Neural Wiskott-Aldrich syndrome protein

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O08816 (WASL_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 118. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Neural Wiskott-Aldrich syndrome protein
Short name=N-WASP

Gene names

Name:

Wasl

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	501 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 By similarity.
Subunit structure	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 the WW domains of PRPF40A/FBP11. Interacts with NOSTRIN and SNX9. Binds to TNK2 By similarity. Interacts with PTK2/FAK1. Ref.2
Subcellular location	Cytoplasm › cytoskeleton. Nucleus. Note: Preferentially localized in the cytoplasm when phosphorylated and in the nucleus when unphosphorylated By similarity. Ref.2
Sequence similarities	Contains 1 CRIB domain. Contains 1 WH1 domain. Contains 2 WH2 domains.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Cytoskeleton Nucleus
Domain	Repeat
Ligand	Actin-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin polymerization or depolymerization Inferred from electronic annotation. Source: InterPro membrane budding Inferred from direct assay PubMed 20730103. Source: BHF-UCL membrane invagination Inferred from direct assay PubMed 20730103. Source: BHF-UCL membrane tubulation Inferred from direct assay PubMed 20730103. Source: BHF-UCL positive regulation of clathrin-mediated endocytosis Inferred from direct assay PubMed 20730103. Source: BHF-UCL positive regulation of filopodium assembly Inferred from direct assay PubMed 20730103. Source: BHF-UCL protein complex assembly Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW vesicle transport along actin filament Inferred from direct assay PubMed 20730103. Source: BHF-UCL
Cellular_component	Golgi membrane Inferred from direct assay PubMed 15147909. Source: RGD actin cytoskeleton Inferred from electronic annotation. Source: InterPro cytoplasmic membrane-bounded vesicle Inferred from direct assay PubMed 20730103. Source: BHF-UCL nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	small GTPase regulator activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-6142604,EBI-6142604
CDC42	P60953	2	EBI-6142604,EBI-81752	From a different organism.
PFN1	P07737	4	EBI-6142604,EBI-713780	From a different organism.
PFN2	P35080	3	EBI-6142604,EBI-473138	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 501

501

Neural Wiskott-Aldrich syndrome protein

PRO_0000189002

Regions

Domain

31 – 138

108

WH1

Domain

200 – 213

CRIB

Domain

401 – 418

WH2 1

Domain

429 – 446

WH2 2

Compositional bias

274 – 385

112

Pro-rich

Compositional bias

482 – 501

Asp-rich

Amino acid modifications

Modified residue

239

Phosphoserine; by TNK2 By similarity

Modified residue

253

Phosphotyrosine; by FAK1 and TNK2 Ref.2

Modified residue

480

Phosphoserine By similarity

Modified residue

481

Phosphoserine By similarity

Secondary structure

501

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

O08816 [UniParc].

Last modified January 1, 1998. Version 2.
Checksum: 480E21F26F7FC77E
Show »

FASTA

501

54,325

        10         20         30         40         50         60 
MSSGQQPPRR VTNVGSLLLT PQENESLFSF LGKKCVTMSS AVVQLYAADR NCMWSKKCSG 

        70         80         90        100        110        120 
VACLVKDNPQ RSYFLRIFDI KDGKLLWEQE LYNNFVYNSP RGYFHTFAGD TCQVALNFAN 

       130        140        150        160        170        180 
EEEAKKFRKA VTDLLGRRQR KSEKRRDAPN GPNLPMATVD IKNPEITTNR FYSSQVNNIS 

       190        200        210        220        230        240 
HTKEKKKGKA KKKRLTKADI GTPSNFQHIG HVGWDPNTGF DLNNLDPELK NLFDMCGISE 

       250        260        270        280        290        300 
AQLKDRETSK VIYDFIEKTG GVEAVKNELR RQAPPPPPPS RGGPPPPPPP PHSSGPPPPP 

       310        320        330        340        350        360 
ARGRGAPPPP PSRAPTAAPP PPPPSRPGVV VPPPPPNRMY PPPPPALPSS APSGPPPPPP 

       370        380        390        400        410        420 
LSMAGSTAPP PPPPPPPPPG PPPPPGLPSD GDHQVPASSG NKAALLDQIR EGAQLKKVEQ 

       430        440        450        460        470        480 
NSRPVSCSGR DALLDQIRQG IQLKSVSDGQ ESTPPTPAPT SGIVGALMEV MQKRSKAIHS 

       490        500 
SDEDEDDDDE EDFQDDDEWE D

« Hide

References

[1]	"Identification of N-WASP homologs in human and rat brain." Fukuoka M., Miki H., Takenawa T. Gene 196:43-48(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Focal adhesion kinase regulation of N-WASP subcellular localization and function." Wu X., Suetsugu S., Cooper L.A., Takenawa T., Guan J.L. J. Biol. Chem. 279:9565-9576(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PTK2/FAK1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-253.
[3]	"Structure of the N-WASP EVH1 domain-WIP complex: insight into the molecular basis of Wiskott-Aldrich Syndrome." Volkman B.F., Prehoda K.E., Scott J.A., Peterson F.C., Lim W.A. Cell 111:565-576(2002) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 37-485.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D88461 mRNA. Translation: BAA21534.1.

IPI

IPI00196440.

UniGene

Rn.126640.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MKE	NMR	-	A	26-147	[»]
2IFS	NMR	-	A	26-147	[»]

ProteinModelPortal

O08816.

SMR

O08816. Positions 26-147, 201-272.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-17016N.

IntAct

O08816. 9 interactions.

MINT

MINT-250197.

STRING

10116.ENSRNOP00000009261.

PTM databases

PhosphoSite

O08816.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

UCSC

RGD:735144. rat.

Organism-specific databases

RGD

735144. Wasl.

Phylogenomic databases

eggNOG

NOG270974.

HOGENOM

HOG000214052.

HOVERGEN

HBG000222.

InParanoid

O08816.

OrthoDB

EOG4JM7Q1.

Gene expression databases

ArrayExpress

O08816.

Genevestigator

O08816.

GermOnline

ENSRNOG00000006975. Rattus norvegicus.

Family and domain databases

Gene3D

2.30.29.30. 1 hit.

InterPro

IPR000697. EVH1.
IPR000095. PAK_box_Rho-bd.
IPR011993. PH_like_dom.
IPR011026. WASP_C.
IPR003124. WH2_dom.
[Graphical view]

Pfam

PF00786. PBD. 1 hit.
PF00568. WH1. 1 hit.
PF02205. WH2. 2 hits.
[Graphical view]

SMART

SM00285. PBD. 1 hit.
SM00461. WH1. 1 hit.
SM00246. WH2. 2 hits.
[Graphical view]

SUPFAM

SSF47912. WASP_C. 2 hits.

PROSITE

PS50108. CRIB. 1 hit.
PS50229. WH1. 1 hit.
PS51082. WH2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O08816.

Entry information

Entry name

WASL_RAT

Accession

Primary (citable) accession number: O08816

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	January 1, 1998
Last modified:	April 3, 2013
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents