Reviewed, UniProtKB/Swiss-Prot P26038 (MOES_HUMAN)

Names and origin

Protein names

Recommended name:
    Moesin
Alternative name(s):
    Membrane-organizing extension spike protein

Gene names

Name:

MSN

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	577 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Probably involved in connections of major cytoskeletal structures to the plasma membrane.
Subunit structure	In resting T-cells, part of a PAG1-SLC9A3R1-MSN complex which is disrupted upon TCR activation By similarity. Binds SLC9A3R1.
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasm › cytoskeleton By similarity. Apical cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell projection › microvillus membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Phosphorylated form is enriched in microvilli-like structures at apical membrane By similarity.
Tissue specificity	In all tissues and cultured cells studied.
Post-translational modification	Phosphorylation on Thr-558 is crucial for the formation of microvilli-like structures By similarity.
Sequence similarities	Contains 1 FERM domain.

Ontologies

Keywords
Cellular component	Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	leukocyte adhesion Inferred from expression pattern. Source: UniProtKB leukocyte migration Inferred from expression pattern. Source: UniProtKB membrane to membrane docking Inferred from expression pattern. Source: UniProtKB
Cellular component	apical plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Ref.1 Traceable author statement. Source: UniProtKB extrinsic to membrane Inferred from electronic annotation. Source: InterPro filopodium Inferred from direct assay. Source: UniProtKB microvillus membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cell adhesion molecule binding Inferred from physical interaction. Source: UniProtKB cytoskeletal protein binding Inferred from electronic annotation. Source: InterPro receptor binding Inferred from physical interaction. Source: UniProtKB structural constituent of cytoskeleton Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HLA-B	P30480	1	EBI-528768,EBI-1054175
SLC9A3R1	O14745	1	EBI-528768,EBI-349787

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1 Ref.4

Chain

2 – 577

576

Moesin

PRO_0000219416

Regions

Domain

2 – 295

294

FERM

Amino acid modifications

Modified residue

64

1

N6-acetyllysine Ref.6

Modified residue

116

1

Phosphotyrosine By similarity

Modified residue

558

1

Phosphothreonine By similarity

Modified residue

576

1

Phosphoserine Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

577

Helix Strand Turn

Details...

Beta strand

5 – 11

7

Beta strand

14 – 20

7

Helix

26 – 37

12

Helix

42 – 44

3

Beta strand

45 – 51

7

Beta strand

56 – 58

3

Beta strand

61 – 64

4

Helix

65 – 67

3

Beta strand

74 – 84

11

Helix

89 – 92

4

Helix

96 – 111

16

Helix

119 – 134

16

Turn

139 – 141

3

Turn

144 – 149

6

Helix

155 – 160

6

Helix

165 – 178

14

Turn

179 – 181

3

Helix

184 – 195

12

Turn

199 – 202

4

Beta strand

204 – 209

6

Beta strand

215 – 221

7

Beta strand

224 – 229

6

Beta strand

233 – 235

3

Beta strand

237 – 241

5

Helix

242 – 244

3

Beta strand

245 – 251

7

Beta strand

254 – 264

11

Beta strand

267 – 270

4

Helix

274 – 295

22

Helix

301 – 343

43

Beta strand

489 – 493

5

Helix

504 – 507

4

Helix

511 – 514

4

Helix

516 – 530

15

Helix

540 – 550

11

Helix

555 – 562

8

Helix

567 – 575

9

Sequences

	Sequence		Length	Mass (Da)
	P26038-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 865A6C5CB14AE586	FASTA	577	67,820
	10 20 30 40 50 60 MPKTISVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWFFGLQYQ DTKGFSTWLK 70 80 90 100 110 120 LNKKVTAQDV RKESPLLFKF RAKFYPEDVS EELIQDITQR LFFLQVKEGI LNDDIYCPPE 130 140 150 160 170 180 TAVLLASYAV QSKYGDFNKE VHKSGYLAGD KLLPQRVLEQ HKLNKDQWEE RIQVWHEEHR 190 200 210 220 230 240 GMLREDAVLE YLKIAQDLEM YGVNYFSIKN KKGSELWLGV DALGLNIYEQ NDRLTPKIGF 250 260 270 280 290 300 PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI 310 320 330 340 350 360 EVQQMKAQAR EEKHQKQMER AMLENEKKKR EMAEKEKEKI EREKEELMER LKQIEEQTKK 370 380 390 400 410 420 AQQELEEQTR RALELEQERK RAQSEAEKLA KERQEAEEAK EALLQASRDQ KKTQEQLALE 430 440 450 460 470 480 MAELTARISQ LEMARQKKES EAVEWQQKAQ MVQEDLEKTR AELKTAMSTP HVAEPAENEQ 490 500 510 520 530 540 DEQDENGAEA SADLRADAMA KDRSEEERTT EAEKNERVQK HLKALTSELA NARDESKKTA 550 560 570 NDMIHAENMR LGRDKYKTLR QIRQGNTKQR IDEFESM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 1924289] [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: 15772651] [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: 15489334] [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: 12665801] [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: 9314537] [Abstract] Cited for: INTERACTION WITH SLC9A3R1.
[6]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-64, MASS SPECTROMETRY. Tissue: Epithelium.
[7]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, MASS SPECTROMETRY.
[8]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[9]	"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: 10847681] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 4-577.
[10]	"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: 11401550] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-346.
[11]	"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: 15020681] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 1-297 IN COMPLEX WITH SLC9A3R1.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBLGenBankDDBJ

M69066 mRNA. Translation: AAA36322.1.
Z98946 Genomic DNA. Translation: CAB46379.1.
BC017293 mRNA. Translation: AAH17293.1.

IPI

IPI00219365.

PIR

A41289.

RefSeq

NP_002435.1.

UniGene

Hs.87752

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E5W	X-ray	2.70	A	1-346	[»]
1EF1	X-ray	1.90	A/B	4-297	[»]
			C/D	488-577	[»]
1SGH	X-ray	3.50	A	1-297	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P26038. 10 interactions.

PTM databases

PhosphoSite

P26038.

2-D gel databases

Aarhus/Ghent-2DPAGE

3515. IEF.
3516. IEF.

OGP

P26038.

Proteomic databases

PeptideAtlas

P26038.

PRIDE

P26038.

Genome annotation databases

Ensembl

ENSG00000147065. Homo sapiens. [Contig view]

GeneID

4478.

KEGG

hsa:4478.

Organism-specific databases

GeneCards

GC0XP064804.

H-InvDB

HIX0016842.

HGNC

HGNC:7373. MSN.

HPA

CAB004505.
CAB010898.
HPA000263.
HPA011135.
HPA011227.

MIM

309845. gene.

PharmGKB

PA31178.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P26038.

HOVERGEN

P26038.

OMA

P26038. ANARDET.

Enzyme and pathway databases

Pathway_Interaction_DB

er_nongenomic_pathway. Plasma membrane estrogen receptor signaling.

Gene expression databases

ArrayExpress

P26038.

Bgee

P26038.

CleanEx

HS_MSN.

GermOnline

ENSG00000147065. Homo sapiens.

Family and domain databases

InterPro

IPR019749. Band_41_domain.
IPR019750. Band_41_sg.
IPR011174. ERM.
IPR011259. ERM_C.
IPR000798. Ez/rad/moesin.
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.
IPR011993. PH_type.
[Graphical view]

Gene3D

G3DSA:1.20.80.10. ACBP. 1 hit.
G3DSA:2.30.29.30. PH_type. 1 hit.

Pfam

PF00769. ERM. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
[Graphical view]

PIRSF

PIRSF002305. ERM. 1 hit.

PRINTS

PR00935. BAND41.
PR00661. ERMFAMILY.

SMART

SM00295. B41. 1 hit.
[Graphical view]

PROSITE

PS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

17331.

PMAP-CutDB

P26038.

SOURCE

Search...

Entry information

Entry name

MOES_HUMAN

Accession

Primary (citable) accession number: P26038

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 108 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)