Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
DR1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
DR1 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. 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. Interacts with NFIL3. Component of the ADA2A-containing complex (ATAC), composed of CSRP2BP, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1. Belongs to the NC2 beta/DR1 family. Note: This description may include information from UniProtKB.
Protein type: Transcription, coactivator/corepressor
Chromosomal Location of Human Ortholog: 1p22.1
Cellular Component: nucleus
Molecular Function: protein binding; DNA binding; protein heterodimerization activity; sequence-specific DNA binding; TATA-binding protein binding; transcription factor binding; transcription corepressor activity
Biological Process: establishment and/or maintenance of chromatin architecture; transcription, DNA-dependent; negative regulation of transcription from RNA polymerase II promoter
Reference #:  Q01658 (UniProtKB)
Alt. Names/Synonyms: Down-regulator of transcription 1; down-regulator of transcription 1, TBP-binding (negative cofactor 2); DR1; NC2; NC2-beta; NC2B; Negative cofactor 2-beta; Protein Dr1; TATA-binding protein-associated phosphoprotein
Gene Symbols: DR1
Molecular weight: 19,444 Da
Basal Isoelectric point: 4.69  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

DR1

Protein Structure Not Found.


STRING  |  cBioPortal  |  Wikipedia  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 S3-p _____MAsSsGNDDD
0 1 S5-p ___MAsSsGNDDDLT
0 1 T25 INKMIKETLPNVRVA
0 1 S67-p KSEKKTIsPEHVIQA
0 3 T96-p EVLQECKtVALKRRK
0 154 S105-p ALKRRKAssRLENLG
0 8 S106-p LKRRKAssRLENLGI
0 1 K128 QQQELFAKARQQQAE
0 1 S166-p SASNQAGssQDEEDD
0 1 S167-p ASNQAGssQDEEDDD
  mouse

 
S3 _____MASSSGNDDD
S5 ___MASSSGNDDDLT
T25-p INKMIKEtLPNVRVA
S67 KSEKKTISPEHVIQA
T96 EVLQECKTVALKRRK
S105-p ALKRRKAssRLENLG
S106-p LKRRKAssRLENLGI
K128 QQQELFAKARQQQAE
S166 SASTQAGSSQDEEDD
S167 ASTQAGSSQDEEDDD
  rat

 
S3 _____MASSSGNDDD
S5 ___MASSSGNDDDLT
T25 INKMIKETLPNVRVA
S67 KSEKKTISPEHVIQA
T96 EVLQECKTVALKRRK
S105-p ALKRRKAsSRLENLG
S106 LKRRKAsSRLENLGI
K128-ac QQQELFAkARQQQAE
S166 SASNQAGSSQDEDDD
S167 ASNQAGSSQDEDDDD
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.