MT2_HUMAN
ID MT2_HUMAN Reviewed; 61 AA.
AC P02795; Q14823; Q2HXR9; Q53XT9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Metallothionein-2;
DE Short=MT-2;
DE AltName: Full=Metallothionein-2A;
DE AltName: Full=Metallothionein-II;
DE Short=MT-II;
GN Name=MT2A {ECO:0000312|HGNC:HGNC:7406}; Synonyms=CES1, MT2;
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 PRELIMINARY PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=913597; DOI=10.1016/0014-5793(77)80594-2;
RA Kissling M.M., Kaegi J.H.R.;
RT "Primary structure of human hepatic metallothionein.";
RL FEBS Lett. 82:247-250(1977).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7133118; DOI=10.1038/299797a0;
RA Karin M., Richards R.I.;
RT "Human metallothionein genes -- primary structure of the metallothionein-II
RT gene and a related processed gene.";
RL Nature 299:797-802(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6896577; DOI=10.1093/nar/10.10.3165;
RA Karin M., Richards R.I.;
RT "Human metallothionein genes: molecular cloning and sequence analysis of
RT the mRNA.";
RL Nucleic Acids Res. 10:3165-3173(1982).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2780570; DOI=10.1073/pnas.86.18.7260;
RA Duguid J.R., Bohmont C.W., Liu N.G., Tourtellotte W.W.;
RT "Changes in brain gene expression shared by scrapie and Alzheimer
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:7260-7264(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1339282;
RA Yamazaki S., Nakanishi M., Hamamoto T., Hirata H., Ebihara A., Tokue A.,
RA Kagawa Y.;
RT "Expression of human metallothionein-II fusion protein in Escherichia
RT coli.";
RL Biochem. Int. 28:451-460(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lambert E., Kille P., Kay J., Swaminathan R.;
RT "Cloning and sequencing a novel metallothionein 1 isoform expressed in
RT human reticulocytes.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-42.
RG NIEHS SNPs program;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Kidney;
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 [10]
RP INTERACTION WITH EOLA1.
RX PubMed=15541360; DOI=10.1016/j.bbrc.2004.10.124;
RA Liang Z., Yang Z.;
RT "Identification and characterization of a novel gene EOLA1 stimulating
RT ECV304 cell proliferation.";
RL Biochem. Biophys. Res. Commun. 325:798-802(2004).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13] {ECO:0007744|PDB:1MHU, ECO:0007744|PDB:2MHU}
RP STRUCTURE BY NMR IN COMPLEX WITH CADMIUM IONS, AND DOMAIN.
RX PubMed=2388267; DOI=10.1016/0022-2836(90)90291-s;
RA Messerle B.A., Schaeffer A., Vasak M., Kaegi J.H.R., Wuethrich K.;
RT "Three-dimensional structure of human [113Cd7]metallothionein-2 in solution
RT determined by nuclear magnetic resonance spectroscopy.";
RL J. Mol. Biol. 214:765-779(1990).
RN [14]
RP STRUCTURE BY NMR IN COMPLEX WITH ZINC IONS.
RX PubMed=1593628; DOI=10.1016/0022-2836(92)90930-i;
RA Messerle B.A., Schaeffer A., Vasak M., Kaegi J.H.R., Wuethrich K.;
RT "Comparison of the solution conformations of human [Zn7]-metallothionein-2
RT and [Cd7]-metallothionein-2 using nuclear magnetic resonance
RT spectroscopy.";
RL J. Mol. Biol. 225:433-443(1992).
CC -!- FUNCTION: Metallothioneins have a high content of cysteine residues
CC that bind various heavy metals; these proteins are transcriptionally
CC regulated by both heavy metals and glucocorticoids.
CC -!- SUBUNIT: Interacts with EOLA1. {ECO:0000269|PubMed:15541360}.
CC -!- INTERACTION:
CC P02795; P02649: APOE; NbExp=3; IntAct=EBI-996616, EBI-1222467;
CC P02795; Q96A83-2: COL26A1; NbExp=3; IntAct=EBI-996616, EBI-21553822;
CC P02795; O14645: DNALI1; NbExp=3; IntAct=EBI-996616, EBI-395638;
CC P02795; Q8TE69: EOLA1; NbExp=2; IntAct=EBI-996616, EBI-996609;
CC P02795; P21333-2: FLNA; NbExp=3; IntAct=EBI-996616, EBI-9641086;
CC P02795; P42858: HTT; NbExp=6; IntAct=EBI-996616, EBI-466029;
CC P02795; Q9UMF0: ICAM5; NbExp=3; IntAct=EBI-996616, EBI-6398041;
CC P02795; O14901: KLF11; NbExp=3; IntAct=EBI-996616, EBI-948266;
CC P02795; P31153: MAT2A; NbExp=3; IntAct=EBI-996616, EBI-1050743;
CC P02795; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-996616, EBI-2811583;
CC P02795; D3DTS7: PMP22; NbExp=3; IntAct=EBI-996616, EBI-25882629;
CC P02795; Q15139: PRKD1; NbExp=7; IntAct=EBI-996616, EBI-1181072;
CC P02795; P37840: SNCA; NbExp=3; IntAct=EBI-996616, EBI-985879;
CC P02795; P14678-2: SNRPB; NbExp=3; IntAct=EBI-996616, EBI-372475;
CC P02795; P58062: SPINK7; NbExp=7; IntAct=EBI-996616, EBI-1182445;
CC -!- DOMAIN: Class I metallothioneins contain 2 metal-binding domains: four
CC divalent ions are chelated within cluster A of the alpha domain and are
CC coordinated via cysteinyl thiolate bridges to 11 cysteine ligands.
CC Cluster B, the corresponding region within the beta domain, can ligate
CC three divalent ions to 9 cysteines. {ECO:0000269|PubMed:2388267}.
CC -!- MISCELLANEOUS: This metallothionein binds zinc.
CC -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 1 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/mt2a/";
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DR EMBL; J00271; AAA59583.1; -; Genomic_DNA.
DR EMBL; V00594; CAA23841.1; -; mRNA.
DR EMBL; M26637; AAA59584.1; ALT_SEQ; mRNA.
DR EMBL; S52379; AAB24908.1; -; mRNA.
DR EMBL; X97260; CAA65915.1; -; mRNA.
DR EMBL; BT007315; AAP35979.1; -; mRNA.
DR EMBL; DQ370420; ABC79300.1; -; Genomic_DNA.
DR EMBL; BC007034; AAH07034.1; -; mRNA.
DR EMBL; BC070289; AAH70289.1; -; mRNA.
DR CCDS; CCDS10763.1; -.
DR PIR; A03271; SMHU2.
DR PIR; I63131; I63131.
DR RefSeq; NP_005944.1; NM_005953.3.
DR PDB; 1MHU; NMR; -; A=31-61.
DR PDB; 2MHU; NMR; -; A=1-30.
DR PDBsum; 1MHU; -.
DR PDBsum; 2MHU; -.
DR AlphaFoldDB; P02795; -.
DR BMRB; P02795; -.
DR SMR; P02795; -.
DR BioGRID; 110608; 28.
DR DIP; DIP-35232N; -.
DR IntAct; P02795; 39.
DR MINT; P02795; -.
DR STRING; 9606.ENSP00000245185; -.
DR BindingDB; P02795; -.
DR DrugBank; DB00958; Carboplatin.
DR DrugBank; DB00515; Cisplatin.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB00526; Oxaliplatin.
DR DrugBank; DB12965; Silver.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR iPTMnet; P02795; -.
DR MetOSite; P02795; -.
DR PhosphoSitePlus; P02795; -.
DR BioMuta; MT2A; -.
DR EPD; P02795; -.
DR jPOST; P02795; -.
DR MassIVE; P02795; -.
DR MaxQB; P02795; -.
DR PaxDb; P02795; -.
DR PeptideAtlas; P02795; -.
DR PRIDE; P02795; -.
DR ProteomicsDB; 51601; -.
DR TopDownProteomics; P02795; -.
DR Antibodypedia; 58432; 146 antibodies from 19 providers.
DR DNASU; 4502; -.
DR Ensembl; ENST00000245185.6; ENSP00000245185.5; ENSG00000125148.7.
DR GeneID; 4502; -.
DR KEGG; hsa:4502; -.
DR MANE-Select; ENST00000245185.6; ENSP00000245185.5; NM_005953.5; NP_005944.1.
DR UCSC; uc002ejh.4; human.
DR CTD; 4502; -.
DR DisGeNET; 4502; -.
DR GeneCards; MT2A; -.
DR HGNC; HGNC:7406; MT2A.
DR HPA; ENSG00000125148; Tissue enhanced (liver).
DR MIM; 156360; gene.
DR neXtProt; NX_P02795; -.
DR OpenTargets; ENSG00000125148; -.
DR PharmGKB; PA31214; -.
DR VEuPathDB; HostDB:ENSG00000125148; -.
DR eggNOG; KOG4738; Eukaryota.
DR GeneTree; ENSGT00950000182967; -.
DR HOGENOM; CLU_171204_2_0_1; -.
DR InParanoid; P02795; -.
DR OMA; CAGCICK; -.
DR PhylomeDB; P02795; -.
DR TreeFam; TF336054; -.
DR PathwayCommons; P02795; -.
DR Reactome; R-HSA-5661231; Metallothioneins bind metals.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SignaLink; P02795; -.
DR BioGRID-ORCS; 4502; 101 hits in 1045 CRISPR screens.
DR ChiTaRS; MT2A; human.
DR EvolutionaryTrace; P02795; -.
DR GeneWiki; Metallothionein_2A; -.
DR GenomeRNAi; 4502; -.
DR Pharos; P02795; Tbio.
DR PRO; PR:P02795; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P02795; protein.
DR Bgee; ENSG00000125148; Expressed in pericardium and 204 other tissues.
DR ExpressionAtlas; P02795; baseline and differential.
DR Genevisible; P02795; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006878; P:cellular copper ion homeostasis; TAS:ProtInc.
DR GO; GO:0071276; P:cellular response to cadmium ion; IBA:GO_Central.
DR GO; GO:0071280; P:cellular response to copper ion; IBA:GO_Central.
DR GO; GO:0036018; P:cellular response to erythropoietin; IEP:UniProtKB.
DR GO; GO:0036016; P:cellular response to interleukin-3; IEP:UniProtKB.
DR GO; GO:0071294; P:cellular response to zinc ion; IEP:UniProtKB.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IBA:GO_Central.
DR GO; GO:0010273; P:detoxification of copper ion; IBA:GO_Central.
DR GO; GO:0045926; P:negative regulation of growth; ISS:UniProtKB.
DR Gene3D; 4.10.10.10; -; 1.
DR InterPro; IPR003019; Metalthion.
DR InterPro; IPR017854; Metalthion_dom_sf.
DR InterPro; IPR023587; Metalthion_dom_sf_vert.
DR InterPro; IPR000006; Metalthion_vert.
DR InterPro; IPR018064; Metalthion_vert_metal_BS.
DR PANTHER; PTHR23299; PTHR23299; 1.
DR Pfam; PF00131; Metallothio; 1.
DR PRINTS; PR00860; MTVERTEBRATE.
DR SUPFAM; SSF57868; SSF57868; 1.
DR PROSITE; PS00203; METALLOTHIONEIN_VRT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cadmium; Direct protein sequencing;
KW Metal-binding; Metal-thiolate cluster; Phosphoprotein; Reference proteome;
KW Zinc.
FT CHAIN 1..61
FT /note="Metallothionein-2"
FT /id="PRO_0000197245"
FT REGION 1..29
FT /note="Beta"
FT REGION 30..61
FT /note="Alpha"
FT BINDING 5
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /ligand_note="in cluster B"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:2MHU"
FT BINDING 7
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /ligand_note="in cluster B"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:2MHU"
FT BINDING 7
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="in cluster B"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:2MHU"
FT BINDING 13
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="in cluster B"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:2MHU"
FT BINDING 15
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="in cluster B"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:2MHU"
FT BINDING 15
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /ligand_note="in cluster B"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:2MHU"
FT BINDING 19
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /ligand_note="in cluster B"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:2MHU"
FT BINDING 21
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /ligand_note="in cluster B"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:2MHU"
FT BINDING 24
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /ligand_note="in cluster B"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:2MHU"
FT BINDING 24
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /ligand_note="in cluster B"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:2MHU"
FT BINDING 26
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="in cluster B"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:2MHU"
FT BINDING 29
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /ligand_note="in cluster B"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:2MHU"
FT BINDING 33
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="4"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:1MHU"
FT BINDING 34
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="4"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:1MHU"
FT BINDING 34
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="5"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:1MHU"
FT BINDING 36
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="5"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:1MHU"
FT BINDING 37
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="5"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:1MHU"
FT BINDING 37
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="6"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:1MHU"
FT BINDING 41
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="6"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:1MHU"
FT BINDING 44
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="4"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:1MHU"
FT BINDING 44
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="6"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:1MHU"
FT BINDING 48
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="4"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:1MHU"
FT BINDING 50
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="5"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:1MHU"
FT BINDING 50
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="7"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:1MHU"
FT BINDING 57
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="7"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:1MHU"
FT BINDING 59
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="7"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:1MHU"
FT BINDING 60
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="6"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:1MHU"
FT BINDING 60
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="7"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:2388267,
FT ECO:0007744|PDB:1MHU"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 42
FT /note="A -> V (in dbSNP:rs35109646)"
FT /evidence="ECO:0000269|Ref.8"
FT /id="VAR_025840"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:2MHU"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:2MHU"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1MHU"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:1MHU"
SQ SEQUENCE 61 AA; 6042 MW; 7B0A7E1F99843078 CRC64;
MDPNCSCAAG DSCTCAGSCK CKECKCTSCK KSCCSCCPVG CAKCAQGCIC KGASDKCSCC
A
