ID MT1H_HUMAN Reviewed; 61 AA. AC P80294; B2RUY6; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 10-JUN-2026, entry version 198. DE RecName: Full=Metallothionein-1H; DE Short=MT-1H; DE AltName: Full=Metallothionein-0; DE Short=MT-0; DE AltName: Full=Metallothionein-IH; DE Short=MT-IH; GN Name=MT1H; 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 PROTEIN SEQUENCE, AND ACETYLATION AT MET-1. RC TISSUE=Liver; RA Hunziker P.E.; RL Submitted (NOV-1993) to UniProtKB. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 3-22. RC TISSUE=Embryonic liver; RX PubMed=1425708; DOI=10.1111/j.1432-1033.1992.tb17374.x; RA Soumillion A., van Damme J., de Ley M.; RT "Cloning and specific polymerised-chain-reaction amplification of a third RT charge-separable human metallothionein isoform."; RL Eur. J. Biochem. 209:999-1004(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 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 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 [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, Pancreas, and Prostate; 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 [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-31, AND PROTEIN SEQUENCE OF 1-30. RC TISSUE=Monocyte; 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). 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: Monomer. CC -!- INTERACTION: CC P80294; P58062: SPINK7; NbExp=3; IntAct=EBI-296567, 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. CC -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 1 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X64834; CAA46046.1; -; Genomic_DNA. DR EMBL; X64177; CAA45516.1; -; mRNA. DR EMBL; BT007171; AAP35835.1; -; mRNA. DR EMBL; CH471092; EAW82884.1; -; Genomic_DNA. DR EMBL; BC008408; AAH08408.1; -; mRNA. DR EMBL; BC059780; AAH59780.1; -; mRNA. DR EMBL; BC146930; AAI46931.1; -; mRNA. DR EMBL; BC146934; AAI46935.1; -; mRNA. DR EMBL; S68948; AAB30081.1; -; mRNA. DR CCDS; CCDS10767.1; -. DR PIR; S47651; S47651. DR RefSeq; NP_005942.1; NM_005951.2. DR AlphaFoldDB; P80294; -. DR SMR; P80294; -. DR BioGRID; 110602; 4. DR FunCoup; P80294; 19. DR IntAct; P80294; 2. DR NDEx; IQUERY-CP-MT1H; 2 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000330587; -. DR DrugBank; DB09130; Copper. DR DrugBank; DB12965; Silver. DR GlyGen; P80294; 1 site, 3 N-linked glycans (1 site). DR iPTMnet; P80294; -. DR PhosphoSitePlus; P80294; -. DR BioMuta; MT1H; -. DR jPOST; P80294; -. DR MassIVE; P80294; -. DR PaxDb; 9606-ENSP00000330587; -. DR PeptideAtlas; P80294; -. DR ProteomicsDB; 57675; -. DR Pumba; P80294; -. DR Antibodypedia; 76404; 26 antibodies from 6 providers. DR DNASU; 4496; -. DR Ensembl; ENST00000332374.5; ENSP00000330587.5; ENSG00000205358.5. DR GeneID; 4496; -. DR KEGG; hsa:4496; -. DR MANE-Select; ENST00000332374.5; ENSP00000330587.5; NM_005951.2; NP_005942.1. DR UCSC; uc002ejw.3; human. DR AGR; HGNC:7400; -. DR ClinPGx; PA31205; -. DR CTD; 4496; -. DR DisGeNET; 4496; -. DR GeneCards; MT1H; -. DR HGNC; HGNC:7400; MT1H. DR HPA; ENSG00000205358; Tissue enhanced (kidney, liver). DR MIM; 156354; gene. DR OpenTargets; ENSG00000205358; -. DR VEuPathDB; HostDB:ENSG00000205358; -. DR eggNOG; KOG4738; Eukaryota. DR GeneTree; ENSGT00950000182967; -. DR HOGENOM; CLU_171204_2_0_1; -. DR InParanoid; P80294; -. DR OMA; GCVCKES; -. DR OrthoDB; 10542655at2759; -. DR PAN-GO; P80294; 8 GO annotations based on evolutionary models. DR PathwayCommons; P80294; -. DR Reactome; R-HSA-5661231; Metallothioneins bind metals. DR SignaLink; P80294; -. DR Agora; ENSG00000205358; -. DR BioGRID-ORCS; 4496; 71 hits in 1052 CRISPR screens. DR GeneWiki; MT1H; -. DR GenomeRNAi; 4496; -. DR Pharos; P80294; Tbio. DR PRO; PR:P80294; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; P80294; protein. DR Bgee; ENSG00000205358; Expressed in ileal mucosa and 195 other cell types or tissues. DR ExpressionAtlas; P80294; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. 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: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:0071294; P:cellular response to zinc ion; IEP:UniProtKB. DR GO; GO:0010273; P:detoxification of copper ion; IBA:GO_Central. DR GO; GO:0006882; P:intracellular zinc ion homeostasis; IBA:GO_Central. DR GO; GO:0045926; P:negative regulation of growth; ISS:UniProtKB. DR FunFam; 4.10.10.10:FF:000001; Metallothionein; 1. DR Gene3D; 4.10.10.10; Metallothionein Isoform II; 1. 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; METALLOTHIONEIN; 1. DR PANTHER; PTHR23299:SF4; METALLOTHIONEIN-1H; 1. DR Pfam; PF00131; Metallothio; 1. DR PRINTS; PR00860; MTVERTEBRATE. DR SUPFAM; SSF57868; Metallothionein; 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; Proteomics identification; KW Reference proteome; Zinc. FT CHAIN 1..61 FT /note="Metallothionein-1H" FT /id="PRO_0000197239" 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:0000269|PubMed:8119276, ECO:0000269|Ref.1" FT MOD_RES 58 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P02795" SQ SEQUENCE 61 AA; 6039 MW; 03D866E4F437A2CC CRC64; MDPNCSCEAG GSCACAGSCK CKKCKCTSCK KSCCSCCPLG CAKCAQGCIC KGASEKCSCC A //