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Q92558 (WASF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 family member 1

Short name=WASP family protein member 1
Alternative name(s):
Protein WAVE-1
Verprolin homology domain-containing protein 1
Gene names
Name:WASF1
Synonyms:KIAA0269, SCAR1, WAVE1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length559 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Downstream effector molecule involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Promotes formation of actin filaments. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex.

Subunit structure

Component of the WAVE1 complex composed of ABI2, CYFIP1 or CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a heterdimer containing NCKAP1 and CYFIP1 interacts with a heterotrimer formed by WAVE1, ABI2 and BRK1. CYFIP2 binds to activated RAC1 which causes the complex to dissociate, releasing activated WASF1. The complex can also be activated by NCK1. Binds actin and the Arp2/3 complex. Interacts with BAIAP2. Interacts with SHANK3; the interaction mediates the association of SHANK3 with the WAVE1 complex. Interacts with ABI1 (via N-terminus). Ref.7 Ref.8

Subcellular location

Cytoplasmcytoskeleton. Cell junctionsynapse By similarity. Note: Dot-like pattern in the cytoplasm. Concentrated in Rac-regulated membrane-ruffling areas.

Tissue specificity

Highly expressed in brain. Lowly expressed in testis, ovary, colon, kidney, pancreas, thymus, small intestine and peripheral blood.

Domain

Binds the Arp2/3 complex through the C-terminal region and actin through verprolin homology (VPH) domain.

Sequence similarities

Belongs to the SCAR/WAVE family.

Contains 1 WH2 domain.

Sequence caution

The sequence BAA13399.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PFN1P077372EBI-1548747,EBI-713780

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 559559Wiskott-Aldrich syndrome protein family member 1
PRO_0000188992

Regions

Domain497 – 51418WH2
Compositional bias278 – 2836Poly-Pro
Compositional bias322 – 33211Poly-Pro
Compositional bias348 – 35912Poly-Pro
Compositional bias369 – 3746Poly-Pro
Compositional bias424 – 43512Poly-Pro

Secondary structure

...................... 559
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q92558 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 44B4527BDB77BC6E

FASTA55961,652
        10         20         30         40         50         60 
MPLVKRNIDP RHLCHTALPR GIKNELECVT NISLANIIRQ LSSLSKYAED IFGELFNEAH 

        70         80         90        100        110        120 
SFSFRVNSLQ ERVDRLSVSV TQLDPKEEEL SLQDITMRKA FRSSTIQDQQ LFDRKTLPIP 

       130        140        150        160        170        180 
LQETYDVCEQ PPPLNILTPY RDDGKEGLKF YTNPSYFFDL WKEKMLQDTE DKRKEKRKQK 

       190        200        210        220        230        240 
QKNLDRPHEP EKVPRAPHDR RREWQKLAQG PELAEDDANL LHKHIEVANG PASHFETRPQ 

       250        260        270        280        290        300 
TYVDHMDGSY SLSALPFSQM SELLTRAEER VLVRPHEPPP PPPMHGAGDA KPIPTCISSA 

       310        320        330        340        350        360 
TGLIENRPQS PATGRTPVFV SPTPPPPPPP LPSALSTSSL RASMTSTPPP PVPPPPPPPA 

       370        380        390        400        410        420 
TALQAPAVPP PPAPLQIAPG VLHPAPPPIA PPLVQPSPPV ARAAPVCETV PVHPLPQGEV 

       430        440        450        460        470        480 
QGLPPPPPPP PLPPPGIRPS SPVTVTALAH PPSGLHPTPS TAPGPHVPLM PPSPPSQVIP 

       490        500        510        520        530        540 
ASEPKRHPST LPVISDARSV LLEAIRKGIQ LRKVEEQREQ EAKHERIEND VATILSRRIA 

       550 
VEYSDSEDDS EFDEVDWLE 

« Hide

References

« Hide 'large scale' references
[1]"SCAR, a WASP-related protein, isolated as a suppressor of receptor defects in late Dictyostelium development."
Bear J.E., Rawls J.F., Saxe C.L. III
J. Cell Biol. 142:1325-1335(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Bone marrow.
[3]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[6]"Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex."
Machesky L.M., Insall R.H.
Curr. Biol. 8:1347-1356(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[7]"IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling."
Miki H., Yamaguchi H., Suetsugu S., Takenawa T.
Nature 408:732-735(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BAIAP2.
[8]"Structure and control of the actin regulatory WAVE complex."
Chen Z., Borek D., Padrick S.B., Gomez T.S., Metlagel Z., Ismail A.M., Umetani J., Billadeau D.D., Otwinowski Z., Rosen M.K.
Nature 468:533-538(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF WAVE1 COMPLEX, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF134303 mRNA. Translation: AAD33052.1.
D87459 mRNA. Translation: BAA13399.2. Different initiation.
AL590009 Genomic DNA. Translation: CAI12485.1.
CH471051 Genomic DNA. Translation: EAW48325.1.
CH471051 Genomic DNA. Translation: EAW48326.1.
CH471051 Genomic DNA. Translation: EAW48327.1.
CH471051 Genomic DNA. Translation: EAW48328.1.
CH471051 Genomic DNA. Translation: EAW48329.1.
BC044591 mRNA. Translation: AAH44591.1.
RefSeqNP_001020105.1. NM_001024934.1.
NP_001020106.1. NM_001024935.1.
NP_001020107.1. NM_001024936.1.
NP_003922.1. NM_003931.2.
XP_005267260.1. XM_005267203.2.
XP_005267261.1. XM_005267204.1.
XP_005267262.1. XM_005267205.1.
XP_005267263.1. XM_005267206.1.
XP_005267264.1. XM_005267207.1.
UniGeneHs.75850.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3P8CX-ray2.29D1-559[»]
4N78X-ray2.43D1-559[»]
ProteinModelPortalQ92558.
SMRQ92558. Positions 21-227, 496-544.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114449. 14 interactions.
DIPDIP-39391N.
IntActQ92558. 17 interactions.
MINTMINT-144109.
STRING9606.ENSP00000352425.

PTM databases

PhosphoSiteQ92558.

Polymorphism databases

DMDM2495730.

Proteomic databases

PaxDbQ92558.
PRIDEQ92558.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359451; ENSP00000352425; ENSG00000112290.
ENST00000392586; ENSP00000376365; ENSG00000112290.
ENST00000392587; ENSP00000376366; ENSG00000112290.
ENST00000392588; ENSP00000376367; ENSG00000112290.
ENST00000392589; ENSP00000376368; ENSG00000112290.
GeneID8936.
KEGGhsa:8936.
UCSCuc003ptv.1. human.

Organism-specific databases

CTD8936.
GeneCardsGC06M110421.
HGNCHGNC:12732. WASF1.
HPACAB022161.
HPA004105.
MIM605035. gene.
neXtProtNX_Q92558.
PharmGKBPA37343.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG299696.
HOGENOMHOG000021456.
HOVERGENHBG058482.
InParanoidQ92558.
KOK05753.
OMAYMEHLDG.
OrthoDBEOG7VHSXK.
PhylomeDBQ92558.
TreeFamTF315031.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ92558.
BgeeQ92558.
CleanExHS_WASF1.
GenevestigatorQ92558.

Family and domain databases

InterProIPR028288. SCAR/WAVE_fam.
IPR003124. WH2_dom.
[Graphical view]
PANTHERPTHR12902. PTHR12902. 1 hit.
PfamPF02205. WH2. 1 hit.
[Graphical view]
SMARTSM00246. WH2. 1 hit.
[Graphical view]
PROSITEPS51082. WH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSWASF1. human.
EvolutionaryTraceQ92558.
GeneWikiWASF1.
GenomeRNAi8936.
NextBio33600.
PMAP-CutDBQ92558.
PROQ92558.
SOURCESearch...

Entry information

Entry nameWASF1_HUMAN
AccessionPrimary (citable) accession number: Q92558
Secondary accession number(s): E1P5F2, Q5SZK7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM