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Protein Page:
N-WASP (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
N-WASP Regulates actin polymerization by stimulating the actin- nucleating activity of the Arp2/3 complex. Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression. Binds actin and the Arp2/3 complex. Interacts with CDC42. Binds to SH3 domains of GRB2. Interacts with the C-terminal SH3 domain of DNMBP. Interacts with SNX9. Interacts with the WW domains of PRPF40A/FBP11. Interacts with PTK2/FAK1. Interacts with NOSTRIN. Interacts with Shigella flexneri protein IcsA. The interaction with IcsA enhances the affinity of WASL for Arp2/3, thus assembling a tight complex which has maximal activity in actin assembly. Interacts with E.coli effector protein EspF(U). Identified in a complex containing at least WASL, BAIAP2L1 and E.coli EspF(U). Binds to TNK2. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Adaptor/scaffold
Cellular Component: lamellipodium; cytoplasmic membrane-bound vesicle; plasma membrane; actin cap; nucleus; cytosol; actin cytoskeleton
Molecular Function: protein binding; actin binding; small GTPase regulator activity
Biological Process: positive regulation of filopodium formation; mitosis; axon guidance; transcription, DNA-dependent; vesicle organization and biogenesis; nitric oxide metabolic process; spindle localization; vesicle transport along actin filament; regulation of protein localization; regulation of transcription, DNA-dependent; response to bacterium; actin polymerization and/or depolymerization; innate immune response; protein complex assembly; regulation of nitric-oxide synthase activity; cell motility; membrane budding
Reference #:  O00401 (UniProtKB)
Alt. Names/Synonyms: DKFZp779G0847; MGC48327; N-WASP; Neural Wiskott-Aldrich syndrome protein; NWASP; WASL; Wiskott-Aldrich syndrome gene-like; Wiskott-Aldrich syndrome gene-like protein; Wiskott-Aldrich syndrome-like
Gene Symbols: WASL
Molecular weight: 54,827 Da
Basal Isoelectric point: 8.05  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

N-WASP

Protein Structure Not Found.


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Sites Implicated In
cell adhesion, induced: Y256‑p
cytoskeletal reorganization: Y256‑p
activity, induced: Y256‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 S58-p ADRNCMWsKKCSGVA
0 1 Y95-p LLWEQELyNNFVyNS
0 1 Y100-p ELyNNFVyNSPRGYF
0 1 T135-p KKFRKAVtDLLGRRQ
0 1 K144 LLGRRQRKSEKRRDP
0 1 K147 RRQRKSEKRRDPPNG
1 5 Y175-p EITTNRFyGPQVNNI
0 1 K186 VNNISHTKEKKKGKA
1 0 T199 KAKKKRLTKADIGTP
1 0 T205 LTKADIGTPSNFQHI
1 0 S242 LFDMCGISEAQLKDR
0 1 T251 AQLKDRETSKVIyDF
0 1 S252 QLKDRETSKVIyDFI
7 1332 Y256-p RETSKVIyDFIEKTG
1 0 T262 IyDFIEKTGGVEAVK
0 15 R307-m1 PPPPARGrGAPPPPP
0 1 S430-p EQNSRPVsCSGRDAL
0 1 S456-p SVADGQEstPPtPAP
0 3 T457-p VADGQEstPPtPAPt
0 3 T460-p GQEstPPtPAPtSGI
0 1 T464-p tPPtPAPtSGIVGAL
3 10 S484-p KRSKAIHssDEDEDE
2 9 S485-p RSKAIHssDEDEDED
  mouse

 
A55 ADRNCMWAKKCSGVA
Y92 LLWEQELYNNFVYNS
Y97 ELYNNFVYNSPRGYF
T132 KKFRKAVTDLLGRRQ
K141-ac LLGRRQRkSEkRRDA
K144-ac RRQRkSEkRRDAPNG
Y172 EITTNRFYGSQVNNI
K183-ub VNNISHTkEKKKGKA
T196 KAKKKRLTKADIGTP
T202 LTKADIGTPSNFQHI
S239 LFDMCGISEAQLKDR
T248 AQLKDRETSKVIyDF
S249 QLKDRETSKVIyDFI
Y253-p RETSKVIyDFIEKTG
T259 IyDFIEKTGGVEAVK
R304-m1 PPPPARGrGAPPPPP
S426-p EQNSRPVsCSGRDAL
S452 SVSDGQESTPPTPAP
T453 VSDGQESTPPTPAPT
T456 GQESTPPTPAPTSGI
T460 TPPTPAPTSGIVGAL
S480-p KRSKAIHssDEDEDD
S481-p RSKAIHssDEDEDDD
  rat

 
S55 ADRNCMWSKKCSGVA
Y92 LLWEQELYNNFVYNS
Y97 ELYNNFVYNSPRGYF
T132 KKFRKAVTDLLGRRQ
K141 LLGRRQRKSEKRRDA
K144 RRQRKSEKRRDAPNG
Y172 EITTNRFYSSQVNNI
K183 VNNISHTKEKKKGKA
T196-p KAKKKRLtKADIGtP
T202-p LtKADIGtPSNFQHI
S239-p LFDMCGIsEAQLKDR
T248-p AQLKDREtsKVIyDF
S249-p QLKDREtsKVIyDFI
Y253-p REtsKVIyDFIEKtG
T259-p IyDFIEKtGGVEAVK
R304 PPPPARGRGAPPPPP
S426 EQNSRPVSCSGRDAL
S452 SVSDGQESTPPTPAP
T453 VSDGQESTPPTPAPT
T456 GQESTPPTPAPTSGI
T460 TPPTPAPTSGIVGAL
S480-p KRSKAIHssDEDEDD
S481-p RSKAIHssDEDEDDD
  cow

 
S58 ADRNCMWSKKCSGVA
Y95 LLWEQELYNNFVYNS
Y100 ELYNNFVYNSPRGYF
T135 KKFRKAVTDLLGRRQ
K144 LLGRRQRKSEKRRDP
K147 RRQRKSEKRRDPPNG
Y175-p EITTNRFyGPQINNI
K186 INNISHTKEKKKGKA
T199 KAKKKRLTKADIGTP
T205 LTKADIGTPSNFQHI
S242 LFDMCGISEAQLKDR
T251 AQLKDRETSKVIyDF
S252 QLKDRETSKVIyDFI
Y256-p RETSKVIyDFIEKTG
T262 IyDFIEKTGGVEAVK
R307 PPPPARGRGAPPPPP
S430 EQNSRPVSCSGRDAL
S456 SVTDAPESTPPAPAP
T457 VTDAPESTPPAPAPT
A460 APESTPPAPAPTSGI
T464 TPPAPAPTSGIVGAL
S484 KRSKAIHSSDEDEDE
S485 RSKAIHSSDEDEDED
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