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Reviewed, UniProtKB/Swiss-Prot O43516 (WIPF1_HUMAN)

Last modified November 25, 2008. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

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

Protein attributes

Sequence length503 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

May have direct activity on the actin cytoskeleton. Induces actin polymerization and redistribution. 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 By similarity. Plays an important role in the intracellular motility of vaccinia virus by functioning as an adapter for recruiting WASL to vaccinia virus.

Subunit structure

Binds to WAS, profilin and actin. Binds to WASL By similarity.

Subcellular location

Cytoplasmic vesicleBy similarity. CytoplasmcytoskeletonBy similarity. Note= Vesicle surfaces and along actin tails. Co-localized with actin stress fibers. When co-expressed with WASL, no longer associated with actin filaments but accumulated in perinuclear and cortical areas like WASL By similarity.

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.

Domain

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

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.

Ontologies

Keywords

   Cellular componentCytoplasm
Cytoplasmic vesicle
Cytoskeleton
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandActin-binding
   PTMPhosphoprotein
   Technical term3D-structure

Gene Ontology (GO)

   Biological processactin polymerization or depolymerization Ref.1

Traceable author statement. Source: ProtInc

protein complex assembly Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentactin cytoskeleton Ref.1

Traceable author statement. Source: ProtInc

cytoplasmic vesicle

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionactin binding Ref.1

Traceable author statement. Source: ProtInc

profilin binding Ref.1

Traceable author statement. Source: ProtInc

Complete GO annotation...

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
Notes: No experimental confirmation available.
Isoform 4 (identifier: O43516-4)

The sequence of this isoform differs from the canonical sequence as follows:
     220-364: Missing.
Notes: 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 residue3501Phosphoserine

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 variant1981L → P: dbSNP rs4972450.
VAR_046526
Natural variant4951A → G
VAR_010295

Experimental info

Sequence conflict1191N → D in CAE45928. Ref.3
Sequence conflict1201D → H in AAH02914. Ref.5
Sequence conflict303 – 3097SSQAPPP → PHRPHLR in AAC03767. Ref.1
Sequence conflict303 – 3097SSQAPPP → PHRPHLR in CAA60014. Ref.2
Sequence conflict3601P → PV in CAA60014. Ref.2

Secondary structure

... 503
Helix Strand Turn

Details...

Sequences

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

Last modified March 1, 2005. Version 2.
Checksum: 05FEF91E6D11B86D

FASTA50351,275
        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 PRPIQSSLHN 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: E1D0FD646D9F0FB0
Show »

49350,297
Isoform 3 [UniParc].

Checksum: FAA8FEB6396FA7F5
Show »

51051,996
Isoform 4 [UniParc].

Checksum: 124197B8BB8321F1
Show »

35836,442

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: 9405671] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT 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), VARIANT GLY-495.
Tissue: Tonsil.
[3]The German cDNA consortium
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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: 15815621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-198.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Skin.
[6]"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: 10202051] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 192-503 (ISOFORM 1), INTERACTION WITH WASP.
[7]"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: 10878810] [Abstract]
Cited for: FUNCTION.
[8]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF031588 mRNA. Translation: AAC03767.1.
X86019 mRNA. Translation: CAA60014.1.
BX640870 mRNA. Translation: CAE45928.1.
AC010894 Genomic DNA. Translation: AAY14708.1.
BC002914 mRNA. Translation: AAH02914.1.
AF106062 mRNA. Translation: AAD45972.1.
RefSeqNP_001070737.1.
NP_003378.3.
UniGeneHs.654521

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1MKENMR-A-[»]
2A41X-ray2.60C29-60[»]
SMRO43516. Positions 451-495.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:17015N.
IntActO43516.

PTM databases

PhosphoSiteO43516.

Genome annotation databases

EnsemblENSG00000115935. Homo sapiens. [Contig view]
GeneID7456.
KEGGhsa:7456.

Organism-specific databases

H-InvDBHIX0034792.
HGNCHGNC:12736. WIPF1.
HPACAB009737.
MIM602357. gene.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENO43516.

Gene expression databases

ArrayExpressO43516.
CleanExHS_WIPF1.
GermOnlineENSG00000115935. Homo sapiens.

Family and domain databases

InterProIPR003124. WH2_actin_bd.
[Graphical view]
PfamPF02205. WH2. 1 hit.
[Graphical view]
SMARTSM00246. WH2. 1 hit.
[Graphical view]
PROSITEPS51082. WH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio29198.
SOURCESearch...

Entry information

Entry nameWIPF1_HUMAN
AccessionPrimary (citable) accession number: O43516
Secondary accession number(s): Q15220 expand/collapse secondary AC list , Q53TA9, Q6MZU9, Q9BU37, Q9UNP1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: March 1, 2005
Last modified: November 25, 2008
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 2

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents