SERC_HUMAN
ID SERC_HUMAN Reviewed; 370 AA.
AC Q9Y617; Q5T7G5; Q5T7G6; Q96AW2; Q9BQ12;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Phosphoserine aminotransferase;
DE EC=2.6.1.52;
DE AltName: Full=Phosphohydroxythreonine aminotransferase;
DE Short=PSAT;
GN Name=PSAT1; Synonyms=PSA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=12633500; DOI=10.1042/bj20030144;
RA Baek J.Y., Jun Y.D., Taub D., Kim Y.H.;
RT "Characterization of human phosphoserine aminotransferase involved in the
RT phosphorylated pathway of L-serine biosynthesis.";
RL Biochem. J. 373:191-200(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, Lymph, and Placenta;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [7]
RP BIOPHYSICOCHEMICAL PROPERTIES, INVOLVEMENT IN PSATD, VARIANT PSATD ALA-100,
RP AND CHARACTERIZATION OF VARIANT PSATD ALA-100.
RX PubMed=17436247; DOI=10.1086/517888;
RA Hart C.E., Race V., Achouri Y., Wiame E., Sharrard M., Olpin S.E.,
RA Watkinson J., Bonham J.R., Jaeken J., Matthijs G., Van Schaftingen E.;
RT "Phosphoserine aminotransferase deficiency: a novel disorder of the serine
RT biosynthesis pathway.";
RL Am. J. Hum. Genet. 80:931-937(2007).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51; LYS-269; LYS-318; LYS-323 AND
RP LYS-333, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
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., Buerckstuemmer T.,
RA 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP INVOLVEMENT IN NLS2, AND VARIANTS NLS2 VAL-99 AND LEU-179.
RX PubMed=25152457; DOI=10.1016/j.ajhg.2014.07.012;
RA Acuna-Hidalgo R., Schanze D., Kariminejad A., Nordgren A.,
RA Kariminejad M.H., Conner P., Grigelioniene G., Nilsson D., Nordenskjold M.,
RA Wedell A., Freyer C., Wredenberg A., Wieczorek D., Gillessen-Kaesbach G.,
RA Kayserili H., Elcioglu N., Ghaderi-Sohi S., Goodarzi P., Setayesh H.,
RA van de Vorst M., Steehouwer M., Pfundt R., Krabichler B., Curry C.,
RA MacKenzie M.G., Boycott K.M., Gilissen C., Janecke A.R., Hoischen A.,
RA Zenker M.;
RT "Neu-Laxova syndrome is a heterogeneous metabolic disorder caused by
RT defects in enzymes of the L-serine biosynthesis pathway.";
RL Am. J. Hum. Genet. 95:285-293(2014).
CC -!- FUNCTION: Catalyzes the reversible conversion of 3-
CC phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-
CC phosphonooxybutanoate to phosphohydroxythreonine.
CC {ECO:0000250|UniProtKB:P10658}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate +
CC L-glutamate; Xref=Rhea:RHEA:14329, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:18110, ChEBI:CHEBI:29985, ChEBI:CHEBI:57524; EC=2.6.1.52;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 4-(phosphooxy)-L-threonine = (R)-3-hydroxy-2-
CC oxo-4-phosphooxybutanoate + L-glutamate; Xref=Rhea:RHEA:16573,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:58452,
CC ChEBI:CHEBI:58538; EC=2.6.1.52;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 uM for phosphoserine {ECO:0000269|PubMed:17436247};
CC Vmax=1.35 umol/min/mg enzyme {ECO:0000269|PubMed:17436247};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 2/3.
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9Y617; P27797: CALR; NbExp=3; IntAct=EBI-709652, EBI-1049597;
CC Q9Y617; P12830: CDH1; NbExp=3; IntAct=EBI-709652, EBI-727477;
CC Q9Y617; P36957: DLST; NbExp=3; IntAct=EBI-709652, EBI-351007;
CC Q9Y617; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-709652, EBI-1055945;
CC Q9Y617; Q9Y617: PSAT1; NbExp=3; IntAct=EBI-709652, EBI-709652;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Alpha;
CC IsoId=Q9Y617-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta;
CC IsoId=Q9Y617-2; Sequence=VSP_000237;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the brain, liver,
CC kidney and pancreas, and very weakly expressed in the thymus, prostate,
CC testis and colon.
CC -!- DISEASE: Phosphoserine aminotransferase deficiency (PSATD)
CC [MIM:610992]: Characterized biochemically by low plasma and
CC cerebrospinal fluid concentrations of serine and glycine and clinically
CC by intractable seizures, acquired microcephaly, hypertonia, and
CC psychomotor retardation. {ECO:0000269|PubMed:17436247}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Neu-Laxova syndrome 2 (NLS2) [MIM:616038]: A form of Neu-
CC Laxova syndrome, a lethal, autosomal recessive multiple malformation
CC syndrome characterized by ichthyosis, marked intrauterine growth
CC restriction, microcephaly, short neck, limb deformities, hypoplastic
CC lungs, edema, and central nervous system anomalies. These include
CC lissencephaly, cerebellar hypoplasia and/or abnormal/agenesis of the
CC corpus callosum. Abnormal facial features include severe proptosis with
CC ectropion, hypertelorism, micrognathia, flattened nose, and malformed
CC ears. {ECO:0000269|PubMed:25152457}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. SerC subfamily. {ECO:0000305}.
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DR EMBL; AF113132; AAD42052.1; -; mRNA.
DR EMBL; AY131232; AAN71736.1; -; mRNA.
DR EMBL; BT006840; AAP35486.1; -; mRNA.
DR EMBL; AL353594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471089; EAW62621.1; -; Genomic_DNA.
DR EMBL; CH471089; EAW62617.1; -; Genomic_DNA.
DR EMBL; BC000971; AAH00971.1; -; mRNA.
DR EMBL; BC004863; AAH04863.1; -; mRNA.
DR EMBL; BC016645; AAH16645.1; -; mRNA.
DR EMBL; BC018129; AAH18129.1; -; mRNA.
DR CCDS; CCDS6659.1; -. [Q9Y617-2]
DR CCDS; CCDS6660.1; -. [Q9Y617-1]
DR RefSeq; NP_066977.1; NM_021154.4. [Q9Y617-2]
DR RefSeq; NP_478059.1; NM_058179.3. [Q9Y617-1]
DR PDB; 3E77; X-ray; 2.50 A; A/B/C=17-370.
DR PDBsum; 3E77; -.
DR AlphaFoldDB; Q9Y617; -.
DR SMR; Q9Y617; -.
DR BioGRID; 119001; 68.
DR IntAct; Q9Y617; 18.
DR MINT; Q9Y617; -.
DR STRING; 9606.ENSP00000365773; -.
DR DrugBank; DB00142; Glutamic acid.
DR DrugBank; DB00114; Pyridoxal phosphate.
DR DrugCentral; Q9Y617; -.
DR GlyGen; Q9Y617; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y617; -.
DR MetOSite; Q9Y617; -.
DR PhosphoSitePlus; Q9Y617; -.
DR SwissPalm; Q9Y617; -.
DR BioMuta; PSAT1; -.
DR DMDM; 20141815; -.
DR REPRODUCTION-2DPAGE; IPI00001734; -.
DR EPD; Q9Y617; -.
DR jPOST; Q9Y617; -.
DR MassIVE; Q9Y617; -.
DR MaxQB; Q9Y617; -.
DR PaxDb; Q9Y617; -.
DR PeptideAtlas; Q9Y617; -.
DR PRIDE; Q9Y617; -.
DR ProteomicsDB; 86580; -. [Q9Y617-1]
DR ProteomicsDB; 86581; -. [Q9Y617-2]
DR Antibodypedia; 27405; 257 antibodies from 31 providers.
DR CPTC; Q9Y617; 4 antibodies.
DR DNASU; 29968; -.
DR Ensembl; ENST00000347159.6; ENSP00000317606.2; ENSG00000135069.14. [Q9Y617-2]
DR Ensembl; ENST00000376588.4; ENSP00000365773.3; ENSG00000135069.14. [Q9Y617-1]
DR GeneID; 29968; -.
DR KEGG; hsa:29968; -.
DR MANE-Select; ENST00000376588.4; ENSP00000365773.3; NM_058179.4; NP_478059.1.
DR UCSC; uc004ala.5; human. [Q9Y617-1]
DR CTD; 29968; -.
DR DisGeNET; 29968; -.
DR GeneCards; PSAT1; -.
DR HGNC; HGNC:19129; PSAT1.
DR HPA; ENSG00000135069; Tissue enhanced (brain, liver).
DR MalaCards; PSAT1; -.
DR MIM; 610936; gene.
DR MIM; 610992; phenotype.
DR MIM; 616038; phenotype.
DR neXtProt; NX_Q9Y617; -.
DR OpenTargets; ENSG00000135069; -.
DR Orphanet; 583602; Neu-laxova syndrome due to phosphoserine aminotransferase deficiency.
DR Orphanet; 284417; Phosphoserine aminotransferase deficiency, infantile/juvenile form.
DR PharmGKB; PA128395782; -.
DR VEuPathDB; HostDB:ENSG00000135069; -.
DR eggNOG; KOG2790; Eukaryota.
DR GeneTree; ENSGT00940000153241; -.
DR HOGENOM; CLU_034866_0_1_1; -.
DR InParanoid; Q9Y617; -.
DR OMA; GYRASMY; -.
DR PhylomeDB; Q9Y617; -.
DR TreeFam; TF312975; -.
DR BioCyc; MetaCyc:HS05946-MON; -.
DR BRENDA; 2.6.1.4; 2681.
DR BRENDA; 2.6.1.52; 2681.
DR PathwayCommons; Q9Y617; -.
DR Reactome; R-HSA-977347; Serine biosynthesis.
DR SABIO-RK; Q9Y617; -.
DR SignaLink; Q9Y617; -.
DR SIGNOR; Q9Y617; -.
DR UniPathway; UPA00135; UER00197.
DR UniPathway; UPA00244; UER00311.
DR BioGRID-ORCS; 29968; 106 hits in 1050 CRISPR screens.
DR ChiTaRS; PSAT1; human.
DR EvolutionaryTrace; Q9Y617; -.
DR GeneWiki; PSAT1; -.
DR GenomeRNAi; 29968; -.
DR Pharos; Q9Y617; Tbio.
DR PRO; PR:Q9Y617; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9Y617; protein.
DR Bgee; ENSG00000135069; Expressed in ventricular zone and 176 other tissues.
DR ExpressionAtlas; Q9Y617; baseline and differential.
DR Genevisible; Q9Y617; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0006564; P:L-serine biosynthetic process; IBA:GO_Central.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; NAS:UniProtKB.
DR CDD; cd00611; PSAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00160; SerC_aminotrans_5; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR022278; Pser_aminoTfrase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43247; PTHR43247; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000525; SerC; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01364; serC_1; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Amino-acid biosynthesis;
KW Aminotransferase; Disease variant; Phosphoprotein; Pyridoxal phosphate;
KW Reference proteome; Serine biosynthesis; Transferase.
FT CHAIN 1..370
FT /note="Phosphoserine aminotransferase"
FT /id="PRO_0000150135"
FT BINDING 45
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 79..80
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 241..242
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 51
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 127
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99K85"
FT MOD_RES 200
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 269
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 318
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 323
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 333
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 291..336
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12633500,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_000237"
FT VARIANT 87
FT /note="P -> A (in dbSNP:rs11540974)"
FT /id="VAR_048235"
FT VARIANT 99
FT /note="A -> V (in NLS2; dbSNP:rs587777778)"
FT /evidence="ECO:0000269|PubMed:25152457"
FT /id="VAR_072571"
FT VARIANT 100
FT /note="D -> A (in PSATD; reduced Vmax; dbSNP:rs118203967)"
FT /evidence="ECO:0000269|PubMed:17436247"
FT /id="VAR_037252"
FT VARIANT 179
FT /note="S -> L (in NLS2; dbSNP:rs587777777)"
FT /evidence="ECO:0000269|PubMed:25152457"
FT /id="VAR_072572"
FT CONFLICT 40
FT /note="L -> V (in Ref. 5; AAH16645)"
FT /evidence="ECO:0000305"
FT HELIX 19..27
FT /evidence="ECO:0007829|PDB:3E77"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:3E77"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:3E77"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3E77"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:3E77"
FT HELIX 47..64
FT /evidence="ECO:0007829|PDB:3E77"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:3E77"
FT HELIX 78..90
FT /evidence="ECO:0007829|PDB:3E77"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:3E77"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:3E77"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:3E77"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:3E77"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:3E77"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:3E77"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:3E77"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:3E77"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:3E77"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:3E77"
FT TURN 178..182
FT /evidence="ECO:0007829|PDB:3E77"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:3E77"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:3E77"
FT TURN 198..202
FT /evidence="ECO:0007829|PDB:3E77"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:3E77"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:3E77"
FT HELIX 230..234
FT /evidence="ECO:0007829|PDB:3E77"
FT TURN 235..238
FT /evidence="ECO:0007829|PDB:3E77"
FT HELIX 245..260
FT /evidence="ECO:0007829|PDB:3E77"
FT HELIX 263..283
FT /evidence="ECO:0007829|PDB:3E77"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:3E77"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:3E77"
FT STRAND 300..309
FT /evidence="ECO:0007829|PDB:3E77"
FT HELIX 314..326
FT /evidence="ECO:0007829|PDB:3E77"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:3E77"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:3E77"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:3E77"
FT HELIX 351..368
FT /evidence="ECO:0007829|PDB:3E77"
SQ SEQUENCE 370 AA; 40423 MW; BAF9A10E71B165B4 CRC64;
MDAPRQVVNF GPGPAKLPHS VLLEIQKELL DYKGVGISVL EMSHRSSDFA KIINNTENLV
RELLAVPDNY KVIFLQGGGC GQFSAVPLNL IGLKAGRCAD YVVTGAWSAK AAEEAKKFGT
INIVHPKLGS YTKIPDPSTW NLNPDASYVY YCANETVHGV EFDFIPDVKG AVLVCDMSSN
FLSKPVDVSK FGVIFAGAQK NVGSAGVTVV IVRDDLLGFA LRECPSVLEY KVQAGNSSLY
NTPPCFSIYV MGLVLEWIKN NGGAAAMEKL SSIKSQTIYE IIDNSQGFYV CPVEPQNRSK
MNIPFRIGNA KGDDALEKRF LDKALELNML SLKGHRSVGG IRASLYNAVT IEDVQKLAAF
MKKFLEMHQL
