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Database: UniProt
Entry: P04424
LinkDB: P04424
Original site: P04424 
ID   ARLY_HUMAN              Reviewed;         464 AA.
AC   P04424; E7EMI0; E9PE48; Q6LDS5; Q96HS2;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   26-NOV-2014, entry version 174.
DE   RecName: Full=Argininosuccinate lyase;
DE            Short=ASAL;
DE            EC=4.3.2.1;
DE   AltName: Full=Arginosuccinase;
GN   Name=ASL;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=3391281; DOI=10.1016/0014-5793(88)80124-8;
RA   Matuo S., Tatsuno M., Kobayashi K., Saheki T., Miyata T.;
RT   "Isolation of cDNA clones of human argininosuccinate lyase and
RT   corrected amino acid sequence.";
RL   FEBS Lett. 234:395-399(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=3463959; DOI=10.1073/pnas.83.19.7211;
RA   O'Brien W.E., McInnes R., Kalumuck K., Adcock M.;
RT   "Cloning and sequence analysis of cDNA for human argininosuccinate
RT   lyase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:7211-7215(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=2644168; DOI=10.1016/0888-7543(89)90314-5;
RA   Todd S., McGill J.R., McCombs J.L., Moore C.M., Weider I.,
RA   Naylor S.L.;
RT   "cDNA sequence, interspecies comparison, and gene mapping analysis of
RT   argininosuccinate lyase.";
RL   Genomics 4:53-59(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Matuo S.;
RT   "Cloning and sequence analysis of cDNA for human argininosuccinate
RT   lyase.";
RL   Kagoshima Daigaku Igaku Zasshi 40:147-160(1988).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RA   Linnebank M., Tschiedel E., Koch H.G.;
RT   "Complete sequence of the human ASL gene.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA   Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA   Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA   Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA   Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA   Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA   Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA   Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA   Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA   Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA   Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA   Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA   Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA   Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA   Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA   Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA   Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA   Waterston R.H., Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain, and Cervix;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-97 (ISOFORM 1/2/3).
RX   PubMed=3368457; DOI=10.1073/pnas.85.10.3479;
RA   Piatigorsky J., O'Brien W.E., Norman B.L., Kalumuck K., Wistow G.J.,
RA   Borras T., Nickerson J.M., Wawrousek E.F.;
RT   "Gene sharing by delta-crystallin and argininosuccinate lyase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:3479-3483(1988).
RN   [9]
RP   ACETYLATION AT LYS-69 AND LYS-288, ENZYME REGULATION, MUTAGENESIS OF
RP   LYS-288, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20167786; DOI=10.1126/science.1179689;
RA   Zhao S., Xu W., Jiang W., Yu W., Lin Y., Zhang T., Yao J., Zhou L.,
RA   Zeng Y., Li H., Li Y., Shi J., An W., Hancock S.M., He F., Qin L.,
RA   Chin J., Yang P., Chen X., Lei Q., Xiong Y., Guan K.L.;
RT   "Regulation of cellular metabolism by protein lysine acetylation.";
RL   Science 327:1000-1004(2010).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (4.2 ANGSTROMS).
RC   TISSUE=Liver;
RX   PubMed=9256435; DOI=10.1073/pnas.94.17.9063;
RA   Turner M.A., Simpson A., McInnes R.R., Howell P.L.;
RT   "Human argininosuccinate lyase: a structural basis for intragenic
RT   complementation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:9063-9068(1997).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF VARIANT ARG-286.
RX   PubMed=11747432; DOI=10.1021/bi011525m;
RA   Sampaleanu L.M., Vallee F., Thompson G.D., Howell P.L.;
RT   "Three-dimensional structure of the argininosuccinate lyase frequently
RT   complementing allele Q286R.";
RL   Biochemistry 40:15570-15580(2001).
RN   [13]
RP   VARIANTS ARGINSA TRP-111; GLN-193 AND ARG-286, AND MUTAGENESIS.
RX   PubMed=1705937;
RA   Barbosa P., Cialkowski M., O'Brien W.E.;
RT   "Analysis of naturally occurring and site-directed mutations in the
RT   argininosuccinate lyase gene.";
RL   J. Biol. Chem. 266:5286-5290(1991).
RN   [14]
RP   VARIANT ARGINSA CYS-95.
RX   PubMed=2263616; DOI=10.1073/pnas.87.24.9625;
RA   Walker D.C., McCloskey D.A., Simard L.R., McInnes R.R.;
RT   "Molecular analysis of human argininosuccinate lyase: mutant
RT   characterization and alternative splicing of the coding region.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:9625-9629(1990).
RN   [15]
RP   VARIANTS ARGINSA MET-178; CYS-379 AND CYS-385.
RX   PubMed=12408190; DOI=10.1023/A:1020108002877;
RA   Kleijer W.J., Garritsen V.H., Linnebank M., Mooyer P.,
RA   Huijmans J.G.M., Mustonen A., Simola K.O.J., Arslan-Kirchner M.,
RA   Battini R., Briones P., Cardo E., Mandel H., Tschiedel E.,
RA   Wanders R.J.A., Koch H.G.;
RT   "Clinical, enzymatic, and molecular genetic characterization of a
RT   biochemical variant type of argininosuccinic aciduria: prenatal and
RT   postnatal diagnosis in five unrelated families.";
RL   J. Inherit. Metab. Dis. 25:399-410(2002).
RN   [16]
RP   VARIANTS [LARGE SCALE ANALYSIS] SER-181 AND VAL-200.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
RN   [17]
RP   VARIANTS ARGINSA ASN-31; GLN-113; MET-178; GLN-186; TRP-236; ARG-286;
RP   LEU-335; ARG-382 AND TRP-456.
RX   PubMed=17326097; DOI=10.1002/humu.20498;
RA   Trevisson E., Salviati L., Baldoin M.C., Toldo I., Casarin A.,
RA   Sacconi S., Cesaro L., Basso G., Burlina A.B.;
RT   "Argininosuccinate lyase deficiency: mutational spectrum in Italian
RT   patients and identification of a novel ASL pseudogene.";
RL   Hum. Mutat. 28:694-702(2007).
CC   -!- CATALYTIC ACTIVITY: 2-(N(omega)-L-arginino)succinate = fumarate +
CC       L-arginine.
CC   -!- ENZYME REGULATION: Enzyme activity is regulated by acetylation.
CC       {ECO:0000250}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC       arginine from L-ornithine and carbamoyl phosphate: step 3/3.
CC   -!- PATHWAY: Nitrogen metabolism; urea cycle; L-arginine and fumarate
CC       from (N(omega)-L-arginino)succinate: step 1/1.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P04424-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P04424-2; Sequence=VSP_047256;
CC         Note=Gene prediction based on EST data.;
CC       Name=3;
CC         IsoId=P04424-3; Sequence=VSP_047255;
CC         Note=Gene prediction based on EST data.;
CC   -!- PTM: Acetylation modifies enzyme activity in response to
CC       alterations of extracellular nutrient availability. Acetylation
CC       increased with trichostin A (TSA) or with nicotinamide (NAM).
CC       Glucose increases acetylation by about a factor of 3 with
CC       decreasing enzyme activity. Acetylation on Lys-288 is decreased on
CC       the addition of extra amino acids resulting in activation of
CC       enzyme activity. {ECO:0000269|PubMed:20167786}.
CC   -!- DISEASE: Argininosuccinic aciduria (ARGINSA) [MIM:207900]: An
CC       autosomal recessive disorder of the urea cycle. The disease is
CC       characterized by mental and physical retardation, liver
CC       enlargement, skin lesions, dry and brittle hair showing
CC       trichorrhexis nodosa microscopically and fluorescing red,
CC       convulsions, and episodic unconsciousness.
CC       {ECO:0000269|PubMed:12408190, ECO:0000269|PubMed:1705937,
CC       ECO:0000269|PubMed:17326097, ECO:0000269|PubMed:2263616}. Note=The
CC       disease is caused by mutations affecting the gene represented in
CC       this entry.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA51786.1; Type=Frameshift; Positions=387, 452; Evidence={ECO:0000305};
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DR   EMBL; Y00753; CAA68722.1; -; mRNA.
DR   EMBL; M14218; AAA51786.1; ALT_FRAME; mRNA.
DR   EMBL; J03058; AAA51787.1; -; mRNA.
DR   EMBL; M57638; AAA51788.1; -; mRNA.
DR   EMBL; AF376770; AAL57276.1; -; Genomic_DNA.
DR   EMBL; AC068533; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC008195; AAH08195.1; -; mRNA.
DR   EMBL; BC033146; AAH33146.1; -; mRNA.
DR   EMBL; M21007; AAA35566.1; -; Genomic_DNA.
DR   EMBL; M21006; AAA35566.1; JOINED; Genomic_DNA.
DR   CCDS; CCDS47597.1; -. [P04424-2]
DR   CCDS; CCDS47598.1; -. [P04424-3]
DR   CCDS; CCDS5531.1; -. [P04424-1]
DR   PIR; A31658; WZHURS.
DR   RefSeq; NP_000039.2; NM_000048.3. [P04424-1]
DR   RefSeq; NP_001020114.1; NM_001024943.1. [P04424-1]
DR   RefSeq; NP_001020115.1; NM_001024944.1. [P04424-2]
DR   RefSeq; NP_001020117.1; NM_001024946.1. [P04424-3]
DR   UniGene; Hs.632015; -.
DR   PDB; 1AOS; X-ray; 4.20 A; A/B=1-464.
DR   PDB; 1K62; X-ray; 2.65 A; A/B=1-464.
DR   PDBsum; 1AOS; -.
DR   PDBsum; 1K62; -.
DR   ProteinModelPortal; P04424; -.
DR   SMR; P04424; 6-464.
DR   BioGrid; 106927; 15.
DR   IntAct; P04424; 5.
DR   STRING; 9606.ENSP00000307188; -.
DR   DrugBank; DB00125; L-Arginine.
DR   PhosphoSite; P04424; -.
DR   MaxQB; P04424; -.
DR   PaxDb; P04424; -.
DR   PRIDE; P04424; -.
DR   DNASU; 435; -.
DR   Ensembl; ENST00000304874; ENSP00000307188; ENSG00000126522. [P04424-1]
DR   Ensembl; ENST00000380839; ENSP00000370219; ENSG00000126522. [P04424-3]
DR   Ensembl; ENST00000395331; ENSP00000378740; ENSG00000126522. [P04424-2]
DR   Ensembl; ENST00000395332; ENSP00000378741; ENSG00000126522. [P04424-1]
DR   GeneID; 435; -.
DR   KEGG; hsa:435; -.
DR   UCSC; uc003tuo.3; human. [P04424-1]
DR   CTD; 435; -.
DR   GeneCards; GC07P065540; -.
DR   GeneReviews; ASL; -.
DR   HGNC; HGNC:746; ASL.
DR   HPA; CAB003696; -.
DR   HPA; HPA016646; -.
DR   MIM; 207900; phenotype.
DR   MIM; 608310; gene.
DR   neXtProt; NX_P04424; -.
DR   Orphanet; 23; Argininosuccinic aciduria.
DR   PharmGKB; PA25046; -.
DR   eggNOG; COG0165; -.
DR   GeneTree; ENSGT00390000014045; -.
DR   HOGENOM; HOG000242744; -.
DR   HOVERGEN; HBG004281; -.
DR   InParanoid; P04424; -.
DR   KO; K01755; -.
DR   OMA; DATTLME; -.
DR   OrthoDB; EOG7PS1FN; -.
DR   PhylomeDB; P04424; -.
DR   TreeFam; TF300656; -.
DR   BioCyc; MetaCyc:HS10034-MONOMER; -.
DR   Reactome; REACT_847; Urea cycle.
DR   SABIO-RK; P04424; -.
DR   UniPathway; UPA00068; UER00114.
DR   UniPathway; UPA00158; UER00273.
DR   ChiTaRS; ASL; human.
DR   EvolutionaryTrace; P04424; -.
DR   GenomeRNAi; 435; -.
DR   NextBio; 1821; -.
DR   PRO; PR:P04424; -.
DR   Bgee; P04424; -.
DR   CleanEx; HS_ASL; -.
DR   ExpressionAtlas; P04424; baseline.
DR   Genevestigator; P04424; -.
DR   GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; EXP:Reactome.
DR   GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
DR   GO; GO:0006527; P:arginine catabolic process; TAS:ProtInc.
DR   GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
DR   GO; GO:0006475; P:internal protein amino acid acetylation; IDA:UniProtKB.
DR   GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR   GO; GO:0000050; P:urea cycle; TAS:Reactome.
DR   Gene3D; 1.10.275.10; -; 1.
DR   HAMAP; MF_00006; Arg_succ_lyase; 1.
DR   InterPro; IPR029419; Arg_succ_lyase_C.
DR   InterPro; IPR009049; Argininosuccinate_lyase.
DR   InterPro; IPR024083; Fumarase/histidase_N.
DR   InterPro; IPR020557; Fumarate_lyase_CS.
DR   InterPro; IPR000362; Fumarate_lyase_fam.
DR   InterPro; IPR022761; Fumarate_lyase_N.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   PANTHER; PTHR11444; PTHR11444; 1.
DR   PANTHER; PTHR11444:SF3; PTHR11444:SF3; 1.
DR   Pfam; PF14698; ASL_C2; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   TIGRFAMs; TIGR00838; argH; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome;
KW   Disease mutation; Lyase; Polymorphism; Reference proteome; Urea cycle.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    464       Argininosuccinate lyase.
FT                                /FTId=PRO_0000137712.
FT   MOD_RES       2      2       N-acetylalanine. {ECO:0000250}.
FT   MOD_RES       7      7       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES      69     69       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:20167786}.
FT   MOD_RES     288    288       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:20167786}.
FT   VAR_SEQ     176    201       Missing (in isoform 3). {ECO:0000305}.
FT                                /FTId=VSP_047255.
FT   VAR_SEQ     307    326       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_047256.
FT   VARIANT      31     31       D -> N (in ARGINSA).
FT                                {ECO:0000269|PubMed:17326097}.
FT                                /FTId=VAR_043106.
FT   VARIANT      95     95       R -> C (in ARGINSA; dbSNP:rs28940585).
FT                                {ECO:0000269|PubMed:2263616}.
FT                                /FTId=VAR_000676.
FT   VARIANT     111    111       R -> W (in ARGINSA).
FT                                {ECO:0000269|PubMed:1705937}.
FT                                /FTId=VAR_000677.
FT   VARIANT     113    113       R -> Q (in ARGINSA).
FT                                {ECO:0000269|PubMed:17326097}.
FT                                /FTId=VAR_043107.
FT   VARIANT     178    178       V -> M (in ARGINSA; dbSNP:rs28941473).
FT                                {ECO:0000269|PubMed:12408190,
FT                                ECO:0000269|PubMed:17326097}.
FT                                /FTId=VAR_017572.
FT   VARIANT     181    181       T -> S (in a breast cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_036281.
FT   VARIANT     186    186       R -> Q (in ARGINSA).
FT                                {ECO:0000269|PubMed:17326097}.
FT                                /FTId=VAR_043108.
FT   VARIANT     193    193       R -> Q (in ARGINSA).
FT                                {ECO:0000269|PubMed:1705937}.
FT                                /FTId=VAR_000678.
FT   VARIANT     200    200       G -> V (in a breast cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_036282.
FT   VARIANT     236    236       R -> W (in ARGINSA).
FT                                {ECO:0000269|PubMed:17326097}.
FT                                /FTId=VAR_043109.
FT   VARIANT     286    286       Q -> R (in ARGINSA; dbSNP:rs28941472).
FT                                {ECO:0000269|PubMed:1705937,
FT                                ECO:0000269|PubMed:17326097}.
FT                                /FTId=VAR_000679.
FT   VARIANT     335    335       V -> L (in ARGINSA).
FT                                {ECO:0000269|PubMed:17326097}.
FT                                /FTId=VAR_043110.
FT   VARIANT     379    379       R -> C (in ARGINSA; dbSNP:rs28940287).
FT                                {ECO:0000269|PubMed:12408190}.
FT                                /FTId=VAR_017573.
FT   VARIANT     382    382       M -> R (in ARGINSA).
FT                                {ECO:0000269|PubMed:17326097}.
FT                                /FTId=VAR_043111.
FT   VARIANT     385    385       R -> C (in ARGINSA; dbSNP:rs28940286).
FT                                {ECO:0000269|PubMed:12408190}.
FT                                /FTId=VAR_017574.
FT   VARIANT     456    456       R -> W (in ARGINSA).
FT                                {ECO:0000269|PubMed:17326097}.
FT                                /FTId=VAR_043112.
FT   MUTAGEN      51     51       K->N: 2-fold reduction in activity.
FT                                {ECO:0000269|PubMed:1705937}.
FT   MUTAGEN      89     89       H->Q: 10-fold reduction in activity.
FT                                {ECO:0000269|PubMed:1705937}.
FT   MUTAGEN     288    288       K->R: Refractory to inhibition by TSA and
FT                                NAM and by addition of extra amino acids.
FT                                No effect on protein structure.
FT                                {ECO:0000269|PubMed:20167786}.
FT   CONFLICT    246    246       A -> R (in Ref. 1; CAA68722, 2; AAA51786,
FT                                3; AAA51787, 4; AAA51788 and 5;
FT                                AAL57276). {ECO:0000305}.
FT   CONFLICT    431    431       G -> R (in Ref. 1; CAA68722).
FT                                {ECO:0000305}.
FT   HELIX        19     25       {ECO:0000244|PDB:1K62}.
FT   HELIX        28     31       {ECO:0000244|PDB:1K62}.
FT   HELIX        32     34       {ECO:0000244|PDB:1K62}.
FT   HELIX        35     51       {ECO:0000244|PDB:1K62}.
FT   HELIX        57     76       {ECO:0000244|PDB:1K62}.
FT   HELIX        88    100       {ECO:0000244|PDB:1K62}.
FT   HELIX       101    106       {ECO:0000244|PDB:1K62}.
FT   TURN        107    110       {ECO:0000244|PDB:1K62}.
FT   HELIX       113    150       {ECO:0000244|PDB:1K62}.
FT   STRAND      154    159       {ECO:0000244|PDB:1K62}.
FT   STRAND      162    168       {ECO:0000244|PDB:1K62}.
FT   HELIX       169    194       {ECO:0000244|PDB:1K62}.
FT   STRAND      195    197       {ECO:0000244|PDB:1K62}.
FT   TURN        202    205       {ECO:0000244|PDB:1K62}.
FT   HELIX       213    219       {ECO:0000244|PDB:1K62}.
FT   STRAND      223    225       {ECO:0000244|PDB:1K62}.
FT   HELIX       229    232       {ECO:0000244|PDB:1K62}.
FT   HELIX       237    264       {ECO:0000244|PDB:1K62}.
FT   TURN        266    268       {ECO:0000244|PDB:1K62}.
FT   HELIX       291    314       {ECO:0000244|PDB:1K62}.
FT   HELIX       323    327       {ECO:0000244|PDB:1K62}.
FT   HELIX       328    352       {ECO:0000244|PDB:1K62}.
FT   HELIX       357    362       {ECO:0000244|PDB:1K62}.
FT   HELIX       366    369       {ECO:0000244|PDB:1K62}.
FT   HELIX       370    379       {ECO:0000244|PDB:1K62}.
FT   HELIX       384    400       {ECO:0000244|PDB:1K62}.
FT   HELIX       405    407       {ECO:0000244|PDB:1K62}.
FT   HELIX       410    414       {ECO:0000244|PDB:1K62}.
FT   HELIX       423    428       {ECO:0000244|PDB:1K62}.
FT   HELIX       430    434       {ECO:0000244|PDB:1K62}.
FT   STRAND      442    444       {ECO:0000244|PDB:1K62}.
FT   HELIX       445    463       {ECO:0000244|PDB:1K62}.
SQ   SEQUENCE   464 AA;  51658 MW;  F751625C1A581883 CRC64;
     MASESGKLWG GRFVGAVDPI MEKFNASIAY DRHLWEVDVQ GSKAYSRGLE KAGLLTKAEM
     DQILHGLDKV AEEWAQGTFK LNSNDEDIHT ANERRLKELI GATAGKLHTG RSRNDQVVTD
     LRLWMRQTCS TLSGLLWELI RTMVDRAEAE RDVLFPGYTH LQRAQPIRWS HWILSHAVAL
     TRDSERLLEV RKRINVLPLG SGAIAGNPLG VDRELLRAEL NFGAITLNSM DATSERDFVA
     EFLFWASLCM THLSRMAEDL ILYCTKEFSF VQLSDAYSTG SSLMPQKKNP DSLELIRSKA
     GRVFGRCAGL LMTLKGLPST YNKDLQEDKE AVFEVSDTMS AVLQVATGVI STLQIHQENM
     GQALSPDMLA TDLAYYLVRK GMPFRQAHEA SGKAVFMAET KGVALNQLSL QELQTISPLF
     SGDVICVWDY GHSVEQYGAL GGTARSSVDW QIRQVRALLQ AQQA
//
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