HUMAN:BIP

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	HSPA5 (ECO:0000312 with HGNC:HGNC:5238) (synonyms: GRP78 (ECO:0000303 with PMID:2840249^[1]))
Protein Name(s)	Endoplasmic reticulum chaperone BiP (ECO:0000305) 78 kDa glucose-regulated protein (ECO:0000303 with PMID:2840249^[1]) GRP-78 (ECO:0000303 with PMID:2840249^[1]) Binding-immunoglobulin protein (ECO:0000303 with Ref.4) BiP (ECO:0000303 with Ref.4) Heat shock protein 70 family protein 5 (ECO:0000305) HSP70 family protein 5 (ECO:0000305) Heat shock protein family A member 5 (ECO:0000312 with HGNC:HGNC:5238) Immunoglobulin heavy chain-binding protein (ECO:0000303 with Ref.4)
External Links
UniProt	P11021
EMBL	M19645 X87949 AJ271729 AF216292 DQ385847 AL354710 CH471090 BC020235 X59969 AF188611
CCDS	CCDS6863.1
PIR	A29821
RefSeq	NP_005338.1
UniGene	Hs.743241
PDB	3IUC 3LDL 3LDN 3LDO 3LDP 5E84 5E85 5E86 5EVZ 5EX5 5EXW 5EY4 5F0X 5F1X 5F2R 6ASY
PDBsum	3IUC 3LDL 3LDN 3LDO 3LDP 5E84 5E85 5E86 5EVZ 5EX5 5EXW 5EY4 5F0X 5F1X 5F2R 6ASY
ProteinModelPortal	P11021
SMR	P11021
BioGrid	109541
CORUM	P11021
DIP	DIP-33189N
ELM	P11021
IntAct	P11021
MINT	P11021
STRING	9606.ENSP00000324173
BindingDB	P11021
ChEMBL	CHEMBL1781865
DrugBank	DB00945 DB00025
TCDB	1.A.33.1.6
iPTMnet	P11021
PhosphoSitePlus	P11021
SwissPalm	P11021
BioMuta	HSPA5
DMDM	14916999
DOSAC-COBS-2DPAGE	P11021
OGP	P11021
REPRODUCTION-2DPAGE	P11021
SWISS-2DPAGE	P11021
UCD-2DPAGE	P11021
EPD	P11021
PaxDb	P11021
PeptideAtlas	P11021
PRIDE	P11021
TopDownProteomics	P11021
DNASU	3309
Ensembl	ENST00000324460
GeneID	3309
KEGG	hsa:3309
CTD	3309
DisGeNET	3309
EuPathDB	HostDB:ENSG00000044574.7
GeneCards	HSPA5
HGNC	HGNC:5238
HPA	CAB005221 HPA038845 HPA038846
MIM	138120
neXtProt	NX_P11021
OpenTargets	ENSG00000044574
PharmGKB	PA29504
eggNOG	KOG0101 COG0443
GeneTree	ENSGT00910000144045
HOGENOM	HOG000228135
HOVERGEN	HBG051845
InParanoid	P11021
KO	K09490
OMA	CVGVMQK
OrthoDB	EOG091G0352
PhylomeDB	P11021
TreeFam	TF105044
Reactome	R-HSA-114608 R-HSA-3371453 R-HSA-381033 R-HSA-381042 R-HSA-381070 R-HSA-381183 R-HSA-983170
SIGNOR	P11021
ChiTaRS	HSPA5
EvolutionaryTrace	P11021
GeneWiki	Binding_immunoglobulin_protein
GenomeRNAi	3309
PRO	PR:P11021
Proteomes	UP000005640
Bgee	ENSG00000044574
CleanEx	HS_HSPA5
ExpressionAtlas	P11021
Genevisible	P11021
GO	GO:0009986 GO:0005783 GO:0034663 GO:0005788 GO:0005789 GO:0005793 GO:0070062 GO:0031012 GO:0005925 GO:0030176 GO:0042470 GO:0016020 GO:0030496 GO:0005739 GO:0043209 GO:0005634 GO:0005886 GO:0043234 GO:0005790 GO:0005524 GO:0016887 GO:0045296 GO:0005509 GO:0051087 GO:0019899 GO:0051787 GO:0019904 GO:0043022 GO:0031625 GO:0051082 GO:0006987 GO:0036500 GO:0071236 GO:0071277 GO:0071320 GO:0035690 GO:0071480 GO:0042149 GO:0071353 GO:0071287 GO:1990090 GO:0021680 GO:0021589 GO:0030968 GO:0006983 GO:0036498 GO:0035437 GO:0043066 GO:1903895 GO:0090074 GO:0030512 GO:0051402 GO:0030182 GO:0036499 GO:0030335 GO:0010976 GO:0031398 GO:1990440 GO:0034975 GO:1903891 GO:1903894 GO:1903897 GO:0060904 GO:0042220 GO:1904313 GO:0097501 GO:0021762 GO:1901998 GO:0030433
Gene3D	1.20.1270.10 2.60.34.10
InterPro	IPR018181 IPR029048 IPR029047 IPR013126
PANTHER	PTHR19375
Pfam	PF00012
PRINTS	PR00301
SUPFAM	SSF100920 SSF100934
PROSITE	PS00014 PS00297 PS00329 PS01036

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0016887	ATPase activity	PMID:23975754^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Fig. 6	complete CACAO 8861
involved_in	GO:1903895	negative regulation of IRE1-mediated unfolded protein response	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:G3I8R9	P		Seeded From UniProt	complete
involved_in	GO:0090074	negative regulation of protein homodimerization activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:G3I8R9	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:22689054^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0043231	intracellular membrane-bounded organelle	PMID:22689054^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:22689054^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:22689054^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0031204	posttranslational protein targeting to membrane, translocation	PMID:29719251^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:23349634^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0045296	cadherin binding	PMID:25468996^[6]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:20335166^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005925	focal adhesion	PMID:21423176^[8]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000057)	Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:19946888^[9]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:23921388^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q8WXB1	F		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19199708^[11]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001831)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[12]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[13]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[13]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000639)	Seeded From UniProt	complete
involved_in	GO:0021762	substantia nigra development	PMID:22926577^[14]	ECO:0007007	high throughput expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21630459^[15]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000019)	Seeded From UniProt	complete
part_of	GO:0030176	integral component of endoplasmic reticulum membrane	PMID:11181571^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0051787	misfolded protein binding	PMID:18400946^[17]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	PMID:12665508^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	PMID:10760948^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042149	cellular response to glucose starvation	PMID:10085239^[20]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0035437	maintenance of protein localization in endoplasmic reticulum	PMID:23990668^[21]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0034663	endoplasmic reticulum chaperone complex	PMID:18400946^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:8666824^[22]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P19474	F		Seeded From UniProt	complete
part_of	GO:0030496	midbody	PMID:15166316^[23]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0030335	positive regulation of cell migration	PMID:23990668^[21]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	PMID:12411443^[24]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q8IXB1	F		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P07823	F		Seeded From UniProt	complete
colocalizes_with	GO:0008180	COP9 signalosome	PMID:18850735^[25]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005793	endoplasmic reticulum-Golgi intermediate compartment	PMID:15308636^[26]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:11943137^[27]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:11943137^[27]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0051787	misfolded protein binding	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:95835 PANTHER:PTN002321897 RGD:2843 UniProtKB:P11021	F		Seeded From UniProt	complete
involved_in	GO:0051085	chaperone cofactor-dependent protein refolding	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10241 MGI:MGI:105384 PANTHER:PTN002321897	P		Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10241 MGI:MGI:105384 PANTHER:PTN002321897 RGD:2843 RGD:621725 SGD:S000000004 SGD:S000000171 SGD:S000000905 SGD:S000001106 SGD:S000001556 SGD:S000002388 SGD:S000003571 SGD:S000003947 SGD:S000005153 UniProtKB:P0DMV8 UniProtKB:P0DMV9 UniProtKB:P11142 UniProtKB:P17066 UniProtKB:P34931 UniProtKB:P54652	F		Seeded From UniProt	complete
enables	GO:0044183	protein folding chaperone	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10241 PANTHER:PTN002321897 UniProtKB:P0DMV8 UniProtKB:P0DMV9	F		Seeded From UniProt	complete
enables	GO:0042623	ATPase activity, coupled	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:105384 PANTHER:PTN002321897 RGD:621725 UniProtKB:P0DMV8 UniProtKB:P0DMV9 UniProtKB:P17066	F		Seeded From UniProt	complete
involved_in	GO:0042026	protein refolding	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002321897 SGD:S000000004 SGD:S000000756 SGD:S000003806 UniProtKB:P0DMV8 UniProtKB:P0DMV9 UniProtKB:P11142 UniProtKB:P17066 UniProtKB:P34931 UniProtKB:P54652	P		Seeded From UniProt	complete
part_of	GO:0034663	endoplasmic reticulum chaperone complex	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:95835 PANTHER:PTN001834223 UniProtKB:P11021	C		Seeded From UniProt	complete
involved_in	GO:0034620	cellular response to unfolded protein	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10241 PANTHER:PTN002321897 UniProtKB:P0DMV8	P		Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	CGD:CAL0000184706 PANTHER:PTN002321897 RGD:621725 SGD:S000000905 UniProtKB:A5I640 UniProtKB:P0DMV8 UniProtKB:P0DMV9 UniProtKB:P17066	P		Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002321897 RGD:1311806 UniProtKB:K7NTP5 UniProtKB:O73885 UniProtKB:P0DMV8 UniProtKB:P0DMV9 UniProtKB:P11142 UniProtKB:P17066 UniProtKB:P34931 UniProtKB:Q8IB24	F		Seeded From UniProt	complete
involved_in	GO:0030968	endoplasmic reticulum unfolded protein response	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:95835 PANTHER:PTN001834223 WB:WBGene00002007 WB:WBGene00002008	P		Seeded From UniProt	complete
involved_in	GO:0030433	ubiquitin-dependent ERAD pathway	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001834223 SGD:S000003571 TAIR:locus:2182783	P		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10241 EcoGene:EG12130 EcoGene:EG13653 PANTHER:PTN002321897 PomBase:SPAC664.11 RGD:621725 SGD:S000000004 SGD:S000000171 SGD:S000002388 SGD:S000003571 SGD:S000003806 SGD:S000005153 UniProtKB:P0DMV8 UniProtKB:P0DMV9 UniProtKB:P11021 UniProtKB:P11142 WB:WBGene00002005	F		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001834223 RGD:2843 UniProtKB:Q39043	C		Seeded From UniProt	complete
involved_in	GO:0006986	response to unfolded protein	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002321897 RGD:1593284 RGD:2840 SGD:S000001556 SGD:S000003571 UniProtKB:P0DMV8	P		Seeded From UniProt	complete
part_of	GO:0005788	endoplasmic reticulum lumen	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:95835 PANTHER:PTN001834223 PomBase:SPAC22A12.15c	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10241 FB:FBgn0266599 MGI:MGI:105384 MGI:MGI:96244 PANTHER:PTN002321897 PomBase:SPCC1739.13 RGD:1311806 RGD:2843 RGD:621725 SGD:S000000004 SGD:S000000905 SGD:S000001106 SGD:S000002388 SGD:S000003947 UniProtKB:O73885 UniProtKB:P08106 UniProtKB:P0DMV8 UniProtKB:P0DMV9 UniProtKB:P17066 UniProtKB:P22953 UniProtKB:Q27975 UniProtKB:Q8IB24 WB:WBGene00002005	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001834223 UniProtKB:P11021 UniProtKB:Q39043	C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10241 EcoGene:EG12130 PANTHER:PTN002321897 RGD:621725 SGD:S000001556 SGD:S000003947 TAIR:locus:2101222 TAIR:locus:2121022 TAIR:locus:2135897 TAIR:locus:2144801 UniProtKB:P08106 UniProtKB:P0DMV8 UniProtKB:P0DMV9 UniProtKB:P11142 UniProtKB:Q7SX63	F		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:16223484^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1990090	cellular response to nerve growth factor stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P06761 ensembl:ENSRNOP00000025064	P		Seeded From UniProt	complete
involved_in	GO:1904313	response to methamphetamine hydrochloride	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P06761 ensembl:ENSRNOP00000025064	P		Seeded From UniProt	complete
involved_in	GO:0097501	stress response to metal ion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P06761 ensembl:ENSRNOP00000025064	P		Seeded From UniProt	complete
involved_in	GO:0071480	cellular response to gamma radiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P06761 ensembl:ENSRNOP00000025064	P		Seeded From UniProt	complete
involved_in	GO:0071320	cellular response to cAMP	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P06761 ensembl:ENSRNOP00000025064	P		Seeded From UniProt	complete
involved_in	GO:0071287	cellular response to manganese ion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P06761 ensembl:ENSRNOP00000025064	P		Seeded From UniProt	complete
involved_in	GO:0071277	cellular response to calcium ion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P06761 ensembl:ENSRNOP00000025064	P		Seeded From UniProt	complete
involved_in	GO:0071236	cellular response to antibiotic	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P06761 ensembl:ENSRNOP00000025064	P		Seeded From UniProt	complete
enables	GO:0051787	misfolded protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P06761 ensembl:ENSRNOP00000025064	F		Seeded From UniProt	complete
involved_in	GO:0051402	neuron apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P06761 ensembl:ENSRNOP00000025064	P		Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P06761 ensembl:ENSRNOP00000025064	F		Seeded From UniProt	complete
involved_in	GO:0042220	response to cocaine	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P06761 ensembl:ENSRNOP00000025064	P		Seeded From UniProt	complete
involved_in	GO:0035690	cellular response to drug	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P06761 ensembl:ENSRNOP00000025064	P		Seeded From UniProt	complete
involved_in	GO:0034976	response to endoplasmic reticulum stress	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P06761 ensembl:ENSRNOP00000025064	P		Seeded From UniProt	complete
involved_in	GO:0030182	neuron differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P06761 ensembl:ENSRNOP00000025064	P		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P06761 ensembl:ENSRNOP00000025064	C		Seeded From UniProt	complete
involved_in	GO:0010976	positive regulation of neuron projection development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P06761 ensembl:ENSRNOP00000025064	P		Seeded From UniProt	complete
involved_in	GO:0009314	response to radiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P06761 ensembl:ENSRNOP00000025064	P		Seeded From UniProt	complete
part_of	GO:0005790	smooth endoplasmic reticulum	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P06761 ensembl:ENSRNOP00000025064	C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P06761 ensembl:ENSRNOP00000025064	C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P06761 ensembl:ENSRNOP00000025064	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P06761 ensembl:ENSRNOP00000025064	C		Seeded From UniProt	complete
involved_in	GO:0001554	luteolysis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P06761 ensembl:ENSRNOP00000025064	P		Seeded From UniProt	complete
involved_in	GO:1901998	toxin transport	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20029 ensembl:ENSMUSP00000028222	P		Seeded From UniProt	complete
involved_in	GO:0071353	cellular response to interleukin-4	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20029 ensembl:ENSMUSP00000028222	P		Seeded From UniProt	complete
enables	GO:0051787	misfolded protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20029 ensembl:ENSMUSP00000028222	F		Seeded From UniProt	complete
involved_in	GO:0051603	proteolysis involved in cellular protein catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20029 ensembl:ENSMUSP00000028222	P		Seeded From UniProt	complete
enables	GO:0043022	ribosome binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20029 ensembl:ENSMUSP00000028222	F		Seeded From UniProt	complete
part_of	GO:0034663	endoplasmic reticulum chaperone complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20029 ensembl:ENSMUSP00000028222	C		Seeded From UniProt	complete
involved_in	GO:0031398	positive regulation of protein ubiquitination	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20029 ensembl:ENSMUSP00000028222	P		Seeded From UniProt	complete
involved_in	GO:0030968	endoplasmic reticulum unfolded protein response	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20029 ensembl:ENSMUSP00000028222	P		Seeded From UniProt	complete
involved_in	GO:0030512	negative regulation of transforming growth factor beta receptor signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20029 ensembl:ENSMUSP00000028222	P		Seeded From UniProt	complete
involved_in	GO:0021680	cerebellar Purkinje cell layer development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20029 ensembl:ENSMUSP00000028222	P		Seeded From UniProt	complete
involved_in	GO:0021589	cerebellum structural organization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20029 ensembl:ENSMUSP00000028222	P		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20029 ensembl:ENSMUSP00000028222	C		Seeded From UniProt	complete
involved_in	GO:0006983	ER overload response	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20029 ensembl:ENSMUSP00000028222	P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20029 ensembl:ENSMUSP00000028222	C		Seeded From UniProt	complete
part_of	GO:0005793	endoplasmic reticulum-Golgi intermediate compartment	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20029 ensembl:ENSMUSP00000028222	C		Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20029 ensembl:ENSMUSP00000028222	C		Seeded From UniProt	complete
part_of	GO:0005788	endoplasmic reticulum lumen	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20029 ensembl:ENSMUSP00000028222	C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20029 ensembl:ENSMUSP00000028222	C		Seeded From UniProt	complete
involved_in	GO:1903891	regulation of ATF6-mediated unfolded protein response	PMID:22934019^[30]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903894	regulation of IRE1-mediated unfolded protein response	PMID:22934019^[30]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903897	regulation of PERK-mediated unfolded protein response	PMID:22934019^[30]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:22013210^[31] PMID:14685163^[32] PMID:16130169^[33]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	part_of:(GO:0034976)	Seeded From UniProt	complete
involved_in	GO:0034975	protein folding in endoplasmic reticulum	PMID:22013210^[31]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1990440	positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress	PMID:14685163^[32]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0090074	negative regulation of protein homodimerization activity	PMID:14685163^[32]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	has_regulation_target:(UniProtKB:O75460) part_of:(GO:0034976)\|has_regulation_target(UniProtKB:Q76MJ5) part_of:(GO:0034976)\|has_regulation_target(UniProtKB:Q9NZJ5) part_of:(GO:0034976)	Seeded From UniProt	complete
involved_in	GO:0060904	regulation of protein folding in endoplasmic reticulum	PMID:19816510^[34]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0051087	chaperone binding	PMID:19816510^[34]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0030968	endoplasmic reticulum unfolded protein response	PMID:19816510^[34]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030433	ubiquitin-dependent ERAD pathway	PMID:19816510^[34]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	PMID:16130169^[33]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:16130169^[33]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005509	calcium ion binding	PMID:16130169^[33]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0036500	ATF6-mediated unfolded protein response	Reactome:R-HSA-381033	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0036499	PERK-mediated unfolded protein response	Reactome:R-HSA-381042	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0036498	IRE1-mediated unfolded protein response	Reactome:R-HSA-381070	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	Reactome:R-HSA-381217 Reactome:R-HSA-381158 Reactome:R-HSA-381086 Reactome:R-HSA-1791150	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005788	endoplasmic reticulum lumen	Reactome:R-HSA-381217 Reactome:R-HSA-381158 Reactome:R-HSA-381086	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0256	C		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		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
part_of	GO:0005788	endoplasmic reticulum lumen	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0096	C		Seeded From UniProt	complete
edit table

Notes

References

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

↑ ^1.0 ^1.1 ^1.2 Ting, J & Lee, AS (1988) Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: structure, conservation, and regulation. DNA 7 275-86 PubMed GONUTS page
↑ Kharenko, OA et al. (2013) Identification and characterization of interactions between abscisic acid and human heat shock protein 70 family members. J. Biochem. 154 383-91 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 Li, N et al. (2013) GRP78 regulates clusterin stability, retrotranslocation and mitochondrial localization under ER stress in prostate cancer. Oncogene 32 1933-42 PubMed GONUTS page
↑ Haßdenteufel, S et al. (2018) Chaperone-Mediated Sec61 Channel Gating during ER Import of Small Precursor Proteins Overcomes Sec61 Inhibitor-Reinforced Energy Barrier. Cell Rep 23 1373-1386 PubMed GONUTS page
↑ Cloutier, P et al. (2013) A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity. PLoS Genet. 9 e1003210 PubMed GONUTS page
↑ Guo, Z et al. (2014) E-cadherin interactome complexity and robustness resolved by quantitative proteomics. Sci Signal 7 rs7 PubMed GONUTS page
↑ Bernal-Bayard, J et al. (2010) The Salmonella type III secretion effector, salmonella leucine-rich repeat protein (SlrP), targets the human chaperone ERdj3. J. Biol. Chem. 285 16360-8 PubMed GONUTS page
↑ Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page
↑ Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
↑ Jakobsson, ME et al. (2013) Identification and characterization of a novel human methyltransferase modulating Hsp70 protein function through lysine methylation. J. Biol. Chem. 288 27752-63 PubMed GONUTS page
↑ Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ ^13.0 ^13.1 Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
↑ Chen, S et al. (2012) Quantitative proteomic analysis of human substantia nigra in Alzheimer's disease, Huntington's disease and Multiple sclerosis. Neurochem. Res. 37 2805-13 PubMed GONUTS page
↑ de Mateo, S et al. (2011) Proteomic characterization of the human sperm nucleus. Proteomics 11 2714-26 PubMed GONUTS page
↑ Takeda, K et al. (2001) WFS1 (Wolfram syndrome 1) gene product: predominant subcellular localization to endoplasmic reticulum in cultured cells and neuronal expression in rat brain. Hum. Mol. Genet. 10 477-84 PubMed GONUTS page
↑ ^17.0 ^17.1 Dong, M et al. (2008) ERdj4 and ERdj5 are required for endoplasmic reticulum-associated protein degradation of misfolded surfactant protein C. Mol. Biol. Cell 19 2620-30 PubMed GONUTS page
↑ Reddy, RK et al. (2003) Endoplasmic reticulum chaperone protein GRP78 protects cells from apoptosis induced by topoisomerase inhibitors: role of ATP binding site in suppression of caspase-7 activation. J. Biol. Chem. 278 20915-24 PubMed GONUTS page
↑ Miyake, H et al. (2000) Stress protein GRP78 prevents apoptosis induced by calcium ionophore, ionomycin, but not by glycosylation inhibitor, tunicamycin, in human prostate cancer cells. J. Cell. Biochem. 77 396-408 PubMed GONUTS page
↑ Barbosa-Tessmann, IP et al. (1999) Transcriptional regulation of the human asparagine synthetase gene by carbohydrate availability. Biochem. J. 339 ( Pt 1) 151-8 PubMed GONUTS page
↑ ^21.0 ^21.1 Evensen, NA et al. (2013) Unraveling the role of KIAA1199, a novel endoplasmic reticulum protein, in cancer cell migration. J. Natl. Cancer Inst. 105 1402-16 PubMed GONUTS page
↑ Cheng, ST et al. (1996) Calreticulin binds hYRNA and the 52-kDa polypeptide component of the Ro/SS-A ribonucleoprotein autoantigen. J. Immunol. 156 4484-91 PubMed GONUTS page
↑ Skop, AR et al. (2004) Dissection of the mammalian midbody proteome reveals conserved cytokinesis mechanisms. Science 305 61-6 PubMed GONUTS page
↑ Cunnea, PM et al. (2003) ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress. J. Biol. Chem. 278 1059-66 PubMed GONUTS page
↑ Fang, L et al. (2008) Characterization of the human COP9 signalosome complex using affinity purification and mass spectrometry. J. Proteome Res. 7 4914-25 PubMed GONUTS page
↑ Breuza, L et al. (2004) Proteomics of endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies ERGIC-32, a new cycling protein that interacts with human Erv46. J. Biol. Chem. 279 47242-53 PubMed GONUTS page
↑ ^27.0 ^27.1 Rao, RV et al. (2002) Coupling endoplasmic reticulum stress to the cell death program: role of the ER chaperone GRP78. FEBS Lett. 514 122-8 PubMed GONUTS page
↑ ^28.00 ^28.01 ^28.02 ^28.03 ^28.04 ^28.05 ^28.06 ^28.07 ^28.08 ^28.09 ^28.10 ^28.11 ^28.12 ^28.13 ^28.14 ^28.15 ^28.16 ^28.17 ^28.18 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Lidén, M et al. (2005) The C-terminal region of cis-retinol/androgen dehydrogenase 1 (CRAD1) confers ER localization and in vivo enzymatic function. Exp. Cell Res. 311 205-17 PubMed GONUTS page
↑ ^30.0 ^30.1 ^30.2 Brown, MK & Naidoo, N (2012) The endoplasmic reticulum stress response in aging and age-related diseases. Front Physiol 3 263 PubMed GONUTS page
↑ ^31.0 ^31.1 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
↑ ^32.0 ^32.1 ^32.2 Oyadomari, S & Mori, M (2004) Roles of CHOP/GADD153 in endoplasmic reticulum stress. Cell Death Differ. 11 381-9 PubMed GONUTS page
↑ ^33.0 ^33.1 ^33.2 ^33.3 Bruneel, A et al. (2005) Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis. Proteomics 5 3876-84 PubMed GONUTS page
↑ ^34.0 ^34.1 ^34.2 ^34.3 Wang, M et al. (2010) Essential role of the unfolded protein response regulator GRP78/BiP in protection from neuronal apoptosis. Cell Death Differ. 17 488-98 PubMed GONUTS page

[PMID:2840249-1] 1.0 ^1.1 ^1.2 Ting, J & Lee, AS (1988) Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: structure, conservation, and regulation. DNA 7 275-86 PubMed GONUTS page

[PMID:23975754-2] Kharenko, OA et al. (2013) Identification and characterization of interactions between abscisic acid and human heat shock protein 70 family members. J. Biochem. 154 383-91 PubMed GONUTS page

[PMID:22689054-3] 3.0 ^3.1 ^3.2 ^3.3 Li, N et al. (2013) GRP78 regulates clusterin stability, retrotranslocation and mitochondrial localization under ER stress in prostate cancer. Oncogene 32 1933-42 PubMed GONUTS page

[PMID:29719251-4] Haßdenteufel, S et al. (2018) Chaperone-Mediated Sec61 Channel Gating during ER Import of Small Precursor Proteins Overcomes Sec61 Inhibitor-Reinforced Energy Barrier. Cell Rep 23 1373-1386 PubMed GONUTS page

[PMID:23349634-5] Cloutier, P et al. (2013) A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity. PLoS Genet. 9 e1003210 PubMed GONUTS page

[PMID:25468996-6] Guo, Z et al. (2014) E-cadherin interactome complexity and robustness resolved by quantitative proteomics. Sci Signal 7 rs7 PubMed GONUTS page

[PMID:20335166-7] Bernal-Bayard, J et al. (2010) The Salmonella type III secretion effector, salmonella leucine-rich repeat protein (SlrP), targets the human chaperone ERdj3. J. Biol. Chem. 285 16360-8 PubMed GONUTS page

[PMID:21423176-8] Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page

[PMID:19946888-9] Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page

[PMID:23921388-10] Jakobsson, ME et al. (2013) Identification and characterization of a novel human methyltransferase modulating Hsp70 protein function through lysine methylation. J. Biol. Chem. 288 27752-63 PubMed GONUTS page

[PMID:19199708-11] Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page

[PMID:19056867-12] Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page

[PMID:20458337-13] 13.0 ^13.1 Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page

[PMID:22926577-14] Chen, S et al. (2012) Quantitative proteomic analysis of human substantia nigra in Alzheimer's disease, Huntington's disease and Multiple sclerosis. Neurochem. Res. 37 2805-13 PubMed GONUTS page

[PMID:21630459-15] Mateo, S et al. (2011) Proteomic characterization of the human sperm nucleus. Proteomics 11 2714-26 PubMed GONUTS page

[PMID:11181571-16] Takeda, K et al. (2001) WFS1 (Wolfram syndrome 1) gene product: predominant subcellular localization to endoplasmic reticulum in cultured cells and neuronal expression in rat brain. Hum. Mol. Genet. 10 477-84 PubMed GONUTS page

[PMID:18400946-17] 17.0 ^17.1 Dong, M et al. (2008) ERdj4 and ERdj5 are required for endoplasmic reticulum-associated protein degradation of misfolded surfactant protein C. Mol. Biol. Cell 19 2620-30 PubMed GONUTS page

[PMID:12665508-18] Reddy, RK et al. (2003) Endoplasmic reticulum chaperone protein GRP78 protects cells from apoptosis induced by topoisomerase inhibitors: role of ATP binding site in suppression of caspase-7 activation. J. Biol. Chem. 278 20915-24 PubMed GONUTS page

[PMID:10760948-19] Miyake, H et al. (2000) Stress protein GRP78 prevents apoptosis induced by calcium ionophore, ionomycin, but not by glycosylation inhibitor, tunicamycin, in human prostate cancer cells. J. Cell. Biochem. 77 396-408 PubMed GONUTS page

[PMID:10085239-20] Barbosa-Tessmann, IP et al. (1999) Transcriptional regulation of the human asparagine synthetase gene by carbohydrate availability. Biochem. J. 339 ( Pt 1) 151-8 PubMed GONUTS page

[PMID:23990668-21] 21.0 ^21.1 Evensen, NA et al. (2013) Unraveling the role of KIAA1199, a novel endoplasmic reticulum protein, in cancer cell migration. J. Natl. Cancer Inst. 105 1402-16 PubMed GONUTS page

[PMID:8666824-22] Cheng, ST et al. (1996) Calreticulin binds hYRNA and the 52-kDa polypeptide component of the Ro/SS-A ribonucleoprotein autoantigen. J. Immunol. 156 4484-91 PubMed GONUTS page

[PMID:15166316-23] Skop, AR et al. (2004) Dissection of the mammalian midbody proteome reveals conserved cytokinesis mechanisms. Science 305 61-6 PubMed GONUTS page

[PMID:12411443-24] Cunnea, PM et al. (2003) ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress. J. Biol. Chem. 278 1059-66 PubMed GONUTS page

[PMID:18850735-25] Fang, L et al. (2008) Characterization of the human COP9 signalosome complex using affinity purification and mass spectrometry. J. Proteome Res. 7 4914-25 PubMed GONUTS page

[PMID:15308636-26] Breuza, L et al. (2004) Proteomics of endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies ERGIC-32, a new cycling protein that interacts with human Erv46. J. Biol. Chem. 279 47242-53 PubMed GONUTS page

[PMID:11943137-27] 27.0 ^27.1 Rao, RV et al. (2002) Coupling endoplasmic reticulum stress to the cell death program: role of the ER chaperone GRP78. FEBS Lett. 514 122-8 PubMed GONUTS page

[PMID:21873635-28] 28.00 ^28.01 ^28.02 ^28.03 ^28.04 ^28.05 ^28.06 ^28.07 ^28.08 ^28.09 ^28.10 ^28.11 ^28.12 ^28.13 ^28.14 ^28.15 ^28.16 ^28.17 ^28.18 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:16223484-29] Lidén, M et al. (2005) The C-terminal region of cis-retinol/androgen dehydrogenase 1 (CRAD1) confers ER localization and in vivo enzymatic function. Exp. Cell Res. 311 205-17 PubMed GONUTS page

[PMID:22934019-30] 30.0 ^30.1 ^30.2 Brown, MK & Naidoo, N (2012) The endoplasmic reticulum stress response in aging and age-related diseases. Front Physiol 3 263 PubMed GONUTS page

[PMID:22013210-31] 31.0 ^31.1 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:14685163-32] 32.0 ^32.1 ^32.2 Oyadomari, S & Mori, M (2004) Roles of CHOP/GADD153 in endoplasmic reticulum stress. Cell Death Differ. 11 381-9 PubMed GONUTS page

[PMID:16130169-33] 33.0 ^33.1 ^33.2 ^33.3 Bruneel, A et al. (2005) Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis. Proteomics 5 3876-84 PubMed GONUTS page

[PMID:19816510-34] 34.0 ^34.1 ^34.2 ^34.3 Wang, M et al. (2010) Essential role of the unfolded protein response regulator GRP78/BiP in protection from neuronal apoptosis. Cell Death Differ. 17 488-98 PubMed GONUTS page

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