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Protein

Dr1-associated corepressor

Gene

DRAP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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
  • DNA binding transcription factor activity Source: ProtInc
  • identical protein binding Source: IntAct
  • protein heterodimerization activity Source: InterPro
  • RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: NTNU_SB
  • transcription corepressor activity Source: ProtInc

GO - Biological processi

  • negative regulation of transcription by RNA polymerase II Source: ProtInc
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Molecular functionDNA-binding, Repressor
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-HSA-1181150 Signaling by NODAL
R-HSA-1502540 Signaling by Activin
SIGNORiQ14919

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

EuPathDBiHostDB:ENSG00000175550.7
HGNCiHGNC:3019 DRAP1
MIMi602289 gene
neXtProtiNX_Q14919

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi10589
OpenTargetsiENSG00000175550
PharmGKBiPA27476

Polymorphism and mutation databases

BioMutaiDRAP1
DMDMi56404465

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000800012 – 205Dr1-associated corepressorAdd BLAST204

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
PeptideAtlasiQ14919
PRIDEiQ14919

PTM databases

iPTMnetiQ14919
PhosphoSitePlusiQ14919

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

BgeeiENSG00000175550
CleanExiHS_DRAP1
ExpressionAtlasiQ14919 baseline and differential
GenevisibleiQ14919 HS

Organism-specific databases

HPAiHPA006790

Interactioni

Subunit structurei

Heterodimer with DR1. Binds BTAF1.1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein heterodimerization activity Source: InterPro

Protein-protein interaction databases

BioGridi115838, 31 interactors
CORUMiQ14919
IntActiQ14919, 31 interactors
MINTiQ14919
STRINGi9606.ENSP00000307850

Structurei

Secondary structure

1205
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi14 – 21Combined sources8
Helixi34 – 58Combined sources25
Helixi67 – 71Combined sources5

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ14919

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 77Histone-foldAdd BLAST64

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi4 – 7Poly-Lys4
Compositional biasi158 – 195Pro-richAdd BLAST38

Sequence similaritiesi

Belongs to the NC2 alpha/DRAP1 family.Curated

Phylogenomic databases

eggNOGiKOG1659 Eukaryota
COG5247 LUCA
GeneTreeiENSGT00390000012424
HOGENOMiHOG000113741
HOVERGENiHBG051403
InParanoidiQ14919
KOiK21752
PhylomeDBiQ14919
TreeFamiTF313964

Family and domain databases

Gene3Di1.10.20.10, 1 hit
InterProiView protein in InterPro
IPR003958 CBFA_NFYB_domain
IPR009072 Histone-fold
PfamiView protein in Pfam
PF00808 CBFD_NFYB_HMF, 1 hit
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)DescriptionActionsGraphical viewLength
Sequence conflicti2 – 15PSKKK…RFPPA → EF AA sequence (PubMed:8608938).CuratedAdd BLAST14

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_012215111G → WTVPSQR in isoform 2. 1 Publication1

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

Similar proteinsi

Entry informationi

Entry nameiNC2A_HUMAN
AccessioniPrimary (citable) accession number: Q14919
Secondary accession number(s): Q13448
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 149 of the entry and version 3 of the sequence. See 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health