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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

  1. cell adhesion molecule binding Source: BHF-UCL
  2. double-stranded RNA binding Source: MGI
  3. protein kinase binding Source: UniProtKB
  4. receptor binding Source: UniProtKB
  5. structural constituent of cytoskeleton Source: ProtInc

GO - Biological processi

  1. establishment of endothelial barrier Source: UniProtKB
  2. leukocyte cell-cell adhesion Source: BHF-UCL
  3. leukocyte migration Source: BHF-UCL
  4. membrane to membrane docking Source: BHF-UCL
  5. movement of cell or subcellular component Source: UniProtKB
  6. positive regulation of gene expression Source: UniProtKB
  7. regulation of lymphocyte migration Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_22365. Recycling pathway of L1.

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
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:7373. MSN.

Subcellular locationi

Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cytoplasmcytoskeleton By similarity. Apical cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cell projectionmicrovillus membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
Note: Phosphorylated form is enriched in microvilli-like structures at apical membrane (By similarity). Increased cell membrane localization of both phosphorylated and non-phosphorylated forms seen after thrombin treatment.By similarity1 Publication

GO - Cellular componenti

  1. apical part of cell Source: BHF-UCL
  2. apical plasma membrane Source: UniProtKB-SubCell
  3. basolateral plasma membrane Source: Ensembl
  4. blood microparticle Source: UniProtKB
  5. cell periphery Source: UniProtKB
  6. cytoplasm Source: HPA
  7. cytoskeleton Source: UniProtKB
  8. extracellular space Source: UniProtKB
  9. extracellular vesicular exosome Source: UniProtKB
  10. extrinsic component of membrane Source: InterPro
  11. filopodium Source: BHF-UCL
  12. focal adhesion Source: UniProtKB
  13. microvillus Source: BHF-UCL
  14. microvillus membrane Source: UniProtKB-SubCell
  15. plasma membrane Source: HPA
  16. uropod Source: Ensembl
  17. vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi556 – 5561Y → R: Impairs phosphorylation by STK10. 1 Publication
Mutagenesisi558 – 5581T → A: Abolishes phosphorylation by STK10. 1 Publication
Mutagenesisi558 – 5581T → D: Phosphomimetic mutant. 1 Publication

Organism-specific databases

PharmGKBiPA31178.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 577576MoesinPRO_0000219416Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601N6-acetyllysineBy similarity
Modified residuei79 – 791N6-acetyllysine1 Publication
Modified residuei83 – 831N6-succinyllysineBy similarity
Modified residuei116 – 1161Phosphotyrosine1 Publication
Modified residuei139 – 1391N6-acetyllysine1 Publication
Modified residuei146 – 1461PhosphotyrosineBy similarity
Modified residuei165 – 1651N6-acetyllysineBy similarity
Modified residuei558 – 5581Phosphothreonine; by ROCK2 and STK101 Publication

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP26038.
PaxDbiP26038.
PeptideAtlasiP26038.
PRIDEiP26038.

2D gel databases

OGPiP26038.

PTM databases

PhosphoSiteiP26038.

Miscellaneous databases

PMAP-CutDBP26038.

Expressioni

Tissue specificityi

In all tissues and cultured cells studied.

Gene expression databases

BgeeiP26038.
CleanExiHS_MSN.
ExpressionAtlasiP26038. baseline and differential.
GenevestigatoriP26038.

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
LRRK2Q5S00715EBI-528768,EBI-5323863
Lrrk2Q5S0062EBI-528768,EBI-2693710From a different organism.
SLC9A3R1O147455EBI-528768,EBI-349787

Protein-protein interaction databases

BioGridi110584. 74 interactions.
IntActiP26038. 15 interactions.
MINTiMINT-3010439.
STRINGi9606.ENSP00000353408.

Structurei

Secondary structure

1
577
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 117Combined sources
Beta strandi14 – 207Combined sources
Helixi26 – 3712Combined sources
Helixi42 – 443Combined sources
Beta strandi45 – 517Combined sources
Beta strandi56 – 583Combined sources
Beta strandi61 – 644Combined sources
Helixi65 – 673Combined sources
Beta strandi74 – 8411Combined sources
Helixi89 – 924Combined sources
Helixi96 – 11116Combined sources
Helixi119 – 13416Combined sources
Turni139 – 1413Combined sources
Turni144 – 1496Combined sources
Helixi155 – 1606Combined sources
Helixi165 – 17814Combined sources
Turni179 – 1813Combined sources
Helixi184 – 19512Combined sources
Turni199 – 2024Combined sources
Beta strandi204 – 2096Combined sources
Beta strandi215 – 2217Combined sources
Beta strandi224 – 2296Combined sources
Beta strandi233 – 2353Combined sources
Beta strandi237 – 2415Combined sources
Helixi242 – 2443Combined sources
Beta strandi245 – 2517Combined sources
Beta strandi254 – 26411Combined sources
Beta strandi267 – 2704Combined sources
Helixi274 – 29522Combined sources
Helixi301 – 34343Combined sources
Helixi504 – 5074Combined sources
Helixi511 – 5144Combined sources
Helixi516 – 53015Combined sources
Helixi540 – 55011Combined sources
Helixi555 – 5628Combined sources
Helixi567 – 5759Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP26038.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 295294FERMPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 FERM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG236035.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiP26038.
KOiK05763.
OMAiHKKMERA.
OrthoDBiEOG7BGHK6.
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_like_dom.
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.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF48678. SSF48678. 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.87752.

Genome annotation databases

EnsembliENST00000360270; ENSP00000353408; ENSG00000147065.
GeneIDi4478.
KEGGihsa:4478.
UCSCiuc004dwf.3. human.

Polymorphism databases

DMDMi127234.

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.87752.

3D structure databases

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

Protein-protein interaction databases

BioGridi110584. 74 interactions.
IntActiP26038. 15 interactions.
MINTiMINT-3010439.
STRINGi9606.ENSP00000353408.

PTM databases

PhosphoSiteiP26038.

Polymorphism databases

DMDMi127234.

2D gel databases

OGPiP26038.

Proteomic databases

MaxQBiP26038.
PaxDbiP26038.
PeptideAtlasiP26038.
PRIDEiP26038.

Protocols and materials databases

DNASUi4478.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360270; ENSP00000353408; ENSG00000147065.
GeneIDi4478.
KEGGihsa:4478.
UCSCiuc004dwf.3. human.

Organism-specific databases

CTDi4478.
GeneCardsiGC0XP064887.
HGNCiHGNC:7373. MSN.
HPAiCAB010898.
CAB047336.
CAB047338.
HPA000263.
HPA011135.
HPA011227.
MIMi309845. gene.
neXtProtiNX_P26038.
PharmGKBiPA31178.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG236035.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiP26038.
KOiK05763.
OMAiHKKMERA.
OrthoDBiEOG7BGHK6.
PhylomeDBiP26038.
TreeFamiTF313935.

Enzyme and pathway databases

ReactomeiREACT_22365. Recycling pathway of L1.

Miscellaneous databases

ChiTaRSiMSN. human.
EvolutionaryTraceiP26038.
GeneWikiiMoesin.
GenomeRNAii4478.
NextBioi17331.
PMAP-CutDBP26038.
PROiP26038.
SOURCEiSearch...

Gene expression databases

BgeeiP26038.
CleanExiHS_MSN.
ExpressionAtlasiP26038. baseline and differential.
GenevestigatoriP26038.

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_like_dom.
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.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF48678. SSF48678. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Moesin: a member of the protein 4.1-talin-ezrin family of proteins."
    Lankes W.T., Furthmayr H.
    Proc. Natl. Acad. Sci. U.S.A. 88:8297-8301(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-16; 54-60 AND 414-435.
    Tissue: Placenta.
  2. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pancreas.
  4. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-8.
    Tissue: Platelet.
  5. "Identification of EBP50: a PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family."
    Reczek D., Berryman M., Bretscher A.
    J. Cell Biol. 139:169-179(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC9A3R1.
  6. "ITAM-based interaction of ERM proteins with Syk mediates signaling by the leukocyte adhesion receptor PSGL-1."
    Urzainqui A., Serrador J.M., Viedma F., Yanez-Mo M., Rodriguez A., Corbi A.L., Alonso-Lebrero J.L., Luque A., Deckert M., Vazquez J., Sanchez-Madrid F.
    Immunity 17:401-412(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SELPLG AND SYK.
  7. "TIMAP is a positive regulator of pulmonary endothelial barrier function."
    Csortos C., Czikora I., Bogatcheva N.V., Adyshev D.M., Poirier C., Olah G., Verin A.D.
    Am. J. Physiol. 295:L440-L450(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PPP1R16B.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "LOK is a major ERM kinase in resting lymphocytes and regulates cytoskeletal rearrangement through ERM phosphorylation."
    Belkina N.V., Liu Y., Hao J.J., Karasuyama H., Shaw S.
    Proc. Natl. Acad. Sci. U.S.A. 106:4707-4712(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-558, MUTAGENESIS OF TYR-556 AND THR-558.
  10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79 AND LYS-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "PDZD8 is a novel moesin-interacting cytoskeletal regulatory protein that suppresses infection by herpes simplex virus type 1."
    Henning M.S., Stiedl P., Barry D.S., McMahon R., Morham S.G., Walsh D., Naghavi M.H.
    Virology 415:114-121(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MSN.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain."
    Pearson M.A., Reczek D., Bretscher A., Karplus P.A.
    Cell 101:259-270(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 4-577.
  17. "The 2.7 A crystal structure of the activated FERM domain of moesin: an analysis of structural changes on activation."
    Edwards S.D., Keep N.H.
    Biochemistry 40:7061-7068(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-346.
  18. "The EBP50-moesin interaction involves a binding site regulated by direct masking on the FERM domain."
    Finnerty C.M., Chambers D., Ingraffea J., Faber H.R., Karplus P.A., Bretscher A.
    J. Cell Sci. 117:1547-1552(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 1-297 IN COMPLEX WITH SLC9A3R1.

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: March 4, 2015
This is version 171 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

External Data

Dasty 3

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 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.