HUMAN:CALX

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	CANX
Protein Name(s)	Calnexin IP90 Major histocompatibility complex class I antigen-binding protein p88 p90
External Links
UniProt	P27824
EMBL	L10284 L18887 M94859 M98452 AK294702 AK304420 AK312334 AC113426 AC136604 CH471165 CH471165 CH471165 BC003552 BC042843 AJ271880
CCDS	CCDS4447.1
PIR	A46164 A46673 I53260
RefSeq	NP_001019820.1 NP_001737.1 XP_011532967.1
UniGene	Hs.567968
ProteinModelPortal	P27824
SMR	P27824
BioGrid	107271
DIP	DIP-457N
IntAct	P27824
MINT	MINT-5000964
STRING	9606.ENSP00000247461
BindingDB	P27824
ChEMBL	CHEMBL2719
DrugBank	DB00025 DB00031
PhosphoSite	P27824
BioMuta	CANX
DMDM	543920
MaxQB	P27824
PaxDb	P27824
PeptideAtlas	P27824
PRIDE	P27824
DNASU	821
Ensembl	ENST00000247461 ENST00000452673 ENST00000504734
GeneID	821
KEGG	hsa:821
UCSC	uc003mkk.3 uc011dgp.2
CTD	821
GeneCards	GC05P179105
HGNC	HGNC:1473
HPA	CAB004738 HPA009433 HPA009696
MIM	114217
neXtProt	NX_P27824
PharmGKB	PA26055
eggNOG	NOG305105
GeneTree	ENSGT00430000030841
HOGENOM	HOG000192436
HOVERGEN	HBG005407
InParanoid	P27824
KO	K08054
OMA	VDDWASD
OrthoDB	EOG77126Z
PhylomeDB	P27824
TreeFam	TF300618
Reactome	REACT_121399 REACT_23810 REACT_6277 REACT_75795
ChiTaRS	CANX
GeneWiki	Calnexin
GenomeRNAi	821
NextBio	3360
PRO	PR:P27824
Proteomes	UP000005640
Bgee	P27824
CleanEx	HS_CANX
ExpressionAtlas	P27824
Genevisible	P27824
GO	GO:0030424 GO:0032839 GO:0043197 GO:0005783 GO:0005788 GO:0005789 GO:0044233 GO:0070062 GO:0071556 GO:0042470 GO:0016020 GO:0043209 GO:0043025 GO:0043234 GO:0005840 GO:0005791 GO:0005790 GO:0005509 GO:0030246 GO:0044822 GO:0007568 GO:0019886 GO:0002474 GO:0044267 GO:0061077 GO:0072583 GO:0043687 GO:0006457 GO:0034975 GO:0018279 GO:0009306 GO:0048488
Gene3D	2.10.250.10 2.60.120.200
InterPro	IPR001580 IPR018124 IPR009033 IPR013320
PANTHER	PTHR11073
Pfam	PF00262
PRINTS	PR00626
SUPFAM	SSF49899 SSF63887
PROSITE	PS00803 PS00804 PS00805

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
part_of	GO:0005783	endoplasmic reticulum	PMID:24454821^[1]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	PMID:23814182^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
NOT\|part_of	GO:0070062	extracellular exosome	PMID:21235781^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:19946888^[5]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:24263861^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:8136357^[7]	ECO:0000303	author statement without traceable support used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0072583	clathrin-dependent endocytosis	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35564	P	Seeded From UniProt	complete
involved_in	GO:0048488	synaptic vesicle endocytosis	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35564	P	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22681889^[8]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22658674^[9]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:23826168^[10]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0044233	mitochondria-associated endoplasmic reticulum membrane	PMID:23455425^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	PMID:20531390^[12]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	PMID:19723497^[13]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:22572157^[14]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:21190736^[15]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:18458083^[16]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:14966132^[17]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0072583	clathrin-dependent endocytosis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35564 ensembl:ENSMUSP00000137440	P	Seeded From UniProt	complete
involved_in	GO:0048488	synaptic vesicle endocytosis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35564 ensembl:ENSMUSP00000137440	P	Seeded From UniProt	complete
part_of	GO:0044322	endoplasmic reticulum quality control compartment	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35564 ensembl:ENSMUSP00000137440	C	Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35564 ensembl:ENSMUSP00000137440	C	Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35564 ensembl:ENSMUSP00000137440	C	Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35564 ensembl:ENSMUSP00000137440	C	Seeded From UniProt	complete
part_of	GO:0099059	integral component of presynaptic active zone membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35565 ensembl:ENSRNOP00000040859	C	Seeded From UniProt	complete
part_of	GO:0099055	integral component of postsynaptic membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35565 ensembl:ENSRNOP00000040859	C	Seeded From UniProt	complete
part_of	GO:0098978	glutamatergic synapse	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35565 ensembl:ENSRNOP00000040859	C	Seeded From UniProt	complete
part_of	GO:0043197	dendritic spine	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35565 ensembl:ENSRNOP00000040859	C	Seeded From UniProt	complete
part_of	GO:0043025	neuronal cell body	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35565 ensembl:ENSRNOP00000040859	C	Seeded From UniProt	complete
enables	GO:0035255	ionotropic glutamate receptor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35565 ensembl:ENSRNOP00000040859	F	Seeded From UniProt	complete
enables	GO:0034185	apolipoprotein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35565 ensembl:ENSRNOP00000040859	F	Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35565 ensembl:ENSRNOP00000040859	C	Seeded From UniProt	complete
part_of	GO:0032839	dendrite cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35565 ensembl:ENSRNOP00000040859	C	Seeded From UniProt	complete
part_of	GO:0030424	axon	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35565 ensembl:ENSRNOP00000040859	C	Seeded From UniProt	complete
involved_in	GO:0007568	aging	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35565 ensembl:ENSRNOP00000040859	P	Seeded From UniProt	complete
part_of	GO:0005840	ribosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35565 ensembl:ENSRNOP00000040859	C	Seeded From UniProt	complete
part_of	GO:0005791	rough endoplasmic reticulum	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35565 ensembl:ENSRNOP00000040859	C	Seeded From UniProt	complete
part_of	GO:0005790	smooth endoplasmic reticulum	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35565 ensembl:ENSRNOP00000040859	C	Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35565 ensembl:ENSRNOP00000040859	C	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35565 ensembl:ENSRNOP00000040859	C	Seeded From UniProt	complete
enables	GO:0005509	calcium ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001580 InterPro:IPR009033 InterPro:IPR018124	F	Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001580	C	Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001580	P	Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001580	F	Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	PMID:23814182^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0034975	protein folding in endoplasmic reticulum	PMID:22013210^[18]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0009306	protein secretion	PMID:8055875^[19]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0005509	calcium ion binding	PMID:8136357^[7]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0071556	integral component of lumenal side of endoplasmic reticulum membrane	Reactome:R-HSA-983146 Reactome:R-HSA-983145	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0070757	interleukin-35-mediated signaling pathway	Reactome:R-HSA-8984722	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0070106	interleukin-27-mediated signaling pathway	Reactome:R-HSA-9020956	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0019886	antigen processing and presentation of exogenous peptide antigen via MHC class II	Reactome:R-HSA-2132295	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	Reactome:R-HSA-532668	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005788	endoplasmic reticulum lumen	Reactome:R-HSA-901047 Reactome:R-HSA-8951500 Reactome:R-HSA-8950740 Reactome:R-HSA-8950398 Reactome:R-HSA-8950387 Reactome:R-HSA-8950362 Reactome:R-HSA-8950342 Reactome:R-HSA-548890 Reactome:R-HSA-535717 Reactome:R-HSA-2213241 Reactome:R-HSA-2130478	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0002474	antigen processing and presentation of peptide antigen via MHC class I	Reactome:R-HSA-983169	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C	Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0256 UniProtKB-SubCell:SL-0095	C	Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	C	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
enables	GO:0030246	carbohydrate binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0430	F	Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0097	C	Seeded From UniProt	complete
part_of	GO:0042470	melanosome	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0161	C	Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ Zhang, C et al. (2014) Transmembrane and coiled-coil domain family 1 is a novel protein of the endoplasmic reticulum. PLoS ONE 9 e85206 PubMed GONUTS page
↑ ^2.0 ^2.1 Gosselin, P et al. (2013) Tracking a refined eIF4E-binding motif reveals Angel1 as a new partner of eIF4E. Nucleic Acids Res. 41 7783-92 PubMed GONUTS page
↑ Lässer, C et al. (2011) Human saliva, plasma and breast milk exosomes contain RNA: uptake by macrophages. J Transl Med 9 9 PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
↑ Sakata, K et al. (2013) HCV NS3 protease enhances liver fibrosis via binding to and activating TGF-β type I receptor. Sci Rep 3 3243 PubMed GONUTS page
↑ ^7.0 ^7.1 Tjoelker, LW et al. (1994) Human, mouse, and rat calnexin cDNA cloning: identification of potential calcium binding motifs and gene localization to human chromosome 5. Biochemistry 33 3229-36 PubMed GONUTS page
↑ Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page
↑ Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page
↑ Marques, PI et al. (2013) SERPINA2 is a novel gene with a divergent function from SERPINA1. PLoS ONE 8 e66889 PubMed GONUTS page
↑ Hamasaki, M et al. (2013) Autophagosomes form at ER-mitochondria contact sites. Nature 495 389-93 PubMed GONUTS page
↑ Shiwaku, H et al. (2010) Suppression of the novel ER protein Maxer by mutant ataxin-1 in Bergman glia contributes to non-cell-autonomous toxicity. EMBO J. 29 2446-60 PubMed GONUTS page
↑ Harrison, KD et al. (2009) Nogo-B receptor stabilizes Niemann-Pick type C2 protein and regulates intracellular cholesterol trafficking. Cell Metab. 10 208-18 PubMed GONUTS page
↑ Quiel, A et al. () Sensitive detection of idiotypic platelet-reactive alloantibodies by an electrical protein chip. Biosens Bioelectron 36 207-11 PubMed GONUTS page
↑ Georgel, P et al. (2011) The non-conventional MHC class I MR1 molecule controls infection by Klebsiella pneumoniae in mice. Mol. Immunol. 48 769-75 PubMed GONUTS page
↑ Cao, J et al. (2008) Molecular identification of a novel mammalian brain isoform of acyl-CoA:lysophospholipid acyltransferase with prominent ethanolamine lysophospholipid acylating activity, LPEAT2. J. Biol. Chem. 283 19049-57 PubMed GONUTS page
↑ Cao, J et al. (2004) A predominant role of acyl-CoA:monoacylglycerol acyltransferase-2 in dietary fat absorption implicated by tissue distribution, subcellular localization, and up-regulation by high fat diet. J. Biol. Chem. 279 18878-86 PubMed GONUTS page
↑ Hetz, C et al. (2011) The unfolded protein response: integrating stress signals through the stress sensor IRE1α. Physiol. Rev. 91 1219-43 PubMed GONUTS page
↑ Honoré, B et al. () The molecular chaperones HSP28, GRP78, endoplasmin, and calnexin exhibit strikingly different levels in quiescent keratinocytes as compared to their proliferating normal and transformed counterparts: cDNA cloning and expression of calnexin. Electrophoresis 15 482-90 PubMed GONUTS page

[PMID:24454821-1] Zhang, C et al. (2014) Transmembrane and coiled-coil domain family 1 is a novel protein of the endoplasmic reticulum. PLoS ONE 9 e85206 PubMed GONUTS page

[PMID:23814182-2] 2.0 ^2.1 Gosselin, P et al. (2013) Tracking a refined eIF4E-binding motif reveals Angel1 as a new partner of eIF4E. Nucleic Acids Res. 41 7783-92 PubMed GONUTS page

[PMID:21235781-3] Lässer, C et al. (2011) Human saliva, plasma and breast milk exosomes contain RNA: uptake by macrophages. J Transl Med 9 9 PubMed GONUTS page

[PMID:23533145-4] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:19946888-5] Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page

[PMID:24263861-6] Sakata, K et al. (2013) HCV NS3 protease enhances liver fibrosis via binding to and activating TGF-β type I receptor. Sci Rep 3 3243 PubMed GONUTS page

[PMID:8136357-7] 7.0 ^7.1 Tjoelker, LW et al. (1994) Human, mouse, and rat calnexin cDNA cloning: identification of potential calcium binding motifs and gene localization to human chromosome 5. Biochemistry 33 3229-36 PubMed GONUTS page

[PMID:22681889-8] Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page

[PMID:22658674-9] Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page

[PMID:23826168-10] Marques, PI et al. (2013) SERPINA2 is a novel gene with a divergent function from SERPINA1. PLoS ONE 8 e66889 PubMed GONUTS page

[PMID:23455425-11] Hamasaki, M et al. (2013) Autophagosomes form at ER-mitochondria contact sites. Nature 495 389-93 PubMed GONUTS page

[PMID:20531390-12] Shiwaku, H et al. (2010) Suppression of the novel ER protein Maxer by mutant ataxin-1 in Bergman glia contributes to non-cell-autonomous toxicity. EMBO J. 29 2446-60 PubMed GONUTS page

[PMID:19723497-13] Harrison, KD et al. (2009) Nogo-B receptor stabilizes Niemann-Pick type C2 protein and regulates intracellular cholesterol trafficking. Cell Metab. 10 208-18 PubMed GONUTS page

[PMID:22572157-14] Quiel, A et al. () Sensitive detection of idiotypic platelet-reactive alloantibodies by an electrical protein chip. Biosens Bioelectron 36 207-11 PubMed GONUTS page

[PMID:21190736-15] Georgel, P et al. (2011) The non-conventional MHC class I MR1 molecule controls infection by Klebsiella pneumoniae in mice. Mol. Immunol. 48 769-75 PubMed GONUTS page

[PMID:18458083-16] Cao, J et al. (2008) Molecular identification of a novel mammalian brain isoform of acyl-CoA:lysophospholipid acyltransferase with prominent ethanolamine lysophospholipid acylating activity, LPEAT2. J. Biol. Chem. 283 19049-57 PubMed GONUTS page

[PMID:14966132-17] Cao, J et al. (2004) A predominant role of acyl-CoA:monoacylglycerol acyltransferase-2 in dietary fat absorption implicated by tissue distribution, subcellular localization, and up-regulation by high fat diet. J. Biol. Chem. 279 18878-86 PubMed GONUTS page

[PMID:22013210-18] Hetz, C et al. (2011) The unfolded protein response: integrating stress signals through the stress sensor IRE1α. Physiol. Rev. 91 1219-43 PubMed GONUTS page

[PMID:8055875-19] Honoré, B et al. () The molecular chaperones HSP28, GRP78, endoplasmin, and calnexin exhibit strikingly different levels in quiescent keratinocytes as compared to their proliferating normal and transformed counterparts: cDNA cloning and expression of calnexin. Electrophoresis 15 482-90 PubMed GONUTS page

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HUMAN:CALX

Contents

Annotations

Notes

References

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