Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Wiskott-Aldrich syndrome protein  

UniProtKB / Swiss-Prot ID :  WASP_HUMAN

Gene Name (Synonyms) : 
WAS, IMD2  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm, cytoskeleton. 

Protein 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. 

Protein Sequence MSGGPMGGRPGGRGAPAVQQNIPSTLLQDHENQRLFEMLGRKCLTLATAVVQLYLALPPGAEHWTKEHCG...
Predicted Secondary Structure CCCCCCCCCCCCCCCCHHHHCCCHHHCCCCCHHHHHHHHCHHHHHHHHHHHHHHHCCCCCHHHHHCCCCE...
Protein Variant
LocationDescription
27L -> F (in THC1). VAR_005823
30Missing (in THC1). VAR_005824
31E -> K (in WAS). VAR_005825
43C -> W (in WAS; moderate form). VAR_008105
45T -> M (in WAS and THC1). VAR_008106
48T -> I (in THC1). VAR_005826
52Q -> H (in WAS). VAR_012710
56A -> V (in THC1). VAR_005827
58P -> L (in WAS). VAR_022806
58P -> R (in THC1; dbSNP:rs28935178). VAR_033255
70G -> W (in WAS). VAR_012711
73C -> R (in WAS; severe form). VAR_008107
75V -> M (in THC1). VAR_005828
82S -> P (in WAS; attenuated form). VAR_005829
83Y -> C (in THC1). VAR_008108
84F -> L (in WAS; severe form). VAR_008109
86R -> C (in WAS). VAR_005832
86R -> H (in WAS). VAR_005830
86R -> L (in WAS). VAR_005831
89G -> D (in WAS; mild form). VAR_008110
97W -> C (in WAS; attenuated form). VAR_005833
131E -> K (in WAS). VAR_005834
133E -> K (in WAS; severe form). VAR_005835
134A -> T (in WAS). VAR_022807
187G -> C (in WAS). VAR_005836
236A -> E (in THC1). VAR_005837
270L -> P (in XLN; a constitutivelyactivating mutation; dbSNP:rs28936079).
476K -> E (in WAS). VAR_005838
477R -> K (in THC1). VAR_005839
481I -> N (in THC1). VAR_033257
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
144Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LVQEKIQKR
HHHHHHHHH
33.09Phosphositeplus
Link-
221PhosphoserineAPGPSPADK
CCCCCCCCC
38.34Phosphositeplus
Link-
291DePhosphotyrosineSKLIYDFIE
CCCCCEEEC
18.42HPRD
Link-
291PhosphotyrosineSKLIYDFIE
CCCCCEEEC
18.42Phosphositeplus
Link-
291PhosphotyrosineSKLIYDFIE
CCCCCEEEC
18.42SysPTM
Link-
291Phosphotyrosine (BTK)SKLIYDFIE
CCCCCEEEC
18.42HPRD
Link-
291Phosphotyrosine (HCK)SKLIYDFIE
CCCCCEEEC
18.42HPRD
Link-
291Phosphotyrosine (HCK;BTK)SKLIYDFIE
CCCCCEEEC
18.42PhosphoELM
Link-
291Phosphotyrosine; by FYN and HCK.SKLIYDFIE
CCCCCEEEC
18.42UniProtKB
Link-
321N2,N2-dimethylargininePPPSRGGNQ
CCCCCCCCC
63.91MeMo
Link-
355PhosphothreoninePPPPTPRGP
CCCCCCCCC
31.24HPRD
Link-
357N2,N2-dimethylargininePPTPRGPPP
CCCCCCCCC
73.12MeMo
Link-
364N2,N2-dimethylargininePPPGRGGPP
CCCCCCCCC
53.31MeMo
Link-
483PhosphoserineRAIHSSDEG
HHHCCCCCC
33.11PhosphoELM
Link-
483PhosphoserineRAIHSSDEG
HHHCCCCCC
33.11Phosphositeplus
Link-
483PhosphoserineRAIHSSDEG
HHHCCCCCC
33.11SysPTM
Link-
483Phosphoserine (CSNK2A1)RAIHSSDEG
HHHCCCCCC
33.11HPRD
Link-
483Phosphoserine (CSNK2A2)RAIHSSDEG
HHHCCCCCC
33.11HPRD
Link-
483Phosphoserine; by CK2.RAIHSSDEG
HHHCCCCCC
33.11UniProtKB
Link-
484PhosphoserineAIHSSDEGE
HHCCCCCCC
26.06Phosphositeplus
Link-
484PhosphoserineAIHSSDEGE
HHCCCCCCC
26.06SysPTM
Link-
484Phosphoserine (CK2_alpha)AIHSSDEGE
HHCCCCCCC
26.06PhosphoELM
Link-
484Phosphoserine (CSNK2A1)AIHSSDEGE
HHCCCCCCC
26.06HPRD
Link-
484Phosphoserine (CSNK2A2)AIHSSDEGE
HHCCCCCCC
26.06HPRD
Link-
484Phosphoserine; by CK2.AIHSSDEGE
HHCCCCCCC
26.06UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
PPIP1_HUMANphysical interactionMINT-50147MINT14707117
GAS7_HUMANphysical interactionMINT-72917MINT16055720
WBP4_HUMANphysical interactionMINT-73063MINT16055720
HCK_HUMANphysical interactionMINT-16642MINT12029088
NCK1_HUMANphysical interactionMINT-14452MINT7565724
NCK1_HUMANphysical interactionMINT-14451MINT7565724
PTN12_HUMANphysical interactionMINT-50152MINT14707117
RHG01_HUMANphysical interactionMINT-16068MINT8805223
RHG01_HUMANphysical interactionMINT-16070MINT8805223
RHG01_HUMANphysical interactionMINT-16069MINT8805223
CIP4_HUMANphysical interactionMINT-15181MINT10713100
CIP4_HUMANphysical interactionMINT-15182MINT10713100
CDC42_HUMANphysical interactionDIP:11000EDIP10360578
WIPF1_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
physical interaction
physical interaction
physical int
EBI-603205
EBI-603228
EBI-603
intact10202051
10202051
9405671
9405671
9405671
9405671
9405671
CDC42_HUMANdirect interaction
physical interaction
physical interaction
direct interaction
direct interaction
physical interaction
physical interacti
EBI-603513
EBI-477278
EBI-476
intact10360578
15361624
15361624
9660763
9660763
9660763
9660763
9660763
ARPC3_HUMANphysical interactionEBI-603125
intact12769847
ARP2_HUMANphysical interactionEBI-603125
intact12769847
ARP3_HUMANphysical interactionEBI-603125
intact12769847
ARPC4_HUMANphysical interactionEBI-603125
intact12769847
HCK_HUMANphysical interaction
physical interaction
EBI-346395
EBI-347022
intact12029088
12029088
WASP_HUMANphysical interaction
physical interaction
physical interaction
EBI-603142
EBI-457408
EBI-457
intact12769847
10724160
10724160
ACTC_HUMANin vivoHPRD:02314HPRD12029088
GRB2_HUMANin vivoHPRD:02314HPRD10224664
9307968
FYN_HUMANin vivoHPRD:02314HPRD10224664
8805332
10532312
7565724
PLCG1_HUMANin vitroHPRD:02314HPRD8892607
FGR_HUMANin vitro
in vivo
HPRD:02314HPRD8824280
10358777
7565724
P85A_HUMANin vitroHPRD:02314HPRD10358777
ITK_HUMANin vitro
in vivo
HPRD:02314HPRD8810341
SRC_HUMANin vitroHPRD:02314HPRD8805332
WASP_HUMANin vitroHPRD:02314HPRD10724160
DLG1_HUMANin vitro
in vivo
HPRD:02314HPRD15699074
HCLS1_HUMANin vivoHPRD:02314HPRD15166239
C5AR_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:02314HPRD12600272
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Disease Reference
Kegg disease
OMIM disease
301000Wiskott-Aldrich syndrome (WAS)
313900Thrombocytopenia 1 (THC1)
300299Neutropenia, severe congenital, X-linked (XLN)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphorylation of tyrosine 291 enhances the ability of WASp tostimulate 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).
Cited for: FUNCTION, PHOSPHORYLATION AT TYR-291 BY HCK, MASS SPECTROMETRY, ANDINTERACTION WITH HCK.
"Phosphorylation of the WASP-VCA domain increases its affinity for theArp2/3 complex and enhances actin polymerization by WASP.";
Cory G.O.C., Cramer R., Blanchoin L., Ridley A.J.;
Mol. Cell 11:1229-1239(2003).
Cited for: PHOSPHORYLATION AT SER-483 AND SER-484, AND INTERACTION WITH THEARP2/3 COMPLEX.
"Fyn and PTP-PEST-mediated regulation of Wiskott-Aldrich syndromeprotein (WASp) tyrosine phosphorylation is required for coupling Tcell antigen receptor engagement to WASp effector function and T cellactivation.";
Badour K., Zhang J., Shi F., Leng Y., Collins M., Siminovitch K.A.;
J. Exp. Med. 199:99-112(2004).
Cited for: PHOSPHORYLATION AT TYR-291 BY FYN.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-291, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-291, AND MASSSPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-291; SER-483 ANDSER-484, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-291; SER-483 ANDSER-484, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures