GenomeNet

Database: UniProt
Entry: MT1M_HUMAN
LinkDB: MT1M_HUMAN
Original site: MT1M_HUMAN 
ID   MT1M_HUMAN              Reviewed;          61 AA.
AC   Q8N339; Q8TDN3;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 2.
DT   29-OCT-2014, entry version 101.
DE   RecName: Full=Metallothionein-1M;
DE            Short=MT-1M;
DE   AltName: Full=Metallothionein-IM;
DE            Short=MT-IM;
GN   Name=MT1M; Synonyms=MT1K;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LYS-20.
RA   Li N.G., Yu L., Zhao S.Y.;
RT   "Cloning of a new human cDNA homologous to monkey metallothionein.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Wang J., Yu L., Zhao S.;
RT   "Cloning of a novel member of the MT gene family -- MT1M.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-20.
RC   TISSUE=Colon;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Metallothioneins have a high content of cysteine
CC       residues that bind various heavy metals; these proteins are
CC       transcriptionally regulated by both heavy metals and
CC       glucocorticoids.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- DOMAIN: Class I metallothioneins contain 2 metal-binding domains:
CC       four divalent ions are chelated within cluster A of the alpha
CC       domain and are coordinated via cysteinyl thiolate bridges to 11
CC       cysteine ligands. Cluster B, the corresponding region within the
CC       beta domain, can ligate three divalent ions to 9 cysteines.
CC   -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 1
CC       family. {ECO:0000305}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF136177; AAP97267.1; -; mRNA.
DR   EMBL; AF348671; AAL83902.1; -; Genomic_DNA.
DR   EMBL; BC028280; AAH28280.1; -; mRNA.
DR   EMBL; BC103841; AAI03842.1; -; mRNA.
DR   CCDS; CCDS42166.1; -.
DR   RefSeq; NP_789846.1; NM_176870.2.
DR   UniGene; Hs.647370; -.
DR   ProteinModelPortal; Q8N339; -.
DR   SMR; Q8N339; 1-61.
DR   BioGrid; 110605; 2.
DR   IntAct; Q8N339; 1.
DR   STRING; 9606.ENSP00000369146; -.
DR   DMDM; 88913543; -.
DR   PaxDb; Q8N339; -.
DR   PRIDE; Q8N339; -.
DR   DNASU; 4499; -.
DR   Ensembl; ENST00000379818; ENSP00000369146; ENSG00000205364.
DR   GeneID; 4499; -.
DR   KEGG; hsa:4499; -.
DR   UCSC; uc002ejn.3; human.
DR   CTD; 4499; -.
DR   GeneCards; GC16P056666; -.
DR   HGNC; HGNC:14296; MT1M.
DR   neXtProt; NX_Q8N339; -.
DR   PharmGKB; PA142671312; -.
DR   eggNOG; NOG278174; -.
DR   GeneTree; ENSGT00730000110883; -.
DR   HOGENOM; HOG000236262; -.
DR   HOVERGEN; HBG009063; -.
DR   InParanoid; Q8N339; -.
DR   KO; K14739; -.
DR   OMA; CEHAYIA; -.
DR   OrthoDB; EOG7PZS1X; -.
DR   PhylomeDB; Q8N339; -.
DR   TreeFam; TF336054; -.
DR   GeneWiki; MT1M; -.
DR   GenomeRNAi; 4499; -.
DR   NextBio; 17395; -.
DR   PRO; PR:Q8N339; -.
DR   Bgee; Q8N339; -.
DR   CleanEx; HS_MT1M; -.
DR   ExpressionAtlas; Q8N339; baseline and differential.
DR   Genevestigator; Q8N339; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0071294; P:cellular response to zinc ion; ISS:UniProtKB.
DR   GO; GO:0045926; P:negative regulation of growth; ISS:UniProtKB.
DR   Gene3D; 4.10.10.10; -; 1.
DR   InterPro; IPR017854; Metalthion_dom.
DR   InterPro; IPR023587; Metalthion_dom_vert.
DR   InterPro; IPR003019; Metalthion_sfam_euk.
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   2: Evidence at transcript level;
KW   Cadmium; Complete proteome; Copper; Metal-binding;
KW   Metal-thiolate cluster; Polymorphism; Reference proteome; Zinc.
FT   CHAIN         1     61       Metallothionein-1M.
FT                                /FTId=PRO_0000223180.
FT   REGION        1     29       Beta.
FT   REGION       30     61       Alpha.
FT   METAL         5      5       Divalent metal cation; cluster B.
FT   METAL         7      7       Divalent metal cation; cluster B.
FT   METAL        13     13       Divalent metal cation; cluster B.
FT   METAL        15     15       Divalent metal cation; cluster B.
FT   METAL        19     19       Divalent metal cation; cluster B.
FT   METAL        21     21       Divalent metal cation; cluster B.
FT   METAL        24     24       Divalent metal cation; cluster B.
FT   METAL        26     26       Divalent metal cation; cluster B.
FT   METAL        29     29       Divalent metal cation; cluster B.
FT   METAL        33     33       Divalent metal cation; cluster A.
FT   METAL        34     34       Divalent metal cation; cluster A.
FT   METAL        36     36       Divalent metal cation; cluster A.
FT   METAL        37     37       Divalent metal cation; cluster A.
FT   METAL        41     41       Divalent metal cation; cluster A.
FT   METAL        44     44       Divalent metal cation; cluster A.
FT   METAL        48     48       Divalent metal cation; cluster A.
FT   METAL        50     50       Divalent metal cation; cluster A.
FT   METAL        57     57       Divalent metal cation; cluster A.
FT   METAL        59     59       Divalent metal cation; cluster A.
FT   METAL        60     60       Divalent metal cation; cluster A.
FT   VARIANT      20     20       T -> K (in dbSNP:rs1827210).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|Ref.1}.
FT                                /FTId=VAR_025310.
SQ   SEQUENCE   61 AA;  6110 MW;  754753ED088411CE CRC64;
     MDPNCSCTTG VSCACTGSCT CKECKCTSCK KSCCSCCPVG CAKCAHGCVC KGTLENCSCC
     A
//
DBGET integrated database retrieval system