Q14188 (TFDP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription factor Dp-2

Alternative name(s):
E2F dimerization partner 2

Gene names

Name:	TFDP2
Synonyms:	DP2

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	446 AA.
Sequence status	Complete.
Protein existence	Evidence 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.11 Ref.12
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.

Ontologies

Keywords
Biological process	Cell cycle Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	DNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G1 phase of mitotic cell cycle Traceable author statement. Source: Reactome heart development Inferred from electronic annotation. Source: Compara 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 transforming growth factor beta receptor signaling pathway Traceable author statement. Source: Reactome
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome transcription factor complex Inferred from electronic annotation. Source: InterPro
Molecular_function	DNA binding Traceable author statement Ref.2. Source: ProtInc 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
Complete GO annotation...

Alternative products

This entry describes 7 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 446

446

Transcription factor Dp-2

PRO_0000219477

Regions

DNA binding

129 – 210

82

Potential

Region

219 – 292

74

Dimerization Potential

Region

229 – 261

33

DCB1

Region

274 – 330

57

DCB2

Motif

103 – 118

16

Nuclear localization signal By similarity

Motif

176 – 210

35

DEF box

Compositional bias

432 – 446

15

Asp/Glu-rich (acidic; NCB domain)

Natural variations

Alternative sequence

1 – 136

136

Missing in isoform 7.

VSP_045455

Alternative sequence

1 – 61

61

Missing in isoform Beta, isoform Gamma, isoform Delta and isoform Epsilon.

VSP_001352

Alternative sequence

1 – 6

6

MTAKNV → MLDPKC in isoform 6.

VSP_043140

Alternative sequence

7 – 103

97

Missing in isoform 6.

VSP_043141

Alternative sequence

103 – 118

16

Missing in isoform Beta and isoform Gamma.

VSP_001353

Alternative sequence

173

1

S → SQ in isoform Gamma and isoform Epsilon.

VSP_001354

Natural variant

64

1

I → T.

VAR_002272

Natural variant

81

1

P → S. Ref.3
Corresponds to variant rs11569200 [ dbSNP | Ensembl ].

VAR_020567

Experimental info

Sequence conflict

269

1

N → S in BAH13914. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

446

Helix Strand Turn

Details...

Helix

131 – 146

16

Beta strand

147 – 149

3

Helix

151 – 163

13

Helix

170 – 172

3

Helix

174 – 193

20

Beta strand

204 – 206

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha (49 kDa) [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 19A6C85BAD61DFF1	FASTA	446	49,236
	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
	Isoform Beta (43 kDa) [UniParc]. Checksum: 95F7F33EAFE93A9E	FASTA	369	40,948
	10 20 30 40 50 60 MIISTPQRLT SSGSVLIGSP YTPAPAMVTQ THIAEATGWV PSKRSKKGDK NGKGLRHFSM 70 80 90 100 110 120 KVCEKVQRKG TTSYNEVADE LVSEFTNSNN HLAADSAYDQ KNIRRRVYDA LNVLMAMNII 130 140 150 160 170 180 SKEKKEIKWI GLPTNSAQEC QNLEIEKQRR IERIKQKRAQ LQELLLQQIA FKNLVQRNRQ 190 200 210 220 230 240 NEQQNQGPPA LNSTIQLPFI IINTSRKTVI DCSISSDKFE YLFNFDNTFE IHDDIEVLKR 250 260 270 280 290 300 MGMSFGLESG KCSLEDLKLA KSLVPKALEG YITDISTGPS WLNQGLLLNS TQSVSNLDLT 310 320 330 340 350 360 TGATLPQSSV NQGLCLDAEV ALATGQFLAP NSHQSSSAAS HCSESRGETP CSFNDEDEED DEEDSSSPE
	Isoform Gamma [UniParc]. Checksum: 35ED26B84C6B4545	FASTA	370	41,076
	10 20 30 40 50 60 MIISTPQRLT SSGSVLIGSP YTPAPAMVTQ THIAEATGWV PSKRSKKGDK NGKGLRHFSM 70 80 90 100 110 120 KVCEKVQRKG TTSYNEVADE LVSEFTNSNN HLAADSQAYD QKNIRRRVYD ALNVLMAMNI 130 140 150 160 170 180 ISKEKKEIKW IGLPTNSAQE CQNLEIEKQR RIERIKQKRA QLQELLLQQI AFKNLVQRNR 190 200 210 220 230 240 QNEQQNQGPP ALNSTIQLPF IIINTSRKTV IDCSISSDKF EYLFNFDNTF EIHDDIEVLK 250 260 270 280 290 300 RMGMSFGLES GKCSLEDLKL AKSLVPKALE GYITDISTGP SWLNQGLLLN STQSVSNLDL 310 320 330 340 350 360 TTGATLPQSS VNQGLCLDAE VALATGQFLA PNSHQSSSAA SHCSESRGET PCSFNDEDEE 370 DDEEDSSSPE
	Isoform Delta (48 kDa) [UniParc]. Checksum: CFB1E7BE8C9439B2	FASTA	385	42,857
	10 20 30 40 50 60 MIISTPQRLT SSGSVLIGSP YTPAPAMVTQ THIAEATGWV PGDRKRARKF IDSDFSESKR 70 80 90 100 110 120 SKKGDKNGKG LRHFSMKVCE KVQRKGTTSY NEVADELVSE FTNSNNHLAA DSAYDQKNIR 130 140 150 160 170 180 RRVYDALNVL MAMNIISKEK KEIKWIGLPT NSAQECQNLE IEKQRRIERI KQKRAQLQEL 190 200 210 220 230 240 LLQQIAFKNL VQRNRQNEQQ NQGPPALNST IQLPFIIINT SRKTVIDCSI SSDKFEYLFN 250 260 270 280 290 300 FDNTFEIHDD IEVLKRMGMS FGLESGKCSL EDLKLAKSLV PKALEGYITD ISTGPSWLNQ 310 320 330 340 350 360 GLLLNSTQSV SNLDLTTGAT LPQSSVNQGL CLDAEVALAT GQFLAPNSHQ SSSAASHCSE 370 380 SRGETPCSFN DEDEEDDEED SSSPE
	Isoform Epsilon [UniParc]. Checksum: 08F760ACCC483846	FASTA	386	42,985
	10 20 30 40 50 60 MIISTPQRLT SSGSVLIGSP YTPAPAMVTQ THIAEATGWV PGDRKRARKF IDSDFSESKR 70 80 90 100 110 120 SKKGDKNGKG LRHFSMKVCE KVQRKGTTSY NEVADELVSE FTNSNNHLAA DSQAYDQKNI 130 140 150 160 170 180 RRRVYDALNV LMAMNIISKE KKEIKWIGLP TNSAQECQNL EIEKQRRIER IKQKRAQLQE 190 200 210 220 230 240 LLLQQIAFKN LVQRNRQNEQ QNQGPPALNS TIQLPFIIIN TSRKTVIDCS ISSDKFEYLF 250 260 270 280 290 300 NFDNTFEIHD DIEVLKRMGM SFGLESGKCS LEDLKLAKSL VPKALEGYIT DISTGPSWLN 310 320 330 340 350 360 QGLLLNSTQS VSNLDLTTGA TLPQSSVNQG LCLDAEVALA TGQFLAPNSH QSSSAASHCS 370 380 ESRGETPCSF NDEDEEDDEE DSSSPE
	Isoform 6 [UniParc]. Checksum: 230EEB6A470CACA9	FASTA	349	39,238
	10 20 30 40 50 60 MLDPKCDRKR ARKFIDSDFS ESKRSKKGDK NGKGLRHFSM KVCEKVQRKG TTSYNEVADE 70 80 90 100 110 120 LVSEFTNSNN HLAADSAYDQ KNIRRRVYDA LNVLMAMNII SKEKKEIKWI GLPTNSAQEC 130 140 150 160 170 180 QNLEIEKQRR IERIKQKRAQ LQELLLQQIA FKNLVQRNRQ NEQQNQGPPA LNSTIQLPFI 190 200 210 220 230 240 IINTSRKTVI DCSISSDKFE YLFNFDNTFE IHDDIEVLKR MGMSFGLESG KCSLEDLKLA 250 260 270 280 290 300 KSLVPKALEG YITDISTGPS WLNQGLLLNS TQSVSNLDLT TGATLPQSSV NQGLCLDAEV 310 320 330 340 ALATGQFLAP NSHQSSSAAS HCSESRGETP CSFNDEDEED DEEDSSSPE
	Isoform 7 [UniParc]. Checksum: 47C7A015A2A79CB0	FASTA	310	34,686
	10 20 30 40 50 60 MKVCEKVQRK GTTSYNEVAD ELVSEFTNSN NHLAADSAYD QKNIRRRVYD ALNVLMAMNI 70 80 90 100 110 120 ISKEKKEIKW IGLPTNSAQE CQNLEIEKQR RIERIKQKRA QLQELLLQQI AFKNLVQRNR 130 140 150 160 170 180 QNEQQNQGPP ALNSTIQLPF IIINTSRKTV IDCSISSDKF EYLFNFDNTF EIHDDIEVLK 190 200 210 220 230 240 RMGMSFGLES GKCSLEDLKL AKSLVPKALE GYITDISTGP SWLNQGLLLN STQSVSNLDL 250 260 270 280 290 300 TTGATLPQSS VNQGLCLDAE VALATGQFLA PNSHQSSSAA SHCSESRGET PCSFNDEDEE 310 DDEEDSSSPE

References

	« Hide 'large scale' referencesShow '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. , 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]	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].
[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]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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

NIEHS-SNPs

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.
U35117 mRNA. Translation: AAC50642.1.

IPI

IPI00029096.
IPI00218877.
IPI00295550.
IPI00296752.
IPI00915033.
IPI00944999.
IPI00946984.

RefSeq

NP_001171609.1. NM_001178138.1.
NP_001171610.1. NM_001178139.1.
NP_001171612.1. NM_001178141.1.
NP_001171613.1. NM_001178142.1.
NP_006277.1. NM_006286.4.

UniGene

Hs.379018.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CF7	X-ray	2.60	B	121-215	[»]

ProteinModelPortal

Q14188.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-294N.

IntAct

Q14188. 5 interactions.

MINT

MINT-88143.

STRING

9606.ENSP00000309622.

PTM databases

PhosphoSite

Q14188.

Polymorphism databases

DMDM

8039810.

Proteomic databases

PaxDb

Q14188.

PRIDE

Q14188.

Protocols and materials databases

DNASU

7029.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000310282; ENSP00000309622; ENSG00000114126.
ENST00000467072; ENSP00000418590; ENSG00000114126.
ENST00000477292; ENSP00000418971; ENSG00000114126.
ENST00000479040; ENSP00000417585; ENSG00000114126.
ENST00000486111; ENSP00000420599; ENSG00000114126.
ENST00000489671; ENSP00000420616; ENSG00000114126.
ENST00000495310; ENSP00000419036; ENSG00000114126.
ENST00000499676; ENSP00000439782; ENSG00000114126.

GeneID

7029.

KEGG

hsa:7029.

UCSC

uc003eul.4. human.
uc003eun.4. human.
uc011bnf.2. human.

Organism-specific databases

CTD

7029.

GeneCards

GC03M141665.

HGNC

HGNC:11751. TFDP2.

HPA

CAB018396.

MIM

602160. gene.

neXtProt

NX_Q14188.

PharmGKB

PA36466.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG271896.

HOGENOM

HOG000030696.

HOVERGEN

HBG009894.

InParanoid

Q14188.

KO

K09392.

OMA

EGYITDM.

OrthoDB

EOG4D52XZ.

PhylomeDB

Q14188.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q14188.

Bgee

Q14188.

CleanEx

HS_TFDP2.

Genevestigator

Q14188.

GermOnline

ENSG00000114126. Homo sapiens.

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

EvolutionaryTrace

Q14188.

GenomeRNAi

7029.

NextBio

27461.

SOURCE

Search...

Entry information

Entry name

TFDP2_HUMAN

Accession

Primary (citable) accession number: Q14188
Secondary accession number(s): B7Z8C8 , B7Z8L5, D3DNG1, E9PFC3, Q13331, Q14187, Q6R754, Q8WU88

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	May 30, 2000
Last modified:	May 29, 2013
This is version 130 of the entry and version 2 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.