PCGF1 and MUC7

Number of citations of the paper that reports this interaction (PubMedID 27107012)
72

Data Source:
BioGRID (two hybrid)

		PCGF1	MUC7
Description		polycomb group ring finger 1	mucin 7, secreted
Image			No pdb structure
GO Annotations	Cellular Component	Nucleus Nucleoplasm PcG Protein Complex PRC1 Complex	Extracellular Region Golgi Lumen Plasma Membrane Extracellular Exosome
	Molecular Function	Protein Binding Zinc Ion Binding Metal Ion Binding Promoter-specific Chromatin Binding	Protein Binding
	Biological Process	Negative Regulation Of Transcription By RNA Polymerase II Chromatin Remodeling Regulation Of DNA-templated Transcription	Killing Of Cells Of Another Organism Antimicrobial Humoral Immune Response Mediated By Antimicrobial Peptide
Pathways			Defective GALNT3 causes HFTC Defective C1GALT1C1 causes TNPS Defective GALNT12 causes CRCS1 Dectin-2 family O-linked glycosylation of mucins Termination of O-glycan biosynthesis
Drugs
Diseases
GWAS			Diabetic nephropathy in type 1 diabetes ( 31537649)
Interacting Genes		10 interacting genes: CALCOCO2 CBX7 FCHO1 H2AC4 MUC7 RNF125 RNF2 TRIM55 UBE2D3 UBE2U	8 interacting genes: AMY1A GALNT10 GALNT12 GALNT14 HTN3 LTF PCGF1 SELL
Entrez ID		84759	4589
HPRD ID		11404	11759
Ensembl ID		ENSG00000115289	ENSG00000171195
Uniprot IDs		Q9BSM1	Q8TAX7
PDB IDs		4HPL 4HPM 5JH5 8HCU
Enriched GO Terms of Interacting Partners?		Protein Ubiquitination Protein Polyubiquitination Ubiquitin Protein Ligase Activity PRC1 Complex Protein Modification By Small Protein Conjugation Post-translational Protein Modification PcG Protein Complex Ubiquitin Conjugating Enzyme Activity Ubiquitin-protein Transferase Activity Positive Regulation Of Granzyme B Production	Polypeptide N-acetylgalactosaminyltransferase Activity Protein O-linked Glycosylation Via N-acetyl-galactosamine Carbohydrate Binding Metal Ion Binding Protein O-linked Glycosylation Protein Glycosylation Macromolecule Glycosylation Glycosylation Glycosyltransferase Activity Glycoprotein Biosynthetic Process Glycoprotein Metabolic Process Defense Response To Fungus Response To Fungus Negative Regulation Of Tumor Necrosis Factor (ligand) Superfamily Member 11 Production Alpha-amylase Activity Negative Regulation Of Single-species Biofilm Formation In Or On Host Organism Carbohydrate Derivative Biosynthetic Process Antimicrobial Humoral Immune Response Mediated By Antimicrobial Peptide Killing Of Cells Of Another Organism Positive Regulation Of Bone Mineralization Involved In Bone Maturation Phagocytic Vesicle Lumen Membrane Destabilizing Activity Antimicrobial Humoral Response Heparin Binding Negative Regulation Of Osteoclast Development Golgi Membrane Extracellular Space Glycosphingolipid Binding Cell Killing Positive Regulation Of Chondrocyte Proliferation Regulation Of Osteoclast Development Carbohydrate Derivative Metabolic Process Cytolysis By Host Of Symbiont Cells Antifungal Humoral Response Chloride Ion Binding Humoral Immune Response Negative Regulation Of ATP-dependent Activity Negative Regulation Of Membrane Potential Negative Regulation Of Lipopolysaccharide-mediated Signaling Pathway Positive Regulation Of Osteoblast Proliferation Oligosaccharide Binding Specific Granule Positive Regulation Of Toll-like Receptor 4 Signaling Pathway Cation Binding Host-mediated Suppression Of Viral Proces Defense Response To Bacterium
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