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P42768 (WASP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Wiskott-Aldrich syndrome protein

Short name=WASp
Gene names
Name:WAS
Synonyms:IMD2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length502 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Effector protein for Rho-type GTPases. Regulates actin filament reorganization via its interaction with the Arp2/3 complex. Important for efficient actin polymerization. Possible regulator of lymphocyte and platelet function. Mediates actin filament reorganization and the formation of actin pedestals upon infection by pathogenic bacteria. Ref.10 Ref.20 Ref.22

Subunit structure

Interacts with NCK1 (via SH3 domains) By similarity. Interacts with CDC42, RAC, NCK, HCK, FYN, SRC kinase FGR, BTK, ABL1, PSTPIP1, WIP, and to the p85 subunit of PLC-gamma. Binds the Arp2/3 complex. Interacts (via C-terminus) with ALDOA. Interacts with E.coli effector protein EspF(U). Ref.8 Ref.9 Ref.10 Ref.11 Ref.20 Ref.22

Subcellular location

Cytoplasmcytoskeleton.

Tissue specificity

Expressed predominantly in the thymus. Also found, to a much lesser extent, in the spleen. Ref.1

Domain

The WH1 (Wasp homology 1) domain may bind a Pro-rich ligand.

The CRIB (Cdc42/Rac-interactive-binding) region binds to the C-terminal WH2 domain in the autoinhibited state of the protein. Binding of Rho-type GTPases to the CRIB induces a conformation change and leads to activation.

Post-translational modification

Phosphorylated at Tyr-291 by FYN and HCK, inducing WAS effector activity after TCR engagement. Phosphorylation at Tyr-291 enhances WAS activity in promoting actin polymerization and filopodia formation. Ref.10 Ref.11 Ref.12

Involvement in disease

Wiskott-Aldrich syndrome (WAS) [MIM:301000]: An X-linked recessive immunodeficiency characterized by eczema, thrombocytopenia, recurrent infections, and bloody diarrhea. Death usually occurs before age 10.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.23 Ref.24 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.34 Ref.36

Thrombocytopenia 1 (THC1) [MIM:313900]: Thrombocytopenia is defined by a decrease in the number of platelets in circulating blood, resulting in the potential for increased bleeding and decreased ability for clotting.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.24 Ref.25 Ref.32 Ref.34 Ref.35

Neutropenia, severe congenital, X-linked (XLN) [MIM:300299]: A disorder of hematopoiesis characterized by maturation arrest of granulopoiesis at the level of promyelocytes with peripheral blood absolute neutrophil counts below 0.5 x 10(9)/l and early onset of severe bacterial infections.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.33

Sequence similarities

Contains 1 CRIB domain.

Contains 1 WH1 domain.

Contains 1 WH2 domain.

Sequence caution

The sequence AAH02961.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   DiseaseDisease mutation
   DomainRepeat
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processFc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

T cell activation

Inferred from electronic annotation. Source: Ensembl

T cell receptor signaling pathway

Traceable author statement. Source: Reactome

actin filament polymerization

Inferred from electronic annotation. Source: Ensembl

actin filament-based movement

Inferred from electronic annotation. Source: Ensembl

actin polymerization or depolymerization

Traceable author statement PubMed 8625410. Source: ProtInc

blood coagulation

Traceable author statement Ref.1. Source: ProtInc

defense response

Traceable author statement Ref.1. Source: ProtInc

endosomal transport

Inferred from electronic annotation. Source: Ensembl

epidermis development

Traceable author statement Ref.1. Source: ProtInc

immune response

Inferred from mutant phenotype Ref.1. Source: HGNC

innate immune response

Traceable author statement. Source: Reactome

positive regulation of Arp2/3 complex-mediated actin nucleation

Inferred from electronic annotation. Source: InterPro

protein complex assembly

Traceable author statement PubMed 8625410. Source: ProtInc

regulation of catalytic activity

Traceable author statement PubMed 8625410. Source: GOC

   Cellular_componentactin cytoskeleton

Traceable author statement PubMed 8625410. Source: ProtInc

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

vesicle membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionidentical protein binding

Inferred from physical interaction Ref.18Ref.11. Source: IntAct

small GTPase regulator activity

Traceable author statement PubMed 8625410. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 502501Wiskott-Aldrich syndrome protein
PRO_0000188990

Regions

Domain39 – 148110WH1
Domain238 – 25114CRIB
Repeat337 – 34610GRSGPLPPXP motif 1
Repeat376 – 38510GRSGPLPPXP motif 2
Domain430 – 44718WH2
Compositional bias160 – 1656Poly-Pro
Compositional bias312 – 3198Poly-Pro
Compositional bias351 – 3566Poly-Pro
Compositional bias359 – 3624Poly-Pro
Compositional bias367 – 3737Poly-Pro
Compositional bias380 – 3867Poly-Pro
Compositional bias391 – 40414Poly-Pro
Compositional bias485 – 50218Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue2911Phosphotyrosine; by FYN and HCK Ref.10 Ref.12 Ref.13 Ref.14 Ref.15
Modified residue4831Phosphoserine; by CK2 Ref.11 Ref.14 Ref.15
Modified residue4841Phosphoserine; by CK2 Ref.11 Ref.14 Ref.15

Natural variations

Natural variant271L → F in THC1. Ref.24
VAR_005823
Natural variant301Missing in THC1. Ref.23
VAR_005824
Natural variant311E → K in WAS. Ref.23 Ref.28
VAR_005825
Natural variant431C → W in WAS; moderate form. Ref.3 Ref.27
VAR_008105
Natural variant451T → M in WAS and THC1. Ref.3 Ref.27 Ref.28 Ref.32
VAR_008106
Natural variant481T → I in THC1. Ref.24
VAR_005826
Natural variant521Q → H in WAS. Ref.36
VAR_012710
Natural variant561A → V in THC1. Ref.25 Ref.30
VAR_005827
Natural variant581P → L in WAS. Ref.3
VAR_022806
Natural variant581P → R in THC1. Ref.35
Corresponds to variant rs28935178 [ dbSNP | Ensembl ].
VAR_033255
Natural variant701G → W in WAS. Ref.36
VAR_012711
Natural variant731C → R in WAS; severe form. Ref.34
VAR_008107
Natural variant751V → M in THC1. Ref.23 Ref.24 Ref.27 Ref.29 Ref.34
VAR_005828
Natural variant821S → P in WAS; attenuated form. Ref.23
VAR_005829
Natural variant831Y → C in THC1. Ref.34
VAR_008108
Natural variant841F → L in WAS; severe form. Ref.29
VAR_008109
Natural variant861R → C in WAS. Ref.23 Ref.27 Ref.34
VAR_005832
Natural variant861R → H in WAS. Ref.23 Ref.24 Ref.26
VAR_005830
Natural variant861R → L in WAS. Ref.24
VAR_005831
Natural variant891G → D in WAS; mild form. Ref.29
VAR_008110
Natural variant971W → C in WAS; attenuated form. Ref.23
VAR_005833
Natural variant1311E → K in WAS. Ref.24
Corresponds to variant rs146220228 [ dbSNP | Ensembl ].
VAR_005834
Natural variant1331E → K in WAS; severe form. Ref.3 Ref.23 Ref.29 Ref.31 Ref.34
VAR_005835
Natural variant1341A → T in WAS. Ref.3
VAR_022807
Natural variant1871G → C in WAS. Ref.24
VAR_005836
Natural variant2361A → E in THC1. Ref.25
VAR_005837
Natural variant2701L → P in XLN; a constitutively activating mutation. Ref.33
Corresponds to variant rs28936079 [ dbSNP | Ensembl ].
VAR_033256
Natural variant4761K → E in WAS. Ref.23
VAR_005838
Natural variant4771R → K in THC1. Ref.24
VAR_005839
Natural variant4811I → N in THC1. Ref.35
VAR_033257

Experimental info

Sequence conflict3321V → A in AAD26691. Ref.4

Secondary structure

........................ 502
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P42768 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 7228428672B7CB78

FASTA50252,913
        10         20         30         40         50         60 
MSGGPMGGRP GGRGAPAVQQ NIPSTLLQDH ENQRLFEMLG RKCLTLATAV VQLYLALPPG 

        70         80         90        100        110        120 
AEHWTKEHCG AVCFVKDNPQ KSYFIRLYGL QAGRLLWEQE LYSQLVYSTP TPFFHTFAGD 

       130        140        150        160        170        180 
DCQAGLNFAD EDEAQAFRAL VQEKIQKRNQ RQSGDRRQLP PPPTPANEER RGGLPPLPLH 

       190        200        210        220        230        240 
PGGDQGGPPV GPLSLGLATV DIQNPDITSS RYRGLPAPGP SPADKKRSGK KKISKADIGA 

       250        260        270        280        290        300 
PSGFKHVSHV GWDPQNGFDV NNLDPDLRSL FSRAGISEAQ LTDAETSKLI YDFIEDQGGL 

       310        320        330        340        350        360 
EAVRQEMRRQ EPLPPPPPPS RGGNQLPRPP IVGGNKGRSG PLPPVPLGIA PPPPTPRGPP 

       370        380        390        400        410        420 
PPGRGGPPPP PPPATGRSGP LPPPPPGAGG PPMPPPPPPP PPPPSSGNGP APPPLPPALV 

       430        440        450        460        470        480 
PAGGLAPGGG RGALLDQIRQ GIQLNKTPGA PESSALQPPP QSSEGLVGAL MHVMQKRSRA 

       490        500 
IHSSDEGEDQ AGDEDEDDEW DD 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of a novel gene mutated in Wiskott-Aldrich syndrome."
Derry J.M.J., Ochs H.D., Francke U.
Cell 78:635-644(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
Tissue: T-cell.
[2]Erratum
Derry J.M.J., Ochs H.D., Francke U.
Cell 79:923-923(1994) [PubMed] [Europe PMC] [Abstract]
[3]"Identification of mutations in the Wiskott-Aldrich syndrome gene and characterization of a polymorphic dinucleotide repeat at DXS6940, adjacent to the disease gene."
Kwan S.-P., Hagemann T.L., Radtke B.E., Blaese R.M., Rosen F.S.
Proc. Natl. Acad. Sci. U.S.A. 92:4706-4710(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS WAS TRP-43; MET-45; LEU-58; LYS-133 AND THR-134.
[4]"The identification and characterization of two promoters and the complete genomic sequence for the Wiskott-Aldrich syndrome gene."
Hagemann T.L., Kwan S.-P.
Biochem. Biophys. Res. Commun. 256:104-109(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"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].
[6]"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: Lymph.
[7]"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 2-13.
Tissue: Platelet.
[8]"Direct interaction of the Wiskott-Aldrich syndrome protein with the GTPase Cdc42."
Kolluri R., Tolias K.F., Carpenter C.L., Rosen F.S., Kirchhausen T.
Proc. Natl. Acad. Sci. U.S.A. 93:5615-5618(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDC42.
[9]"WIP, a protein associated with Wiskott-Aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells."
Ramesh N., Anton I.M., Hartwig J.H., Geha R.S.
Proc. Natl. Acad. Sci. U.S.A. 94:14671-14676(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WIP.
[10]"Phosphorylation of tyrosine 291 enhances the ability of WASp to stimulate actin polymerization and filopodium formation. Wiskott-Aldrich Syndrome protein."
Cory G.O., Garg R., Cramer R., Ridley A.J.
J. Biol. Chem. 277:45115-45121(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT TYR-291 BY HCK, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH HCK.
[11]"Phosphorylation of the WASP-VCA domain increases its affinity for the Arp2/3 complex and enhances actin polymerization by WASP."
Cory G.O.C., Cramer R., Blanchoin L., Ridley A.J.
Mol. Cell 11:1229-1239(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-483 AND SER-484, INTERACTION WITH THE ARP2/3 COMPLEX.
[12]"Fyn and PTP-PEST-mediated regulation of Wiskott-Aldrich syndrome protein (WASp) tyrosine phosphorylation is required for coupling T cell antigen receptor engagement to WASp effector function and T cell activation."
Badour K., Zhang J., Shi F., Leng Y., Collins M., Siminovitch K.A.
J. Exp. Med. 199:99-112(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-291 BY FYN.
[13]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-291; SER-483 AND SER-484, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[15]"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-291; SER-483 AND SER-484, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"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].
[17]"Structure of Cdc42 in complex with the GTPase-binding domain of the 'Wiskott-Aldrich syndrome' protein."
Abdul-Manan N., Aghazadeh B., Liu G.A., Majumdar A., Ouerfelli O., Siminovitch K.A., Rosen M.K.
Nature 399:379-383(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 230-288 IN COMPLEX WITH CDC42.
[18]"Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein."
Kim A.S., Kakalis L.T., Abdul-Manan N., Liu G.A., Rosen M.K.
Nature 404:151-158(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 242-492, CONFORMATION CHANGE.
[19]"Chemical inhibition of N-WASP by stabilization of a native autoinhibited conformation."
Peterson J.R., Bickford L.C., Morgan D., Kim A.S., Ouerfelli O., Kirschner M.W., Rosen M.K.
Nat. Struct. Mol. Biol. 11:747-755(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 242-310 IN COMPLEX WITH WISKOSTATIN.
[20]"Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly."
Chereau D., Kerff F., Graceffa P., Grabarek Z., Langsetmo K., Dominguez R.
Proc. Natl. Acad. Sci. U.S.A. 102:16644-16649(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 430-458 IN COMPLEX WITH ACTIN, FUNCTION, SUBUNIT.
[21]"A hydrophobic pocket in the active site of glycolytic aldolase mediates interactions with Wiskott-Aldrich syndrome protein."
St-Jean M., Izard T., Sygusch J.
J. Biol. Chem. 282:14309-14315(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 488-502 IN COMPLEX WITH ALDOA.
[22]"Structural mechanism of WASP activation by the enterohaemorrhagic E. coli effector EspF(U)."
Cheng H.C., Skehan B.M., Campellone K.G., Leong J.M., Rosen M.K.
Nature 454:1009-1013(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 242-310, FUNCTION, INTERACTION WITH E.COLI ESPF(U).
[23]"Identification of WASP mutations in patients with Wiskott-Aldrich syndrome and isolated thrombocytopenia reveals allelic heterogeneity at the WAS locus."
Kolluri R., Shehabeldin A., Peacocke M., Lamhonwah A.-M., Teichert-Kuliszewska K., Weissman S.M., Siminovitch K.A.
Hum. Mol. Genet. 4:1119-1126(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WAS HIS-30 DEL; LYS-31; MET-75; PRO-82; CYS-86; HIS-86; CYS-97; LYS-133 AND GLU-476.
[24]"WASP gene mutations in Wiskott-Aldrich syndrome and X-linked thrombocytopenia."
Derry J.M.J., Kerns J.A., Weinberg K.I., Ochs H.D., Volpini V., Estivill X., Walker A.P., Francke U.
Hum. Mol. Genet. 4:1127-1135(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS THC1 PHE-27; ILE-48 AND LYS-477, VARIANTS WAS MET-75; LEU-86; HIS-86; LYS-131 AND CYS-187.
[25]"X-linked thrombocytopenia and Wiskott-Aldrich syndrome are allelic diseases with mutations in the WASP gene."
Villa A., Notarangelo L., Macchi P., Mantuano E., Cavagni G., Brugnoni D., Strina D., Patrosso M.C., Ramenghi U., Sacco M.G., Ugazio A., Vezzoni P.
Nat. Genet. 9:414-417(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS THC1 VAL-56 AND GLU-236.
[26]"Wiskott-Aldrich syndrome: no strict genotype-phenotype correlations but clustering of missense mutations in the amino-terminal part of the WASP gene product."
Schindelhauer D., Weiss M., Hellebrand H., Golla A., Hergersberg M., Seger R., Belohradsky B.H., Meindl A.
Hum. Genet. 98:68-76(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT WAS HIS-86.
[27]"Variable expression of WASP in B cell lines of Wiskott-Aldrich syndrome patients."
Remold-O'Donnell E., Cooley J., Shcherbina A., Hagemann T.L., Kwan S.-P., Kenney D.M., Rosen F.S.
J. Immunol. 158:4021-4025(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WAS TRP-43; MET-45; MET-75 AND CYS-86.
[28]"Mutation analysis of five Japanese families with Wiskott-Aldrich syndrome and determination of the family members' carrier status using three different methods."
Ariga T., Yamada M., Sakiyama Y.
Pediatr. Res. 41:535-540(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WAS LYS-31 AND MET-45.
[29]"Absence of expression of the Wiskott-Aldrich syndrome protein in peripheral blood cells of Wiskott-Aldrich syndrome patients."
MacCarthy-Morrogh L., Gaspar H.B., Wang Y.-C., Katz F., Thompson L., Layton M., Jones A.M., Kinnon C.
Clin. Immunol. Immunopathol. 88:22-27(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WAS MET-75; LEU-84; ASP-89 AND LYS-133.
[30]"Defective actin polymerization in EBV-transformed B-cell lines from patients with the Wiskott-Aldrich syndrome."
Facchetti F., Blanzuoli L., Vermi W., Notarangelo L.D., Giliani S., Fiorini M., Fasth A., Stewart D.M., Nelson D.L.
J. Pathol. 185:99-107(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT WAS VAL-56.
[31]"X-linked Wiskott-Aldrich syndrome in a girl."
Parolini O., Ressmann G., Haas O.A., Pawlowsky J., Gadner H., Knapp W., Holter W.
N. Engl. J. Med. 338:291-295(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT WAS LYS-133.
[32]"Missense C168T in the Wiskott-Aldrich Syndrome protein gene is a common mutation in X-linked thrombocytopenia."
Ho L.L., Ayling J., Prosser I., Kronenberg H., Iland H., Joshua D.
Br. J. Haematol. 112:76-80(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THC1 MET-45.
[33]"Constitutively activating mutation in WASP causes X-linked severe congenital neutropenia."
Devriendt K., Kim A.S., Mathijs G., Frints S.G.M., Schwartz M., Van Den Oord J.J., Verhoef G.E.G., Boogaerts M.A., Fryns J.-P., You D., Rosen M.K., Vandenberghe P.
Nat. Genet. 27:313-317(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT XLN PRO-270, CHARACTERIZATION OF VARIANT XLN PRO-270.
[34]"Novel mutations in the Wiskott-Aldrich syndrome protein gene and their effects on transcriptional, translational, and clinical phenotypes."
Lemahieu V., Gastier J.M., Francke U.
Hum. Mutat. 14:54-66(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WAS ARG-73; CYS-86 AND LYS-133, VARIANTS THC1 MET-75 AND CYS-83.
[35]"Missense mutations of the WASP gene cause intermittent X-linked thrombocytopenia."
Notarangelo L.D., Mazza C., Giliani S., D'Aria C., Gandellini F., Ravelli C., Locatelli M.G., Nelson D.L., Ochs H.D., Notarangelo L.D.
Blood 99:2268-2269(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS THC1 ARG-58 AND ASN-481.
[36]"Wiskott-Aldrich syndrome in Argentina: 17 unique, including nine novel, mutations."
El-Hakeh J., Rosenzweig S., Oleastro M., Basack N., Berozdnik L., Molina F., Rivas E.M., Zelazko M., Danielian S.
Hum. Mutat. 19:186-187(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WAS HIS-52 AND TRP-70.
+Additional computationally mapped references.

Web resources

WASbase

WAS mutation db

WASPbase

WAS mutation db

GeneReviews
Wikipedia

Wiskott-Aldrich syndrome protein entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U12707 mRNA. Translation: AAA62663.1.
U18935 Genomic DNA. Translation: AAA60381.1.
U19927 mRNA. Translation: AAC50140.1.
AF115549 Genomic DNA. Translation: AAD26691.1.
AF196970 Genomic DNA. No translation available.
BC002961 mRNA. Translation: AAH02961.1. Different initiation.
BC012738 mRNA. Translation: AAH12738.1.
PIRA55197. A54747.
RefSeqNP_000368.1. NM_000377.2.
UniGeneHs.2157.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CEENMR-B230-288[»]
1EJ5NMR-A242-492[»]
1T84NMR-A242-492[»]
2A3ZX-ray2.08C430-458[»]
2K42NMR-A242-310[»]
2OT0X-ray2.05E/F/G/H488-502[»]
DisProtDP00215.
ProteinModelPortalP42768.
SMRP42768. Positions 16-157, 242-309, 464-492.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113293. 54 interactions.
DIPDIP-431N.
IntActP42768. 37 interactions.
MINTMINT-94655.
STRING9606.ENSP00000365891.

PTM databases

PhosphoSiteP42768.

Proteomic databases

PaxDbP42768.
PRIDEP42768.

Protocols and materials databases

DNASU7454.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376701; ENSP00000365891; ENSG00000015285.
ENST00000599235; ENSP00000469374; ENSG00000267912.
GeneID7454.
KEGGhsa:7454.
UCSCuc004dkm.4. human.

Organism-specific databases

CTD7454.
GeneCardsGC0XP048534.
HGNCHGNC:12731. WAS.
HPACAB004290.
HPA002022.
MIM300299. phenotype.
300392. gene.
301000. phenotype.
313900. phenotype.
neXtProtNX_P42768.
Orphanet906. Wiskott-Aldrich syndrome.
86788. X-linked severe congenital neutropenia.
852. X-linked thrombocytopenia with normal platelets.
PharmGKBPA37342.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG270974.
HOGENOMHOG000143378.
HOVERGENHBG000222.
InParanoidP42768.
KOK05747.
OMATPANEER.
PhylomeDBP42768.
TreeFamTF316736.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP42768.
BgeeP42768.
CleanExHS_WAS.
GenevestigatorP42768.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
3.90.810.10. 2 hits.
InterProIPR000095. CRIB_dom.
IPR011993. PH_like_dom.
IPR027641. WASP.
IPR011026. WASP_C.
IPR000697. WH1/EVH1.
IPR003124. WH2_dom.
[Graphical view]
PANTHERPTHR12779. PTHR12779. 1 hit.
PfamPF00786. PBD. 1 hit.
PF00568. WH1. 1 hit.
PF02205. WH2. 1 hit.
[Graphical view]
SMARTSM00285. PBD. 1 hit.
SM00461. WH1. 1 hit.
SM00246. WH2. 1 hit.
[Graphical view]
SUPFAMSSF47912. SSF47912. 2 hits.
PROSITEPS50108. CRIB. 1 hit.
PS50229. WH1. 1 hit.
PS51082. WH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSWAS. human.
EvolutionaryTraceP42768.
GeneWikiWiskott%E2%80%93Aldrich_syndrome_protein.
GenomeRNAi7454.
NextBio29188.
PROP42768.
SOURCESearch...

Entry information

Entry nameWASP_HUMAN
AccessionPrimary (citable) accession number: P42768
Secondary accession number(s): Q9BU11, Q9UNJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 170 of the entry and version 4 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

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