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P02795 (MT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Metallothionein-2

Short name=MT-2
Alternative name(s):
Metallothionein-2A
Metallothionein-II
Short name=MT-II
Gene names
Name:MT2A
Synonyms:CES1, MT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length61 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

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.

Miscellaneous

This metallothionein binds zinc.

Sequence similarities

Belongs to the metallothionein superfamily. Type 1 family.

Ontologies

Keywords
   Coding sequence diversityPolymorphism
   LigandMetal-binding
Metal-thiolate cluster
Zinc
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular copper ion homeostasis

Traceable author statement PubMed 6719135. Source: ProtInc

cellular response to drug

Inferred from direct assay PubMed 19536566. Source: UniProtKB

cellular response to erythropoietin

Inferred from expression pattern PubMed 11168427. Source: UniProtKB

cellular response to interleukin-3

Inferred from expression pattern PubMed 11168427. Source: UniProtKB

cellular response to zinc ion

Inferred from expression pattern PubMed 11168427. Source: UniProtKB

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

negative regulation of growth

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functiondrug binding

Inferred from direct assay PubMed 19536566. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 12646258PubMed 12970870PubMed 14550308PubMed 15541360PubMed 16778767. Source: IntAct

zinc ion binding

Inferred from direct assay PubMed 19536566. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6161Metallothionein-2
PRO_0000197245

Regions

Region1 – 2929Beta
Region30 – 6132Alpha

Sites

Metal binding51Divalent metal cation; cluster B Ref.11
Metal binding71Divalent metal cation; cluster B Ref.11
Metal binding131Divalent metal cation; cluster B Ref.11
Metal binding151Divalent metal cation; cluster B Ref.11
Metal binding191Divalent metal cation; cluster B
Metal binding211Divalent metal cation; cluster B
Metal binding241Divalent metal cation; cluster B
Metal binding261Divalent metal cation; cluster B
Metal binding291Divalent metal cation; cluster B
Metal binding331Divalent metal cation; cluster A
Metal binding341Divalent metal cation; cluster A
Metal binding361Divalent metal cation; cluster A
Metal binding371Divalent metal cation; cluster A
Metal binding411Divalent metal cation; cluster A
Metal binding441Divalent metal cation; cluster A
Metal binding481Divalent metal cation; cluster A
Metal binding501Divalent metal cation; cluster A
Metal binding571Divalent metal cation; cluster A
Metal binding591Divalent metal cation; cluster A
Metal binding601Divalent metal cation; cluster A

Amino acid modifications

Modified residue11N-acetylmethionine Ref.1 Ref.10

Natural variations

Natural variant421A → V. Ref.8
Corresponds to variant rs35109646 [ dbSNP | Ensembl ].
VAR_025840

Secondary structure

......... 61
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02795 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 7B0A7E1F99843078

FASTA616,042
        10         20         30         40         50         60 
MDPNCSCAAG DSCTCAGSCK CKECKCTSCK KSCCSCCPVG CAKCAQGCIC KGASDKCSCC 


A 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of human hepatic metallothionein."
Kissling M.M., Kaegi J.H.R.
FEBS Lett. 82:247-250(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE.
Tissue: Liver.
[2]"Human metallothionein genes -- primary structure of the metallothionein-II gene and a related processed gene."
Karin M., Richards R.I.
Nature 299:797-802(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Human metallothionein genes: molecular cloning and sequence analysis of the mRNA."
Karin M., Richards R.I.
Nucleic Acids Res. 10:3165-3173(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Changes in brain gene expression shared by scrapie and Alzheimer disease."
Duguid J.R., Bohmont C.W., Liu N.G., Tourtellotte W.W.
Proc. Natl. Acad. Sci. U.S.A. 86:7260-7264(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Expression of human metallothionein-II fusion protein in Escherichia coli."
Yamazaki S., Nakanishi M., Hamamoto T., Hirata H., Ebihara A., Tokue A., Kagawa Y.
Biochem. Int. 28:451-460(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]"Cloning and sequencing a novel metallothionein 1 isoform expressed in human reticulocytes."
Lambert E., Kille P., Kay J., Swaminathan R.
Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[7]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]NIEHS SNPs program
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-42.
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Kidney.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Three-dimensional structure of human [113Cd7]metallothionein-2 in solution determined by nuclear magnetic resonance spectroscopy."
Messerle B.A., Schaeffer A., Vasak M., Kaegi J.H.R., Wuethrich K.
J. Mol. Biol. 214:765-779(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[12]"Comparison of the solution conformations of human [Zn7]-metallothionein-2 and [Cd7]-metallothionein-2 using nuclear magnetic resonance spectroscopy."
Messerle B.A., Schaeffer A., Vasak M., Kaegi J.H.R., Wuethrich K.
J. Mol. Biol. 225:433-443(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J00271 Genomic DNA. Translation: AAA59583.1.
V00594 mRNA. Translation: CAA23841.1.
M26637 mRNA. Translation: AAA59584.1. Sequence problems.
S52379 mRNA. Translation: AAB24908.1.
X97260 mRNA. Translation: CAA65915.1.
BT007315 mRNA. Translation: AAP35979.1.
DQ370420 Genomic DNA. Translation: ABC79300.1.
BC007034 mRNA. Translation: AAH07034.1.
BC070289 mRNA. Translation: AAH70289.1.
CCDSCCDS10763.1.
PIRSMHU2. A03271.
I63131.
RefSeqNP_005944.1. NM_005953.3.
UniGeneHs.534330.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MHUNMR-A31-61[»]
2MHUNMR-A1-30[»]
ProteinModelPortalP02795.
SMRP02795. Positions 1-61.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110608. 13 interactions.
DIPDIP-35232N.
IntActP02795. 9 interactions.
MINTMINT-2836376.
STRING9606.ENSP00000245185.

PTM databases

PhosphoSiteP02795.

Proteomic databases

MaxQBP02795.
PRIDEP02795.

Protocols and materials databases

DNASU4502.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000245185; ENSP00000245185; ENSG00000125148.
GeneID4502.
KEGGhsa:4502.
UCSCuc002ejh.3. human.

Organism-specific databases

CTD4502.
GeneCardsGC16P056642.
HGNCHGNC:7406. MT2A.
MIM156360. gene.
neXtProtNX_P02795.
PharmGKBPA31214.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000236262.
HOVERGENHBG094456.
InParanoidP02795.
KOK14739.
OMAFLNVFAG.
OrthoDBEOG7PZS1X.
PhylomeDBP02795.
TreeFamTF336054.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP02795.
BgeeP02795.
CleanExHS_CES1.
HS_MT2A.
GenevestigatorP02795.

Family and domain databases

Gene3D4.10.10.10. 1 hit.
InterProIPR017854. Metalthion_dom.
IPR023587. Metalthion_dom_vert.
IPR003019. Metalthion_sfam_euk.
IPR000006. Metalthion_vert.
IPR018064. Metalthion_vert_metal_BS.
[Graphical view]
PANTHERPTHR23299. PTHR23299. 1 hit.
PfamPF00131. Metallothio. 1 hit.
[Graphical view]
PRINTSPR00860. MTVERTEBRATE.
SUPFAMSSF57868. SSF57868. 1 hit.
PROSITEPS00203. METALLOTHIONEIN_VRT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMT2A. human.
EvolutionaryTraceP02795.
GeneWikiMetallothionein_2A.
GenomeRNAi4502.
NextBio17406.
PROP02795.
SOURCESearch...

Entry information

Entry nameMT2_HUMAN
AccessionPrimary (citable) accession number: P02795
Secondary accession number(s): Q14823, Q2HXR9, Q53XT9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Metallothioneins

Classification of metallothioneins and list of entries

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM