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Protein

Dr1-associated corepressor

Gene

Drap1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • transcription corepressor activity Source: MGI
  • transcription factor binding Source: MGI

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-MMU-1181150. Signaling by NODAL.
R-MMU-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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1913806. Drap1.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 205204Dr1-associated corepressorPRO_0000080002Add
BLAST

Post-translational modificationi

Phosphorylation reduces DNA binding, but has no effect on heterodimerization and TBP binding.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9D6N5.
MaxQBiQ9D6N5.
PaxDbiQ9D6N5.
PRIDEiQ9D6N5.

PTM databases

iPTMnetiQ9D6N5.
PhosphoSiteiQ9D6N5.

Expressioni

Gene expression databases

BgeeiQ9D6N5.
ExpressionAtlasiQ9D6N5. baseline and differential.
GenevisibleiQ9D6N5. MM.

Interactioni

Subunit structurei

Heterodimer with DR1. Binds BTAF1 (By similarity).By similarity

GO - Molecular functioni

  • transcription factor binding Source: MGI

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025853.

Structurei

3D structure databases

ProteinModelPortaliQ9D6N5.
SMRiQ9D6N5. Positions 10-75.
ModBaseiSearch...
MobiDBiSearch...

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 biasi156 – 19237Pro-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.
InParanoidiQ9D6N5.
PhylomeDBiQ9D6N5.
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.

Sequencei

Sequence statusi: Complete.

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

Q9D6N5-1 [UniParc]FASTAAdd to basket

« 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
HVDGDKGPRR GRKPGSSGRK NGGTGSKGKD KKLSGTDSEQ EDESEDTDTD
160 170 180 190 200
GEEETPQLPP QASHPPAHFQ SPPTPFIPFT SPLPLPPAPP GPSAADAEDE

EDYDS
Length:205
Mass (Da):22,278
Last modified:January 23, 2007 - v3
Checksum:i59CB729FFD7CB7CE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010152 mRNA. Translation: BAB26737.1.
AK087456 mRNA. Translation: BAC39882.1.
BC002090 mRNA. Translation: AAH02090.1.
CCDSiCCDS29462.1.
RefSeqiNP_001278009.1. NM_001291080.1.
NP_077138.1. NM_024176.2.
UniGeneiMm.275446.

Genome annotation databases

EnsembliENSMUST00000025853; ENSMUSP00000025853; ENSMUSG00000024914.
GeneIDi66556.
KEGGimmu:66556.
UCSCiuc008gcy.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010152 mRNA. Translation: BAB26737.1.
AK087456 mRNA. Translation: BAC39882.1.
BC002090 mRNA. Translation: AAH02090.1.
CCDSiCCDS29462.1.
RefSeqiNP_001278009.1. NM_001291080.1.
NP_077138.1. NM_024176.2.
UniGeneiMm.275446.

3D structure databases

ProteinModelPortaliQ9D6N5.
SMRiQ9D6N5. Positions 10-75.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025853.

PTM databases

iPTMnetiQ9D6N5.
PhosphoSiteiQ9D6N5.

Proteomic databases

EPDiQ9D6N5.
MaxQBiQ9D6N5.
PaxDbiQ9D6N5.
PRIDEiQ9D6N5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025853; ENSMUSP00000025853; ENSMUSG00000024914.
GeneIDi66556.
KEGGimmu:66556.
UCSCiuc008gcy.2. mouse.

Organism-specific databases

CTDi10589.
MGIiMGI:1913806. Drap1.

Phylogenomic databases

eggNOGiKOG1659. Eukaryota.
COG5247. LUCA.
GeneTreeiENSGT00390000012424.
HOGENOMiHOG000113741.
HOVERGENiHBG051403.
InParanoidiQ9D6N5.
PhylomeDBiQ9D6N5.
TreeFamiTF313964.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi322002.
PROiQ9D6N5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D6N5.
ExpressionAtlasiQ9D6N5. baseline and differential.
GenevisibleiQ9D6N5. MM.

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

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Eye and Tongue.
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Lung, Spleen and Testis.

Entry informationi

Entry nameiNC2A_MOUSE
AccessioniPrimary (citable) accession number: Q9D6N5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.