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0NCOA3_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameNCOA3
DescriptionNuclear receptor coactivator 3 (ec 2.3.1.48) (ncoa-3) (thyroid hormone receptor activator molecule 1) (tram-1) (actr) (receptor-associated coactivator 3) (rac-3) (amplified in breast cancer-1 protein) (aib-1) (steroid receptor coactivator protein 3) (src-3) (cbp-interacting protein) (pcip).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005634 nucleus (NAS)
0050681 androgen receptor binding (NAS)
0004402 histone acetyltransferase activity (TAS)
0005515 protein binding (IPI)
0046966 thyroid hormone receptor binding (NAS)
0003713 transcription coactivator activity (NAS)
0030521 androgen receptor signaling pathway (NAS)
0045893 positive regulation of transcription, DNA-d... (NAS)
0006350 transcription (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This domain.hich is usually found tandemly repeated.s found various receptor co-activating proteins.
  IPR010011:Protein of unknown function DUF1518
PAS domains are involved in many signalling proteins where theyare used as a signal sensor domain. PAS domains appear in archaea.acteria and eukaryotes. Several PAS-domain proteins are known todetect their signal by way of an associated cofactor. Haeme.lavin.nd a 4-hydroxycinnamyl chromophore are used in differentproteins. The PAS domain was named after three proteins that itoccurs in: Per- period circadian proteinArnt- Ah receptor nuclear translocator proteinSim- single-minded protein.PAS domains are often associated withPAC domains . It appears that these domains are directly linked.nd that together they form the conserved 3D PAS fold. The division between the PAS and PAC domains is caused by major differences in sequences in the region connecting these two motifs . In human PAS kinase.his region has been shown to be very flexible.nd adopts different conformations depending on the bound ligand .Probably the most surprising identification of a PAS domain was that inEAG-like K+-channels .
  IPR000014:PAS
PAS domains are involved in many signalling proteins where theyare used as a signal sensor domain. PAS domains appear in archaea.acteria and eukaryotes. Several PAS-domain proteins are known todetect their signal by way of an associated cofactor. Haeme.lavin.nd a 4-hydroxycinnamyl chromophore are used in differentproteins. The PAS domain was named after three proteins that itoccurs in: Per- period circadian proteinArnt- Ah receptor nuclear translocator proteinSim- single-minded protein.PAS domains are often associated withPAC domains . It appears that these domains are directly linked.nd that together they form the conserved 3D PAS fold. The division between the PAS and PAC domains is caused by major differences in sequences in the region connecting these two motifs . In human PAS kinase.his region has been shown to be very flexible.nd adopts different conformations depending on the bound ligand .Probably the most surprising identification of a PAS domain was that inEAG-like K+-channels .
  IPR013767:PAS fold
Basic helix-loop-helix proteins (bHLH) are a group of eukaryotic transcription factors that exert a determinative influence in a variety of developmental pathways. These transcription factors are characterised by a highly evolutionary conserved bHLH domain that mediates specific dimerisation . They facilitate the conversion of inactive monomers to trans-activating dimers at appropriate stages of development . The bHLH proteins can be classified into discrete categories. One such subdivision according to dimerisation.NA binding and expression characteristics defines seven groups . Class I proteins form dimers within the group or with class II proteins. Class II can only form heterodimers with class I factors. Class III factors are characterised by the presence of a leucine zipper () adjacent to the bHLH domain. Class IV factors may form homodimers or teterodimers with class III proteins. Class V and class VI proteins act as regulators of class I and class II factors and class VII proteins have a PAS domain ().
  IPR001092:Basic helix-loop-helix dimerisation region bHLH
Coactivators are molecules that have recently been found to be important components of the transactivation activity of steroid hormone receptors. The coactivators were originally defined as factors that increase the total amount of induced gene product with saturating.r pharmacological.oncentrations of hormone. For the p160 Src-1 coactivator this action is thought to involve domains with intrinsic transactivation activity.alled activation domains. Their intrinsic transactivation activity may be related to their histone acetyltransferase (HAT) activity. The ability of coactivators to augment the total amount of induced gene transcripts requires coactivator binding to the agonist-bound receptors and may result from more efficient binding/recruitment of transcription complex core factors. The COOH-terminal active segment of SRC-1 is devoid of activation domains but does contain a HAT activity domain and a receptor interaction domain. This segment also displays a dominant negative repressor activity.hich appears to be due simply to its ability to bind tightly to the receptor ligand binding domain.hereby blocking the binding of other coactivators .
  IPR008955:Nuclear receptor coactivator Src-1
The helix-loop-helix (HLH) DNA-binding domain consists of a closed bundleof four helices in a left-handed twist with two crossover connections. TheHLH domain directs dimerisation.nd is juxtaposed to basic regions tocreate a DNA interaction interface surface that recognises specific DNAsequences. Basic region/HLH (bHLH) proteins regulate diverse biologicalpathways . bHLH proteins include MyoD .REBPs (sterol regulatory element binding proteins).nd yeast Pho4 (phosphatase system) .In certain proteins the bHLH domain contains a leucine-zipper motif. ThebHLH/leucine zipper (bHLHZip) domain specifies dimerisation within a networkof proteins and determines sequence-specific DNA binding . bHLHZip domains occur in the transcription factors Myc.ad.ax and Usf . This entry is bHLHZip.hich covers the bHLH domain and the leucine zipper motif.hen present.
  IPR011598:Helix-loop-helix DNA-binding
IPR010011:DUF1518 
Evalue:-29.6197891235352 
Location:1291-1348IPR000014:PAS 
Evalue:-11.4089353929735 
Location:112-178IPR001092:HLH 
Evalue:-9.06048074738138 
Location:31-88IPR008955:Src1_receptcoact 
Evalue:0 
Location:616-699
SequencesProtein: NCOA3_HUMAN (1424 aa)
mRNA: BC092516 NM_006534 NM_181659
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
A process that increases long-term neuronal synaptic plasticity, the ability of neuronal synapses to change long-term as circumstances require. Long-term neuronal synaptic plasticity generally involves increase or decrease in actual synapse numbers.
sdb:0039 positive regulation of long-term neuronal synaptic plasticity  (Evidence:keywords)
calcium-regulated transcription factor
sdb:0215 calcium-regulated transcription factor  (Evidence:keywords)
KO assignmentK00653
  Level 3 annotation:
    histone acetyltransferase
  Level 2 annotation:
    Other enzymes
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 40 residues, 45564052-45564170Exon2: 28 residues, 45645333-45645412Exon3: 36 residues, 45684379-45684481Exon4: 59 residues, 45686061-45686234Exon5: 35 residues, 45687531-45687632Exon6: 60 residues, 45689152-45689327Exon7: 65 residues, 45689711-45689900Exon8: 36 residues, 45690072-45690174Exon9: 49 residues, 45695646-45695787Exon10: 51 residues, 45696198-45696346Exon11: 132 residues, 45697472-45697864Exon12: 292 residues, 45698041-45698913Exon13: 47 residues, 45699798-45699934Exon14: 67 residues, 45701158-45701353Exon15: 84 residues, 45701727-45701973Exon16: 44 residues, 45702075-45702202Exon17: 59 residues, 45704363-45704535Exon18: 100 residues, 45709223-45709517Exon19: 37 residues, 45711155-45711260Exon20: 99 residues, 45713135-45713427Exon21: 60 residues, 45714556-45714731Exon22: 49 residues, 45715081-45715223Exon23: 105 residues, 45715556-45715866Exon24: 2 residues, -Jump to NCOA3_HUMANExon1: 36 residues, 45564063-45564170Exon2: 28 residues, 45645333-45645412Exon3: 36 residues, 45684379-45684481Exon4: 59 residues, 45686061-45686234Exon5: 35 residues, 45687531-45687632Exon6: 60 residues, 45689152-45689327Exon7: 65 residues, 45689711-45689900Exon8: 36 residues, 45690072-45690174Exon9: 49 residues, 45695646-45695787Exon10: 51 residues, 45696198-45696346Exon11: 132 residues, 45697472-45697864Exon12: 292 residues, 45698041-45698913Exon13: 47 residues, 45699798-45699934Exon14: 67 residues, 45701158-45701353Exon15: 84 residues, 45701727-45701973Exon16: 44 residues, 45702075-45702202Exon17: 59 residues, 45704363-45704535Exon18: 100 residues, 45709223-45709517Exon19: 33 residues, 45711155-45711248Exon20: 100 residues, 45713132-45713427Exon21: 60 residues, 45714556-45714731Exon22: 49 residues, 45715081-45715223Exon23: 1156 residues, 45715556-45719019Exon24: 2 residues, -Jump to NCOA3_HUMANExon1: 36 residues, 45564063-45564170Exon2: 28 residues, 45645333-45645412Exon3: 36 residues, 45684379-45684481Exon4: 59 residues, 45686061-45686234Exon5: 35 residues, 45687531-45687632Exon6: 60 residues, 45689152-45689327Exon7: 65 residues, 45689711-45689900Exon8: 36 residues, 45690072-45690174Exon9: 49 residues, 45695646-45695787Exon10: 51 residues, 45696198-45696346Exon11: 132 residues, 45697472-45697864Exon12: 292 residues, 45698041-45698913Exon13: 47 residues, 45699798-45699934Exon14: 67 residues, 45701158-45701353Exon15: 84 residues, 45701727-45701973Exon16: 44 residues, 45702075-45702202Exon17: 59 residues, 45704363-45704535Exon18: 100 residues, 45709223-45709517Exon19: 37 residues, 45711155-45711260Exon20: 100 residues, 45713132-45713427Exon21: 60 residues, 45714556-45714731Exon22: 49 residues, 45715081-45715223Exon23: 1156 residues, 45715556-45719019Exon24: 2 residues, -Jump to NCOA3_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4526 45271787-45418881 ~-147K 23268(PRKCBP1)(-)Loci: 3263 45564052-45719019 ~-155K 23291(NCOA3)(+)Loci: 3262 45040280-45250897 ~-211K 23265(EYA2)(+)Link out to UCSC