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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: 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:12736. WIPF1.

Subcellular locationi

Cytoplasmic vesicle By similarity. Cytoplasmcytoskeleton By similarity. Cell projectionruffle 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. cell projection Source: UniProtKB-KW
  4. cytoplasmic vesicle Source: UniProtKB-KW
  5. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

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. 22 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 – 4210

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
GeneTreeiENSGT00760000119406.
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) [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.
The sequence CAA60014.1 differs from that shown. Reason: Frameshift at positions 302 and 310.

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS2260.1. [O43516-1 ]
RefSeqi NP_001070737.1. NM_001077269.1. [O43516-1 ]
NP_003378.3. NM_003387.4. [O43516-1 ]
XP_006712790.1. XM_006712727.1. [O43516-1 ]
UniGenei Hs.128067.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2A41 X-ray 2.60 C 29-60 [» ]
ProteinModelPortali O43516.
SMRi O43516. Positions 29-60, 461-488.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113295. 22 interactions.
DIPi DIP-17015N.
IntActi O43516. 18 interactions.
MINTi MINT-238480.
STRINGi 9606.ENSP00000352802.

PTM databases

PhosphoSitei O43516.

Proteomic databases

MaxQBi O43516.
PaxDbi O43516.
PRIDEi O43516.

Protocols and materials databases

DNASUi 7456.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000272746 ; ENSP00000272746 ; ENSG00000115935 . [O43516-3 ]
ENST00000359761 ; ENSP00000352802 ; ENSG00000115935 . [O43516-1 ]
ENST00000392546 ; ENSP00000376329 ; ENSG00000115935 . [O43516-1 ]
ENST00000392547 ; ENSP00000376330 ; ENSG00000115935 . [O43516-1 ]
ENST00000409891 ; ENSP00000386431 ; ENSG00000115935 . [O43516-2 ]
GeneIDi 7456.
KEGGi hsa:7456.
UCSCi uc002uiz.3. human. [O43516-1 ]
uc002ujb.2. human. [O43516-2 ]
uc010fqt.1. human. [O43516-3 ]

Organism-specific databases

CTDi 7456.
GeneCardsi GC02M175424.
H-InvDB HIX0034792.
HGNCi HGNC:12736. WIPF1.
HPAi CAB009737.
HPA003739.
MIMi 602357. gene.
614493. phenotype.
neXtProti NX_O43516.
Orphaneti 906. Wiskott-Aldrich syndrome.
PharmGKBi PA162409189.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG149184.
GeneTreei ENSGT00760000119406.
HOVERGENi HBG054157.
InParanoidi O43516.
OMAi QSSLHNR.
OrthoDBi EOG7PS1GQ.
PhylomeDBi O43516.
TreeFami TF332135.

Enzyme and pathway databases

Reactomei REACT_160086. Regulation of actin dynamics for phagocytic cup formation.

Miscellaneous databases

EvolutionaryTracei O43516.
GeneWikii WIPF1.
GenomeRNAii 7456.
NextBioi 29198.
PROi O43516.
SOURCEi Search...

Gene expression databases

Bgeei O43516.
CleanExi HS_WIPF1.
ExpressionAtlasi O43516. baseline and differential.
Genevestigatori O43516.

Family and domain databases

InterProi IPR003124. WH2_dom.
IPR028295. WIP.
[Graphical view ]
PANTHERi PTHR23202:SF30. PTHR23202:SF30. 1 hit.
Pfami PF02205. WH2. 1 hit.
[Graphical view ]
SMARTi SM00246. WH2. 1 hit.
[Graphical view ]
PROSITEi PS51082. WH2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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.

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: October 29, 2014
This is version 136 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