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

Home Page

FLASH GENE

Symbol

ERLIN2

contributors: npt/shn/mct - updated : 06-01-2016

HGNC name	ER lipid raft associated 2
HGNC id	1356

FLASH GENE DNA RNA EXPRESSION PROTEIN DISORDER ANIMAL & CELL MODELS

DNA

TYPE	functioning gene
STRUCTURE	21.22 kb     12 Exon(s)

MAPPING

cloned

Y

linked

status

provisional

Map	pter - D8S1747 - D8S571 - ERLIN2 - D8S1722 - D8S536 - qter

RNA

TRANSCRIPTS	type	messenger

identification nb exons type bp product Protein kDa AA specific expression Year Pubmed NM_007175 (transcript variant 1) 12 splicing 4836 NP_009106 37 339 - - NM_001003791 (transcript variant 3) 7 splicing 1538 NP_001003791 - 152 - - NM_001003790 (transcript variant 2) 7 splicing 1765 NP_001003790 - 152 - -

EXPRESSION

Type	ubiquitous

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 Digestive intestine small intestine

tissue

System Tissue Tissue level 1 Tissue level 2 Level Pubmed Species Stage Rna symbol Connective bone

cell lineage

cell lines

fluid/secretion

at STAGE

physiological period

pregnancy

Text

placenta

PROTEIN

PHYSICAL PROPERTIES

STRUCTURE

motifs/domains	extreme N-terminus of ERLIN2 were found to be sufficient for heterologous targeting of GFP to the ER in the absence of classical ER retrieval motifs
	a SPFH domain

HOMOLOGY

interspecies	ortholog to Erlin2, Mus musculus
	ortholog to Erlin2, Rattus norvegicus
	ortholog to erlin2, Danio rerio
	ortholog to ERLIN2, Pan troglodytes

Homologene

FAMILY

prohibitin domain containing family of proteins

CATEGORY

unknown/unspecified

SUBCELLULAR LOCALIZATION	intracellular
	intracellular,cytoplasm,organelle,membrane
	intracellular,cytoplasm,organelle,endoplasmic reticulum
text	reside in detergent resistant membranes (DRMs) in the ER

basic FUNCTION	a mediator of the endoplasmic reticulum degradation (ERAD) pathway
	ERLIN1/ERLIN2 complex is a factor that selectively mediates the ERAD of activated IP(3) receptors
	novel mediator of ER-associated degradation
	is a novel oncogenic factor associated with the ER stress response pathway
	may confer a selective growth advantage for breast cancer cells by facilitating a cytoprotective response to various cellular stresses associated with oncogenesis
	is a regulator of cytosolic lipid content in cancer cells has important implications for understanding the molecular basis of tumorigenesis and the treatment of cancer
	gamma-secretase associated protein (GSAP), residing in detergent resistant membranes (DRMs) in the ER
	ERLIN1, ERLIN2 promote stability of the SREBF-SCAP-INSIG complex and may contribute to the highly cooperative control of this system

CELLULAR PROCESS

PHYSIOLOGICAL PROCESS

PATHWAY

metabolism

signaling

a component

ERLIN1/2 complex is composed of an assemblage of lower-order hetero-oligomers, probably heterotrimers, linked together by assembly domain hydrophobic AAs

INTERACTION

DNA

RNA

small molecule

protein	form a heterodimer with SPFH1 (
	ER membrane proteins, ERLIN2 and TMUB1, are associated proteins of mammalian AMFR, a membrane-bound ubiquitin ligase that mediates sterol-accelerated ERAD of the cholesterol biosynthetic enzyme HMGCR
	associated with active gamma-secretase in brain tissue (GSAP)
	interacts with gamma-secretase in brain, and reduces APP production while the effect on notch processing is limited
	multimeric ER proteins ERLIN1 and ERLIN2 are additional SREBF1, SREBF2 regulators

cell & other

REGULATION

ASSOCIATED DISORDERS

corresponding disease(s)

IDMDC , SPG18 , PLSJ2

Other morbid association(s)

Type Gene Modification Chromosome rearrangement Protein expression Protein Function tumoral     --over   of ZNF703, ERLIN2, PROSC, GPR124, and BRF2 in urothelial carcinoma

Susceptibility

Variant & Polymorphism

Candidate gene
Marker
Therapy target
	System Type Disorder Pubmed neurology neurodegenerative alzheimer interfering with the ERLIN2/gamma-secretase interaction might reduce APP production without affecting Notch processing, and thus be a pharmacological strategy for treatment of AD

ANIMAL & CELL MODELS