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O43516 (WIPF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
WAS/WASL-interacting protein family member 1
Alternative name(s):
Protein PRPL-2
Wiskott-Aldrich syndrome protein-interacting protein
Short name=WASP-interacting protein
Gene names
Name:WIPF1
Synonyms:WASPIP, WIP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length503 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in the reorganization of the actin cytoskeleton. Contributes with NCK1 and GRB2 in the recruitment and activation of WASL. May participate in regulating the subcellular localization of WASL, resulting in the disassembly of stress fibers in favor of filopodia formation. Plays a role in the formation of cell ruffles By similarity. Plays an important role in the intracellular motility of vaccinia virus by functioning as an adapter for recruiting WASL to vaccinia virus. Ref.1 Ref.8 Ref.12

Subunit structure

Binds to WAS, profilin and actin. Binds to WASL By similarity. Interacts with DBNL. Ref.1 Ref.7 Ref.12

Subcellular location

Cytoplasmic vesicle By similarity. Cytoplasmcytoskeleton By similarity. Cell projectionruffle. Note: Vesicle surfaces and along actin tails. Colocalizes with actin stress fibers. When coexpressed with WASL, no longer associated with actin filaments but accumulated in perinuclear and cortical areas like WASL By similarity. Ref.12

Tissue specificity

Highly expressed in peripheral blood mononuclear cells, spleen, placenta, small intestine, colon and thymus. Lower expression in ovary, heart, brain, lung, liver, skeletal muscle, kidney, pancreas, prostate and testis. Ref.1

Domain

Binds to WAS within the N-terminal region 170, at a site distinct from the CDC42-binding site.

Involvement in disease

Wiskott-Aldrich syndrome 2 (WAS2) [MIM:614493]: An immunodeficiency disorder characterized by eczema, thrombocytopenia, recurrent infections, defective T-cell proliferation, and impaired natural killer cell function.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15

Miscellaneous

Recruited to PIP5K-induced vesicle surfaces in the absence of functional WASL By similarity.

Sequence similarities

Belongs to the verprolin family.

Contains 1 WH2 domain.

Sequence caution

The sequence AAC03767.1 differs from that shown. Reason: Frameshift at positions 302 and 310.

The sequence CAA60014.1 differs from that shown. Reason: Frameshift at positions 302 and 310.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43516-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O43516-2)

The sequence of this isoform differs from the canonical sequence as follows:
     487-503: GSNRRERGAPPLPPIPR → EYFCQGF
Isoform 3 (identifier: O43516-3)

The sequence of this isoform differs from the canonical sequence as follows:
     503-503: R → RPPKQAAE
Note: No experimental confirmation available.
Isoform 4 (identifier: O43516-4)

The sequence of this isoform differs from the canonical sequence as follows:
     220-364: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 503503WAS/WASL-interacting protein family member 1
PRO_0000065941

Regions

Domain32 – 4918WH2
Repeat352 – 36110XRSGPXPPXP motif 1
Repeat374 – 38310XRSGPXPPXP motif 2
Repeat410 – 41910XRSGPXPPXP motif 3
Region45 – 484Binds actin
Compositional bias2 – 1312Poly-Pro
Compositional bias64 – 9633Gly-rich
Compositional bias241 – 2444Poly-Ser
Compositional bias264 – 433170Pro-rich

Amino acid modifications

Modified residue1421Phosphoserine By similarity
Modified residue3401Phosphoserine Ref.13
Modified residue3451Phosphothreonine Ref.10 Ref.13
Modified residue3501Phosphoserine Ref.10 Ref.11 Ref.13

Natural variations

Alternative sequence220 – 364145Missing in isoform 4.
VSP_012964
Alternative sequence487 – 50317GSNRR…PPIPR → EYFCQGF in isoform 2.
VSP_012965
Alternative sequence5031R → RPPKQAAE in isoform 3.
VSP_012966
Natural variant1981P → L. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 Ref.7
Corresponds to variant rs4972450 [ dbSNP | Ensembl ].
VAR_046526
Natural variant4951A → G. Ref.1 Ref.2
VAR_010295

Experimental info

Sequence conflict1191N → D in CAE45928. Ref.3
Sequence conflict1201D → H in AAH02914. Ref.6
Sequence conflict3601P → PV in CAA60014. Ref.2

Secondary structure

... 503
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 30, 2010. Version 3.
Checksum: 09B7A95E6808A46D

FASTA50351,258
        10         20         30         40         50         60 
MPVPPPPAPP PPPTFALANT EKPTLNKTEQ AGRNALLSDI SKGKKLKKTV TNDRSAPILD 

        70         80         90        100        110        120 
KPKGAGAGGG GGGFGGGGGF GGGGGGGGGG SFGGGGPPGL GGLFQAGMPK LRSTANRDND 

       130        140        150        160        170        180 
SGGSRPPLLP PGGRSTSAKP FSPPSGPGRF PVPSPGHRSG PPEPQRNRMP PPRPDVGSKP 

       190        200        210        220        230        240 
DSIPPPVPST PRPIQSSPHN RGSPPVPGGP RQPSPGPTPP PFPGNRGTAL GGGSIRQSPL 

       250        260        270        280        290        300 
SSSSPFSNRP PLPPTPSRAL DDKPPPPPPP VGNRPSIHRE AVPPPPPQNN KPPVPSTPRP 

       310        320        330        340        350        360 
SASSQAPPPP PPPSRPGPPP LPPSSSGNDE TPRLPQRNLS LSSSTPPLPS PGRSGPLPPP 

       370        380        390        400        410        420 
PSERPPPPVR DPPGRSGPLP PPPPVSRNGS TSRALPATPQ LPSRSGVDSP RSGPRPPLPP 

       430        440        450        460        470        480 
DRPSAGAPPP PPPSTSIRNG FQDSPCEDEW ESRFYFHPIS DLPPPEPYVQ TTKSYPSKLA 

       490        500 
RNESRSGSNR RERGAPPLPP IPR 

« Hide

Isoform 2 [UniParc].

Checksum: E6BD4D77F6F2B6F4
Show »

FASTA49350,281
Isoform 3 [UniParc].

Checksum: 9AEF92B15E4FE7F9
Show »

FASTA51051,980
Isoform 4 [UniParc].

Checksum: 0473FF11AFC330B4
Show »

FASTA35836,426

References

« Hide 'large scale' references
[1]"WIP, a protein associated with Wiskott-Aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells."
Ramesh N., Anton I.M., Hartwig J.H., Geha R.S.
Proc. Natl. Acad. Sci. U.S.A. 94:14671-14676(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS LEU-198 AND GLY-495, FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH WASP; PROFILIN AND ACTIN.
[2]Kreideweiss S., Delany-Heiken P., Nordheim A., Ruhlmann A.
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS LEU-198 AND GLY-495.
Tissue: Tonsil.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT LEU-198.
Tissue: Endometrial tumor.
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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], VARIANT LEU-198.
[6]"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] (ISOFORM 4), VARIANT LEU-198.
Tissue: Skin.
[7]"Mutations that cause the Wiskott-Aldrich syndrome impair the interaction of Wiskott-Aldrich syndrome protein (WASP) with WASP interacting protein."
Stewart D.M., Tian L., Nelson D.L.
J. Immunol. 162:5019-5024(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 192-503 (ISOFORM 1), INTERACTION WITH WASP, VARIANT LEU-198.
[8]"A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization."
Moreau V., Frischknecht F., Reckmann I., Vincentelli R., Rabut G., Stewart D.M., Way M.
Nat. Cell Biol. 2:441-448(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-345 AND SER-350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"Actin-binding protein-1 interacts with WASp-interacting protein to regulate growth factor-induced dorsal ruffle formation."
Cortesio C.L., Perrin B.J., Bennin D.A., Huttenlocher A.
Mol. Biol. Cell 21:186-197(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DBNL.
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340; THR-345 AND SER-350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"A novel primary human immunodeficiency due to deficiency in the WASP-interacting protein WIP."
Lanzi G., Moratto D., Vairo D., Masneri S., Delmonte O., Paganini T., Parolini S., Tabellini G., Mazza C., Savoldi G., Montin D., Martino S., Tovo P., Pessach I.M., Massaad M.J., Ramesh N., Porta F., Plebani A. expand/collapse author list , Notarangelo L.D., Geha R.S., Giliani S.
J. Exp. Med. 209:29-34(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN WAS2.
[16]"Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly."
Chereau D., Kerff F., Graceffa P., Grabarek Z., Langsetmo K., Dominguez R.
Proc. Natl. Acad. Sci. U.S.A. 102:16644-16649(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 29-60 IN COMPLEX WITH ACTIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF031588 mRNA. Translation: AAC03767.1. Frameshift.
X86019 mRNA. Translation: CAA60014.1. Frameshift.
BX640870 mRNA. Translation: CAE45928.1.
AC010894 Genomic DNA. Translation: AAY14708.1.
AC104595 Genomic DNA. No translation available.
CH471058 Genomic DNA. Translation: EAX11131.1.
CH471058 Genomic DNA. Translation: EAX11132.1.
CH471058 Genomic DNA. Translation: EAX11133.1.
BC002914 mRNA. Translation: AAH02914.1.
AF106062 mRNA. Translation: AAD45972.1.
RefSeqNP_001070737.1. NM_001077269.1.
NP_003378.3. NM_003387.4.
UniGeneHs.128067.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2A41X-ray2.60C29-60[»]
ProteinModelPortalO43516.
SMRO43516. Positions 29-60, 461-488.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113295. 21 interactions.
DIPDIP-17015N.
IntActO43516. 17 interactions.
MINTMINT-238480.
STRING9606.ENSP00000352802.

PTM databases

PhosphoSiteO43516.

Proteomic databases

PaxDbO43516.
PRIDEO43516.

Protocols and materials databases

DNASU7456.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000272746; ENSP00000272746; ENSG00000115935. [O43516-3]
ENST00000359761; ENSP00000352802; ENSG00000115935. [O43516-1]
ENST00000392546; ENSP00000376329; ENSG00000115935. [O43516-1]
ENST00000392547; ENSP00000376330; ENSG00000115935. [O43516-1]
ENST00000409891; ENSP00000386431; ENSG00000115935. [O43516-2]
GeneID7456.
KEGGhsa:7456.
UCSCuc002uiz.3. human. [O43516-1]
uc002ujb.2. human. [O43516-2]
uc010fqt.1. human. [O43516-3]

Organism-specific databases

CTD7456.
GeneCardsGC02M175424.
H-InvDBHIX0034792.
HGNCHGNC:12736. WIPF1.
HPACAB009737.
HPA003739.
MIM602357. gene.
614493. phenotype.
neXtProtNX_O43516.
Orphanet906. Wiskott-Aldrich syndrome.
PharmGKBPA162409189.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG149184.
HOVERGENHBG054157.
InParanoidO43516.
OMAQSSLHNR.
OrthoDBEOG7PS1GQ.
PhylomeDBO43516.
TreeFamTF332135.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressO43516.
BgeeO43516.
CleanExHS_WIPF1.
GenevestigatorO43516.

Family and domain databases

InterProIPR003124. WH2_dom.
IPR028295. WIP.
[Graphical view]
PANTHERPTHR23202:SF6. PTHR23202:SF6. 1 hit.
PfamPF02205. WH2. 1 hit.
[Graphical view]
SMARTSM00246. WH2. 1 hit.
[Graphical view]
PROSITEPS51082. WH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO43516.
GeneWikiWIPF1.
GenomeRNAi7456.
NextBio29198.
PROO43516.
SOURCESearch...

Entry information

Entry nameWIPF1_HUMAN
AccessionPrimary (citable) accession number: O43516
Secondary accession number(s): B8ZZM1 expand/collapse secondary AC list , D3DPE4, Q15220, Q53TA9, Q6MZU9, Q9BU37, Q9UNP1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 30, 2010
Last modified: April 16, 2014
This is version 130 of the entry and version 3 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM