Selected-GenAtlas references	SOURCE	GeneCards	NCBI Gene	Swiss-Prot	Ensembl
	HGNC	UniGene	Nucleotide	OMIM	UCSC

Home Page

FLASH GENE

Symbol

ZNRF4

contributors: mct - updated : 12-10-2011

HGNC name	zinc and ring finger 4
HGNC id	17726

FLASH GENE DNA RNA EXPRESSION PROTEIN DISORDER ANIMAL & CELL MODELS

RNA

TRANSCRIPTS	type	messenger

identification nb exons type bp product Protein kDa AA specific expression Year Pubmed NM_181710 1 - 1442 - 429 - 1999 10191088

EXPRESSION

Type

expressed in	(based on citations)
organ(s)	System Organ level 1 Organ level 2 Organ level 3 Organ level 4 Level Pubmed Species Stage Rna symbol Reproductive male system testis

cell lineage

cell lines

fluid/secretion

at STAGE

PROTEIN

PHYSICAL PROPERTIES

STRUCTURE

motifs/domains	one predicted transmembrane region separating an N-terminal protease-associated (PA) domain
	three potential N-glycosylation sites (NXS) from a C-terminal RING finger domain (RING)

HOMOLOGY

interspecies	ortholog to murine Znrf4
	ortholog to rattus znrf4

Homologene

FAMILY

Zn-finger family

CATEGORY

transcription factor

SUBCELLULAR LOCALIZATION	plasma membrane
	intracellular
	intracellular,cytoplasm,organelle,membrane
	intracellular,cytoplasm,organelle,endoplasmic reticulum
text	ER localization (subcellular fractionation revealed the presence of Nixin in the ER-enriched light membrane fraction together with the ER-localized protein calreticulin)

basic FUNCTION	ubiquitin-protein ligase activity
	central role for the regulation of calnexin (CANX)turnover
	induces a proteasome-mediated degradation of calnexin
	recognizes and ubiquitinates calnexin, which in turn would lead to the dislocation of CANX from the ER by VCP and subsequent degradation by the proteasome

CELLULAR PROCESS

nucleotide, transcription, regulation

PHYSIOLOGICAL PROCESS

PATHWAY

metabolism

signaling

a component

INTERACTION

DNA

RNA

small molecule	metal binding,
	Zn2+

protein

physically interacts with CANX in a glycosylation-independent manner, induces calnexin ubiquitination, and VCP-dependent degradation, indicating an ER-associated degradation-like mechanism of calnexin turnover

cell & other

REGULATION

ASSOCIATED DISORDERS

ANIMAL & CELL MODELS