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Q96AB6 (NTAN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein N-terminal asparagine amidohydrolase

EC=3.5.1.-
Alternative name(s):
Protein NH2-terminal asparagine amidohydrolase
Short name=PNAA
Protein NH2-terminal asparagine deamidase
Short name=PNAD
Short name=Protein N-terminal Asn amidase
Short name=Protein N-terminal asparagine amidase
Short name=Protein NTN-amidase
Gene names
Name:NTAN1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length310 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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, nor on acetylated N-terminal peptidyl Asn. Ref.3

Enzyme regulation

Inhibited by micromolar concentrations of copper and zinc ions. Ref.3

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.0-7.5. Ref.3

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult locomotory behavior

Inferred from electronic annotation. Source: Ensembl

memory

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionprotein-N-terminal asparagine amidohydrolase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 310309Protein N-terminal asparagine amidohydrolase
PRO_0000057971

Sites

Site751Essential for catalytic activity

Natural variations

Natural variant2831H → N.
Corresponds to variant rs1136001 [ dbSNP | Ensembl ].
VAR_051244
Natural variant2871S → P.
Corresponds to variant rs1135999 [ dbSNP | Ensembl ].
VAR_051245

Experimental info

Mutagenesis21P → G: 3-fold reduction in catalytic activity. Ref.3
Mutagenesis751C → A, S or T: Abolishes catalytic activity. Ref.3
Sequence conflict61E → D in AAP97215. Ref.1
Sequence conflict141Q → R in AAP97215. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q96AB6 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C7FE8C550883DFC3

FASTA31034,677
        10         20         30         40         50         60 
MPLLVEGRRV RLPQSAGDLV RAHPPLEERA RLLRGQSVQQ VGPQGLLYVQ QRELAVTSPK 

        70         80         90        100        110        120 
DGSISILGSD DATTCHIVVL RHTGNGATCL THCDGTDTKA EVPLIMNSIK SFSDHAQCGR 

       130        140        150        160        170        180 
LEVHLVGGFS DDRQLSQKLT HQLLSEFDRQ EDDIHLVTLC VTELNDREEN ENHFPVIYGI 

       190        200        210        220        230        240 
AVNIKTAEIY RASFQDRGPE EQLRAARTLA GGPMISIYDA ETEQLRIGPY SWTPFPHVDF 

       250        260        270        280        290        300 
WLHQDDKQIL ENLSTSPLAE PPHFVEHIRS TLMFLKKHPS PAHTLFSGNK ALLYKKNEDG 

       310 
LWEKISSPGS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of a novel human cDNA homology to murine N-terminal asparagine amidohydrolase (Ntan1) mRNA."
Jiang C.L., Yu L., Fan Y.X., Tu Q., Jiang J.X., Zhao S.Y.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
Tissue: Skin.
[3]"Expression and biochemical characterization of the human enzyme N-terminal asparagine amidohydrolase."
Cantor J.R., Stone E.M., Georgiou G.
Biochemistry 50:3025-3033(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, REMOVAL OF INITIATOR METHIONINE, MUTAGENESIS OF PRO-2 AND CYS-75.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF092440 mRNA. Translation: AAP97215.1.
BC017336 mRNA. Translation: AAH17336.1.
CCDSCCDS10558.1.
RefSeqNP_001257695.1. NM_001270766.1.
NP_001257696.1. NM_001270767.1.
NP_775745.1. NM_173474.3.
UniGeneHs.592045.

3D structure databases

ProteinModelPortalQ96AB6.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ96AB6.

Polymorphism databases

DMDM37082118.

Proteomic databases

MaxQBQ96AB6.
PaxDbQ96AB6.
PRIDEQ96AB6.

Protocols and materials databases

DNASU123803.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000287706; ENSP00000287706; ENSG00000157045.
GeneID123803.
KEGGhsa:123803.
UCSCuc002ddd.4. human.

Organism-specific databases

CTD123803.
GeneCardsGC16M015131.
HGNCHGNC:29909. NTAN1.
HPACAB029997.
HPA051418.
MIM615367. gene.
neXtProtNX_Q96AB6.
PharmGKBPA134863573.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG76939.
HOGENOMHOG000047800.
HOVERGENHBG052674.
InParanoidQ96AB6.
KOK14662.
OMATHCDGSD.
OrthoDBEOG773XGD.
PhylomeDBQ96AB6.
TreeFamTF325597.

Gene expression databases

ArrayExpressQ96AB6.
BgeeQ96AB6.
CleanExHS_NTAN1.
GenevestigatorQ96AB6.

Family and domain databases

InterProIPR026750. NTAN1.
[Graphical view]
PANTHERPTHR12498. PTHR12498. 1 hit.
PfamPF14736. N_Asn_amidohyd. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi123803.
NextBio81157.
PROQ96AB6.
SOURCESearch...

Entry information

Entry nameNTAN1_HUMAN
AccessionPrimary (citable) accession number: Q96AB6
Secondary accession number(s): Q7Z4Z0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 83 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM