HSPA5 and RPN1

Number of citations of the paper that reports this interaction (PMID 10588643)
19

Data Source:
BioGRID (pull down)

		HSPA5	RPN1
Gene Name		heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa)	ribophorin I
Image			No pdb structure
Gene Ontology Annotations	Cellular Component	Nucleus Mitochondrion Endoplasmic Reticulum Endoplasmic Reticulum Lumen Endoplasmic Reticulum Membrane Smooth Endoplasmic Reticulum Endoplasmic Reticulum-Golgi Intermediate Compartment Plasma Membrane Focal Adhesion COP9 Signalosome Cell Surface Membrane Integral Component Of Endoplasmic Reticulum Membrane Midbody Endoplasmic Reticulum Chaperone Complex Melanosome Extracellular Vesicular Exosome	Endoplasmic Reticulum Membrane Rough Endoplasmic Reticulum Oligosaccharyltransferase Complex Membrane Integral Component Of Membrane Melanosome
	Molecular Function	Glycoprotein Binding Calcium Ion Binding Protein Binding ATP Binding ATPase Activity Enzyme Binding Protein Domain Specific Binding Ubiquitin Protein Ligase Binding Ribosome Binding Unfolded Protein Binding Chaperone Binding Misfolded Protein Binding	Dolichyl-diphosphooligosaccharide-protein Glycotransferase Activity Protein Binding Poly(A) RNA Binding
	Biological Process	Platelet Degranulation ER Overload Response Activation Of Signaling Protein Activity Involved In Unfolded Protein Response Blood Coagulation Cerebellum Structural Organization Cerebellar Purkinje Cell Layer Development Substantia Nigra Development Platelet Activation Positive Regulation Of Cell Migration ER-associated Ubiquitin-dependent Protein Catabolic Process Negative Regulation Of Transforming Growth Factor Beta Receptor Signaling Pathway Endoplasmic Reticulum Unfolded Protein Response Positive Regulation Of Protein Ubiquitination Maintenance Of Protein Localization In Endoplasmic Reticulum Cellular Response To Glucose Starvation Negative Regulation Of Apoptotic Process Cellular Protein Metabolic Process Regulation Of Protein Folding In Endoplasmic Reticulum Cellular Response To Antibiotic Cellular Response To Interleukin-4 Toxin Transport	Translation Cellular Protein Modification Process SRP-dependent Cotranslational Protein Targeting To Membrane Gene Expression Protein N-linked Glycosylation Via Asparagine Post-translational Protein Modification Cellular Protein Metabolic Process
Pathways		Platelet degranulation Antigen Presentation: Folding, assembly and peptide loading of class I MHC ATF6-alpha activates chaperone genes IRE1alpha activates chaperones Response to elevated platelet cytosolic Ca2+ Class I MHC mediated antigen processing & presentation Platelet activation, signaling and aggregation ATF6-alpha activates chaperones PERK regulates gene expression Unfolded Protein Response (UPR) Adaptive Immune System	Defective ALG2 causes ALG2-CDG (CDG-1i) Diseases of glycosylation Translation Defective ALG3 causes ALG3-CDG (CDG-1d) Post-translational protein modification SRP-dependent cotranslational protein targeting to membrane Defective DPAGT1 causes DPAGT1-CDG (CDG-1j) and CMSTA2 Defective ALG14 causes congenital myasthenic syndrome (ALG14-CMS) Defective MGAT2 causes MGAT2-CDG (CDG-2a) Defective ALG1 causes ALG1-CDG (CDG-1k) Defective B4GALT1 causes B4GALT1-CDG (CDG-2d) Defective RFT1 causes RFT1-CDG (CDG-1n) Defective ALG6 causes ALG6-CDG (CDG-1c) Defective MOGS causes MOGS-CDG (CDG-2b) Asparagine N-linked glycosylation Defective ALG8 causes ALG8-CDG (CDG-1h) Defective ALG9 causes ALG9-CDG (CDG-1l) Defective MAN1B1 causes MRT15 Defective MPDU1 causes MPDU1-CDG (CDG-1f) Defective ALG12 causes ALG12-CDG (CDG-1g) Diseases associated with N-glycosylation of proteins Defective ALG11 causes ALG11-CDG (CDG-1p)
Drugs		Antihemophilic Factor
Diseases
GWAS			Monocyte count ( 23314186) White blood cell count ( 21738480)
Protein-Protein Interactions		53 interactors: A2M APC APOB BCAR1 CASP7 CPT1A DDX24 DNAJC1 DNAJC10 DPH1 DPYSL5 EIF2AK3 ERN1 ERP29 F8 FCHSD2 GRB2 GRIA1 HLA-C HSPBP1 HTR3A ID2 IGHM KRT14 KRT18 KRT8 LCT LDLR METTL21A MTNR1A MTNR1B NDRG1 PAWR PCSK7 PRNP PSME3 RPN1 SEC61A1 SH3BP4 SIL1 SREBF2 STMN1 SUMO4 TCERG1 TG TMEM132A TMEM62 TRA TSHR UBQLN4 VHL VWF YWHAB	13 interactors: ADRM1 ASB11 DPF1 ERBB3 HSPA5 RAD23A RBBP4 SGTA SIGIRR UBQLN1 UBQLN2 UBQLN4 WSB2
Entrez ID		3309	6184
HPRD ID		00682	01598
Ensembl ID		ENSG00000044574	ENSG00000163902
Uniprot IDs		P11021	P04843
PDB IDs		3IUC 3LDL 3LDN 3LDO 3LDP
Enriched GO Terms of Interacting Partners?		Response To Stimulus Cellular Response To Stimulus Apoptotic Signaling Pathway Response To Stress Blood Coagulation, Intrinsic Pathway Cell Activation Signal Transduction Apoptotic Process Positive Regulation Of Metabolic Process Programmed Cell Death Signaling Positive Regulation Of Cellular Metabolic Process Intrinsic Apoptotic Signaling Pathway Cell Death Death Cell Communication Platelet Activation Regulation Of Proteolysis Intrinsic Apoptotic Signaling Pathway In Response To Endoplasmic Reticulum Stress Regulation Of Protein Metabolic Process Regulation Of Cellular Protein Metabolic Process Regulation Of Body Fluid Levels Negative Regulation Of Cellular Protein Metabolic Process Blood Coagulation Negative Regulation Of Cellular Metabolic Process Protein Oligomerization Hemostasis Response To External Stimulus Cellular Response To Organic Substance Protein Folding Regulation Of Lipid Metabolic Process Response To Organic Substance Response To Inorganic Substance Negative Regulation Of Protein Metabolic Process Platelet Degranulation Lipoprotein Catabolic Process Regulation Of Apoptotic Process Regulation Of Cholesterol Homeostasis Hepatocyte Apoptotic Process Protein Metabolic Process Regulation Of Phosphorus Metabolic Process Positive Regulation Of Cholesterol Storage Negative Regulation Of T Cell Receptor Signaling Pathway Axonogenesis Regulation Of Proteasomal Protein Catabolic Process Positive Regulation Of Protein Metabolic Process Viral Process Cellular Response To Stress Cell Development Anatomical Structure Morphogenesis	Regulation Of Protein Metabolic Process Regulation Of Cellular Protein Metabolic Process Regulation Of Protein Folding In Endoplasmic Reticulum Cerebellum Structural Organization
Tagcloud ?		17q 22cm canine centromeric cfa9 correspond cosmid cryba1 distal dog grp78 hsa17 hsa17q hsa9q hsa9q34 lies linkage loci map mmu2 nf1 occupy painting places probable rxra syntenic telomeric thirds	26s adopts atp atph coexisting commitment conformational conformations cryo dataset deconvolutes deubiquitylation em ensemble essentially executes gammas hydrolyzing interpretable landscape lid machine module move polyubiquitylated proteasome rendered static topology
Tagcloud (Difference) ?		17q 22cm canine centromeric cfa9 correspond cosmid cryba1 distal dog grp78 hsa17 hsa17q hsa9q hsa9q34 lies linkage loci map mmu2 nf1 occupy painting places probable rxra syntenic telomeric thirds	26s adopts atp atph coexisting commitment conformational conformations cryo dataset deconvolutes deubiquitylation em ensemble essentially executes gammas hydrolyzing interpretable landscape lid machine module move polyubiquitylated proteasome rendered static topology
Tagcloud (Intersection) ?