S100A8 and PPIA

Number of citations of the paper that reports this interaction (PubMedID 16169070)
888

Data Source:
BioGRID (two hybrid)
HPRD (two hybrid)

		S100A8	PPIA
Description		S100 calcium binding protein A8	peptidylprolyl isomerase A
Image
GO Annotations	Cellular Component	Extracellular Region Extracellular Space Nucleus Cytosol Cytoskeleton Plasma Membrane Secretory Granule Lumen Intermediate Filament Cytoskeleton Collagen-containing Extracellular Matrix Extracellular Exosome	Extracellular Region Extracellular Space Nucleus Cytoplasm Cytosol Focal Adhesion Membrane Vesicle Protein-containing Complex Secretory Granule Lumen Intracellular Membrane-bounded Organelle Extracellular Exosome Ficolin-1-rich Granule Lumen
	Molecular Function	Calcium Ion Binding Protein Binding Microtubule Binding Zinc Ion Binding Toll-like Receptor 4 Binding Calcium-dependent Protein Binding Arachidonic Acid Binding RAGE Receptor Binding	RNA Binding Peptidyl-prolyl Cis-trans Isomerase Activity Integrin Binding Protein Binding Cyclosporin A Binding Virion Binding Unfolded Protein Binding Heparan Sulfate Binding
	Biological Process	Leukocyte Migration Involved In Inflammatory Response Acute Inflammatory Response Chronic Inflammatory Response Positive Regulation Of Peptide Secretion Autophagy Apoptotic Process Activation Of Cysteine-type Endopeptidase Activity Involved In Apoptotic Process Inflammatory Response Response To Zinc Ion Astrocyte Development Peptidyl-cysteine S-nitrosylation Positive Regulation Of Cell Growth Neutrophil Chemotaxis Sequestering Of Zinc Ion Response To Lipopolysaccharide Autocrine Signaling Wound Healing Defense Response To Bacterium Innate Immune Response Response To Ethanol Positive Regulation Of Inflammatory Response Defense Response To Fungus Positive Regulation Of NF-kappaB Transcription Factor Activity Regulation Of Cytoskeleton Organization Neutrophil Aggregation Positive Regulation Of Intrinsic Apoptotic Signaling Pathway	Protein Peptidyl-prolyl Isomerization Negative Regulation Of Protein Phosphorylation Positive Regulation Of Protein Phosphorylation Protein Folding Negative Regulation Of Protein Kinase Activity Apoptotic Process Viral Release From Host Cell Platelet Activation Neuron Differentiation Neutrophil Chemotaxis Leukocyte Chemotaxis Activation Of Protein Kinase B Activity Negative Regulation Of Stress-activated MAPK Cascade Lipid Droplet Organization Cellular Response To Oxidative Stress Positive Regulation Of Protein Dephosphorylation Endothelial Cell Activation Positive Regulation Of MAPK Cascade Regulation Of Viral Genome Replication Positive Regulation Of Viral Genome Replication Positive Regulation Of Protein Secretion Positive Regulation Of NF-kappaB Transcription Factor Activity Cell Adhesion Molecule Production Negative Regulation Of Protein K48-linked Ubiquitination Platelet Aggregation Negative Regulation Of Oxidative Stress-induced Intrinsic Apoptotic Signaling Pathway Negative Regulation Of Viral Life Cycle Regulation Of Apoptotic Signaling Pathway
Pathways		ER-Phagosome pathway MyD88:MAL(TIRAP) cascade initiated on plasma membrane MyD88 deficiency (TLR2/4) IRAK4 deficiency (TLR2/4) RHO GTPases Activate NADPH Oxidases Regulation of TLR by endogenous ligand Neutrophil degranulation Metal sequestration by antimicrobial proteins	Platelet degranulation Uncoating of the HIV Virion Budding and maturation of HIV virion Integration of provirus Early Phase of HIV Life Cycle Minus-strand DNA synthesis Plus-strand DNA synthesis Binding and entry of HIV virion Assembly Of The HIV Virion APOBEC3G mediated resistance to HIV-1 infection Calcineurin activates NFAT Basigin interactions Neutrophil degranulation Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation
Drugs		Calcium Zinc Copper Zinc acetate Zinc chloride Zinc sulfate, unspecified form	Cyclosporine Proline (3r)-1-Acetyl-3-Methylpiperidine Ethyl Oxo(Piperidin-1-Yl)Acetate Sanglifehrin A Copper Artenimol
Diseases
GWAS		Asthma ( 31619474) Matrix metalloproteinase-8 levels ( 29212897) Monocyte count ( 32888494)	Mean reticulocyte volume ( 32888494) Red blood cell count ( 32888494)
Interacting Genes		22 interacting genes: APP CDKN1A CEACAM3 CHGB ERG28 GDF9 IGSF21 KLC2 LRIF1 NCF2 PABPC4 PDCD11 PPIA PRMT1 PTEN RAB17 S100A9 TP53 TUBA1A TUBA4A TUBB UNC119	28 interacting genes: APP BSG CD99 ERCC6 ERRFI1 G3BP1 ITK JAK2 LIG4 LNX1 N4BP2L2 NOTCH3 PAXIP1 PRLR PRR13 PRSS23 PTPRN RB1 S100A8 SRPK1 SRPK2 SUPT5H TCF4 TERT UBE3A USP4 WBP4 YY1
Entrez ID		6279	5478
HPRD ID		00471	00457
Ensembl ID		ENSG00000143546	ENSG00000196262
Uniprot IDs		P05109	P62937 V9HWF5
PDB IDs		1MR8 1XK4 4GGF 4XJK 5HLO 5HLV 5W1F 6DS2	1AK4 1AWQ 1AWR 1AWS 1AWT 1AWU 1AWV 1BCK 1CWA 1CWB 1CWC 1CWF 1CWH 1CWI 1CWJ 1CWK 1CWL 1CWM 1CWO 1FGL 1M63 1M9C 1M9D 1M9E 1M9F 1M9X 1M9Y 1MF8 1MIK 1NMK 1OCA 1RMH 1VBS 1VBT 1W8L 1W8M 1W8V 1YND 1ZKF 2ALF 2CPL 2CYH 2MS4 2MZU 2N0T 2RMA 2RMB 2X25 2X2A 2X2C 2X2D 2XGY 3CYH 3CYS 3K0M 3K0N 3K0O 3K0P 3K0Q 3K0R 3ODI 3ODL 3RDD 4CYH 4IPZ 4N1M 4N1N 4N1O 4N1P 4N1Q 4N1R 4N1S 4YUG 4YUH 4YUI 4YUJ 4YUK 4YUL 4YUM 4YUN 4YUO 4YUP 5CYH 5F66 5FJB 5KUL 5KUN 5KUO 5KUQ 5KUR 5KUS 5KUU 5KUV 5KUW 5KUZ 5KV0 5KV1 5KV2 5KV3 5KV4 5KV5 5KV6 5KV7 5LUD 5NOQ 5NOR 5NOS 5NOT 5NOU 5NOV 5NOW 5NOX 5NOY 5NOZ 5T9U 5T9W 5T9Z 5TA2 5TA4 5WC7 6BTA 6GJI 6GJJ 6GJL 6GJM 6GJN 6GJP 6GJR 6GJY 6GS6 6I42 6U5C 6U5D 6U5E 6U5G 6X3R 6X3Y 6X4M 6X4N 6X4O 6X4P 6X4Q 6Y9V 6Y9W 6Y9X 6Y9Y 6Y9Z 6ZDJ
Enriched GO Terms of Interacting Partners?
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