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UniProtKB/Swiss-Prot entry O43516


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name WIPF1_HUMAN
Primary accession number O43516
Secondary accession numbers Q15220 Q53TA9 Q6MZU9 Q9BU37 Q9UNP1
Integrated into Swiss-Prot on February 21, 2001
Sequence was last modified on March 1, 2005 (Sequence version 2)
Annotations were last modified on    September 23, 2008 (Entry version 76)
Name and origin of the protein
Protein name WAS/WASL-interacting protein family member 1
Synonyms Wiskott-Aldrich syndrome protein-interacting protein
WASP-interacting protein
Protein PRPL-2
Gene name
Name: WIPF1
Synonyms: WASPIP, WIP
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-495, FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH WASP; PROFILIN AND ACTIN.
DOI=10.1073/pnas.94.26.14671; PubMed=9405671 [NCBI, ExPASy, EBI, Israel, Japan]
Ramesh N., Anton I.M., Hartwig J.H., Geha R.S.;
"WIP, a protein associated with Wiskott-Aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells.";
Proc. Natl. Acad. Sci. U.S.A. 94:14671-14676(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT GLY-495.
TISSUE=Tonsil;
Kreideweiss S., Delany-Heiken P., Nordheim A., Ruhlmann A.;
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Endometrial tumor;
The German cDNA consortium;
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-198.
DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 192-503 (ISOFORM 1), AND INTERACTION WITH WASP.
PubMed=10202051 [NCBI, ExPASy, EBI, Israel, Japan]
Stewart D.M., Tian L., Nelson D.L.;
"Mutations that cause the Wiskott-Aldrich syndrome impair the interaction of Wiskott-Aldrich syndrome protein (WASP) with WASP interacting protein.";
J. Immunol. 162:5019-5024(1999).
[7]
FUNCTION.
DOI=10.1038/35017080; PubMed=10878810 [NCBI, ExPASy, EBI, Israel, Japan]
Moreau V., Frischknecht F., Reckmann I., Vincentelli R., Rabut G., Stewart D.M., Way M.;
"A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization.";
Nat. Cell Biol. 2:441-448(2000).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF031588; AAC03767.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X86019; CAA60014.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX640870; CAE45928.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC010894; AAY14708.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002914; AAH02914.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF106062; AAD45972.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001070737.1; -.
NP_003378.3; -.
UniGene Hs.654521
3D structure databases
PDB
1MKE; NMR; -; A=-.[ExPASy / RCSB / EBI]
2A41; X-ray; 2.60 A; C=29-60.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1MKE; -.
2A41; -.
SMR O43516; 451-495.
ModBase O43516.
Protein-protein interaction databases
DIP DIP:17015N; -.
IntAct O43516; -.
PTM databases
PhosphoSite O43516; -.
Organism-specific databases
H-InvDB HIX0034792; -.
HGNC HGNC:12736; WIPF1.
GenAtlas WIPF1.
HPA CAB009737; -.
MIM 602357; gene. [NCBI / EBI]
GeneCards O43516.
Gene expression databases
ArrayExpress O43516; -.
CleanEx HS_WIPF1; -.
GermOnline ENSG00000115935; Homo sapiens.
Ontologies
GO
GO:0015629; Cellular component: actin cytoskeleton (traceable author statement from ProtInc).
GO:0003779; Molecular function: actin binding (traceable author statement from ProtInc).
GO:0005522; Molecular function: profilin binding (traceable author statement from ProtInc).
GO:0008154; Biological process: actin polymerization or depolymerization (traceable author statement from ProtInc).
GO:0006461; Biological process: protein complex assembly (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR003124; WH2_actin_bd.
Graphical view of domain structure.
Pfam PF02205; WH2; 1.
Pfam graphical view of domain structure.
SMART SM00246; WH2; 1.
SMART graphical view of domain structure.
PROSITE PS51082; WH2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS O43516.
Genome annotation databases
Ensembl ENSG00000115935; Homo sapiens. [Contig view]
GeneID 7456; -.
KEGG hsa:7456; -.
Phylogenomic databases
HOVERGEN O43516; -.
Other
SOURCE WIPF1; Homo sapiens.
ProtoNet O43516.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Actin-binding; Alternative splicing; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Phosphoprotein; Polymorphism; Repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   503  503     WAS/WASL-interacting protein family member 1. PRO_0000065941
DOMAIN   32    49  18     WH2. 
REPEAT   352   361  10     XRSGPXPPXP motif 1. 
REPEAT   374   383  10     XRSGPXPPXP motif 2. 
REPEAT   410   419  10     XRSGPXPPXP motif 3. 
REGION   45    48  4     Binds actin. 
COMPBIAS   2    13  12     Poly-Pro. 
COMPBIAS   64    96  33     Gly-rich. 
COMPBIAS   241   244  4     Poly-Ser. 
COMPBIAS   264   433  170     Pro-rich. 
MOD_RES   350   350        Phosphoserine. 
VAR_SEQ   220   364        Missing (in isoform 4). VSP_012964
VAR_SEQ   487   503        GSNRRERGAPPLPPIPR -> EYFCQGF (in isoform 2). VSP_012965
VAR_SEQ   503   503        R -> RPPKQAAE (in isoform 3). VSP_012966
VARIANT   198   198  1     L -> P (in dbSNP:rs4972450 [NCBI]). VAR_046526 
VARIANT   495   495  1     A -> G. VAR_010295 
CONFLICT   119   119        N -> D (in Ref. 3; CAE45928). 
CONFLICT   120   120        D -> H (in Ref. 5; AAH02914). 
CONFLICT   303   309        SSQAPPP -> PHRPHLR (in Ref. 1; AAC03767 and 2; CAA60014). 
CONFLICT   360   360        P -> PV (in Ref. 2; CAA60014). 
HELIX   33    42  10      
Sequence information
Length: 503 AA [This is the length of the unprocessed precursor] Molecular weight: 51275 Da [This is the MW of the unprocessed precursor] CRC64: 05FEF91E6D11B86D [This is a checksum on the sequence]
        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 

O43516 in FASTA format

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