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P80297 (MT1X_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Metallothionein-1X
Short name=MT-1X
Alternative name(s):
Metallothionein-IX
Short name=MT-IX
Gene names
Name:MT1X
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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.

Subunit structure

Monomer.

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.

Sequence similarities

Belongs to the metallothionein superfamily. Type 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6161Metallothionein-1X
PRO_0000197243

Regions

Region1 – 2929Beta
Region30 – 6132Alpha

Sites

Metal binding51Divalent metal cation; cluster B
Metal binding71Divalent metal cation; cluster B
Metal binding131Divalent metal cation; cluster B
Metal binding151Divalent metal cation; cluster B
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.6 Ref.7
Modified residue81Phosphoserine Ref.7

Sequences

Sequence LengthMass (Da)Tools
P80297 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 381966F942E986B2

FASTA616,068
        10         20         30         40         50         60 
MDPNCSCSPV GSCACAGSCK CKECKCTSCK KSCCSCCPVG CAKCAQGCIC KGTSDKCSCC 


A

« Hide

References

« Hide 'large scale' references
[1]Soumillion A., van Weyenbergh J., de Ley M.
Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]Hunziker P.E.
Submitted (NOV-1993) to UniProtKB
Cited for: PROTEIN SEQUENCE.
Tissue: Liver.
[3]"Characterisation of six additional human metallothionein genes."
Stennard F.A., Holloway A.F., Hamilton J., West A.K.
Biochim. Biophys. Acta 1218:357-365(1994) [PubMed: 8049263] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Placenta.
[4]"The sequence and analysis of duplication-rich human chromosome 16."
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. expand/collapse author list , 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.
Nature 432:988-994(2004) [PubMed: 15616553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Colon.
[6]"Induction by zinc of specific metallothionein isoforms in human monocytes."
Pauwels M., van Weyenbergh J., Soumillion A., Proost P., Ley M.
Eur. J. Biochem. 220:105-110(1994) [PubMed: 8119276] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-31.
[7]"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: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X76717 mRNA. Translation: CAA54136.1.
X65607 Genomic DNA. Translation: CAA46557.1.
AC026461 Genomic DNA. No translation available.
BC032338 mRNA. Translation: AAH32338.1.
S68956 mRNA. Translation: AAB30084.1.
IPIIPI00008753.
PIRS47652.
RefSeqNP_005943.1. NM_005952.3.
UniGeneHs.374950.

3D structure databases

ProteinModelPortalP80297.
SMRP80297. Positions 1-61.
ModBaseSearch...

Protein-protein interaction databases

STRINGP80297.

PTM databases

PhosphoSiteP80297.

Polymorphism databases

DMDM462637.

Proteomic databases

PRIDEP80297.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000394485; ENSP00000377995; ENSG00000187193.
GeneID4501.
KEGGhsa:4501.
UCSCuc002ejy.1. human.

Organism-specific databases

CTD4501.
GeneCardsGC16P056711.
H-InvDBHIX0021646.
HGNCHGNC:7405. MT1X.
MIM156359. gene.
neXtProtNX_P80297.
PharmGKBPA31213.
GenAtlasSearch...

Phylogenomic databases

eggNOGmaNOG21730.
HOVERGENHBG094464.
OrthoDBEOG46WZB6.

Gene expression databases

ArrayExpressP80297.
BgeeP80297.
CleanExHS_MT1X.
GenevestigatorP80297.
GermOnlineENSG00000187193. Homo sapiens.

Family and domain databases

InterProIPR017854. Metalthion_dom.
IPR023587. Metalthion_dom_vert.
IPR003019. Metalthion_sfam_euk.
IPR000006. Metalthion_vert.
IPR018064. Metalthion_vert_metal_BS.
[Graphical view]
Gene3DG3DSA:4.10.10.10. Metallothionein_vert. 1 hit.
KOK14739.
PANTHERPTHR23299. Metallothionein_vert. 1 hit.
PfamPF00131. Metallothio. 1 hit.
[Graphical view]
PRINTSPR00860. MTVERTEBRATE.
SUPFAMSSF57868. Metallothionein_sfam. 1 hit.
PROSITEPS00203. METALLOTHIONEIN_VRT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio17402.
SOURCESearch...

Entry information

Entry nameMT1X_HUMAN
AccessionPrimary (citable) accession number: P80297
Secondary accession number(s): A8MUC7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: January 25, 2012
This is version 97 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

Metallothioneins

Classification of metallothioneins and list of entries

Human chromosome 16

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

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents