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P26038

- MOES_HUMAN

UniProt

P26038 - MOES_HUMAN

Protein

Moesin

Gene

MSN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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 binding Source: UniProtKB
    4. protein kinase binding Source: UniProtKB
    5. receptor binding Source: UniProtKB
    6. structural constituent of cytoskeleton Source: ProtInc

    GO - Biological processi

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

    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: UniProt
    5. cytoplasm Source: HPA
    6. cytoskeleton Source: UniProtKB
    7. extracellular space Source: UniProt
    8. extracellular vesicular exosome Source: UniProtKB
    9. extrinsic component of membrane Source: InterPro
    10. filopodium Source: BHF-UCL
    11. microvillus Source: BHF-UCL
    12. microvillus membrane Source: UniProtKB-SubCell
    13. plasma membrane Source: HPA
    14. uropod Source: Ensembl
    15. vesicle Source: UniProtKB

    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 residuei79 – 791N6-acetyllysine1 Publication
    Modified residuei116 – 1161Phosphotyrosine1 Publication
    Modified residuei139 – 1391N6-acetyllysine1 Publication
    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 similarity2 Publications

    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.
    GenevestigatoriP26038.

    Organism-specific databases

    HPAiCAB010898.
    CAB047336.
    CAB047338.
    HPA000263.
    HPA000763.
    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
    LRRK2Q5S00712EBI-528768,EBI-5323863
    SLC9A3R1O147455EBI-528768,EBI-349787

    Protein-protein interaction databases

    BioGridi110584. 73 interactions.
    IntActiP26038. 14 interactions.
    MINTiMINT-3010439.
    STRINGi9606.ENSP00000353408.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    OMAiPHVTEPM.
    OrthoDBiEOG7BGHK6.
    PhylomeDBiP26038.
    TreeFamiTF313935.

    Family and domain databases

    Gene3Di1.20.80.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProiIPR019749. Band_41_domain.
    IPR019750. Band_41_fam.
    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

    MPKTISVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWFFGLQYQ    50
    DTKGFSTWLK LNKKVTAQDV RKESPLLFKF RAKFYPEDVS EELIQDITQR 100
    LFFLQVKEGI LNDDIYCPPE TAVLLASYAV QSKYGDFNKE VHKSGYLAGD 150
    KLLPQRVLEQ HKLNKDQWEE RIQVWHEEHR GMLREDAVLE YLKIAQDLEM 200
    YGVNYFSIKN KKGSELWLGV DALGLNIYEQ NDRLTPKIGF PWSEIRNISF 250
    NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI 300
    EVQQMKAQAR EEKHQKQMER AMLENEKKKR EMAEKEKEKI EREKEELMER 350
    LKQIEEQTKK AQQELEEQTR RALELEQERK RAQSEAEKLA KERQEAEEAK 400
    EALLQASRDQ KKTQEQLALE MAELTARISQ LEMARQKKES EAVEWQQKAQ 450
    MVQEDLEKTR AELKTAMSTP HVAEPAENEQ DEQDENGAEA SADLRADAMA 500
    KDRSEEERTT EAEKNERVQK HLKALTSELA NARDESKKTA NDMIHAENMR 550
    LGRDKYKTLR QIRQGNTKQR IDEFESM 577
    Length:577
    Mass (Da):67,820
    Last modified:January 23, 2007 - v3
    Checksum:i865A6C5CB14AE586
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M69066 mRNA. Translation: AAA36322.1 .
    Z98946 Genomic DNA. Translation: CAB46379.1 .
    BC017293 mRNA. Translation: AAH17293.1 .
    CCDSi CCDS14382.1.
    PIRi A41289.
    RefSeqi NP_002435.1. NM_002444.2.
    UniGenei Hs.87752.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1E5W X-ray 2.70 A 2-346 [» ]
    1EF1 X-ray 1.90 A/B 4-297 [» ]
    C/D 488-577 [» ]
    1SGH X-ray 3.50 A 1-297 [» ]
    ProteinModelPortali P26038.
    SMRi P26038. Positions 1-577.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110584. 73 interactions.
    IntActi P26038. 14 interactions.
    MINTi MINT-3010439.
    STRINGi 9606.ENSP00000353408.

    PTM databases

    PhosphoSitei P26038.

    Polymorphism databases

    DMDMi 127234.

    2D gel databases

    OGPi P26038.

    Proteomic databases

    MaxQBi P26038.
    PaxDbi P26038.
    PeptideAtlasi P26038.
    PRIDEi P26038.

    Protocols and materials databases

    DNASUi 4478.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360270 ; ENSP00000353408 ; ENSG00000147065 .
    GeneIDi 4478.
    KEGGi hsa:4478.
    UCSCi uc004dwf.3. human.

    Organism-specific databases

    CTDi 4478.
    GeneCardsi GC0XP064887.
    HGNCi HGNC:7373. MSN.
    HPAi CAB010898.
    CAB047336.
    CAB047338.
    HPA000263.
    HPA000763.
    HPA011135.
    HPA011227.
    MIMi 309845. gene.
    neXtProti NX_P26038.
    PharmGKBi PA31178.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG236035.
    HOGENOMi HOG000007113.
    HOVERGENi HBG002185.
    InParanoidi P26038.
    KOi K05763.
    OMAi PHVTEPM.
    OrthoDBi EOG7BGHK6.
    PhylomeDBi P26038.
    TreeFami TF313935.

    Enzyme and pathway databases

    Reactomei REACT_22365. Recycling pathway of L1.

    Miscellaneous databases

    ChiTaRSi MSN. human.
    EvolutionaryTracei P26038.
    GeneWikii Moesin.
    GenomeRNAii 4478.
    NextBioi 17331.
    PMAP-CutDB P26038.
    PROi P26038.
    SOURCEi Search...

    Gene expression databases

    Bgeei P26038.
    CleanExi HS_MSN.
    Genevestigatori P26038.

    Family and domain databases

    Gene3Di 1.20.80.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProi IPR019749. Band_41_domain.
    IPR019750. Band_41_fam.
    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 ]
    Pfami PF00769. ERM. 1 hit.
    PF09380. FERM_C. 1 hit.
    PF00373. FERM_M. 1 hit.
    PF09379. FERM_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002305. ERM. 1 hit.
    PRINTSi PR00935. BAND41.
    PR00661. ERMFAMILY.
    SMARTi SM00295. B41. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47031. SSF47031. 1 hit.
    SSF48678. SSF48678. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEi PS00660. FERM_1. 1 hit.
    PS00661. FERM_2. 1 hit.
    PS50057. FERM_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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.
    16. "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.
    17. "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: October 1, 2014
    This is version 166 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