Details for: SLC31A1

Gene ID: 1317

Symbol: SLC31A1

Ensembl ID: ENSG00000136868

Description: solute carrier family 31 member 1

Associated with

Other Information

Genular Protein ID: 2779579040

Symbol: COPT1_HUMAN

Name: Solute carrier family 31 member 1

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 9207117

Title: hCTR1: a human gene for copper uptake identified by complementation in yeast.

PubMed ID: 9207117

DOI: 10.1073/pnas.94.14.7481

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 17974005

Title: The full-ORF clone resource of the German cDNA consortium.

PubMed ID: 17974005

DOI: 10.1186/1471-2164-8-399

PubMed ID: 15164053

Title: DNA sequence and analysis of human chromosome 9.

PubMed ID: 15164053

DOI: 10.1038/nature02465

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 12023893

Title: Biochemical characterization and subcellular localization of human copper transporter 1 (hCTR1).

PubMed ID: 12023893

DOI: 10.1042/bj20011803

PubMed ID: 11734551

Title: Biochemical characterization of the human copper transporter Ctr1.

PubMed ID: 11734551

DOI: 10.1074/jbc.m104728200

PubMed ID: 15326162

Title: Cisplatin stabilizes a multimeric complex of the human Ctr1 copper transporter: requirement for the extracellular methionine-rich clusters.

PubMed ID: 15326162

DOI: 10.1074/jbc.m407777200

PubMed ID: 16135512

Title: The mechanism of copper uptake mediated by human CTR1: a mutational analysis.

PubMed ID: 16135512

DOI: 10.1074/jbc.m508822200

PubMed ID: 17525160

Title: O-linked glycosylation at threonine 27 protects the copper transporter hCTR1 from proteolytic cleavage in mammalian cells.

PubMed ID: 17525160

DOI: 10.1074/jbc.m701806200

PubMed ID: 19740744

Title: Copper-dependent recycling of hCTR1, the human high affinity copper transporter.

PubMed ID: 19740744

DOI: 10.1074/jbc.m109.000166

PubMed ID: 20451502

Title: The role of the N-terminus of mammalian copper transporter 1 in the cellular accumulation of cisplatin.

PubMed ID: 20451502

DOI: 10.1016/j.bcp.2010.04.030

PubMed ID: 20569931

Title: Ctr1 transports silver into mammalian cells.

PubMed ID: 20569931

DOI: 10.1016/j.jtemb.2010.01.009

PubMed ID: 23658018

Title: Rate and regulation of copper transport by human copper transporter 1 (hCTR1).

PubMed ID: 23658018

DOI: 10.1074/jbc.m112.442426

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24167251

Title: Ctr2 regulates biogenesis of a cleaved form of mammalian Ctr1 metal transporter lacking the copper- and cisplatin-binding ecto-domain.

PubMed ID: 24167251

DOI: 10.1073/pnas.1311749110

PubMed ID: 24837030

Title: Probing the structural flexibility of the human copper metallochaperone Atox1 dimer and its interaction with the CTR1 c-terminal domain.

PubMed ID: 24837030

DOI: 10.1021/jp412589b

PubMed ID: 26205368

Title: The copper transporter 1 (CTR1) is required to maintain the stability of copper transporter 2 (CTR2).

PubMed ID: 26205368

DOI: 10.1039/c5mt00131e

PubMed ID: 26745413

Title: The C-Terminus of Human Copper Importer Ctr1 Acts as a Binding Site and Transfers Copper to Atox1.

PubMed ID: 26745413

DOI: 10.1016/j.bpj.2015.11.016

PubMed ID: 27143361

Title: Cathepsin Protease Controls Copper and Cisplatin Accumulation via Cleavage of the Ctr1 Metal-binding Ectodomain.

PubMed ID: 27143361

DOI: 10.1074/jbc.m116.731281

PubMed ID: 26945057

Title: Dynamic internalization and recycling of a metal ion transporter: Cu homeostasis and CTR1, the human Cu(+) uptake system.

PubMed ID: 26945057

DOI: 10.1242/jcs.173351

PubMed ID: 30489586

Title: The N-terminal 14-mer model peptide of human Ctr1 can collect Cu(ii) from albumin. Implications for copper uptake by Ctr1.

PubMed ID: 30489586

DOI: 10.1039/c8mt00274f

PubMed ID: 31292775

Title: Copper-zinc superoxide dismutase (Sod1) activation terminates interaction between its copper chaperone (Ccs) and the cytosolic metal-binding domain of the copper importer Ctr1.

PubMed ID: 31292775

DOI: 10.1007/s10534-019-00206-3

PubMed ID: 32914794

Title: How trimerization of CTR1 N-terminal model peptides tunes Cu-binding and redox-chemistry.

PubMed ID: 32914794

DOI: 10.1039/d0cc04693k

PubMed ID: 33294387

Title: Promotion of cadmium uptake and cadmium-induced toxicity by the copper transporter CTR1 in HepG2 and ZFL cells.

PubMed ID: 33294387

DOI: 10.1016/j.toxrep.2020.11.005

PubMed ID: 35027734

Title: Cysteine oxidation of copper transporter CTR1 drives VEGFR2 signalling and angiogenesis.

PubMed ID: 35027734

DOI: 10.1038/s41556-021-00822-7

PubMed ID: 35601835

Title: Multinuclear Metal-Binding Ability of the N-Terminal Region of Human Copper Transporter Ctr1: Dependence Upon pH and Metal Oxidation State.

PubMed ID: 35601835

DOI: 10.3389/fmolb.2022.897621

PubMed ID: 16501047

Title: Projection structure of the human copper transporter CTR1 at 6-A resolution reveals a compact trimer with a novel channel-like architecture.

PubMed ID: 16501047

DOI: 10.1073/pnas.0509929103

PubMed ID: 22615137

Title: Structural insights into the transmembrane domains of human copper transporter 1.

PubMed ID: 22615137

DOI: 10.1002/psc.2415

PubMed ID: 35913762

Title: Newly identified disorder of copper metabolism caused by variants in CTR1, a high-affinity copper transporter.

PubMed ID: 35913762

DOI: 10.1093/hmg/ddac156

PubMed ID: 36562171

Title: Fatal congenital copper transport defect caused by a homozygous likely pathogenic variant of SLC31A1.

PubMed ID: 36562171

DOI: 10.1111/cge.14289

Sequence Information:

  • Length: 190
  • Mass: 21091
  • Checksum: 1E08FBAB72A9C014
  • Sequence:
  • MDHSHHMGMS YMDSNSTMQP SHHHPTTSAS HSHGGGDSSM MMMPMTFYFG FKNVELLFSG 
    LVINTAGEMA GAFVAVFLLA MFYEGLKIAR ESLLRKSQVS IRYNSMPVPG PNGTILMETH 
    KTVGQQMLSF PHLLQTVLHI IQVVISYFLM LIFMTYNGYL CIAVAAGAGT GYFLFSWKKA 
    VVVDITEHCH

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.