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O43516 - WIPF1_HUMAN

UniProt

O43516 - WIPF1_HUMAN

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Protein

WAS/WASL-interacting protein family member 1

Gene

WIPF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity3 Publications

GO - Molecular functioni

  1. actin binding Source: ProtInc
  2. profilin binding Source: ProtInc

GO - Biological processi

  1. actin filament-based movement Source: Ensembl
  2. actin polymerization or depolymerization Source: ProtInc
  3. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  4. innate immune response Source: Reactome
  5. protein complex assembly Source: ProtInc
  6. response to other organism Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:WIPF1
Synonyms:WASPIP, WIP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:12736. WIPF1.

Subcellular locationi

Cytoplasmic vesicle By similarity. Cytoplasm › cytoskeleton By similarity. Cell projection › ruffle 1 Publication
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).By similarity

GO - Cellular componenti

  1. actin cytoskeleton Source: ProtInc
  2. actin filament Source: Ensembl
  3. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
  4. cytosol Source: Reactome
  5. ruffle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Wiskott-Aldrich syndrome 21 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn immunodeficiency disorder characterized by eczema, thrombocytopenia, recurrent infections, defective T-cell proliferation, and impaired natural killer cell function.

See also OMIM:614493

Organism-specific databases

MIMi614493. phenotype.
Orphaneti906. Wiskott-Aldrich syndrome.
PharmGKBiPA162409189.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 503503WAS/WASL-interacting protein family member 1PRO_0000065941Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei142 – 1421PhosphoserineBy similarity
Modified residuei340 – 3401Phosphoserine1 Publication
Modified residuei345 – 3451Phosphothreonine2 Publications
Modified residuei350 – 3501Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO43516.
PaxDbiO43516.
PRIDEiO43516.

PTM databases

PhosphoSiteiO43516.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiO43516.
CleanExiHS_WIPF1.
ExpressionAtlasiO43516. baseline and differential.
GenevestigatoriO43516.

Organism-specific databases

HPAiCAB009737.
HPA003739.

Interactioni

Subunit structurei

Binds to WAS, profilin and actin. Binds to WASL (By similarity). Interacts with DBNL.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CttnQ605983EBI-346356,EBI-397955From a different organism.
GRB2P629933EBI-346356,EBI-401755
HCKP086313EBI-346356,EBI-346340
HCLS1P143172EBI-346356,EBI-750369
NCK1P163332EBI-346356,EBI-389883
WASP4276811EBI-346356,EBI-346375
WASLO004014EBI-346356,EBI-957615

Protein-protein interaction databases

BioGridi113295. 28 interactions.
DIPiDIP-17015N.
IntActiO43516. 18 interactions.
MINTiMINT-238480.
STRINGi9606.ENSP00000352802.

Structurei

Secondary structure

1
503
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi33 – 4210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A41X-ray2.60C29-60[»]
ProteinModelPortaliO43516.
SMRiO43516. Positions 29-60, 461-488.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43516.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 4918WH2PROSITE-ProRule annotationAdd
BLAST
Repeati352 – 36110XRSGPXPPXP motif 1
Repeati374 – 38310XRSGPXPPXP motif 2
Repeati410 – 41910XRSGPXPPXP motif 3

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 484Binds actin

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 1312Poly-ProAdd
BLAST
Compositional biasi64 – 9633Gly-richAdd
BLAST
Compositional biasi241 – 2444Poly-Ser
Compositional biasi264 – 433170Pro-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the verprolin family.Curated
Contains 1 WH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG149184.
GeneTreeiENSGT00780000122052.
HOVERGENiHBG054157.
InParanoidiO43516.
OMAiQSSLHNR.
OrthoDBiEOG7PS1GQ.
PhylomeDBiO43516.
TreeFamiTF332135.

Family and domain databases

InterProiIPR003124. WH2_dom.
IPR028295. WIP.
[Graphical view]
PANTHERiPTHR23202:SF30. PTHR23202:SF30. 1 hit.
PfamiPF02205. WH2. 1 hit.
[Graphical view]
SMARTiSM00246. WH2. 1 hit.
[Graphical view]
PROSITEiPS51082. WH2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O43516-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MPVPPPPAPP PPPTFALANT EKPTLNKTEQ AGRNALLSDI SKGKKLKKTV 
        60         70         80         90        100
TNDRSAPILD KPKGAGAGGG GGGFGGGGGF GGGGGGGGGG SFGGGGPPGL 
       110        120        130        140        150
GGLFQAGMPK LRSTANRDND SGGSRPPLLP PGGRSTSAKP FSPPSGPGRF 
       160        170        180        190        200
PVPSPGHRSG PPEPQRNRMP PPRPDVGSKP DSIPPPVPST PRPIQSSPHN 
       210        220        230        240        250
RGSPPVPGGP RQPSPGPTPP PFPGNRGTAL GGGSIRQSPL SSSSPFSNRP 
       260        270        280        290        300
PLPPTPSRAL DDKPPPPPPP VGNRPSIHRE AVPPPPPQNN KPPVPSTPRP 
       310        320        330        340        350
SASSQAPPPP PPPSRPGPPP LPPSSSGNDE TPRLPQRNLS LSSSTPPLPS 
       360        370        380        390        400
PGRSGPLPPP PSERPPPPVR DPPGRSGPLP PPPPVSRNGS TSRALPATPQ 
       410        420        430        440        450
LPSRSGVDSP RSGPRPPLPP DRPSAGAPPP PPPSTSIRNG FQDSPCEDEW 
       460        470        480        490        500
ESRFYFHPIS DLPPPEPYVQ TTKSYPSKLA RNESRSGSNR RERGAPPLPP 

IPR
Length:503
Mass (Da):51,258
Last modified:November 30, 2010 - v3
Checksum:i09B7A95E6808A46D
GO
Isoform 2 (identifier: O43516-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     487-503: GSNRRERGAPPLPPIPR → EYFCQGF

Show »
Length:493
Mass (Da):50,281
Checksum:iE6BD4D77F6F2B6F4
GO
Isoform 3 (identifier: O43516-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     503-503: R → RPPKQAAE

Note: No experimental confirmation available.

Show »
Length:510
Mass (Da):51,980
Checksum:i9AEF92B15E4FE7F9
GO
Isoform 4 (identifier: O43516-4) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:358
Mass (Da):36,426
Checksum:i0473FF11AFC330B4
GO

Sequence cautioni

The sequence AAC03767.1 differs from that shown. Reason: Frameshift at positions 302 and 310. Curated
The sequence CAA60014.1 differs from that shown. Reason: Frameshift at positions 302 and 310. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 1191N → D in CAE45928. (PubMed:17974005)Curated
Sequence conflicti120 – 1201D → H in AAH02914. (PubMed:15489334)Curated
Sequence conflicti360 – 3601P → PV in CAA60014. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti198 – 1981P → L.6 Publications
Corresponds to variant rs4972450 [ dbSNP | Ensembl ].		VAR_046526
Natural varianti495 – 4951A → G.2 Publications
VAR_010295

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei220 – 364145Missing in isoform 4. 1 PublicationVSP_012964Add
BLAST
Alternative sequencei487 – 50317GSNRR…PPIPR → EYFCQGF in isoform 2. 1 PublicationVSP_012965Add
BLAST
Alternative sequencei503 – 5031R → RPPKQAAE in isoform 3. 1 PublicationVSP_012966

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2260.1. [O43516-1]
RefSeqiNP_001070737.1. NM_001077269.1. [O43516-1]
NP_003378.3. NM_003387.4. [O43516-1]
XP_006712790.1. XM_006712727.1. [O43516-1]
UniGeneiHs.128067.

Genome annotation databases

EnsembliENST00000272746; ENSP00000272746; ENSG00000115935. [O43516-3]
ENST00000359761; ENSP00000352802; ENSG00000115935. [O43516-1]
ENST00000392546; ENSP00000376329; ENSG00000115935. [O43516-1]
ENST00000392547; ENSP00000376330; ENSG00000115935. [O43516-1]
ENST00000409891; ENSP00000386431; ENSG00000115935. [O43516-2]
GeneIDi7456.
KEGGihsa:7456.
UCSCiuc002uiz.3. human. [O43516-1]
uc002ujb.2. human. [O43516-2]
uc010fqt.1. human. [O43516-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2260.1. [O43516-1]
RefSeqiNP_001070737.1. NM_001077269.1. [O43516-1]
NP_003378.3. NM_003387.4. [O43516-1]
XP_006712790.1. XM_006712727.1. [O43516-1]
UniGeneiHs.128067.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A41X-ray2.60C29-60[»]
ProteinModelPortaliO43516.
SMRiO43516. Positions 29-60, 461-488.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113295. 28 interactions.
DIPiDIP-17015N.
IntActiO43516. 18 interactions.
MINTiMINT-238480.
STRINGi9606.ENSP00000352802.

PTM databases

PhosphoSiteiO43516.

Proteomic databases

MaxQBiO43516.
PaxDbiO43516.
PRIDEiO43516.

Protocols and materials databases

DNASUi7456.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000272746; ENSP00000272746; ENSG00000115935. [O43516-3]
ENST00000359761; ENSP00000352802; ENSG00000115935. [O43516-1]
ENST00000392546; ENSP00000376329; ENSG00000115935. [O43516-1]
ENST00000392547; ENSP00000376330; ENSG00000115935. [O43516-1]
ENST00000409891; ENSP00000386431; ENSG00000115935. [O43516-2]
GeneIDi7456.
KEGGihsa:7456.
UCSCiuc002uiz.3. human. [O43516-1]
uc002ujb.2. human. [O43516-2]
uc010fqt.1. human. [O43516-3]

Organism-specific databases

CTDi7456.
GeneCardsiGC02M175424.
H-InvDBHIX0034792.
HGNCiHGNC:12736. WIPF1.
HPAiCAB009737.
HPA003739.
MIMi602357. gene.
614493. phenotype.
neXtProtiNX_O43516.
Orphaneti906. Wiskott-Aldrich syndrome.
PharmGKBiPA162409189.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG149184.
GeneTreeiENSGT00780000122052.
HOVERGENiHBG054157.
InParanoidiO43516.
OMAiQSSLHNR.
OrthoDBiEOG7PS1GQ.
PhylomeDBiO43516.
TreeFamiTF332135.

Enzyme and pathway databases

ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.

Miscellaneous databases

EvolutionaryTraceiO43516.
GeneWikiiWIPF1.
GenomeRNAii7456.
NextBioi29198.
PROiO43516.
SOURCEiSearch...

Gene expression databases

BgeeiO43516.
CleanExiHS_WIPF1.
ExpressionAtlasiO43516. baseline and differential.
GenevestigatoriO43516.

Family and domain databases

InterProiIPR003124. WH2_dom.
IPR028295. WIP.
[Graphical view]
PANTHERiPTHR23202:SF30. PTHR23202:SF30. 1 hit.
PfamiPF02205. WH2. 1 hit.
[Graphical view]
SMARTiSM00246. WH2. 1 hit.
[Graphical view]
PROSITEiPS51082. WH2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. 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.

Entry informationi

Entry nameiWIPF1_HUMAN
AccessioniPrimary (citable) accession number: O43516
Secondary accession number(s): B8ZZM1
, D3DPE4, Q15220, Q53TA9, Q6MZU9, Q9BU37, Q9UNP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 30, 2010
Last modified: February 4, 2015
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.