true2003-09-262024-01-24146NTAN1_HUMANCloning 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.2003-07EMBL/GenBank/DDBJNUCLEOTIDE SEQUENCE [MRNA]The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).The MGC Project Teamdoi:10.1101/gr.25965042004Genome Res.142121-2127NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]SkinExpression and biochemical characterization of the human enzyme N-terminal asparagine amidohydrolase.Cantor J.R.Stone E.M.Georgiou G.doi:10.1021/bi101832w2011Biochemistry503025-3033FUNCTIONCATALYTIC ACTIVITYACTIVITY REGULATIONBIOPHYSICOCHEMICAL PROPERTIESREMOVAL OF INITIATOR METHIONINEMUTAGENESIS OF PRO-2 AND CYS-751.95A/B=1-3102.38A/B=1-3103.19A/B=1-3102.00A/B=1-310122121 antibodies from 20 providershumanNTAN1Low tissue specificitygeneEukaryota268112 hits in 1154 CRISPR screenshumanTbioProteinExpressed in subcutaneous adipose tissue and 100 other cell types or tissuesbaseline and differentialHSNTAN1N-TERMINAL ASPARAGINE AMIDOHYDROLASEPROTEIN N-TERMINAL ASPARAGINE AMIDOHYDROLASEN_Asn_amidohydProtein N-terminal asparagine amidohydrolase3.5.1.121Protein NH2-terminal asparagine amidohydrolasePNAAProtein NH2-terminal asparagine deamidasePNADProtein N-terminal Asn amidaseProtein N-terminal asparagine amidaseProtein NTN-amidaseNTAN1N-terminal asparagine deamidase that mediates 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 NTAN1/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.Inhibited by micromolar concentrations of copper and zinc ions.Optimum pH is 6.0-7.5.Monomer.Protein N-terminal asparagine amidohydrolase346771310Essential for catalytic activity75N283P2873-fold reduction in catalytic activity.G2Abolishes catalytic activity.ASTD6R143516222435394146485357666976828385889398110116118121127135148150152154161162165166169172176180183184186189195201209220223224227238242246253254256257259264277282284285292296302305false3MEOX22007-01-23334677f35a20e7978131175b6d5786568abe4aMPLLVEGRRVRLPQSAGDLVRAHPPLEERARLLRGQSVQQVGPQGLLYVQQRELAVTSPKDGSISILGSDDATTCHIVVLRHTGNGATCLTHCDGTDTKAEVPLIMNSIKSFSDHAQCGRLEVHLVGGFSDDRQLSQKLTHQLLSEFDRQEDDIHLVTLCVTELNDREENENHFPVIYGIAVNIKTAEIYRASFQDRGPEEQLRAARTLAGGPMISIYDAETEQLRIGPYSWTPFPHVDFWLHQDDKQILENLSTSPLAEPPHFVEHIRSTLMFLKKHPSPAHTLFSGNKALLYKKNEDGLWEKISSPGStruetruetruetruetrue