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P70315 (WASP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Wiskott-Aldrich syndrome protein homolog

Short name=WASp
Gene names
Name:Was
Synonyms:Wasp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
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.

Subunit structure

Interacts with CDC42, RAC, NCK, FYN, HCK, 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 By similarity. Interacts with NCK1 (via SH3 domains). Ref.2 Ref.3

Subcellular location

Cytoplasmcytoskeleton.

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-293 by FYN and HCK, inducing WAS effector activity after TCR engagement. Phosphorylation at Tyr-293 enhances WAS activity in promoting actin polymerization and filopodia formation By similarity.

Sequence similarities

Contains 1 CRIB domain.

Contains 1 WH1 domain.

Contains 1 WH2 domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 520520Wiskott-Aldrich syndrome protein homolog
PRO_0000188991

Regions

Domain41 – 150110WH1
Domain240 – 25314CRIB
Repeat354 – 36310GRSGPLPPXP motif 1
Repeat393 – 40210GRSGPLPPXP motif 2
Domain448 – 46518WH2
Compositional bias162 – 1676Poly-Pro
Compositional bias314 – 3218Poly-Pro
Compositional bias324 – 34118Poly-Gly
Compositional bias368 – 3736Poly-Pro
Compositional bias376 – 3794Poly-Pro
Compositional bias384 – 3907Poly-Pro
Compositional bias397 – 4037Poly-Pro
Compositional bias408 – 42417Poly-Pro
Compositional bias503 – 52018Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue2931Phosphotyrosine; alternate Ref.4 Ref.5
Modified residue2931Phosphotyrosine; by FYN and HCK; alternate By similarity
Modified residue5011Phosphoserine Ref.5
Modified residue5021Phosphoserine Ref.5

Sequences

Sequence LengthMass (Da)Tools
P70315 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 9C223733C59F0C8A

FASTA52054,192
        10         20         30         40         50         60 
MNSGPGPVGG RPGGRGGPAV QQNIPSNLLQ DHENQRLFEL LGRKCWTLAT TVVQLYLALP 

        70         80         90        100        110        120 
PGAEHWTMEH CGAVCFVKDN PQKSYFIRLY GLQAGRLLWE QELYSQLVYL TPTPFFHTFA 

       130        140        150        160        170        180 
GDDCQVGLNF ADESEAQAFR ALVQEKIQKR NQRQSGERRQ LPPPPAPINE ERRGGLPPVP 

       190        200        210        220        230        240 
PHPGGDHGGP SGGPLSLGLV TVDIQNPDIT SSRYRGLPAP GPGPTDKKRS GKKKISKADI 

       250        260        270        280        290        300 
GAPSGFKHVS HVGWDPQNGF DVNNLDPDLR SLFSRAGISE AQLTDAETSK LIYDFIEDQG 

       310        320        330        340        350        360 
GLEAVRQEMR RQEPLPPPPP PCRGGGGGGG GGGGGGGGGG GQPLRPPVVG SNKGRSGPLP 

       370        380        390        400        410        420 
PVPMGGAPPP PTPRGPPPPG RGGPPPPPPP ATGRSGPPPP PLPGAGGPPA PPPPPPPPPP 

       430        440        450        460        470        480 
PPCPGSGPAP PPLPPTPVSG GSPAPGGGRG ALLDQIRQGI QLNKTPGALE NSVQQPPAQQ 

       490        500        510        520 
SEGLVGALMH VMQKRSRVIH SSDEGEDQTG EDEEDDEWDD 

« Hide

References

« Hide 'large scale' references
[1]"The mouse homolog of the Wiskott-Aldrich syndrome protein (WASP) gene is highly conserved and maps near the scurfy (sf) mutation on the X chromosome."
Derry J.M.J., Wiedemann P., Blair P., Wang Y., Kerns J.A., Lemahieu V., Godfrey V.L., Wilkinson J.E., Francke U.
Genomics 29:471-477(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[2]"Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling."
Quilliam L.A., Lambert Q.T., Mickelson-Young L.A., Westwick J.K., Sparks A.B., Kay B.K., Jenkins N.A., Gilbert D.J., Copeland N.G., Der C.J.
J. Biol. Chem. 271:28772-28776(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NCK1.
[3]"Tyrosine phosphorylation regulates the SH3-mediated binding of the Wiskott-Aldrich syndrome protein to PSTPIP, a cytoskeletal-associated protein."
Wu Y., Spencer S.D., Lasky L.A.
J. Biol. Chem. 273:5765-5770(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PSTPIP1.
[4]"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-293, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Mast cell.
[5]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-293; SER-501 AND SER-502, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U54788 mRNA. Translation: AAC52556.1.
RefSeqNP_033541.1. NM_009515.2.
UniGeneMm.4735.

3D structure databases

ProteinModelPortalP70315.
SMRP70315. Positions 18-159, 244-311, 482-510.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204544. 7 interactions.
IntActP70315. 12 interactions.
MINTMINT-1532664.

PTM databases

PhosphoSiteP70315.

Proteomic databases

PaxDbP70315.
PRIDEP70315.

Protocols and materials databases

DNASU22376.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033505; ENSMUSP00000033505; ENSMUSG00000031165.
GeneID22376.
KEGGmmu:22376.
UCSCuc009sns.2. mouse.

Organism-specific databases

CTD7454.
MGIMGI:105059. Was.

Phylogenomic databases

eggNOGNOG270974.
HOVERGENHBG000222.
InParanoidP70315.
KOK05747.
OMATPANEER.
OrthoDBEOG7FJH20.
PhylomeDBP70315.
TreeFamTF316736.

Enzyme and pathway databases

ReactomeREACT_98458. Immune System.

Gene expression databases

ArrayExpressP70315.
BgeeP70315.
CleanExMM_WAS.
GenevestigatorP70315.

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

NextBio302721.
PROP70315.
SOURCESearch...

Entry information

Entry nameWASP_MOUSE
AccessionPrimary (citable) accession number: P70315
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot