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Q01658

- NC2B_HUMAN

UniProt

Q01658 - NC2B_HUMAN

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Protein

Protein Dr1

Gene

DR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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 H4.2 Publications

GO - Molecular functioni

  1. DNA binding Source: ProtInc
  2. sequence-specific DNA binding Source: InterPro
  3. TBP-class protein binding Source: BHF-UCL
  4. transcription corepressor activity Source: ProtInc
  5. transcription factor binding Source: ProtInc

GO - Biological processi

  1. chromatin organization Source: Reactome
  2. histone H3 acetylation Source: BHF-UCL
  3. negative regulation of transcription from RNA polymerase II promoter Source: ProtInc
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_172610. HATs acetylate histones.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3017. DR1.

Subcellular locationi

GO - Cellular componenti

  1. Ada2/Gcn5/Ada3 transcription activator complex Source: BHF-UCL
  2. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27475.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 176175Protein Dr1PRO_0000072440Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei166 – 1661Phosphoserine1 Publication
Modified residuei167 – 1671Phosphoserine1 Publication

Post-translational modificationi

Phosphorylation regulates its interaction with TBP. Not phosphorylated when bound to DRAP1.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ01658.
PaxDbiQ01658.
PeptideAtlasiQ01658.
PRIDEiQ01658.

PTM databases

PhosphoSiteiQ01658.

Expressioni

Gene expression databases

BgeeiQ01658.
CleanExiHS_DR1.
ExpressionAtlasiQ01658. baseline and differential.
GenevestigatoriQ01658.

Organism-specific databases

HPAiHPA050785.
HPA055308.

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 DR1.4 Publications

Protein-protein interaction databases

BioGridi108144. 34 interactions.
IntActiQ01658. 5 interactions.
MINTiMINT-204839.
STRINGi9606.ENSP00000359290.

Structurei

Secondary structure

1
176
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 2511Combined sources
Helixi33 – 6028Combined sources
Beta strandi64 – 663Combined sources
Helixi68 – 7811Combined sources
Helixi81 – 833Combined sources
Helixi84 – 11027Combined sources
Beta strandi111 – 1133Combined sources
Helixi115 – 14026Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JFIX-ray2.62B1-176[»]
ProteinModelPortaliQ01658.
SMRiQ01658. Positions 9-143.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01658.

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

eggNOGiCOG5150.
HOGENOMiHOG000178641.
HOVERGENiHBG002051.
InParanoidiQ01658.
OMAiACDHITK.
OrthoDBiEOG7T4MMT.
PhylomeDBiQ01658.
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.

Q01658-1 [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 EDDDDI
Length:176
Mass (Da):19,444
Last modified:July 1, 1993 - v1
Checksum:i36E7E59F2FD6CAB5
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti171 – 1711E → D.
Corresponds to variant rs3088371 [ dbSNP | Ensembl ].
VAR_034506

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97388 mRNA. Translation: AAA58442.1.
BT006972 mRNA. Translation: AAP35618.1.
AL137159 Genomic DNA. Translation: CAC17578.1.
BC002809 mRNA. Translation: AAH02809.1.
BC035507 mRNA. Translation: AAH35507.1.
BC068553 mRNA. Translation: AAH68553.1.
CCDSiCCDS744.1.
PIRiA43320.
RefSeqiNP_001929.1. NM_001938.2.
UniGeneiHs.348418.

Genome annotation databases

EnsembliENST00000370267; ENSP00000359290; ENSG00000117505.
ENST00000370272; ENSP00000359295; ENSG00000117505.
GeneIDi1810.
KEGGihsa:1810.
UCSCiuc001dpu.3. human.

Polymorphism databases

DMDMi401162.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97388 mRNA. Translation: AAA58442.1 .
BT006972 mRNA. Translation: AAP35618.1 .
AL137159 Genomic DNA. Translation: CAC17578.1 .
BC002809 mRNA. Translation: AAH02809.1 .
BC035507 mRNA. Translation: AAH35507.1 .
BC068553 mRNA. Translation: AAH68553.1 .
CCDSi CCDS744.1.
PIRi A43320.
RefSeqi NP_001929.1. NM_001938.2.
UniGenei Hs.348418.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JFI X-ray 2.62 B 1-176 [» ]
ProteinModelPortali Q01658.
SMRi Q01658. Positions 9-143.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108144. 34 interactions.
IntActi Q01658. 5 interactions.
MINTi MINT-204839.
STRINGi 9606.ENSP00000359290.

PTM databases

PhosphoSitei Q01658.

Polymorphism databases

DMDMi 401162.

Proteomic databases

MaxQBi Q01658.
PaxDbi Q01658.
PeptideAtlasi Q01658.
PRIDEi Q01658.

Protocols and materials databases

DNASUi 1810.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000370267 ; ENSP00000359290 ; ENSG00000117505 .
ENST00000370272 ; ENSP00000359295 ; ENSG00000117505 .
GeneIDi 1810.
KEGGi hsa:1810.
UCSCi uc001dpu.3. human.

Organism-specific databases

CTDi 1810.
GeneCardsi GC01P093811.
HGNCi HGNC:3017. DR1.
HPAi HPA050785.
HPA055308.
MIMi 601482. gene.
neXtProti NX_Q01658.
PharmGKBi PA27475.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5150.
HOGENOMi HOG000178641.
HOVERGENi HBG002051.
InParanoidi Q01658.
OMAi ACDHITK.
OrthoDBi EOG7T4MMT.
PhylomeDBi Q01658.
TreeFami TF317588.

Enzyme and pathway databases

Reactomei REACT_172610. HATs acetylate histones.

Miscellaneous databases

EvolutionaryTracei Q01658.
GeneWikii DR1_(gene).
GenomeRNAii 1810.
NextBioi 7377.
PROi Q01658.
SOURCEi Search...

Gene expression databases

Bgeei Q01658.
CleanExi HS_DR1.
ExpressionAtlasi Q01658. baseline and differential.
Genevestigatori Q01658.

Family and domain databases

Gene3Di 1.10.20.10. 1 hit.
InterProi IPR003958. CBFA_NFYB_domain.
IPR009072. Histone-fold.
[Graphical view ]
Pfami PF00808. CBFD_NFYB_HMF. 1 hit.
[Graphical view ]
SUPFAMi SSF47113. SSF47113. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Dr1, a TATA-binding protein-associated phosphoprotein and inhibitor of class II gene transcription."
    Inostroza J.A., Mermelstein F.H., Ha I., Lane W.S., Reinberg D.
    Cell 70:477-489(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Lymph, Testis and Uterus.
  5. "A mechanism for repression of class II gene transcription through specific binding of NC2 to TBP-promoter complexes via heterodimeric histone fold domains."
    Goppelt A.R., Stelzer G., Lottspeich F., Meisterernst M.
    EMBO J. 15:3105-3116(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DRAP1.
  6. "Protein-protein interaction between the transcriptional repressor E4BP4 and the TBP-binding protein Dr1."
    Cowell I.G., Hurst H.C.
    Nucleic Acids Res. 24:3607-3613(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NFIL3.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166 AND SER-167, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  9. "The double-histone-acetyltransferase complex ATAC is essential for mammalian development."
    Guelman S., Kozuka K., Mao Y., Pham V., Solloway M.J., Wang J., Wu J., Lill J.R., Zha J.
    Mol. Cell. Biol. 29:1176-1188(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN ATAC COMPLEX.
  10. "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.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Crystal structure of negative cofactor 2 recognizing the TBP-DNA transcription complex."
    Kamada K., Shu F., Chen H., Malik S., Stelzer G., Roeder R.G., Meisterernst M., Burley S.K.
    Cell 106:71-81(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) IN COMPLEX WITH DRAP1; TBP AND DNA.

Entry informationi

Entry nameiNC2B_HUMAN
AccessioniPrimary (citable) accession number: Q01658
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 26, 2014
This is version 138 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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

External Data

Dasty 3