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N-WASP (human)

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: Golgi membrane; lamellipodium; cytoplasmic membrane-bound vesicle; plasma membrane; actin cap; cytosol; nucleus; actin cytoskeleton Molecular Function: protein binding; actin binding; small GTPase regulator activity Biological Process: positive regulation of filopodium formation; axon guidance; transcription, DNA-dependent; vesicle organization and biogenesis; nitric oxide metabolic process; spindle localization; vesicle transport along actin filament; regulation of transcription, DNA-dependent; response to bacterium; actin polymerization and/or depolymerization; 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®

Select Structure to View Below N-WASP 2FF3 - C=451-465 (human) 2LNH - B=339-402 (human) 2VCP - D/E=392-484 (human) 3M3N - W=417-444 (mouse) 1MKE - A=- (rat) 2IFS - A=26-147 (rat)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 2FF3 2LNH 2VCP  |  Phospho3D  |  DISEASE  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	Sites Implicated In
cell adhesion, altered: Y256‑p cytoskeletal reorganization: Y256‑p activation: 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

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
6	1367		Y256-p	RETSKVIyDFIEKTG
1	0		T262	IyDFIEKTGGVEAVK
0	14		R307-m1	PPPPARGrGAPPPPP
0	1		S430-p	EQNSRPVsCSGRDAL
0	3		T457-p	VADGQEStPPtPAPt
0	3		T460-p	GQEStPPtPAPtSGI
0	1		T464-p	tPPtPAPtSGIVGAL
3	8		S484-p	KRSKAIHssDEDEDE
2	7		S485-p	RSKAIHssDEDEDED

	mouse
A55	ADRNCMWAKKCSGVA
Y92	LLWEQELYNNFVYNS
Y97	ELYNNFVYNSPRGYF
T132	KKFRKAVTDLLGRRQ
K141-a	LLGRRQRkSEkRRDA
K144-a	RRQRkSEkRRDAPNG
Y172	EITTNRFYGSQVNNI
K183-u	VNNISHTkEKKKGKA
T196	KAKKKRLTKADIGTP
T202	LTKADIGTPSNFQHI
S239	LFDMCGISEAQLKDR
T248	AQLKDRETSKVIyDF
S249	QLKDRETSKVIyDFI
Y253-p	RETSKVIyDFIEKTG
T259	IyDFIEKTGGVEAVK
R304-m1	PPPPARGrGAPPPPP
S426	EQNSRPVSCSGRDAL
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
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
T457	VTDAPESTPPAPAPT
A460	APESTPPAPAPTSGI
T464	TPPAPAPTSGIVGAL
S484	KRSKAIHSSDEDEDE
S485	RSKAIHSSDEDEDED

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