Reviewed, UniProtKB/Swiss-Prot P02795 (MT2_HUMAN)

Names and origin

Protein names

Recommended name:
    Metallothionein-2
      Short name=MT-2
Alternative name(s):
    Metallothionein-II
      Short name=MT-II
    Metallothionein-2A

Gene names

Name:	MT2A
Synonyms:	CES1, MT2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	61 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 diversity	Polymorphism
Ligand	Metal-binding Metal-thiolate cluster Zinc
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular copper ion homeostasis Traceable author statement. Source: ProtInc
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CXorf40A	Q8TE69	1	EBI-996616,EBI-996609
PRKD1	Q15139	4	EBI-996616,EBI-1181072
SPINK7	P58062	5	EBI-996616,EBI-1182445

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Chain

1 – 61

61

Metallothionein-2

Regions

Region

1 – 29

29

Beta

Region

30 – 61

32

Alpha

Sites

Metal binding

5

1

Cluster B

Metal binding

7

1

Cluster B

Metal binding

13

1

Cluster B

Metal binding

15

1

Cluster B

Metal binding

19

1

Cluster B

Metal binding

21

1

Cluster B

Metal binding

24

1

Cluster B

Metal binding

26

1

Cluster B

Metal binding

29

1

Cluster B

Metal binding

33

1

Cluster A

Metal binding

34

1

Cluster A

Metal binding

36

1

Cluster A

Metal binding

37

1

Cluster A

Metal binding

41

1

Cluster A

Metal binding

44

1

Cluster A

Metal binding

48

1

Cluster A

Metal binding

50

1

Cluster A

Metal binding

57

1

Cluster A

Metal binding

59

1

Cluster A

Metal binding

60

1

Cluster A

Amino acid modifications

Modified residue

1

1

N-acetylmethionine

Modified residue

51

1

N6-acetyllysine

Natural variations

Natural variant

42

1

A → V

Secondary structure

1

.

.

.

.

.

.

.

.

.

61

Helix Strand Turn

Details...

Beta strand

7 – 11

5

Helix

27 – 29

3

Beta strand

35 – 37

3

Helix

42 – 44

3

Sequences

	Sequence		Length	Mass (Da)
	P02795-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 7B0A7E1F99843078	FASTA	61	6,042
	10 20 30 40 50 60 MDPNCSCAAG DSCTCAGSCK CKECKCTSCK KSCCSCCPVG CAKCAQGCIC KGASDKCSCC A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of human hepatic metallothionein." Kissling M.M., Kaegi J.H.R. FEBS Lett. 82:247-250(1977) [PubMed: 913597] [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: 7133118] [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: 6896577] [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: 2780570] [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: 1339282] [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]	Livingston R.J., Rieder M.J., Shaffer T., Bertucci C., Baier C.N., Rajkumar N., Willa H.T., Daniels M., Downing T.K., Stanaway I.B., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A. 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Kidney.
[10]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51, MASS SPECTROMETRY. Tissue: Epithelium.
[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: 2388267] [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: 1593628] [Abstract] Cited for: STRUCTURE BY NMR.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

PIR

SMHU2. A03271.
I63131.

RefSeq

NP_005944.1.

UniGene

Hs.647371

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MHU	NMR	-	A	31-61	[»]
2MHU	NMR	-	A	1-30	[»]

SMR

P02795. Positions 1-61.

ModBase

Search...

Protein-protein interaction databases

IntAct

P02795.

Genome annotation databases

Ensembl

ENSG00000125148. Homo sapiens. [Contig view]

GeneID

4502.

KEGG

hsa:4502.

Organism-specific databases

H-InvDB

HIX0031527.
HIX0057369.
HIX0059625.

HGNC

HGNC:7406. MT2A.

MIM

156360. gene.

PharmGKB

PA31214.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P02795.

HOVERGEN

P02795.

Gene expression databases

ArrayExpress

P02795.

CleanEx

HS_CES1.
HS_MT2A.

GermOnline

ENSG00000125148. Homo sapiens.

Family and domain databases

InterPro

IPR002400. GF_cysknot.
IPR003019. Metallothionein_sfam_euk.
IPR000006. Metallothionein_vert.
[Graphical view]

Gene3D

G3DSA:4.10.10.10. Metallothionein_vert. 1 hit.

PANTHER

PTHR23299. Metallothionein_vert. 1 hit.

Pfam

PF00131. Metallothio. 1 hit.
[Graphical view]

PRINTS

PR00438. GFCYSKNOT.
PR00860. MTVERTEBRATE.

PROSITE

PS00203. METALLOTHIONEIN_VRT. 1 hit.
[Graphical view]

ProDom

P02795.
[Graphical view] [Entries sharing at least one domain]

BLOCKS

Search...

Other Resources

LinkHub

P02795.

SOURCE

Search...

ProtoNet

Search...

Entry information

Entry name

MT2_HUMAN

Accession

Primary (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 22, 2008
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)