TMX3 : Further reading Wikipedia, the free encyclopedia

TMX3

Gene of the species Homo sapiens

TMX3

Identifiers

Aliases

TMX3, PDIA13, TXNDC10, thioredoxin related transmembrane protein 3

External IDs

OMIM: 616102; MGI: 2442418; HomoloGene: 10381; GeneCards: TMX3; OMA:TMX3 - orthologs

Gene location (Mouse)

Chr.	Chromosome 18 (mouse)^[1]

Band	18\|18 E4	Start	90,528,278 bp^[1]
Band	18\|18 E4	End	90,561,391 bp^[1]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

n/a

Top expressed in

otolith organ

utricle

hand

superior cervical ganglion

olfactory epithelium

endothelial cell of lymphatic vessel

supraoptic nucleus

Epithelium of choroid plexus

substantia nigra

dorsomedial hypothalamic nucleus

BioGPS


More reference expression data

Gene ontology
Molecular function	protein binding isomerase activity thiol oxidase activity protein disulfide isomerase activity
Cellular component	integral component of membrane cell surface endoplasmic reticulum membrane endoplasmic reticulum membrane platelet alpha granule membrane plasma membrane
Biological process	peptidyl-cysteine oxidation protein folding response to endoplasmic reticulum stress cell redox homeostasis platelet degranulation
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


54495


67988

Ensembl


ENSG00000166479


ENSMUSG00000024614

UniProt


Q96JJ7


Q8BXZ1

RefSeq (mRNA)


NM_019022


NM_198295

RefSeq (protein)

NP_061895 NP_001337441 NP_001337442 NP_001337443 NP_001337444
NP_001337445 NP_001337446


NP_938037

Location (UCSC)

n/a

Chr 18: 90.53 – 90.56 Mb

PubMed search

^[2]

^[3]

Wikidata

View/Edit Human

View/Edit Mouse

Protein disulfide-isomerase TMX3 is an enzyme that in humans is encoded by the TMX3 gene.^[4]^[5]

References

^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000024614 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Haugstetter J, Blicher T, Ellgaard L (March 2005). "Identification and characterization of a novel thioredoxin-related transmembrane protein of the endoplasmic reticulum". The Journal of Biological Chemistry. 280 (9): 8371–8380. doi:10.1074/jbc.M413924200. PMID 15623505.
^ "Entrez Gene: TXNDC10 thioredoxin domain containing 10".

Hartley JL, Temple GF, Brasch MA (November 2000). "DNA cloning using in vitro site-specific recombination". Genome Research. 10 (11): 1788–1795. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, et al. (March 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Research. 11 (3): 422–435. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
Nagase T, Nakayama M, Nakajima D, Kikuno R, Ohara O (April 2001). "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 8 (2): 85–95. doi:10.1093/dnares/8.2.85. PMID 11347906.
Wiemann S, Arlt D, Huber W, Wellenreuther R, Schleeger S, Mehrle A, et al. (October 2004). "From ORFeome to biology: a functional genomics pipeline". Genome Research. 14 (10B): 2136–2144. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
Mehrle A, Rosenfelder H, Schupp I, del Val C, Arlt D, Hahne F, et al. (January 2006). "The LIFEdb database in 2006". Nucleic Acids Research. 34 (Database issue): D415–D418. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.
Haugstetter J, Maurer MA, Blicher T, Pagac M, Wider G, Ellgaard L (November 2007). "Structure-function analysis of the endoplasmic reticulum oxidoreductase TMX3 reveals interdomain stabilization of the N-terminal redox-active domain". The Journal of Biological Chemistry. 282 (46): 33859–33867. doi:10.1074/jbc.M706442200. PMID 17881353.