RNF26
entrez
79102
canonical
uniprot
Q9BY78
canonical
ensembl
ENSG00000173456
resolver
ensp
ENSP00000312439
resolver
enst
ENST00000311413
resolver
genesymbol
RNF26
resolver
hgnc
HGNC:14646
resolver
uniprot
Q542Y8
resolver
uniprot_entry
RNF26_HUMAN
resolver
uniprot_sec
Q542Y8
resolver
amino_acid_sequence
MEAVYLVVNGLGLVLDVLTLVLDLNFLLVSSLLASLAWLLAFVYNLPHTVLTSLLHLGRGVLLSLLALIEAVVRFTCGGLQALCTLLYSCCSGLESLKLLGHLASHGALRSREILHRGVLNVVSSGHALLRQACDICAIAMSLVAYVINSLVNICLIGTQNLFSLVLALWDAVTGPLWRMTDVVAAFLAHISSSAVAMAILLWTPCQLALELLASAARLLASFVLVNLTGLVLLACVLAVTVTVLHPDFTLRLATQALSQLHARPSYHRLREDVMRLSRLALGSEAWRRVWSRSLQLASWPNRGGAPGAPQGDPMRVFSVRTRRQDTLPEAGRRSEAEEEEARTIRVTPVRGRERLNEEEPPGGQDPWKLLKEQEERKKCVICQDQSKTVLLLPCRHLCLCQACTEILMRHPVYHRNCPLCRRGILQTLNVYL
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: E3 ubiquitin-protein ligase that plays a key role in endosome organization by retaining vesicles in the perinuclear cloud (PubMed:27368102). Acts as a platform for perinuclear positioning of the endosomal system by mediating ubiquitination of SQSTM1 through interaction with the ubiquitin conjugating enzyme UBE2J1 (PubMed:27368102, PubMed:33472082). Ubiquitinated SQSTM1 attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (PubMed:27368102, PubMed:33472082). Also acts as a regulator of type I interferon production in response to viral infection by mediating the formation of 'Lys-11'-linked polyubiquitin chains on TMEM173/STING, leading to stabilize TMEM173/STING (PubMed:25254379, PubMed:32614325). Also required to limit type I interferon response by promoting autophagic degradation of IRF3 (PubMed:25254379). {ECO:0000269|PubMed:25254379, ECO:0000269|PubMed:27368102, ECO:0000269|PubMed:32614325, ECO:0000269|PubMed:33472082}.
uniprot
proteins
mass_dalton
47737
uniprot
proteins
mutagenesis
MUTAGEN 382; /note="I->R: Strongly decreased E3 ubiquitin-protein ligase activity due to impaired interaction with E2 enzymes. Impaired ability to retain vesicles in the perinuclear cloud."; /evidence="ECO:0000269|PubMed:27368102"; MUTAGEN 395; /note="C->S: Strongly decreased E3 ubiquitin-protein ligase activity. Impaired ability to mediate ubiquitination of TMEM173/STING."; /evidence="ECO:0000269|PubMed:25254379"; MUTAGEN 399; /note="C->S: Strongly decreased E3 ubiquitin-protein ligase activity. Impaired ability to mediate ubiquitination of TMEM173/STING."; /evidence="ECO:0000269|PubMed:25254379"; MUTAGEN 401; /note="C->S: Strongly decreased E3 ubiquitin-protein ligase activity. Impaired ability to mediate ubiquitination of TMEM173/STING."; /evidence="ECO:0000269|PubMed:25254379"; MUTAGEN 432; /note="Y->A: About 4-fold increase of stability (from 30 min to 2 hours)."; /evidence="ECO:0000269|PubMed:32614325
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:25254379, ECO:0000269|PubMed:27368102}.
uniprot
proteins
pubmed
11352657
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16303743
uniprot
proteins
pubmed
21750715
uniprot
proteins
pubmed
25254379
uniprot
proteins
pubmed
27368102
uniprot
proteins
pubmed
32614325
uniprot
proteins
pubmed
33472082
uniprot
proteins
sequence_length
433
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:25254379, ECO:0000269|PubMed:27368102, ECO:0000269|PubMed:32614325}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 24..44; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 60..80; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 147..169; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 183..203; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 220..240; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins