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Protein

Transcription factor Dp-2

Gene

TFDP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 TFDP2: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. Blocks adipocyte differentiation by repressing CEBPA binding to its target gene promoters (PubMed:20176812).1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi129 – 210Sequence analysisAdd BLAST82

GO - Molecular functioni

  • DNA binding Source: ProtInc
  • protein domain specific binding Source: UniProtKB
  • RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: GO_Central
  • transcription cofactor activity Source: ProtInc
  • transcription factor activity, sequence-specific DNA binding Source: ProtInc
  • transcription factor binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-111448. Activation of NOXA and translocation to mitochondria.
R-HSA-113501. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
R-HSA-113510. E2F mediated regulation of DNA replication.
R-HSA-139915. Activation of PUMA and translocation to mitochondria.
R-HSA-1538133. G0 and Early G1.
R-HSA-1912408. Pre-NOTCH Transcription and Translation.
R-HSA-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-2559585. Oncogene Induced Senescence.
R-HSA-6804114. TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
R-HSA-69205. G1/S-Specific Transcription.
R-HSA-69231. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:11751. TFDP2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi7029.
OpenTargetsiENSG00000114126.
PharmGKBiPA36466.

Polymorphism and mutation databases

BioMutaiTFDP2.
DMDMi8039810.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002194772 – 446Transcription factor Dp-2Add BLAST445

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonineCombined sources1
Modified residuei24PhosphoserineCombined sources1
Modified residuei122PhosphoserineCombined sources1

Post-translational modificationi

Ser-24 is probably phosphorylated by CDK2.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ14188.
MaxQBiQ14188.
PaxDbiQ14188.
PeptideAtlasiQ14188.
PRIDEiQ14188.

PTM databases

iPTMnetiQ14188.
PhosphoSitePlusiQ14188.

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

BgeeiENSG00000114126.
CleanExiHS_TFDP2.
ExpressionAtlasiQ14188. baseline and differential.
GenevisibleiQ14188. HS.

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. The complex TFDP2:E2F1 interacts with CEBPA; the interaction prevents CEBPA binding to target genes promoters and represses its transcriptional activity (PubMed:20176812).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
E2F6O754618EBI-752268,EBI-749694
E7P031292EBI-752268,EBI-866453From a different organism.

GO - Molecular functioni

  • protein domain specific binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112887. 16 interactors.
DIPiDIP-294N.
IntActiQ14188. 10 interactors.
MINTiMINT-88143.
STRINGi9606.ENSP00000420616.

Structurei

Secondary structure

1446
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi131 – 146Combined sources16
Beta strandi147 – 149Combined sources3
Helixi151 – 163Combined sources13
Helixi170 – 172Combined sources3
Helixi174 – 193Combined sources20
Beta strandi204 – 206Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CF7X-ray2.60B121-215[»]
ProteinModelPortaliQ14188.
SMRiQ14188.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14188.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni60 – 82Interaction with CEBPA1 PublicationAdd BLAST23
Regioni219 – 292DimerizationSequence analysisAdd BLAST74
Regioni229 – 261DCB1Add BLAST33
Regioni274 – 330DCB2Add BLAST57

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi103 – 118Nuclear localization signalBy similarityAdd BLAST16
Motifi176 – 210DEF boxAdd BLAST35

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi432 – 446Asp/Glu-rich (acidic; NCB domain)Add BLAST15

Sequence similaritiesi

Belongs to the E2F/DP family.Curated

Phylogenomic databases

eggNOGiKOG2829. Eukaryota.
ENOG410Y9QP. LUCA.
GeneTreeiENSGT00390000018222.
HOGENOMiHOG000030696.
HOVERGENiHBG009894.
InParanoidiQ14188.
KOiK09392.
OMAiDSQAYDQ.
OrthoDBiEOG091G0AVY.
PhylomeDBiQ14188.
TreeFamiTF314396.

Family and domain databases

CDDicd14458. DP_DD. 1 hit.
Gene3Di1.10.10.10. 1 hit.
InterProiIPR028314. DP-2.
IPR003316. E2F_WHTH_DNA-bd_dom.
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.
SMARTiSM01138. DP. 1 hit.
SM01372. E2F_TDP. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 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. AlignAdd to basket

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti269N → S in BAH13914 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00227264I → T.Corresponds to variant rs748095099dbSNPEnsembl.1
Natural variantiVAR_02056781P → S.1 PublicationCorresponds to variant rs11569200dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0454551 – 136Missing in isoform 7. 1 PublicationAdd BLAST136
Alternative sequenceiVSP_0474151 – 62MTAKN…VGPQM → MQPEGIIFEAENKPSPGTES AGTFILDLSATSRT in isoform 8. 1 PublicationAdd BLAST62
Alternative sequenceiVSP_0013521 – 61Missing in isoform Beta, isoform Gamma, isoform Delta and isoform Epsilon. 4 PublicationsAdd BLAST61
Alternative sequenceiVSP_0431401 – 6MTAKNV → MLDPKC in isoform 6. 1 Publication6
Alternative sequenceiVSP_0431417 – 103Missing in isoform 6. 1 PublicationAdd BLAST97
Alternative sequenceiVSP_001353103 – 118Missing in isoform Beta and isoform Gamma. CuratedAdd BLAST16
Alternative sequenceiVSP_001354173S → SQ in isoform Gamma and isoform Epsilon. 2 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_016862580.1. XM_017007091.1. [Q14188-1]
XP_016862585.1. XM_017007096.1. [Q14188-5]
XP_016862586.1. XM_017007097.1. [Q14188-4]
XP_016862587.1. XM_017007098.1. [Q14188-5]
XP_016862588.1. XM_017007099.1. [Q14188-4]
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]
ENST00000499676; ENSP00000439782; ENSG00000114126. [Q14188-8]
GeneIDi7029.
KEGGihsa:7029.
UCSCiuc003euk.5. human. [Q14188-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_016862580.1. XM_017007091.1. [Q14188-1]
XP_016862585.1. XM_017007096.1. [Q14188-5]
XP_016862586.1. XM_017007097.1. [Q14188-4]
XP_016862587.1. XM_017007098.1. [Q14188-5]
XP_016862588.1. XM_017007099.1. [Q14188-4]
UniGeneiHs.379018.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CF7X-ray2.60B121-215[»]
ProteinModelPortaliQ14188.
SMRiQ14188.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112887. 16 interactors.
DIPiDIP-294N.
IntActiQ14188. 10 interactors.
MINTiMINT-88143.
STRINGi9606.ENSP00000420616.

PTM databases

iPTMnetiQ14188.
PhosphoSitePlusiQ14188.

Polymorphism and mutation databases

BioMutaiTFDP2.
DMDMi8039810.

Proteomic databases

EPDiQ14188.
MaxQBiQ14188.
PaxDbiQ14188.
PeptideAtlasiQ14188.
PRIDEiQ14188.

Protocols and materials databases

DNASUi7029.
Structural Biology KnowledgebaseSearch...

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]
ENST00000499676; ENSP00000439782; ENSG00000114126. [Q14188-8]
GeneIDi7029.
KEGGihsa:7029.
UCSCiuc003euk.5. human. [Q14188-1]

Organism-specific databases

CTDi7029.
DisGeNETi7029.
GeneCardsiTFDP2.
HGNCiHGNC:11751. TFDP2.
HPAiCAB018396.
MIMi602160. gene.
neXtProtiNX_Q14188.
OpenTargetsiENSG00000114126.
PharmGKBiPA36466.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2829. Eukaryota.
ENOG410Y9QP. LUCA.
GeneTreeiENSGT00390000018222.
HOGENOMiHOG000030696.
HOVERGENiHBG009894.
InParanoidiQ14188.
KOiK09392.
OMAiDSQAYDQ.
OrthoDBiEOG091G0AVY.
PhylomeDBiQ14188.
TreeFamiTF314396.

Enzyme and pathway databases

ReactomeiR-HSA-111448. Activation of NOXA and translocation to mitochondria.
R-HSA-113501. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
R-HSA-113510. E2F mediated regulation of DNA replication.
R-HSA-139915. Activation of PUMA and translocation to mitochondria.
R-HSA-1538133. G0 and Early G1.
R-HSA-1912408. Pre-NOTCH Transcription and Translation.
R-HSA-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-2559585. Oncogene Induced Senescence.
R-HSA-6804114. TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
R-HSA-69205. G1/S-Specific Transcription.
R-HSA-69231. Cyclin D associated events in G1.

Miscellaneous databases

ChiTaRSiTFDP2. human.
EvolutionaryTraceiQ14188.
GeneWikiiTFDP2.
GenomeRNAii7029.
PROiQ14188.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000114126.
CleanExiHS_TFDP2.
ExpressionAtlasiQ14188. baseline and differential.
GenevisibleiQ14188. HS.

Family and domain databases

CDDicd14458. DP_DD. 1 hit.
Gene3Di1.10.10.10. 1 hit.
InterProiIPR028314. DP-2.
IPR003316. E2F_WHTH_DNA-bd_dom.
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.
SMARTiSM01138. DP. 1 hit.
SM01372. E2F_TDP. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
ProtoNetiSearch...

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: November 30, 2016
This is version 164 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.