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
//