MT1X_HUMAN
ID MT1X_HUMAN Reviewed; 61 AA.
AC P80297; A8MUC7;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Metallothionein-1X;
DE Short=MT-1X;
DE AltName: Full=Metallothionein-IX;
DE Short=MT-IX;
GN Name=MT1X;
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].
RC TISSUE=Liver;
RA Soumillion A., van Weyenbergh J., de Ley M.;
RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE.
RC TISSUE=Liver;
RA Hunziker P.E.;
RL Submitted (NOV-1993) to UniProtKB.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=8049263; DOI=10.1016/0167-4781(94)90189-9;
RA Stennard F.A., Holloway A.F., Hamilton J., West A.K.;
RT "Characterisation of six additional human metallothionein genes.";
RL Biochim. Biophys. Acta 1218:357-365(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-31.
RX PubMed=8119276; DOI=10.1111/j.1432-1033.1994.tb18603.x;
RA Pauwels M., van Weyenbergh J., Soumillion A., Proost P., Ley M.;
RT "Induction by zinc of specific metallothionein isoforms in human
RT monocytes.";
RL Eur. J. Biochem. 220:105-110(1994).
RN [7]
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 [8]
RP FUNCTION, AND INTERACTION WITH FAM168A.
RX PubMed=23251525; DOI=10.1371/journal.pone.0051413;
RA Peng B., Gu Y., Xiong Y., Zheng G., He Z.;
RT "Microarray-assisted pathway analysis identifies MT1X & NFkappaB as
RT mediators of TCRP1-associated resistance to cisplatin in oral squamous cell
RT carcinoma.";
RL PLoS ONE 7:E51413-E51413(2012).
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. May be involved in
CC FAM168A anti-apoptotic signaling (PubMed:23251525).
CC {ECO:0000269|PubMed:23251525}.
CC -!- SUBUNIT: Monomer. Interacts with FAM168A (PubMed:23251525).
CC {ECO:0000269|PubMed:23251525}.
CC -!- INTERACTION:
CC P80297; Q8N1H7: SIX6OS1; NbExp=3; IntAct=EBI-11308402, EBI-12182077;
CC P80297; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-11308402, EBI-750109;
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.
CC -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 1 family.
CC {ECO:0000305}.
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DR EMBL; X76717; CAA54136.1; -; mRNA.
DR EMBL; X65607; CAA46557.1; -; Genomic_DNA.
DR EMBL; AC026461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032338; AAH32338.1; -; mRNA.
DR EMBL; S68956; AAB30084.1; -; mRNA.
DR CCDS; CCDS10768.1; -.
DR PIR; S47652; S47652.
DR RefSeq; NP_005943.1; NM_005952.3.
DR AlphaFoldDB; P80297; -.
DR SMR; P80297; -.
DR BioGRID; 110607; 7.
DR IntAct; P80297; 4.
DR STRING; 9606.ENSP00000377995; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB12965; Silver.
DR iPTMnet; P80297; -.
DR PhosphoSitePlus; P80297; -.
DR BioMuta; MT1X; -.
DR EPD; P80297; -.
DR jPOST; P80297; -.
DR MassIVE; P80297; -.
DR MaxQB; P80297; -.
DR PaxDb; P80297; -.
DR PeptideAtlas; P80297; -.
DR PRIDE; P80297; -.
DR ProteomicsDB; 57676; -.
DR TopDownProteomics; P80297; -.
DR Antibodypedia; 71776; 39 antibodies from 8 providers.
DR DNASU; 4501; -.
DR Ensembl; ENST00000394485.5; ENSP00000377995.4; ENSG00000187193.9.
DR GeneID; 4501; -.
DR KEGG; hsa:4501; -.
DR MANE-Select; ENST00000394485.5; ENSP00000377995.4; NM_005952.4; NP_005943.1.
DR UCSC; uc002ejy.4; human.
DR CTD; 4501; -.
DR DisGeNET; 4501; -.
DR GeneCards; MT1X; -.
DR HGNC; HGNC:7405; MT1X.
DR HPA; ENSG00000187193; Tissue enhanced (liver, skeletal muscle).
DR MIM; 156359; gene.
DR neXtProt; NX_P80297; -.
DR OpenTargets; ENSG00000187193; -.
DR PharmGKB; PA31213; -.
DR VEuPathDB; HostDB:ENSG00000187193; -.
DR eggNOG; KOG4738; Eukaryota.
DR GeneTree; ENSGT00950000182967; -.
DR HOGENOM; CLU_171204_2_0_1; -.
DR InParanoid; P80297; -.
DR OMA; CICKEPQ; -.
DR PhylomeDB; P80297; -.
DR TreeFam; TF336054; -.
DR PathwayCommons; P80297; -.
DR Reactome; R-HSA-5661231; Metallothioneins bind metals.
DR SignaLink; P80297; -.
DR BioGRID-ORCS; 4501; 15 hits in 655 CRISPR screens.
DR ChiTaRS; MT1X; human.
DR GeneWiki; MT1X; -.
DR GenomeRNAi; 4501; -.
DR Pharos; P80297; Tbio.
DR PRO; PR:P80297; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P80297; protein.
DR Bgee; ENSG00000187193; Expressed in pericardium and 205 other tissues.
DR ExpressionAtlas; P80297; baseline and differential.
DR Genevisible; P80297; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA: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:0071276; P:cellular response to cadmium ion; IEP:UniProtKB.
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: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 GO; GO:0010038; P:response to metal ion; TAS:ProtInc.
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 Acetylation; Cadmium; Copper; Direct protein sequencing; Metal-binding;
KW Metal-thiolate cluster; Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..61
FT /note="Metallothionein-1X"
FT /id="PRO_0000197243"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02795"
SQ SEQUENCE 61 AA; 6068 MW; 381966F942E986B2 CRC64;
MDPNCSCSPV GSCACAGSCK CKECKCTSCK KSCCSCCPVG CAKCAQGCIC KGTSDKCSCC
A
