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Protein

Moesin

Gene

MSN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probably involved in connections of major cytoskeletal structures to the plasma membrane. May inhibit herpes simplex virus 1 infection at an early stage.1 Publication

Enzyme regulationi

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.By similarity

GO - Molecular functioni

  • cell adhesion molecule binding Source: BHF-UCL
  • double-stranded RNA binding Source: MGI
  • protein kinase binding Source: UniProtKB
  • receptor binding Source: UniProtKB
  • structural constituent of cytoskeleton Source: ProtInc

GO - Biological processi

  • cellular response to testosterone stimulus Source: UniProtKB
  • establishment of endothelial barrier Source: UniProtKB
  • establishment of epithelial cell apical/basal polarity Source: UniProtKB
  • gland morphogenesis Source: UniProtKB
  • leukocyte cell-cell adhesion Source: BHF-UCL
  • leukocyte migration Source: BHF-UCL
  • membrane to membrane docking Source: BHF-UCL
  • movement of cell or subcellular component Source: UniProtKB
  • positive regulation of cellular protein catabolic process Source: UniProtKB
  • positive regulation of early endosome to late endosome transport Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of podosome assembly Source: Ensembl
  • positive regulation of protein localization to early endosome Source: UniProtKB
  • regulation of cell shape Source: UniProtKB
  • regulation of cell size Source: UniProtKB
  • regulation of lymphocyte migration Source: UniProtKB
  • regulation of organelle assembly Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000147065-MONOMER.
ReactomeiR-HSA-437239. Recycling pathway of L1.
SIGNORiP26038.

Names & Taxonomyi

Protein namesi
Recommended name:
Moesin
Alternative name(s):
Membrane-organizing extension spike protein
Gene namesi
Name:MSN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:7373. MSN.

Subcellular locationi

GO - Cellular componenti

  • apical part of cell Source: BHF-UCL
  • apical plasma membrane Source: UniProtKB
  • basolateral plasma membrane Source: Ensembl
  • blood microparticle Source: UniProtKB
  • cell periphery Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • extrinsic component of membrane Source: InterPro
  • filopodium Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • microvillus Source: BHF-UCL
  • microvillus membrane Source: UniProtKB-SubCell
  • myelin sheath Source: Ensembl
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: HPA
  • pseudopodium Source: UniProtKB
  • uropod Source: Ensembl
  • vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi115I → M: Inhibits S-nitrosylation of Cys-117; when associated with M-120. 1 Publication1
Mutagenesisi120E → M: Inhibits S-nitrosylation of Cys-117; when associated with M-115. 1 Publication1
Mutagenesisi556Y → R: Impairs phosphorylation by STK10. 1 Publication1
Mutagenesisi558T → A: Abolishes phosphorylation by STK10. 1 Publication1
Mutagenesisi558T → D: Phosphomimetic mutant. 1 Publication1

Organism-specific databases

DisGeNETi4478.
OpenTargetsiENSG00000147065.
PharmGKBiPA31178.

Polymorphism and mutation databases

BioMutaiMSN.
DMDMi127234.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00002194162 – 577MoesinAdd BLAST576

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei74PhosphoserineCombined sources1
Modified residuei79N6-acetyllysineCombined sources1
Modified residuei83N6-succinyllysineBy similarity1
Modified residuei116PhosphotyrosineCombined sources1
Modified residuei117S-nitrosocysteine1 Publication1
Modified residuei139N6-acetyllysineCombined sources1
Modified residuei165N6-acetyllysineBy similarity1
Modified residuei407PhosphoserineCombined sources1
Modified residuei527PhosphoserineCombined sources1
Modified residuei558Phosphothreonine; by ROCK2 and STK101 Publication1

Post-translational modificationi

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.By similarity1 Publication
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.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

EPDiP26038.
PaxDbiP26038.
PeptideAtlasiP26038.
PRIDEiP26038.

2D gel databases

OGPiP26038.

PTM databases

iPTMnetiP26038.
PhosphoSitePlusiP26038.
SwissPalmiP26038.

Miscellaneous databases

PMAP-CutDBP26038.

Expressioni

Tissue specificityi

In all tissues and cultured cells studied.

Gene expression databases

BgeeiENSG00000147065.
CleanExiHS_MSN.
ExpressionAtlasiP26038. baseline and differential.
GenevisibleiP26038. HS.

Organism-specific databases

HPAiCAB010898.
CAB047336.
CAB047338.
HPA000263.
HPA011135.
HPA011227.

Interactioni

Subunit structurei

In resting T-cells, part of a PAG1-SLC9A3R1-MSN complex which is disrupted upon TCR activation (By similarity). Binds SLC9A3R1. Interacts with PPP1R16B. Interacts with PDZD8. Interacts with SELPLG and SYK; mediates the activation of SYK by SELPLG.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CD44P160706EBI-528768,EBI-490245
LRRK2Q5S00717EBI-528768,EBI-5323863
Lrrk2Q5S0062EBI-528768,EBI-2693710From a different organism.
SLC9A3R1O147454EBI-528768,EBI-349787
TERF1P542742EBI-528768,EBI-710997

GO - Molecular functioni

  • cell adhesion molecule binding Source: BHF-UCL
  • protein kinase binding Source: UniProtKB
  • receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110584. 126 interactors.
DIPiDIP-33841N.
IntActiP26038. 25 interactors.
MINTiMINT-3010439.
STRINGi9606.ENSP00000353408.

Structurei

Secondary structure

1577
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 11Combined sources7
Beta strandi14 – 20Combined sources7
Helixi26 – 37Combined sources12
Helixi42 – 44Combined sources3
Beta strandi45 – 51Combined sources7
Beta strandi56 – 58Combined sources3
Beta strandi61 – 64Combined sources4
Helixi65 – 67Combined sources3
Beta strandi74 – 84Combined sources11
Helixi89 – 92Combined sources4
Helixi96 – 111Combined sources16
Helixi119 – 134Combined sources16
Turni139 – 141Combined sources3
Turni144 – 149Combined sources6
Helixi155 – 160Combined sources6
Helixi165 – 178Combined sources14
Turni179 – 181Combined sources3
Helixi184 – 195Combined sources12
Turni199 – 202Combined sources4
Beta strandi204 – 209Combined sources6
Beta strandi215 – 221Combined sources7
Beta strandi224 – 229Combined sources6
Beta strandi233 – 235Combined sources3
Beta strandi237 – 241Combined sources5
Helixi242 – 244Combined sources3
Beta strandi245 – 251Combined sources7
Beta strandi254 – 264Combined sources11
Beta strandi267 – 270Combined sources4
Helixi274 – 295Combined sources22
Helixi301 – 343Combined sources43
Helixi504 – 507Combined sources4
Helixi511 – 514Combined sources4
Helixi516 – 530Combined sources15
Helixi540 – 550Combined sources11
Helixi555 – 562Combined sources8
Helixi567 – 575Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E5WX-ray2.70A2-346[»]
1EF1X-ray1.90A/B4-297[»]
C/D488-577[»]
1SGHX-ray3.50A1-297[»]
ProteinModelPortaliP26038.
SMRiP26038.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26038.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 295FERMPROSITE-ProRule annotationAdd BLAST294

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi115 – 120[IL]-x-C-x-x-[DE] motif1 Publication6

Domaini

The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex.1 Publication

Sequence similaritiesi

Contains 1 FERM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3529. Eukaryota.
ENOG410XQFP. LUCA.
GeneTreeiENSGT00860000133686.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiP26038.
KOiK05763.
OMAiPHVTEPM.
OrthoDBiEOG091G06UO.
PhylomeDBiP26038.
TreeFamiTF313935.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR019749. Band_41_domain.
IPR011174. ERM.
IPR011259. ERM_C_dom.
IPR000798. Ez/rad/moesin-like.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR018980. FERM_PH-like_C.
IPR008954. Moesin_tail.
IPR011993. PH_dom-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00769. ERM. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
[Graphical view]
PIRSFiPIRSF002305. ERM. 1 hit.
PRINTSiPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTiSM00295. B41. 1 hit.
SM01196. FERM_C. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF48678. SSF48678. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P26038-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKTISVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWFFGLQYQ
60 70 80 90 100
DTKGFSTWLK LNKKVTAQDV RKESPLLFKF RAKFYPEDVS EELIQDITQR
110 120 130 140 150
LFFLQVKEGI LNDDIYCPPE TAVLLASYAV QSKYGDFNKE VHKSGYLAGD
160 170 180 190 200
KLLPQRVLEQ HKLNKDQWEE RIQVWHEEHR GMLREDAVLE YLKIAQDLEM
210 220 230 240 250
YGVNYFSIKN KKGSELWLGV DALGLNIYEQ NDRLTPKIGF PWSEIRNISF
260 270 280 290 300
NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI
310 320 330 340 350
EVQQMKAQAR EEKHQKQMER AMLENEKKKR EMAEKEKEKI EREKEELMER
360 370 380 390 400
LKQIEEQTKK AQQELEEQTR RALELEQERK RAQSEAEKLA KERQEAEEAK
410 420 430 440 450
EALLQASRDQ KKTQEQLALE MAELTARISQ LEMARQKKES EAVEWQQKAQ
460 470 480 490 500
MVQEDLEKTR AELKTAMSTP HVAEPAENEQ DEQDENGAEA SADLRADAMA
510 520 530 540 550
KDRSEEERTT EAEKNERVQK HLKALTSELA NARDESKKTA NDMIHAENMR
560 570
LGRDKYKTLR QIRQGNTKQR IDEFESM
Length:577
Mass (Da):67,820
Last modified:January 23, 2007 - v3
Checksum:i865A6C5CB14AE586
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M69066 mRNA. Translation: AAA36322.1.
Z98946 Genomic DNA. Translation: CAB46379.1.
BC017293 mRNA. Translation: AAH17293.1.
CCDSiCCDS14382.1.
PIRiA41289.
RefSeqiNP_002435.1. NM_002444.2.
UniGeneiHs.713679.
Hs.87752.

Genome annotation databases

EnsembliENST00000360270; ENSP00000353408; ENSG00000147065.
GeneIDi4478.
KEGGihsa:4478.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M69066 mRNA. Translation: AAA36322.1.
Z98946 Genomic DNA. Translation: CAB46379.1.
BC017293 mRNA. Translation: AAH17293.1.
CCDSiCCDS14382.1.
PIRiA41289.
RefSeqiNP_002435.1. NM_002444.2.
UniGeneiHs.713679.
Hs.87752.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E5WX-ray2.70A2-346[»]
1EF1X-ray1.90A/B4-297[»]
C/D488-577[»]
1SGHX-ray3.50A1-297[»]
ProteinModelPortaliP26038.
SMRiP26038.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110584. 126 interactors.
DIPiDIP-33841N.
IntActiP26038. 25 interactors.
MINTiMINT-3010439.
STRINGi9606.ENSP00000353408.

PTM databases

iPTMnetiP26038.
PhosphoSitePlusiP26038.
SwissPalmiP26038.

Polymorphism and mutation databases

BioMutaiMSN.
DMDMi127234.

2D gel databases

OGPiP26038.

Proteomic databases

EPDiP26038.
PaxDbiP26038.
PeptideAtlasiP26038.
PRIDEiP26038.

Protocols and materials databases

DNASUi4478.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360270; ENSP00000353408; ENSG00000147065.
GeneIDi4478.
KEGGihsa:4478.

Organism-specific databases

CTDi4478.
DisGeNETi4478.
GeneCardsiMSN.
HGNCiHGNC:7373. MSN.
HPAiCAB010898.
CAB047336.
CAB047338.
HPA000263.
HPA011135.
HPA011227.
MIMi309845. gene.
neXtProtiNX_P26038.
OpenTargetsiENSG00000147065.
PharmGKBiPA31178.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3529. Eukaryota.
ENOG410XQFP. LUCA.
GeneTreeiENSGT00860000133686.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiP26038.
KOiK05763.
OMAiPHVTEPM.
OrthoDBiEOG091G06UO.
PhylomeDBiP26038.
TreeFamiTF313935.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000147065-MONOMER.
ReactomeiR-HSA-437239. Recycling pathway of L1.
SIGNORiP26038.

Miscellaneous databases

ChiTaRSiMSN. human.
EvolutionaryTraceiP26038.
GeneWikiiMoesin.
GenomeRNAii4478.
PMAP-CutDBP26038.
PROiP26038.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000147065.
CleanExiHS_MSN.
ExpressionAtlasiP26038. baseline and differential.
GenevisibleiP26038. HS.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR019749. Band_41_domain.
IPR011174. ERM.
IPR011259. ERM_C_dom.
IPR000798. Ez/rad/moesin-like.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR018980. FERM_PH-like_C.
IPR008954. Moesin_tail.
IPR011993. PH_dom-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00769. ERM. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
[Graphical view]
PIRSFiPIRSF002305. ERM. 1 hit.
PRINTSiPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTiSM00295. B41. 1 hit.
SM01196. FERM_C. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF48678. SSF48678. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMOES_HUMAN
AccessioniPrimary (citable) accession number: P26038
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 191 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.