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P26038 (MOES_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Moesin
Alternative name(s):
Membrane-organizing extension spike protein
Gene names
Name:MSN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length577 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probably involved in connections of major cytoskeletal structures to the plasma membrane. May inhibit herpes simplex virus 1 infection at an early stage. Ref.13

Enzyme 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 By similarity.

Subunit structure

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. Ref.5 Ref.6 Ref.7 Ref.13

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmcytoskeleton By similarity. Apical cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell projectionmicrovillus membrane; Peripheral membrane protein; 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. Ref.7

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. 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.

Sequence similarities

Contains 1 FERM domain.

Ontologies

Keywords
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular component movement

Traceable author statement PubMed 16130169. Source: UniProtKB

establishment of endothelial barrier

Inferred from genetic interaction PubMed 23264465. Source: UniProt

leukocyte cell-cell adhesion

Inferred from expression pattern PubMed 12082081. Source: BHF-UCL

leukocyte migration

Inferred from expression pattern PubMed 12082081. Source: BHF-UCL

membrane to membrane docking

Inferred from expression pattern PubMed 12082081. Source: BHF-UCL

positive regulation of gene expression

Inferred from genetic interaction PubMed 23264465. Source: UniProt

regulation of lymphocyte migration

Inferred from mutant phenotype Ref.9. Source: UniProtKB

   Cellular_componentapical part of cell

Inferred from direct assay PubMed 12082081. Source: BHF-UCL

apical plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

basolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

blood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

cytoplasm

Inferred from direct assay. Source: HPA

cytoskeleton

Traceable author statement PubMed 16130169. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

extrinsic component of membrane

Inferred from electronic annotation. Source: InterPro

filopodium

Inferred from direct assay PubMed 12082081. Source: BHF-UCL

microvillus

Inferred from direct assay PubMed 12082081. Source: BHF-UCL

microvillus membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay. Source: HPA

uropod

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncell adhesion molecule binding

Inferred from physical interaction PubMed 12082081. Source: BHF-UCL

double-stranded RNA binding

Inferred from direct assay PubMed 21266579. Source: MGI

protein kinase binding

Inferred from physical interaction Ref.9. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 15819698. Source: UniProtKB

structural constituent of cytoskeleton

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.4
Chain2 – 577576Moesin
PRO_0000219416

Regions

Domain2 – 295294FERM

Amino acid modifications

Modified residue791N6-acetyllysine Ref.11
Modified residue1161Phosphotyrosine Ref.10
Modified residue1391N6-acetyllysine Ref.11
Modified residue1651N6-acetyllysine By similarity
Modified residue5581Phosphothreonine; by ROCK2 and STK10 Ref.9

Experimental info

Mutagenesis5561Y → R: Impairs phosphorylation by STK10. Ref.9
Mutagenesis5581T → A: Abolishes phosphorylation by STK10. Ref.9
Mutagenesis5581T → D: Phosphomimetic mutant. Ref.9

Secondary structure

.................................................................... 577
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26038 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 865A6C5CB14AE586

FASTA57767,820
        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 

« Hide

References

« Hide '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] [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. expand/collapse author list , 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]"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] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M69066 mRNA. Translation: AAA36322.1.
Z98946 Genomic DNA. Translation: CAB46379.1.
BC017293 mRNA. Translation: AAH17293.1.
PIRA41289.
RefSeqNP_002435.1. NM_002444.2.
UniGeneHs.87752.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E5WX-ray2.70A1-346[»]
1EF1X-ray1.90A/B4-297[»]
C/D488-577[»]
1SGHX-ray3.50A1-297[»]
ProteinModelPortalP26038.
SMRP26038. Positions 1-577.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110584. 73 interactions.
IntActP26038. 14 interactions.
MINTMINT-3010439.
STRING9606.ENSP00000353408.

PTM databases

PhosphoSiteP26038.

Polymorphism databases

DMDM127234.

2D gel databases

OGPP26038.

Proteomic databases

PaxDbP26038.
PeptideAtlasP26038.
PRIDEP26038.

Protocols and materials databases

DNASU4478.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360270; ENSP00000353408; ENSG00000147065.
GeneID4478.
KEGGhsa:4478.
UCSCuc004dwf.3. human.

Organism-specific databases

CTD4478.
GeneCardsGC0XP064887.
HGNCHGNC:7373. MSN.
HPACAB010898.
CAB047336.
CAB047338.
HPA000263.
HPA000763.
HPA011135.
HPA011227.
MIM309845. gene.
neXtProtNX_P26038.
PharmGKBPA31178.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG236035.
HOGENOMHOG000007113.
HOVERGENHBG002185.
InParanoidP26038.
KOK05763.
OMAPHVTEPM.
OrthoDBEOG7BGHK6.
PhylomeDBP26038.
TreeFamTF313935.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.

Gene expression databases

BgeeP26038.
CleanExHS_MSN.
GenevestigatorP26038.

Family and domain databases

Gene3D1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProIPR019749. 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.
[Graphical view]
PfamPF00769. ERM. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
[Graphical view]
PIRSFPIRSF002305. ERM. 1 hit.
PRINTSPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTSM00295. B41. 1 hit.
[Graphical view]
SUPFAMSSF47031. SSF47031. 1 hit.
SSF48678. SSF48678. 1 hit.
PROSITEPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMSN. human.
EvolutionaryTraceP26038.
GeneWikiMoesin.
GenomeRNAi4478.
NextBio17331.
PMAP-CutDBP26038.
PROP26038.
SOURCESearch...

Entry information

Entry nameMOES_HUMAN
AccessionPrimary (citable) accession number: P26038
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 161 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM