SNX1

Sorting nexin 1
250px PDB rendering based on 2i4k.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2I4K, 4FZS
Identifiers
Symbols	SNX1 ; HsT17379; VPS5
External IDs	OMIM: 601272 MGI: 1928395 HomoloGene: 99716 GeneCards: SNX1 Gene
Gene ontology Molecular function • epidermal growth factor receptor binding • insulin receptor binding • protein binding • phosphatidylinositol binding • identical protein binding • transferrin receptor binding • leptin receptor binding Cellular component • cytoplasm • endosome • Golgi apparatus • cytosol • endosome membrane • membrane • extrinsic component of membrane • lamellipodium • retromer complex • early endosome membrane • intracellular membrane-bounded organelle • protein complex Biological process • intracellular protein transport • vesicle organization • receptor internalization • early endosome to Golgi transport • retrograde transport, endosome to Golgi • positive regulation of protein catabolic process • lamellipodium morphogenesis Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6642	56440
Ensembl	ENSG00000028528	ENSMUSG00000032382
UniProt	Q13596	Q9WV80
RefSeq (mRNA)	NM_001242933	NM_019727
RefSeq (protein)	NP_001229862	NP_062701
Location (UCSC)	Chr 15: 64.09 – 64.15 Mb	Chr 9: 66.09 – 66.13 Mb
PubMed search	[1]	[2]

Sorting nexin-1 is a protein that in humans is encoded by the SNX1 gene. The protein encoded by this gene is a sorting nexin. SNX1 is a component of the retromer complex.

Function

This gene encodes a member of the sorting nexin family. Members of this family contain a phox (PX) domain, which is a phosphoinositide binding domain, and are involved in intracellular trafficking. This endosomal protein regulates the cell-surface expression of epidermal growth factor receptor. This protein also has a role in sorting protease-activated receptor-1 from early endosomes to lysosomes. This protein may form oligomeric complexes with other family members.

External links

• sorting nexins at the US National Library of Medicine Medical Subject Headings (MeSH)

This article incorporates text from the United States National Library of Medicine, which is in the public domain.