EMC9
entrez
51016
canonical
uniprot
Q9Y3B6
canonical
ensembl
ENSG00000100908
resolver
ensembl
ENSG00000285377
resolver
ensp
ENSP00000216799
resolver
ensp
ENSP00000403210
resolver
ensp
ENSP00000454016
resolver
ensp
ENSP00000493482
resolver
ensp
ENSP00000494976
resolver
ensp
ENSP00000495623
resolver
ensp
ENSP00000542666
resolver
ensp
ENSP00000637279
resolver
ensp
ENSP00000745099
resolver
enst
ENST00000216799
resolver
enst
ENST00000419198
resolver
enst
ENST00000560403
resolver
enst
ENST00000642147
resolver
enst
ENST00000644280
resolver
enst
ENST00000646772
resolver
enst
ENST00000872607
resolver
enst
ENST00000967220
resolver
genesymbol
EMC9
resolver
genesymbol_syn
C14orf122
resolver
genesymbol_syn
FAM158A
resolver
hgnc
HGNC:20273
resolver
uniprot
D3DS60
resolver
uniprot
H0YNH6
resolver
uniprot
Q9BUM3
resolver
uniprot_entry
EMC9_HUMAN
resolver
uniprot_entry
H0YNH6_HUMAN
resolver
uniprot_sec
D3DS60
resolver
uniprot_sec
Q9BUM3
resolver
amino_acid_sequence
MGEVEISALAYVKMCLHAARYPHAAVNGLFLAPAPRSGECLCLTDCVPLFHSHLALSVMLEVALNQVDVWGAQAGLVVAGYYHANAAVNDQSPGPLALKIAGRIAEFFPDAVLIMLDNQKLVPQPRVPPVIVLENQGLRWVPKDKNLVMWRDWEESRQMVGALLEDRAHQHLVDFDCHLDDIRQDWTNQRLNTQITQWVGPTNGNGNA
uniprot
proteins
function
FUNCTION: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins (PubMed:29242231, PubMed:29809151, PubMed:30415835, PubMed:32459176). Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues (PubMed:29242231, PubMed:29809151, PubMed:30415835). Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices (PubMed:29809151, PubMed:30415835). It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes (PubMed:29242231, PubMed:29809151). By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors (PubMed:30415835). By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes (Probable). {ECO:0000269|PubMed:29242231, ECO:0000269|PubMed:29809151, ECO:0000269|PubMed:30415835, ECO:0000269|PubMed:32459176, ECO:0000305}.
uniprot
proteins
mass_dalton
23061
uniprot
proteins
protein_family
EMC8/EMC9 family
uniprot
proteins
pubmed
10810093
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
22119785
uniprot
proteins
pubmed
29242231
uniprot
proteins
pubmed
29809151
uniprot
proteins
pubmed
30415835
uniprot
proteins
pubmed
32459176
uniprot
proteins
sequence_length
208
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:32459176}; Peripheral membrane protein {ECO:0000305|PubMed:32459176}; Cytoplasmic side {ECO:0000269|PubMed:22119785}.
uniprot
proteins