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Q14188

- TFDP2_HUMAN

UniProt

Q14188 - TFDP2_HUMAN

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Protein

Transcription factor Dp-2

Gene

TFDP2

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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ14188.
CleanExiHS_TFDP2.
ExpressionAtlasiQ14188. baseline.
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. 13 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.
GeneTreeiENSGT00390000018222.
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

        10         20         30         40         50
MTAKNVGLTS TNAEVRGFID QNLSPTKGNI SFVAFPVSNT NSPTKILPKT
60 70 80 90 100
LGPINVNVGP QMIISTPQRL TSSGSVLIGS PYTPAPAMVT QTHIAEATGW
110 120 130 140 150
VPGDRKRARK FIDSDFSESK RSKKGDKNGK GLRHFSMKVC EKVQRKGTTS
160 170 180 190 200
YNEVADELVS EFTNSNNHLA ADSAYDQKNI RRRVYDALNV LMAMNIISKE
210 220 230 240 250
KKEIKWIGLP TNSAQECQNL EIEKQRRIER IKQKRAQLQE LLLQQIAFKN
260 270 280 290 300
LVQRNRQNEQ QNQGPPALNS TIQLPFIIIN TSRKTVIDCS ISSDKFEYLF
310 320 330 340 350
NFDNTFEIHD DIEVLKRMGM SFGLESGKCS LEDLKLAKSL VPKALEGYIT
360 370 380 390 400
DISTGPSWLN QGLLLNSTQS VSNLDLTTGA TLPQSSVNQG LCLDAEVALA
410 420 430 440
TGQFLAPNSH QSSSAASHCS ESRGETPCSF NDEDEEDDEE DSSSPE
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. 13 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.
GeneTreei ENSGT00390000018222.
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

Bgeei Q14188.
CleanExi HS_TFDP2.
ExpressionAtlasi Q14188. baseline.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 143 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