Q01658 (NC2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

DR1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	176 AA.
Sequence status	Complete.
Protein existence	Evidence 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.8
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.8
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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding
Molecular function	Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	histone H3 acetylation Inferred from direct assay PubMed 18838386. Source: BHF-UCL negative regulation of transcription from RNA polymerase II promoter Traceable author statement Ref.5. Source: ProtInc transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Ada2/Gcn5/Ada3 transcription activator complex Inferred from direct assay PubMed 18838386. Source: BHF-UCL
Molecular_function	DNA binding Traceable author statement Ref.5. Source: ProtInc TBP-class protein binding Inferred from direct assay PubMed 18838386. Source: BHF-UCL sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro transcription corepressor activity Traceable author statement Ref.5. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 176

176

Protein Dr1

PRO_0000072440

Regions

Motif

100 – 103

4

Nuclear localization signal Potential

Compositional bias

121 – 168

48

Ala/Gln-rich

Amino acid modifications

Modified residue

166

1

Phosphoserine Ref.7

Modified residue

167

1

Phosphoserine Ref.7

Natural variations

Natural variant

171

1

E → D.
Corresponds to variant rs3088371 [ dbSNP | Ensembl ].

VAR_034506

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

176

Helix Strand Turn

Details...

Helix

15 – 25

11

Helix

33 – 60

28

Beta strand

64 – 66

3

Helix

68 – 78

11

Helix

81 – 83

3

Helix

84 – 110

27

Beta strand

111 – 113

3

Helix

115 – 140

26

Sequences

	Sequence		Length	Mass (Da)
	Q01658 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 36E7E59F2FD6CAB5	FASTA	176	19,444
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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.
[9]	"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.
[10]	"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].
[11]	"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].
[12]	"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.

IPI

IPI00008991.

PIR

A43320.

RefSeq

NP_001929.1. NM_001938.2.

UniGene

Hs.348418.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JFI	X-ray	2.62	B	1-176	[»]

ProteinModelPortal

Q01658.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q01658. 4 interactions.

MINT

MINT-204839.

STRING

9606.ENSP00000359290.

PTM databases

PhosphoSite

Q01658.

Polymorphism databases

DMDM

401162.

Proteomic databases

PaxDb

Q01658.

PeptideAtlas

Q01658.

PRIDE

Q01658.

Protocols and materials databases

DNASU

1810.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000370267; ENSP00000359290; ENSG00000117505.
ENST00000370272; ENSP00000359295; ENSG00000117505.

GeneID

1810.

KEGG

hsa:1810.

UCSC

uc001dpu.3. human.

Organism-specific databases

CTD

1810.

GeneCards

GC01P093811.

HGNC

HGNC:3017. DR1.

HPA

HPA050785.
HPA055308.

MIM

601482. gene.

neXtProt

NX_Q01658.

PharmGKB

PA27475.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5150.

HOGENOM

HOG000178641.

HOVERGEN

HBG002051.

InParanoid

Q01658.

OMA

NKKTINA.

OrthoDB

EOG4WM4W5.

PhylomeDB

Q01658.

Gene expression databases

ArrayExpress

Q01658.

Bgee

Q01658.

CleanEx

HS_DR1.

Genevestigator

Q01658.

GermOnline

ENSG00000117505. Homo sapiens.

Family and domain databases

Gene3D

1.10.20.10. 1 hit.

InterPro

IPR003958. CBFA_NFYB_domain.
IPR027113. Dr1/Ncb2.
IPR009072. Histone-fold.
IPR003957. Transcrpt_fac_CBFA/NFYB_topo.
[Graphical view]

PANTHER

PTHR11064:SF8. PTHR11064:SF8. 1 hit.

Pfam

PF00808. CBFD_NFYB_HMF. 1 hit.
[Graphical view]

PRINTS

PR00615. CCAATSUBUNTA.

SUPFAM

SSF47113. Histone-fold. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q01658.

GenomeRNAi

1810.

NextBio

7377.

SOURCE

Search...

Entry information

Entry name

NC2B_HUMAN

Accession

Primary (citable) accession number: Q01658

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	May 1, 2013
This is version 124 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.