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Protein

Protein Dr1

Gene

Dr1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

The association of the DR1/DRAP1 heterodimer with TBP results in a functional repression of both activated and basal transcription of class II genes. This interaction precludes the formation of a transcription-competent complex by inhibiting the association of TFIIA and/or TFIIB with TBP. Can bind to DNA on its own. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, Repressor
Biological processTranscription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Protein Dr1
Alternative name(s):
Down-regulator of transcription 1
Negative cofactor 2-beta
Short name:
NC2-beta
TATA-binding protein-associated phosphoprotein
Gene namesi
Name:Dr1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 14

Organism-specific databases

RGDi1305201 Dr1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000724422 – 176Protein Dr1Add BLAST175

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei105PhosphoserineBy similarity1
Modified residuei106PhosphoserineBy similarity1
Modified residuei166PhosphoserineBy similarity1
Modified residuei167PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylation regulates its interaction with TBP. Not phosphorylated when bound to DRAP1 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ5XI68
PRIDEiQ5XI68

PTM databases

iPTMnetiQ5XI68
PhosphoSitePlusiQ5XI68

Expressioni

Gene expression databases

BgeeiENSRNOG00000000070
GenevisibleiQ5XI68 RN

Interactioni

Subunit structurei

Heterodimer with DRAP1. DR1 exists in solution as a homotetramer that dissociates during interaction with TBP and then, after complexing with TBP, reassociates at a slow rate, to reconstitute the tetramer. Component of the ADA2A-containing complex (ATAC), composed of KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000064336

Structurei

3D structure databases

ProteinModelPortaliQ5XI68
SMRiQ5XI68
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini12 – 75Histone-foldSequence analysisAdd BLAST64

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi100 – 103Nuclear localization signalSequence analysis4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi121 – 168Ala/Gln-richAdd BLAST48

Sequence similaritiesi

Belongs to the NC2 beta/DR1 family.Curated

Phylogenomic databases

eggNOGiKOG0871 Eukaryota
COG5150 LUCA
GeneTreeiENSGT00550000075010
HOGENOMiHOG000178641
InParanoidiQ5XI68
KOiK21751
OMAiTIACDHI
OrthoDBiEOG091G0ZDR
PhylomeDBiQ5XI68
TreeFamiTF317588

Family and domain databases

Gene3Di1.10.20.10, 1 hit
InterProiView protein in InterPro
IPR003958 CBFA_NFYB_domain
IPR009072 Histone-fold
PfamiView protein in Pfam
PF00808 CBFD_NFYB_HMF, 1 hit
SUPFAMiSSF47113 SSF47113, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q5XI68-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSSGNDDD LTIPRAAINK MIKETLPNVR VANDARELVV NCCTEFIHLI
60 70 80 90 100
SSEANEICNK SEKKTISPEH VIQALESLGF GSYISEVKEV LQECKTVALK
110 120 130 140 150
RRKASSRLEN LGIPEEELLR QQQELFAKAR QQQAELAQQE WLQMQQAAQQ
160 170
AQLAAASASA SNQAGSSQDE DDDDDI
Length:176
Mass (Da):19,430
Last modified:November 23, 2004 - v1
Checksum:i36E7E59F2FD77AB5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083822 mRNA Translation: AAH83822.1
RefSeqiNP_001011914.1, NM_001011914.1
XP_003751365.1, XM_003751317.4
XP_017460226.1, XM_017604737.1
UniGeneiRn.6666

Genome annotation databases

EnsembliENSRNOT00000000080; ENSRNOP00000000080; ENSRNOG00000000070
ENSRNOT00000074874; ENSRNOP00000064336; ENSRNOG00000048308
GeneIDi100910207
289881
KEGGirno:100910207
rno:289881
UCSCiRGD:1305201 rat

Similar proteinsi

Entry informationi

Entry nameiNC2B_RAT
AccessioniPrimary (citable) accession number: Q5XI68
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: November 23, 2004
Last modified: March 28, 2018
This is version 105 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health