MSN
entrez
4478
canonical
uniprot
P26038
canonical
ensembl
ENSG00000147065
resolver
ensp
ENSP00000353408
resolver
ensp
ENSP00000513133
resolver
ensp
ENSP00000613421
resolver
enst
ENST00000360270
resolver
enst
ENST00000943362
resolver
genesymbol
HEL70
resolver
genesymbol
MSN
resolver
genesymbol_syn
MSN
resolver
hgnc
HGNC:7373
resolver
uniprot
V9HWC0
resolver
uniprot_entry
MOES_HUMAN
resolver
uniprot_entry
V9HWC0_HUMAN
resolver
activity_regulation
ACTIVITY REGULATION: A head-to-tail association, of the N-terminal and C-terminal halves results in a closed conformation (inactive form) which is incapable of actin or membrane-binding. {ECO:0000269|PubMed:10212266}.
uniprot
proteins
amino_acid_sequence
MPKTISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYPEDVSEELIQDITQRLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVLEQHKLNKDQWEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFESM
uniprot
proteins
disease_involvement
DISEASE: Immunodeficiency 50 (IMD50) [MIM:300988]: A primary immunodeficiency disorder characterized by onset of recurrent bacterial or varicella zoster virus infections in early childhood, profound lymphopenia, hypogammaglobulinemia, fluctuating monocytopenia and neutropenia, and a poor immune response to vaccine antigens. {ECO:0000269|PubMed:27405666}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Ezrin-radixin-moesin (ERM) family protein that connects the actin cytoskeleton to the plasma membrane and thereby regulates the structure and function of specific domains of the cell cortex. Tethers actin filaments by oscillating between a resting and an activated state providing transient interactions between moesin and the actin cytoskeleton (PubMed:10212266). Once phosphorylated on its C-terminal threonine, moesin is activated leading to interaction with F-actin and cytoskeletal rearrangement (PubMed:10212266). These rearrangements regulate many cellular processes, including cell shape determination, membrane transport, and signal transduction (PubMed:12387735, PubMed:15039356). The role of moesin is particularly important in immunity acting on both T and B-cells homeostasis and self-tolerance, regulating lymphocyte egress from lymphoid organs (PubMed:9298994, PubMed:9616160). Modulates phagolysosomal biogenesis in macrophages (By similarity). Also participates in immunologic synapse formation (PubMed:27405666). {ECO:0000250|UniProtKB:P26041, ECO:0000269|PubMed:10212266, ECO:0000269|PubMed:12387735, ECO:0000269|PubMed:15039356, ECO:0000269|PubMed:27405666, ECO:0000269|PubMed:9298994, ECO:0000269|PubMed:9616160}.
uniprot
proteins
mass_dalton
67820
uniprot
proteins
mutagenesis
MUTAGEN 115; /note="I->M: Inhibits S-nitrosylation of Cys-117; when associated with M-120."; /evidence="ECO:0000269|PubMed:25417112"; MUTAGEN 120; /note="E->M: Inhibits S-nitrosylation of Cys-117; when associated with M-115."; /evidence="ECO:0000269|PubMed:25417112"; MUTAGEN 556; /note="Y->R: Impairs phosphorylation by STK10."; /evidence="ECO:0000269|PubMed:19255442"; MUTAGEN 558; /note="T->A: Abolishes phosphorylation by STK10."; /evidence="ECO:0000269|PubMed:19255442"; MUTAGEN 558; /note="T->D: Completely abolishes the interaction between N- and C-terminal domains."; /evidence="ECO:0000269|PubMed:10212266"; MUTAGEN 558; /note="T->D: Phosphomimetic mutant."; /evidence="ECO:0000269|PubMed:19255442
uniprot
proteins
post_translational_modification
PTM: Phosphorylation on Thr-558 is crucial for the formation of microvilli-like structures. Phosphorylation by ROCK2 suppresses the head-to-tail association of the N-terminal and C-terminal halves resulting in an opened conformation which is capable of actin and membrane-binding (By similarity). Phosphorylation on Thr-558 by STK10 negatively regulates lymphocyte migration and polarization. {ECO:0000250, ECO:0000269|PubMed:19255442}.; PTM: S-nitrosylation of Cys-117 is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) implicating the iNOS-S100A8/9 transnitrosylase complex. {ECO:0000269|PubMed:25417112}.
uniprot
proteins
pubmed
10212266
uniprot
proteins
pubmed
10847681
uniprot
proteins
pubmed
11401550
uniprot
proteins
pubmed
11728332
uniprot
proteins
pubmed
12387735
uniprot
proteins
pubmed
12665801
uniprot
proteins
pubmed
15020681
uniprot
proteins
pubmed
15039356
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
17046996
uniprot
proteins
pubmed
18586956
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
1924289
uniprot
proteins
pubmed
19255442
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21549406
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25417112
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27405666
uniprot
proteins
pubmed
7884872
uniprot
proteins
pubmed
9213396
uniprot
proteins
pubmed
9298994
uniprot
proteins
pubmed
9314537
uniprot
proteins
pubmed
9616160
uniprot
proteins
sequence_length
577
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11728332, ECO:0000269|PubMed:15039356, ECO:0000269|PubMed:18586956, ECO:0000269|PubMed:7884872, ECO:0000269|PubMed:9298994}; Peripheral membrane protein {ECO:0000250|UniProtKB:P26041}; Cytoplasmic side {ECO:0000250|UniProtKB:P26041}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P26041}. Apical cell membrane {ECO:0000250|UniProtKB:P26041}; Peripheral membrane protein {ECO:0000250|UniProtKB:P26041}; Cytoplasmic side {ECO:0000250|UniProtKB:P26041}. Cell projection, microvillus membrane {ECO:0000250|UniProtKB:P26041}; Peripheral membrane protein {ECO:0000250|UniProtKB:P26041}; Cytoplasmic side {ECO:0000250|UniProtKB:P26041}. Cell projection, microvillus {ECO:0000250|UniProtKB:P26041}. Note=Phosphorylated form is enriched in microvilli-like structures at apical membrane. Increased cell membrane localization of both phosphorylated and non-phosphorylated forms seen after thrombin treatment (By similarity). Localizes at the uropods of T lymphoblasts. {ECO:0000250|UniProtKB:P26041, ECO:0000269|PubMed:18586956, ECO:0000269|PubMed:9298994}.
uniprot
proteins