Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein Dr1

Gene

Dr1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein 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

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1100515. Dr1.

Subcellular locationi

GO - Cellular componenti

  • Ada2/Gcn5/Ada3 transcription activator complex Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 176175Protein Dr1PRO_0000072441Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei105 – 1051PhosphoserineCombined sources
Modified residuei166 – 1661PhosphoserineBy similarity
Modified residuei167 – 1671PhosphoserineBy similarity

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

EPDiQ91WV0.
MaxQBiQ91WV0.
PaxDbiQ91WV0.
PRIDEiQ91WV0.

PTM databases

PhosphoSiteiQ91WV0.

Expressioni

Gene expression databases

BgeeiQ91WV0.
CleanExiMM_DR1.
GenevisibleiQ91WV0. MM.

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. Interacts with NFIL3. Component of the ADA2A-containing complex (ATAC), composed of CSRP2BP, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199303. 1 interaction.
IntActiQ91WV0. 2 interactions.
MINTiMINT-4610141.
STRINGi10090.ENSMUSP00000031190.

Structurei

3D structure databases

ProteinModelPortaliQ91WV0.
SMRiQ91WV0. Positions 9-143.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi100 – 1034Nuclear localization signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi121 – 16848Ala/Gln-richAdd
BLAST

Sequence similaritiesi

Belongs to the NC2 beta/DR1 family.Curated
Contains 1 histone-fold domain.Curated

Phylogenomic databases

eggNOGiKOG0871. Eukaryota.
COG5150. LUCA.
GeneTreeiENSGT00550000075010.
HOGENOMiHOG000178641.
InParanoidiQ91WV0.
OMAiEICNKSD.
OrthoDBiEOG7T4MMT.
PhylomeDBiQ91WV0.
TreeFamiTF317588.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR003958. CBFA_NFYB_domain.
IPR009072. Histone-fold.
[Graphical view]
PfamiPF00808. CBFD_NFYB_HMF. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q91WV0-1 [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 STQAGSSQDE EDDDDI
Length:176
Mass (Da):19,431
Last modified:December 1, 2001 - v1
Checksum:i36E7E59F2FD6D647
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031057 mRNA. Translation: BAE20474.1.
AK075713 mRNA. Translation: BAC35903.1.
AK090113 mRNA. Translation: BAC41099.1.
AK139866 mRNA. Translation: BAE24166.1.
AK146573 mRNA. Translation: BAE27269.1.
BC013461 mRNA. Translation: AAH13461.1.
CCDSiCCDS19509.1.
RefSeqiNP_080382.2. NM_026106.4.
UniGeneiMm.303534.

Genome annotation databases

EnsembliENSMUST00000031190; ENSMUSP00000031190; ENSMUSG00000029265.
GeneIDi13486.
KEGGimmu:13486.
UCSCiuc008ynt.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031057 mRNA. Translation: BAE20474.1.
AK075713 mRNA. Translation: BAC35903.1.
AK090113 mRNA. Translation: BAC41099.1.
AK139866 mRNA. Translation: BAE24166.1.
AK146573 mRNA. Translation: BAE27269.1.
BC013461 mRNA. Translation: AAH13461.1.
CCDSiCCDS19509.1.
RefSeqiNP_080382.2. NM_026106.4.
UniGeneiMm.303534.

3D structure databases

ProteinModelPortaliQ91WV0.
SMRiQ91WV0. Positions 9-143.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199303. 1 interaction.
IntActiQ91WV0. 2 interactions.
MINTiMINT-4610141.
STRINGi10090.ENSMUSP00000031190.

PTM databases

PhosphoSiteiQ91WV0.

Proteomic databases

EPDiQ91WV0.
MaxQBiQ91WV0.
PaxDbiQ91WV0.
PRIDEiQ91WV0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031190; ENSMUSP00000031190; ENSMUSG00000029265.
GeneIDi13486.
KEGGimmu:13486.
UCSCiuc008ynt.1. mouse.

Organism-specific databases

CTDi1810.
MGIiMGI:1100515. Dr1.

Phylogenomic databases

eggNOGiKOG0871. Eukaryota.
COG5150. LUCA.
GeneTreeiENSGT00550000075010.
HOGENOMiHOG000178641.
InParanoidiQ91WV0.
OMAiEICNKSD.
OrthoDBiEOG7T4MMT.
PhylomeDBiQ91WV0.
TreeFamiTF317588.

Miscellaneous databases

NextBioi283989.
PROiQ91WV0.
SOURCEiSearch...

Gene expression databases

BgeeiQ91WV0.
CleanExiMM_DR1.
GenevisibleiQ91WV0. MM.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR003958. CBFA_NFYB_domain.
IPR009072. Histone-fold.
[Graphical view]
PfamiPF00808. CBFD_NFYB_HMF. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Egg, Kidney, Liver, Thymus and Urinary bladder.
  2. "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].
    Strain: FVB/N.
    Tissue: Kidney.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiNC2B_MOUSE
AccessioniPrimary (citable) accession number: Q91WV0
Secondary accession number(s): Q3UT14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: December 1, 2001
Last modified: March 16, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.