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Q01658 (NC2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:DR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length176 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.9

Subunit structure

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. Ref.5 Ref.6 Ref.9

Subcellular location

Nucleus.

Post-translational modification

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

Sequence similarities

Belongs to the NC2 beta/DR1 family.

Contains 1 histone-fold domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 176175Protein Dr1
PRO_0000072440

Regions

Motif100 – 1034Nuclear localization signal Potential
Compositional bias121 – 16848Ala/Gln-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.13
Modified residue1661Phosphoserine Ref.7
Modified residue1671Phosphoserine Ref.7

Natural variations

Natural variant1711E → D.
Corresponds to variant rs3088371 [ dbSNP | Ensembl ].
VAR_034506

Secondary structure

............... 176
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q01658 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 36E7E59F2FD6CAB5

FASTA17619,444
        10         20         30         40         50         60 
MASSSGNDDD LTIPRAAINK MIKETLPNVR VANDARELVV NCCTEFIHLI SSEANEICNK 

        70         80         90        100        110        120 
SEKKTISPEH VIQALESLGF GSYISEVKEV LQECKTVALK RRKASSRLEN LGIPEEELLR 

       130        140        150        160        170 
QQQELFAKAR QQQAELAQQE WLQMQQAAQQ AQLAAASASA SNQAGSSQDE EDDDDI 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS744.1.
PIRA43320.
RefSeqNP_001929.1. NM_001938.2.
UniGeneHs.348418.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JFIX-ray2.62B1-176[»]
ProteinModelPortalQ01658.
SMRQ01658. Positions 9-143.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108144. 33 interactions.
IntActQ01658. 5 interactions.
MINTMINT-204839.
STRING9606.ENSP00000359290.

PTM databases

PhosphoSiteQ01658.

Polymorphism databases

DMDM401162.

Proteomic databases

MaxQBQ01658.
PaxDbQ01658.
PeptideAtlasQ01658.
PRIDEQ01658.

Protocols and materials databases

DNASU1810.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370267; ENSP00000359290; ENSG00000117505.
ENST00000370272; ENSP00000359295; ENSG00000117505.
GeneID1810.
KEGGhsa:1810.
UCSCuc001dpu.3. human.

Organism-specific databases

CTD1810.
GeneCardsGC01P093811.
HGNCHGNC:3017. DR1.
HPAHPA050785.
HPA055308.
MIM601482. gene.
neXtProtNX_Q01658.
PharmGKBPA27475.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5150.
HOGENOMHOG000178641.
HOVERGENHBG002051.
InParanoidQ01658.
OMAACDHITK.
OrthoDBEOG7T4MMT.
PhylomeDBQ01658.
TreeFamTF317588.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.

Gene expression databases

ArrayExpressQ01658.
BgeeQ01658.
CleanExHS_DR1.
GenevestigatorQ01658.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR003958. CBFA_NFYB_domain.
IPR009072. Histone-fold.
[Graphical view]
PfamPF00808. CBFD_NFYB_HMF. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ01658.
GeneWikiDR1_(gene).
GenomeRNAi1810.
NextBio7377.
PROQ01658.
SOURCESearch...

Entry information

Entry nameNC2B_HUMAN
AccessionPrimary (citable) accession number: Q01658
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: July 9, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM