    NP_001171610.1. NM_001178139.1. [Q14188-1]
    NP_001171611.1. NM_001178140.1. [Q14188-8]
    NP_001171612.1. NM_001178141.1. [Q14188-6]
    NP_001171613.1. NM_001178142.1. [Q14188-7]
    NP_006277.1. NM_006286.4. [Q14188-5]
    XP_005247792.1. XM_005247735.2. [Q14188-6]
    UniGeneiHs.379018.

    Genome annotation databases

    EnsembliENST00000467072; 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]
    GeneIDi7029.
    KEGGihsa:7029.
    UCSCiuc003eul.4. human. [Q14188-5]
    uc003eun.4. human. [Q14188-1]
    uc011bnf.2. human. [Q14188-6]

    Polymorphism databases

    DMDMi8039810.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS43159.1. [Q14188-5 ]
    CCDS54647.1. [Q14188-7 ]
    CCDS54648.1. [Q14188-8 ]
    CCDS54649.1. [Q14188-6 ]
    CCDS54650.1. [Q14188-1 ]
    RefSeqi NP_001171609.1. NM_001178138.1. [Q14188-5 ]
    NP_001171610.1. NM_001178139.1. [Q14188-1 ]
    NP_001171611.1. NM_001178140.1. [Q14188-8 ]
    NP_001171612.1. NM_001178141.1. [Q14188-6 ]
    NP_001171613.1. NM_001178142.1. [Q14188-7 ]
    NP_006277.1. NM_006286.4. [Q14188-5 ]
    XP_005247792.1. XM_005247735.2. [Q14188-6 ]
    UniGenei Hs.379018.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CF7 X-ray 2.60 B 121-215 [» ]
    ProteinModelPortali Q14188.
    SMRi Q14188. Positions 129-210, 214-355.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112887. 10 interactions.
    DIPi DIP-294N.
    IntActi Q14188. 9 interactions.
    MINTi MINT-88143.
    STRINGi 9606.ENSP00000309622.

    PTM databases

    PhosphoSitei Q14188.

    Polymorphism databases

    DMDMi 8039810.

    Proteomic databases

    MaxQBi Q14188.
    PaxDbi Q14188.
    PRIDEi Q14188.

    Protocols and materials databases

    DNASUi 7029.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli 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 ]
    GeneIDi 7029.
    KEGGi hsa:7029.
    UCSCi uc003eul.4. human. [Q14188-5 ]
    uc003eun.4. human. [Q14188-1 ]
    uc011bnf.2. human. [Q14188-6 ]

    Organism-specific databases

    CTDi 7029.
    GeneCardsi GC03M141665.
    HGNCi HGNC:11751. TFDP2.
    HPAi CAB018396.
    MIMi 602160. gene.
    neXtProti NX_Q14188.
    PharmGKBi PA36466.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG271896.
    HOGENOMi HOG000030696.
    HOVERGENi HBG009894.
    InParanoidi Q14188.
    KOi K09392.
    OMAi DSQAYDQ.
    OrthoDBi EOG7C2R27.
    PhylomeDBi Q14188.
    TreeFami TF314396.

    Enzyme and pathway databases

    Reactomei REACT_111214. G0 and Early G1.
    REACT_118568. Pre-NOTCH Transcription and Translation.
    REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    REACT_821. Cyclin D associated events in G1.

    Miscellaneous databases

    EvolutionaryTracei Q14188.
    GeneWikii TFDP2.
    GenomeRNAii 7029.
    NextBioi 27461.
    PROi Q14188.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14188.
    Bgeei Q14188.
    CleanExi HS_TFDP2.
    Genevestigatori Q14188.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    InterProi IPR028314. DP-2.
    IPR003316. E2F_TDP.
    IPR014889. Transc_factor_DP_C.
    IPR015648. Transcrpt_fac_DP.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    PANTHERi PTHR12548. PTHR12548. 1 hit.
    PTHR12548:SF5. PTHR12548:SF5. 1 hit.
    Pfami PF08781. DP. 1 hit.
    PF02319. E2F_TDP. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF009404. Transcription_factor_DP. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. 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. 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.

    Entry informationi

    Entry nameiTFDP2_HUMAN
    AccessioniPrimary (citable) accession number: Q14188
    Secondary accession number(s): B7Z8C8
    , B7Z8L5, D3DNG1, E9PFC3, F8WAI2, Q13331, Q14187, Q6R754, Q8WU88, Q9UG28
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 142 of the entry and version 2 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3