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0NARG1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameNARG1
DescriptionNmda receptor regulated protein 1 (n-terminal acetyltransferase) (tubedown-1 protein) (tbdn100) (gastric cancer antigen ga19).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005737 cytoplasm (IDA)
0005634 nucleus (IDA)
0005667 transcription factor complex (IDA)
0005515 protein binding (IPI)
0006474 N-terminal protein amino acid acetylation (IDA)
0045893 positive regulation of transcription, DNA-d... (IDA)

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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 Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by . See: .
  IPR013105:Tetratricopeptide TPR_2
The tetratrico peptide repeat (TPR) is a structural motif present in a wide range of proteins . It mediates proteinprotein interactions and the assembly of multiprotein complexes . The TPR motif consists of 316 tandem-repeats of 34 amino acids residues.lthough individual TPR motifs can be dispersed in the protein sequence. Sequence alignment of the TPR domains reveals a consensus sequence defined by a pattern of small and large amino acids. TPR motifs have been identified in various different organisms.anging from bacteria to humans. Proteins containing TPRs are involved in a variety of biological processes.uch as cell cycle regulation.ranscriptional control.itochondrial and peroxisomal protein transport.eurogenesis and protein folding. The X-ray structure of a domain containing three TPRs from protein phosphatase 5 revealed that TPR adopts a helixturnhelix arrangement.ith adjacent TPR motifs packing in a parallel fashion.esulting in a spiral of repeating anti-parallel alpha-helices . The two helices are denoted helix A and helix B. The packing angle between helix A and helix B is ~24° within a single TPR and generates a right-handed superhelical shape. Helix A interacts with helix B and with helix A of the next TPR. Two protein surfaces are generated: the inner concave surface is contributed to mainly by residue on helices A.nd the other surface presents residues from both helices A and B.
  IPR001440:Tetratricopeptide TPR_1
The Factor for Inversion Stimulation (FIS) protein is a regulator of bacterial functions.nd binds specifically to weakly related DNA sequences . It activates ribosomal RNA transcription.nd is involved in upstream activation of rRNA promoters. The protein has been shown to play a role in the regulation of virulence factors in both Salmonella typhimurium and Escherichia coli . Some of its functions include inhibition of the initiation of DNA replication from the OriC site.nd promotion of Hin-mediated DNA inversion. In its C-terminal extremity.IS encodes a helix-turn-helix (HTH) DNA- binding motif.hich shares a high degree of similarity with other HTH motifs of more primitive bacterial transcriptional regulators.uch as the nitrogen assimilation regulatory proteins (NtrC) from species like Azobacter.hodobacter and Rhizobium. This has led to speculation that both evolved from a single common ancestor .The 3-dimensional structure of the E. coli FIS DNA-binding protein has been determined by means of X-ray diffraction to 2.0A resolution . FIS is composed of four alpha-helices tightly intertwined to form a globular dimer with two protruding HTH motifs. The 24 N-terminal amino acids are poorly defined.ndicating that they might act as feelers suitable for DNA or protein (invertase) recognition . Other proteins belonging to this subfamily include:Escherichia coli: atoC.ydG.trC.hlA.yrR.hizobium spp.: ntrC.ifA.ctD
  IPR002197:Helix-turn-helix, Fis-type
Protein prenyltransferases catalyze the transfer of the carbon moiety of C15 farnesyl pyrophosphate or geranylgeranyl pyrophosphate synthase to a conserved cysteine residue in a CaaX motif of protein and peptide substrates. The addition of a farnesyl group is required to anchor proteins to the cell membrane. In the 3D structure of a mammalian Ras farnesyltransferases (Ftase).oth subunits are largely composed of alpha-helices. The alpha-2 to alpha-15 helices in the alpha subunit fold into a novel helical hairpin structure.esulting in a crescent-shape domain that envelopes part of the subunit. The 12 helices of the beta-subunit form an alpha-alpha barrel. Six additional helices connect the inner core of helices and form the outside of the helical barrel. A deep cleft surrounded by hydrophobic amino acids in the centre of the barrel is proposed as the FPP-binding pocket. A single Zn2+ ion is located at the junction between the hydrophilic surface groove near the subunit interface. The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008940:Protein prenyltransferase
This domain consists of a multi-helical fold comprised of two curved layers of alpha helices arranged in a regular right-handed superhelix.here the repeats that make up this structure are arranged about a common axis . These superhelical structures present an extensive solvent-accessible surface that is well suited to binding large substrates such as proteins and nucleic acids. This topology has been found with a number of repeats and domains.ncluding the tetratricopeptide repeat (TPR) (found in kinesin light chains.NAP regulatory proteins.lathrin heavy chains and bacterial aspartyl-phosphate phosphatases).nd the pentatricopeptide repeat (PPR) (RNA-processing proteins). The TRP is likely to be an ancient repeat.ince it is found in eukaryotes.acteria and archaea.hereas the PPR repeat is found predominantly in higher plants. The superhelix formed from these repeats can bind ligands at a number of different regions.nd has the ability to acquire multiple functional roles .
  IPR011990:Tetratricopeptide-like helical
The tetratrico peptide repeat region (TPR) is a structural motif present in a wide range of proteins . It mediates proteinprotein interactions and the assembly of multiprotein complexes . The TPR motif consists of 316 tandem-repeats of 34 amino acids residues.lthough individual TPR motifs can be dispersed in the protein sequence. Sequence alignment of the TPR domains reveals a consensus sequence defined by a pattern of small and large amino acids. TPR motifs have been identified in various different organisms.anging from bacteria to humans. Proteins containing TPRs are involved in a variety of biological processes.uch as cell cycle regulation.ranscriptional control.itochondrial and peroxisomal protein transport.eurogenesis and protein folding. The X-ray structure of a domain containing three TPRs from protein phosphatase 5 revealed that TPR adopts a helixturnhelix arrangement.ith adjacent TPR motifs packing in a parallel fashion.esulting in a spiral of repeating anti-parallel alpha-helices . The two helices are denoted helix A and helix B. The packing angle between helix A and helix B is ~24° within a single TPR and generates a right-handed superhelical shape. Helix A interacts with helix B and with helix A of the next TPR. Two protein surfaces are generated: the inner concave surface is contributed to mainly by residue on helices A.nd the other surface presents residues from both helices A and B.
  IPR013026:Tetratricopeptide region
IPR013105:TPR_2 
Evalue:-3.92081880569458 
Location:80-113IPR001440:TPR_1 
Evalue:-0.408935397863388 
Location:374-407IPR008940:Prenyl_trans 
Evalue:0 
Location:654-719IPR013026:TPR 
Evalue:0 
Location:408-441IPR013026:TPR 
Evalue:0 
Location:148-181IPR013026:TPR 
Evalue:0 
Location:224-257IPR008940:Prenyl_trans 
Evalue:0 
Location:489-515IPR008940:Prenyl_trans 
Evalue:0 
Location:815-825IPR013026:TPR 
Evalue:1.79239168949825 
Location:46-79
SequencesProtein: NARG1_HUMAN (866 aa)
mRNA: NM_057175
Local Annotation
Synapse Ontology
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)
A process that increases short-term neuronal synaptic plasticity, the ability of neuronal synapses to change in the short-term as circumstances require. Short-term neuronal synaptic plasticity generally involves increasing or decreasing synaptic sensitivity.
sdb:0043 positive regulation of short-term neuronal synaptic plasticity  (Evidence:keywords)
A dendritic spine is a mushroom-shaped bud that protrudes from a dendrite and forms one half of a synapse, especially in synapses of the cortex. The dendrites of cortical neurons typically are densely covered with such spines, which enable single cells to receive input from thousands of others.
sdb:0134 dendritic spine  (Evidence:keywords)
?
sdb:0297 NMDA receptor  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 104 residues, 140442125-140442435Exon2: 30 residues, 140474777-140474862Exon3: 37 residues, 140477451-140477556Exon4: 54 residues, 140481515-140481673Exon5: 47 residues, 140483429-140483564Exon6: 53 residues, 140484789-140484943Exon7: 42 residues, 140490065-140490185Exon8: 34 residues, 140491794-140491890Exon9: 37 residues, 140492108-140492215Exon10: 26 residues, 140494629-140494702Exon11: 58 residues, 140497989-140498159Exon12: 53 residues, 140500346-140500499Exon13: 45 residues, 140501103-140501232Exon14: 73 residues, 140502327-140502541Exon15: 66 residues, 140510814-140511008Exon16: 38 residues, 140516968-140517077Exon17: 35 residues, 140519359-140519458Exon18: 51 residues, 140525435-140525582Exon19: 34 residues, 140526736-140526834Exon20: 968 residues, 140528487-140531385Exon21: 2 residues, -Jump to NARG1_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3426 140442125-140531385 ~-89K 28199(NARG1)(+)Loci: 3427 140594410-140616513 ~-22K 28200(RAB33B)(+)Loci: 3428 140806371-140844854 ~-38K 28202(MGST2)(+)Loci: 4690 140198320-140280056 ~-82K 28195(ELF2)(-)Link out to UCSC