Human Gene NTAN1 (ENST00000287706.8) from GENCODE V44
  Description: Homo sapiens N-terminal asparagine amidase (NTAN1), transcript variant 1, mRNA. (from RefSeq NM_173474)
RefSeq Summary (NM_173474): The protein encoded by this gene functions in a step-wise process of protein degradation through the N-end rule pathway. This protein acts as a tertiary destabilizing enzyme that deamidates N-terminal L-Asn residues on proteins to produce N-terminal L-Asp. L-Asp substrates are subsequently conjugated to L-Arg, which is recognized by specific E3 ubiquitin ligases and targeted to the proteasome. Pseudogenes of this gene are located on the long arms of chromosomes 8, 10 and 12. Alternative splicing results in multiple transcript variants that encode different protein isoforms. [provided by RefSeq, Jul 2012].
Gencode Transcript: ENST00000287706.8
Gencode Gene: ENSG00000157045.9
Transcript (Including UTRs)
   Position: hg38 chr16:15,037,857-15,056,074 Size: 18,218 Total Exon Count: 10 Strand: -
Coding Region
   Position: hg38 chr16:15,038,031-15,055,971 Size: 17,941 Coding Exon Count: 10 

Page IndexSequence and LinksUniProtKB CommentsPrimersMalaCardsCTD
RNA-Seq ExpressionMicroarray ExpressionRNA StructureProtein StructureOther SpeciesGO Annotations
mRNA DescriptionsPathwaysOther NamesMethods
Data last updated at UCSC: 2023-08-18 00:09:47

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chr16:15,037,857-15,056,074)mRNA (may differ from genome)Protein (310 aa)
Gene SorterGenome BrowserOther Species FASTAGene interactionsTable SchemaAlphaFold
BioGPSEnsemblEntrez GeneExonPrimerGencodeGeneCards
HGNCHPRDLynxMalacardsMGIneXtProt
OMIMPubMedUniProtKBBioGrid CRISPR DB

-  Comments and Description Text from UniProtKB
  ID: NTAN1_HUMAN
DESCRIPTION: RecName: Full=Protein N-terminal asparagine amidohydrolase; EC=3.5.1.-; AltName: Full=Protein NH2-terminal asparagine amidohydrolase; Short=PNAA; AltName: Full=Protein NH2-terminal asparagine deamidase; Short=PNAD; Short=Protein N-terminal Asn amidase; Short=Protein NTN-amidase;
FUNCTION: Side-chain deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N- terminal asparagine to aspartate by PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position (By similarity).
SUBUNIT: Monomer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).

-  Primer design for this transcript
 

Primer3Plus can design qPCR Primers that straddle exon-exon-junctions, which amplify only cDNA, not genomic DNA.
Click here to load the transcript sequence and exon structure into Primer3Plus

Exonprimer can design one pair of Sanger sequencing primers around every exon, located in non-genic sequence.
Click here to open Exonprimer with this transcript

To design primers for a non-coding sequence, zoom to a region of interest and select from the drop-down menu: View > In External Tools > Primer3


-  MalaCards Disease Associations
  MalaCards Gene Search: NTAN1
Diseases sorted by gene-association score: tendinitis (5)

-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene           more ... click here to view the complete list

-  RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)
  Highest median expression: 39.33 RPKM in Cervix - Endocervix
Total median expression: 1071.86 RPKM



View in GTEx track of Genome Browser    View at GTEx portal     View GTEx Body Map

+  Microarray Expression Data
  Press "+" in the title bar above to open this section.

-  mRNA Secondary Structure of 3' and 5' UTRs
 
RegionFold EnergyBasesEnergy/Base
Display As
5' UTR -72.70103-0.706 Picture PostScript Text
3' UTR -36.50174-0.210 Picture PostScript Text

The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR026750 - NTAN1

ModBase Predicted Comparative 3D Structure on Q96AB6
FrontTopSide
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
Genome BrowserGenome BrowserNo orthologNo orthologNo orthologNo ortholog
Gene Details     
Gene Sorter     
MGIRGD    
Protein SequenceProtein Sequence    
AlignmentAlignment    

-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0008418 protein-N-terminal asparagine amidohydrolase activity
GO:0016787 hydrolase activity

Biological Process:
GO:0006511 ubiquitin-dependent protein catabolic process
GO:0007613 memory
GO:0008344 adult locomotory behavior

Cellular Component:
GO:0005634 nucleus
GO:0005737 cytoplasm


-  Descriptions from all associated GenBank mRNAs
  AL833023 - Homo sapiens mRNA; cDNA DKFZp666E058 (from clone DKFZp666E058).
AF092440 - Homo sapiens N-terminal asparagine amidohydrolase mRNA, complete cds.
AK092915 - Homo sapiens cDNA FLJ35596 fis, clone SPLEN2008135, moderately similar to PROTEIN N-TERMINAL ASPARAGINE AMIDOHYDROLASE (EC 3.5.1.-).
BC017336 - Homo sapiens N-terminal asparagine amidase, mRNA (cDNA clone MGC:29626 IMAGE:4872717), complete cds.
AK300557 - Homo sapiens cDNA FLJ54159 complete cds, highly similar to Protein N-terminal asparagine amidohydrolase (EC 3.5.1.-).
JD109312 - Sequence 90336 from Patent EP1572962.
JD528202 - Sequence 509226 from Patent EP1572962.
JD113932 - Sequence 94956 from Patent EP1572962.
JD320509 - Sequence 301533 from Patent EP1572962.
KJ895381 - Synthetic construct Homo sapiens clone ccsbBroadEn_04775 NTAN1 gene, encodes complete protein.
CU675948 - Synthetic construct Homo sapiens gateway clone IMAGE:100018104 5' read NTAN1 mRNA.
HQ447215 - Synthetic construct Homo sapiens clone IMAGE:100070516; CCSB007824_01 N-terminal asparagine amidase (NTAN1) gene, encodes complete protein.
JD330219 - Sequence 311243 from Patent EP1572962.
JD021413 - Sequence 2437 from Patent EP1572962.
JD035288 - Sequence 16312 from Patent EP1572962.

-  Biochemical and Signaling Pathways
  BioCyc Knowledge Library
PWY-7799 - Arg/N-end rule pathway (eukaryotic)

-  Other Names for This Gene
  Alternate Gene Symbols: ENST00000287706.1, ENST00000287706.2, ENST00000287706.3, ENST00000287706.4, ENST00000287706.5, ENST00000287706.6, ENST00000287706.7, NM_173474, NTAN1_HUMAN, Q96AB6, uc002ddd.1, uc002ddd.2, uc002ddd.3, uc002ddd.4, uc002ddd.5, uc002ddd.6
UCSC ID: ENST00000287706.8
RefSeq Accession: NM_173474
Protein: Q96AB6 (aka NTAN1_HUMAN)
CCDS: CCDS10558.1

-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.