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Metallothionein-1A (MT-1A) (Metallothionein-IA) (MT-IA)

 MT1A_HUMAN              Reviewed;          61 AA.
P04731; Q86YX5;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
24-NOV-2009, sequence version 2.
22-NOV-2017, entry version 154.
RecName: Full=Metallothionein-1A;
Short=MT-1A;
AltName: Full=Metallothionein-IA;
Short=MT-IA;
Name=MT1A; Synonyms=MT1S;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASN-27.
PubMed=6327055; DOI=10.1016/0092-8674(84)90322-2;
Richards R.I., Heguy A., Karin M.;
"Structural and functional analysis of the human metallothionein-IA
gene: differential induction by metal ions and glucocorticoids.";
Cell 37:263-272(1984).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Wang J., Zheng L., Yu L.;
"Cloning of a novel member of the MT gene family - MT1S.";
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-27.
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Metallothioneins have a high content of cysteine
residues that bind various heavy metals; these proteins are
transcriptionally regulated by both heavy metals and
glucocorticoids.
-!- SUBUNIT: Monomer.
-!- INTERACTION:
Q13585:GPR50; NbExp=3; IntAct=EBI-8045030, EBI-8550965;
P04637:TP53; NbExp=3; IntAct=EBI-8045030, EBI-366083;
-!- DOMAIN: Class I metallothioneins contain 2 metal-binding domains:
four divalent ions are chelated within cluster A of the alpha
domain and are coordinated via cysteinyl thiolate bridges to 11
cysteine ligands. Cluster B, the corresponding region within the
beta domain, can ligate three divalent ions to 9 cysteines.
-!- SIMILARITY: Belongs to the metallothionein superfamily. Type 1
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; K01383; AAA59586.1; -; Genomic_DNA.
EMBL; AY028617; AAK26162.1; -; mRNA.
EMBL; AF348995; AAO32955.1; -; mRNA.
EMBL; AC026461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC029475; AAH29475.1; -; mRNA.
CCDS; CCDS32454.1; -.
PIR; A24502; SMHU1A.
RefSeq; NP_005937.2; NM_005946.2.
UniGene; Hs.655199; -.
ProteinModelPortal; P04731; -.
SMR; P04731; -.
BioGrid; 110595; 1.
IntAct; P04731; 4.
MINT; MINT-1781424; -.
STRING; 9606.ENSP00000290705; -.
DrugBank; DB00958; Carboplatin.
DrugBank; DB00515; Cisplatin.
DrugBank; DB00526; Oxaliplatin.
PhosphoSitePlus; P04731; -.
BioMuta; MT1A; -.
MaxQB; P04731; -.
PaxDb; P04731; -.
PeptideAtlas; P04731; -.
PRIDE; P04731; -.
DNASU; 4489; -.
Ensembl; ENST00000290705; ENSP00000290705; ENSG00000205362.
GeneID; 4489; -.
KEGG; hsa:4489; -.
UCSC; uc002ejq.5; human.
CTD; 4489; -.
DisGeNET; 4489; -.
EuPathDB; HostDB:ENSG00000205362.10; -.
GeneCards; MT1A; -.
H-InvDB; HIX0021628; -.
HGNC; HGNC:7393; MT1A.
HPA; CAB002161; -.
HPA; CAB013056; -.
MIM; 156350; gene.
neXtProt; NX_P04731; -.
OpenTargets; ENSG00000205362; -.
PharmGKB; PA31198; -.
eggNOG; ENOG410JFS1; Eukaryota.
eggNOG; ENOG41113QR; LUCA.
GeneTree; ENSGT00730000110883; -.
HOGENOM; HOG000236262; -.
HOVERGEN; HBG009063; -.
InParanoid; P04731; -.
KO; K14739; -.
OMA; CESACKD; -.
TreeFam; TF336054; -.
Reactome; R-HSA-5661231; Metallothioneins bind metals.
ChiTaRS; MT1A; human.
GeneWiki; Metallothionein_1A; -.
GenomeRNAi; 4489; -.
PRO; PR:P04731; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000205362; -.
CleanEx; HS_MT1A; -.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0071276; P:cellular response to cadmium ion; IEP:UniProtKB.
GO; GO:0071294; P:cellular response to zinc ion; IEP:UniProtKB.
GO; GO:0045926; P:negative regulation of growth; ISS:UniProtKB.
GO; GO:0010038; P:response to metal ion; TAS:Reactome.
Gene3D; 4.10.10.10; -; 1.
InterPro; IPR003019; Metalthion.
InterPro; IPR017854; Metalthion_dom_sf.
InterPro; IPR023587; Metalthion_dom_vert.
InterPro; IPR000006; Metalthion_vert.
InterPro; IPR018064; Metalthion_vert_metal_BS.
PANTHER; PTHR23299; PTHR23299; 1.
Pfam; PF00131; Metallothio; 1.
PRINTS; PR00860; MTVERTEBRATE.
SUPFAM; SSF57868; SSF57868; 1.
PROSITE; PS00203; METALLOTHIONEIN_VRT; 1.
1: Evidence at protein level;
Acetylation; Cadmium; Complete proteome; Copper; Metal-binding;
Metal-thiolate cluster; Phosphoprotein; Polymorphism;
Reference proteome; Zinc.
CHAIN 1 61 Metallothionein-1A.
/FTId=PRO_0000197234.
REGION 1 29 Beta.
REGION 30 61 Alpha.
METAL 5 5 Divalent metal cation; cluster B.
METAL 7 7 Divalent metal cation; cluster B.
METAL 13 13 Divalent metal cation; cluster B.
METAL 15 15 Divalent metal cation; cluster B.
METAL 19 19 Divalent metal cation; cluster B.
METAL 21 21 Divalent metal cation; cluster B.
METAL 24 24 Divalent metal cation; cluster B.
METAL 26 26 Divalent metal cation; cluster B.
METAL 29 29 Divalent metal cation; cluster B.
METAL 33 33 Divalent metal cation; cluster A.
METAL 34 34 Divalent metal cation; cluster A.
METAL 36 36 Divalent metal cation; cluster A.
METAL 37 37 Divalent metal cation; cluster A.
METAL 41 41 Divalent metal cation; cluster A.
METAL 44 44 Divalent metal cation; cluster A.
METAL 48 48 Divalent metal cation; cluster A.
METAL 50 50 Divalent metal cation; cluster A.
METAL 57 57 Divalent metal cation; cluster A.
METAL 59 59 Divalent metal cation; cluster A.
METAL 60 60 Divalent metal cation; cluster A.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P11957}.
MOD_RES 58 58 Phosphoserine.
{ECO:0000250|UniProtKB:P02795}.
VARIANT 27 27 T -> N (in dbSNP:rs11640851).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:6327055}.
/FTId=VAR_060727.
VARIANT 51 51 K -> R (in dbSNP:rs8052394).
/FTId=VAR_059436.
SEQUENCE 61 AA; 6120 MW; 8FBA7C54EE8B6A13 CRC64;
MDPNCSCATG GSCTCTGSCK CKECKCTSCK KSCCSCCPMS CAKCAQGCIC KGASEKCSCC
A


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