DRAP1
Dr1-associated corepressor
Also known as: NC2-alpha, NC2A_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q14919
- Gene
- DRAP1
- Ensembl
- ENSG00000175550
- Chromosome
- 11
- Canonical length
- 205 aa
- Protein class
- Predicted intracellular proteins
- Subcellular location
- Cytosol
OverviewNCBI Gene
Transcriptional repression is a general mechanism for regulating transcriptional initiation in organisms ranging from yeast to humans. Accurate initiation of transcription from eukaryotic protein-encoding genes requires the assembly of a large multiprotein complex consisting of RNA polymerase II and general transcription factors such as TFIIA, TFIIB, and TFIID. DR1 is a repressor that interacts with the TATA-binding protein (TBP) of TFIID and prevents the formation of an active transcription complex by precluding the entry of TFIIA and/or TFIIB into the preinitiation complex. The protein encoded by this gene is a corepressor of transcription that interacts with DR1 to enhance DR1-mediated repression. The interaction between this corepressor and DR1 is required for corepressor function and appears to stabilize the TBP-DR1-DNA complex. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
205 residues, UniProt reviewed canonical sequence.
>Q14919|DRAP1
1 MPSKKKKYNA RFPPARIKKI MQTDEEIGKV AAAVPVIISR ALELFLESLL KKACQVTQSR
61 NAKTMTTSHL KQCIELEQQF DFLKDLVASV PDMQGDGEDN HMDGDKGARR GRKPGSGGRK
121 NGGMGTKSKD KKLSGTDSEQ EDESEDTDTD GEEETSQPPP QASHPSAHFQ SPPTPFLPFA
181 STLPLPPAPP GPSAPDEEDE EDYDSLocalizationUniProt · AlphaFold · HPA
Whether an antibody against DRAP1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Intracellular
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.61
- Highest tissue expression
- 202 nTPM
Expression across tissuesHPA
Tissue
- testis: 202 nTPM
- skeletal muscle: 192 nTPM
- amygdala: 180 nTPM
- cerebral cortex: 178 nTPM
- cerebellum: 167 nTPM
- basal ganglia: 163 nTPM
Single-cell type
- suprabasal keratinocytes: 791 nCPM
- basal keratinocytes: 601 nCPM
- esophageal suprabasal cells: 473 nCPM
- esophageal apical cells: 426 nCPM
- hofbauer cells: 316 nCPM
- decidual stromal cells: 311 nCPM
Immune cell
- non-classical monocyte: 542 nTPM
- intermediate monocyte: 312 nTPM
- eosinophil: 291 nTPM
- NK-cell: 195 nTPM
- myeloid DC: 184 nTPM
- neutrophil: 166 nTPM
Brain region
- hypothalamus: 103 nTPM
- cerebral cortex: 102 nTPM
- white matter: 99 nTPM
- pons: 83 nTPM
- thalamus: 81 nTPM
- cerebellum: 81 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.8
- gnomAD pLI
- 0.13
- gnomAD missense Z
- 0.87
- DepMap mean gene effect
- -0.36
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
Molecular functions
- core promoter sequence-specific DNA binding
- identical protein binding
- protein heterodimerization activity
- RNA polymerase II general transcription initiation factor activity
- RNA polymerase II general transcription initiation factor binding
- TBP-class protein binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of DRAP1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads DRAP1 as an antibody target. Whether an autoantibody or antibody against DRAP1 could matter depends on whether native DRAP1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
DRAP1 is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label DRAP1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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