ID MT1B_HUMAN Reviewed; 61 AA.
AC P07438; Q86YX0;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 27-MAR-2024, entry version 187.
DE RecName: Full=Metallothionein-1B;
DE Short=MT-1B;
DE AltName: Full=Metallothionein-IB;
DE Short=MT-IB;
GN Name=MT1B; Synonyms=MT1Q;
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 [GENOMIC DNA].
RX PubMed=3785191; DOI=10.1128/mcb.6.6.2149-2157.1986;
RA Heguy A., West A., Richards R.I., Karin M.;
RT "Structure and tissue-specific expression of the human metallothionein IB
RT gene.";
RL Mol. Cell. Biol. 6:2149-2157(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Wang J., Zheng L., Yu L.;
RT "Cloning of a novel member of the human metallothionein gene family-MT1Q.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Xie J., Jiang F., Head D., Briggs R.;
RT "Metallothioneins and DNA crosslink damage.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
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 P07438; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-12015462, EBI-11959885;
CC P07438; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-12015462, EBI-12012928;
CC P07438; Q9BYP8: KRTAP17-1; NbExp=3; IntAct=EBI-12015462, EBI-11988175;
CC P07438; Q701N4: KRTAP5-2; NbExp=3; IntAct=EBI-12015462, EBI-11958178;
CC P07438; P49901: SMCP; NbExp=3; IntAct=EBI-12015462, EBI-750494;
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; M13485; AAA36331.1; -; Genomic_DNA.
DR EMBL; M13484; AAA36331.1; JOINED; Genomic_DNA.
DR EMBL; AF349000; AAO32960.2; -; mRNA.
DR EMBL; AF350250; AAO49186.1; -; Genomic_DNA.
DR EMBL; AY168638; AAN86984.1; -; mRNA.
DR EMBL; BC069421; AAH69421.1; -; mRNA.
DR EMBL; BC137478; AAI37479.1; -; mRNA.
DR EMBL; BC137479; AAI37480.1; -; mRNA.
DR CCDS; CCDS10765.1; -.
DR PIR; A25244; SMHU1B.
DR RefSeq; NP_005938.1; NM_005947.2.
DR AlphaFoldDB; P07438; -.
DR SMR; P07438; -.
DR BioGRID; 110596; 5.
DR IntAct; P07438; 5.
DR STRING; 9606.ENSP00000334998; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB12965; Silver.
DR iPTMnet; P07438; -.
DR PhosphoSitePlus; P07438; -.
DR BioMuta; MT1B; -.
DR jPOST; P07438; -.
DR MassIVE; P07438; -.
DR PaxDb; 9606-ENSP00000334998; -.
DR PeptideAtlas; P07438; -.
DR ProteomicsDB; 52003; -.
DR Antibodypedia; 76626; 32 antibodies from 6 providers.
DR DNASU; 4490; -.
DR Ensembl; ENST00000334346.3; ENSP00000334998.2; ENSG00000169688.11.
DR GeneID; 4490; -.
DR KEGG; hsa:4490; -.
DR MANE-Select; ENST00000334346.3; ENSP00000334998.2; NM_005947.3; NP_005938.1.
DR UCSC; uc002ejs.3; human.
DR AGR; HGNC:7394; -.
DR CTD; 4490; -.
DR DisGeNET; 4490; -.
DR GeneCards; MT1B; -.
DR HGNC; HGNC:7394; MT1B.
DR HPA; ENSG00000169688; Tissue enriched (liver).
DR MIM; 156349; gene.
DR neXtProt; NX_P07438; -.
DR OpenTargets; ENSG00000169688; -.
DR PharmGKB; PA31199; -.
DR VEuPathDB; HostDB:ENSG00000169688; -.
DR eggNOG; KOG4738; Eukaryota.
DR GeneTree; ENSGT00950000182967; -.
DR HOGENOM; CLU_171204_2_0_1; -.
DR InParanoid; P07438; -.
DR OMA; ICKGPPS; -.
DR TreeFam; TF336054; -.
DR PathwayCommons; P07438; -.
DR Reactome; R-HSA-5661231; Metallothioneins bind metals.
DR SignaLink; P07438; -.
DR BioGRID-ORCS; 4490; 124 hits in 1067 CRISPR screens.
DR GeneWiki; MT1B; -.
DR GenomeRNAi; 4490; -.
DR Pharos; P07438; Tbio.
DR PRO; PR:P07438; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P07438; Protein.
DR Bgee; ENSG00000169688; Expressed in right lobe of liver and 63 other cell types or tissues.
DR ExpressionAtlas; P07438; 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; IBA:GO_Central.
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 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:SF60; METALLOTHIONEIN-1B; 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 Cadmium; Copper; Metal-binding; Metal-thiolate cluster; Reference proteome;
KW Zinc.
FT CHAIN 1..61
FT /note="Metallothionein-1B"
FT /id="PRO_0000197235"
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"
SQ SEQUENCE 61 AA; 6115 MW; 8DC566E5462810D3 CRC64;
MDPNCSCTTG GSCACAGSCK CKECKCTSCK KCCCSCCPVG CAKCAQGCVC KGSSEKCRCC
A
//
