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Q01658

- NC2B_HUMAN

UniProt

Q01658 - NC2B_HUMAN

Protein

Protein Dr1

Gene

DR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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. protein binding Source: BHF-UCL
    3. sequence-specific DNA binding Source: InterPro
    4. TBP-class protein binding Source: BHF-UCL
    5. transcription corepressor activity Source: ProtInc
    6. 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

    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

    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

    ArrayExpressiQ01658.
    BgeeiQ01658.
    CleanExiHS_DR1.
    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. 33 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 – 2511
    Helixi33 – 6028
    Beta strandi64 – 663
    Helixi68 – 7811
    Helixi81 – 833
    Helixi84 – 11027
    Beta strandi111 – 1133
    Helixi115 – 14026

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MASSSGNDDD LTIPRAAINK MIKETLPNVR VANDARELVV NCCTEFIHLI    50
    SSEANEICNK SEKKTISPEH VIQALESLGF GSYISEVKEV LQECKTVALK 100
    RRKASSRLEN LGIPEEELLR QQQELFAKAR QQQAELAQQE WLQMQQAAQQ 150
    AQLAAASASA SNQAGSSQDE EDDDDI 176
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 33 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

    ArrayExpressi Q01658.
    Bgeei Q01658.
    CleanExi HS_DR1.
    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

    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: October 1, 2014
    This is version 136 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