Tmem114
entrez
74720
canonical
uniprot
Q9D563
canonical
ensembl
ENSMUSG00000022715
resolver
ensp
ENSMUSP00000023400
resolver
enst
ENSMUST00000023400
resolver
genesymbol
Tmem114
resolver
genesymbol_syn
Cldn26
resolver
uniprot_entry
TM114_MOUSE
resolver
amino_acid_sequence
MRVRLGALAGAAALSGALSFVLLAAAIGTDFWYIIDTERLERSSQRMRDQGPANRSQQEPLSSHSGLWRTCRVQSSCTPLMNPFWQENVTVSDSSRQLLTMHGTFVILLPLSLIVMVFGGMTGFLSFLLRAHLLLLLTGILFLFGAMVTLTGISIYIAYSAVAFREAVCLLEERALLDQVDIRFGWSLALGWISFVSELLTGVVFLAAARALSLSQRQDQAI
uniprot
proteins
mass_dalton
24388
uniprot
proteins
mutagenesis
MUTAGEN 54; /note="N->K: Complete loss of glycosylation; when associated with K-88."; /evidence="ECO:0000269|PubMed:21689651"; MUTAGEN 88; /note="N->K: Complete loss of glycosylation; when associated with K-54."; /evidence="ECO:0000269|PubMed:21689651
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17492639
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21276448
uniprot
proteins
pubmed
21689651
uniprot
proteins
sequence_length
222
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:21276448}. Lateral cell membrane {ECO:0000269|PubMed:21689651}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:21689651}; Multi-pass membrane protein {ECO:0000255}. Note=N-glycosylation at Asn-54 and Asn-88 is required for plasma membrane localization. {ECO:0000269|PubMed:21689651}.
uniprot
proteins
transmembrane_region
TRANSMEM 7..27; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 105..125; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 133..153; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 188..208; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins