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Protein

Dr1-associated corepressor

Gene

DRAP1

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

GO - Molecular functioni

  • DNA binding Source: ProtInc
  • transcription corepressor activity Source: ProtInc
  • transcription factor activity, sequence-specific DNA binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-1181150. Signaling by NODAL.
R-HSA-1502540. Signaling by Activin.

Names & Taxonomyi

Protein namesi
Recommended name:
Dr1-associated corepressor
Alternative name(s):
Dr1-associated protein 1
Negative cofactor 2-alpha
Short name:
NC2-alpha
Gene namesi
Name:DRAP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:3019. DRAP1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27476.

Polymorphism and mutation databases

BioMutaiDRAP1.
DMDMi56404465.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 205204Dr1-associated corepressorPRO_0000080001Add
BLAST

Post-translational modificationi

Phosphorylation reduces DNA binding, but has no effect on heterodimerization and TBP binding.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ14919.
MaxQBiQ14919.
PaxDbiQ14919.
PRIDEiQ14919.

PTM databases

iPTMnetiQ14919.
PhosphoSiteiQ14919.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in adult testis, heart, skeletal muscle, pancreas and brain, and in fetal brain, liver and kidney.2 Publications

Gene expression databases

BgeeiQ14919.
CleanExiHS_DRAP1.
ExpressionAtlasiQ14919. baseline and differential.
GenevisibleiQ14919. HS.

Organism-specific databases

HPAiHPA006790.

Interactioni

Subunit structurei

Heterodimer with DR1. Binds BTAF1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
GTF2BQ004033EBI-712941,EBI-389564
LMO2P257913EBI-712941,EBI-739696
NCK2O436393EBI-712941,EBI-713635
NFYBP252084EBI-712941,EBI-389728
POLE3Q9NRF94EBI-712941,EBI-744901
TAF9Q165946EBI-712941,EBI-712521
TAF9BQ9HBM64EBI-712941,EBI-751601

Protein-protein interaction databases

BioGridi115838. 31 interactions.
IntActiQ14919. 22 interactions.
MINTiMINT-1421885.
STRINGi9606.ENSP00000307850.

Structurei

Secondary structure

1
205
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 218Combined sources
Helixi34 – 5825Combined sources
Helixi67 – 715Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JFIX-ray2.62A1-77[»]
ProteinModelPortaliQ14919.
SMRiQ14919. Positions 10-75.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14919.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 7764Histone-foldAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 74Poly-Lys
Compositional biasi158 – 19538Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the NC2 alpha/DRAP1 family.Curated
Contains 1 histone-fold domain.Curated

Phylogenomic databases

eggNOGiKOG1659. Eukaryota.
COG5247. LUCA.
GeneTreeiENSGT00390000012424.
HOGENOMiHOG000113741.
HOVERGENiHBG051403.
InParanoidiQ14919.
OrthoDBiEOG7FBRJ0.
PhylomeDBiQ14919.
TreeFamiTF313964.

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.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14919-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPSKKKKYNA RFPPARIKKI MQTDEEIGKV AAAVPVIISR ALELFLESLL
60 70 80 90 100
KKACQVTQSR NAKTMTTSHL KQCIELEQQF DFLKDLVASV PDMQGDGEDN
110 120 130 140 150
HMDGDKGARR GRKPGSGGRK NGGMGTKSKD KKLSGTDSEQ EDESEDTDTD
160 170 180 190 200
GEEETSQPPP QASHPSAHFQ SPPTPFLPFA STLPLPPAPP GPSAPDEEDE

EDYDS
Length:205
Mass (Da):22,350
Last modified:January 23, 2007 - v3
Checksum:i6154C43C6B8DC877
GO
Isoform 2 (identifier: Q14919-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     111-111: G → WTVPSQR

Show »
Length:211
Mass (Da):23,148
Checksum:iBAB6A4427D03B299
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 1514PSKKK…RFPPA → EF AA sequence (PubMed:8608938).CuratedAdd
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei111 – 1111G → WTVPSQR in isoform 2. 1 PublicationVSP_012215

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X96506 mRNA. Translation: CAA65358.1.
U41843 mRNA. Translation: AAB02192.1.
BC010025 mRNA. Translation: AAH10025.1.
CCDSiCCDS8123.1. [Q14919-1]
PIRiS70618.
RefSeqiNP_006433.2. NM_006442.3. [Q14919-1]
UniGeneiHs.356742.

Genome annotation databases

EnsembliENST00000312515; ENSP00000307850; ENSG00000175550. [Q14919-1]
GeneIDi10589.
KEGGihsa:10589.
UCSCiuc001ogj.3. human. [Q14919-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X96506 mRNA. Translation: CAA65358.1.
U41843 mRNA. Translation: AAB02192.1.
BC010025 mRNA. Translation: AAH10025.1.
CCDSiCCDS8123.1. [Q14919-1]
PIRiS70618.
RefSeqiNP_006433.2. NM_006442.3. [Q14919-1]
UniGeneiHs.356742.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JFIX-ray2.62A1-77[»]
ProteinModelPortaliQ14919.
SMRiQ14919. Positions 10-75.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115838. 31 interactions.
IntActiQ14919. 22 interactions.
MINTiMINT-1421885.
STRINGi9606.ENSP00000307850.

PTM databases

iPTMnetiQ14919.
PhosphoSiteiQ14919.

Polymorphism and mutation databases

BioMutaiDRAP1.
DMDMi56404465.

Proteomic databases

EPDiQ14919.
MaxQBiQ14919.
PaxDbiQ14919.
PRIDEiQ14919.

Protocols and materials databases

DNASUi10589.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312515; ENSP00000307850; ENSG00000175550. [Q14919-1]
GeneIDi10589.
KEGGihsa:10589.
UCSCiuc001ogj.3. human. [Q14919-1]

Organism-specific databases

CTDi10589.
GeneCardsiDRAP1.
HGNCiHGNC:3019. DRAP1.
HPAiHPA006790.
MIMi602289. gene.
neXtProtiNX_Q14919.
PharmGKBiPA27476.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1659. Eukaryota.
COG5247. LUCA.
GeneTreeiENSGT00390000012424.
HOGENOMiHOG000113741.
HOVERGENiHBG051403.
InParanoidiQ14919.
OrthoDBiEOG7FBRJ0.
PhylomeDBiQ14919.
TreeFamiTF313964.

Enzyme and pathway databases

ReactomeiR-HSA-1181150. Signaling by NODAL.
R-HSA-1502540. Signaling by Activin.

Miscellaneous databases

ChiTaRSiDRAP1. human.
EvolutionaryTraceiQ14919.
GeneWikiiDRAP1.
GenomeRNAii10589.
PROiQ14919.
SOURCEiSearch...

Gene expression databases

BgeeiQ14919.
CleanExiHS_DRAP1.
ExpressionAtlasiQ14919. baseline and differential.
GenevisibleiQ14919. HS.

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

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 2-31, FUNCTION, PHOSPHORYLATION, INTERACTION WITH DR1, TISSUE SPECIFICITY.
    Tissue: B-cell.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 20-26; 30-39 AND 72-91, FUNCTION, INTERACTION WITH DR1, PHOSPHORYLATION, TISSUE SPECIFICITY.
    Tissue: Cervix carcinoma.
  3. "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] (ISOFORM 1).
    Tissue: Muscle.
  4. "NC2alpha interacts with BTAF1 and stimulates its ATP-dependent association with TATA-binding protein."
    Klejman M.P., Pereira L.A., van Zeeburg H.J.T., Gilfillan S., Meisterernst M., Timmers H.T.M.
    Mol. Cell. Biol. 24:10072-10082(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BTAF1.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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) OF 1-77 IN COMPLEX WITH DR1; TBP AND DNA.

Entry informationi

Entry nameiNC2A_HUMAN
AccessioniPrimary (citable) accession number: Q14919
Secondary accession number(s): Q13448
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 135 of the entry and version 3 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 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.