MT1H_HUMAN
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 03-AUG-2022, entry version 182.
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}.
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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; 3.
DR IntAct; P80294; 2.
DR STRING; 9606.ENSP00000330587; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB12965; Silver.
DR iPTMnet; P80294; -.
DR PhosphoSitePlus; P80294; -.
DR BioMuta; MT1H; -.
DR EPD; P80294; -.
DR jPOST; P80294; -.
DR MassIVE; P80294; -.
DR MaxQB; P80294; -.
DR PaxDb; P80294; -.
DR PeptideAtlas; P80294; -.
DR PRIDE; P80294; -.
DR ProteomicsDB; 57675; -.
DR Antibodypedia; 76404; 29 antibodies from 6 providers.
DR DNASU; 4496; -.
DR Ensembl; ENST00000332374.5; ENSP00000330587.5; ENSG00000205358.4.
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 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 neXtProt; NX_P80294; -.
DR OpenTargets; ENSG00000205358; -.
DR PharmGKB; PA31205; -.
DR VEuPathDB; HostDB:ENSG00000205358; -.
DR eggNOG; KOG4738; Eukaryota.
DR GeneTree; ENSGT00950000182967; -.
DR HOGENOM; CLU_171204_2_0_1; -.
DR InParanoid; P80294; -.
DR OMA; HICETQC; -.
DR TreeFam; TF336054; -.
DR PathwayCommons; P80294; -.
DR Reactome; R-HSA-5661231; Metallothioneins bind metals.
DR SignaLink; P80294; -.
DR BioGRID-ORCS; 4496; 69 hits in 991 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 tissues.
DR ExpressionAtlas; P80294; baseline and differential.
DR Genevisible; P80294; HS.
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: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 Acetylation; Cadmium; Copper; Direct protein sequencing; Metal-binding;
KW Metal-thiolate cluster; Phosphoprotein; 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
