O43516 (WIPF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	WIPF1
Synonyms:	WASPIP, WIP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	503 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Cytoplasm › cytoskeleton By similarity. Cell projection › ruffle. 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.

Ontologies

Keywords
Cellular component	Cell projection Cytoplasm Cytoplasmic vesicle Cytoskeleton
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	Actin-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Fc-gamma receptor signaling pathway involved in phagocytosis Traceable author statement. Source: Reactome actin filament-based movement Inferred from electronic annotation. Source: Ensembl actin polymerization or depolymerization Traceable author statement Ref.1. Source: ProtInc innate immune response Traceable author statement. Source: Reactome protein complex assembly Traceable author statement Ref.1. Source: ProtInc response to other organism Inferred from electronic annotation. Source: Ensembl
Cellular_component	actin cytoskeleton Traceable author statement Ref.1. Source: ProtInc actin filament Inferred from electronic annotation. Source: Ensembl cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome ruffle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	actin binding Traceable author statement Ref.1. Source: ProtInc profilin binding Traceable author statement Ref.1. Source: ProtInc protein binding Inferred from physical interaction Ref.7PubMed 11331876PubMed 12029088PubMed 12620186PubMed 16488394PubMed 16582881PubMed 20936779PubMed 21398607PubMed 21706016PubMed 21988832PubMed 23414517Ref.1. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Cttn	Q60598	3	EBI-346356,EBI-397955	From a different organism.
GRB2	P62993	3	EBI-346356,EBI-401755
HCK	P08631	3	EBI-346356,EBI-346340
HCLS1	P14317	2	EBI-346356,EBI-750369
NCK1	P16333	2	EBI-346356,EBI-389883
WAS	P42768	11	EBI-346356,EBI-346375
WASL	O00401	4	EBI-346356,EBI-957615

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 503

503

WAS/WASL-interacting protein family member 1

PRO_0000065941

Regions

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

Compositional bias

2 – 13

12

Poly-Pro

Compositional bias

64 – 96

33

Gly-rich

Compositional bias

241 – 244

4

Poly-Ser

Compositional bias

264 – 433

170

Pro-rich

Amino acid modifications

Modified residue

142

1

Phosphoserine By similarity

Modified residue

340

1

Phosphoserine Ref.13

Modified residue

345

1

Phosphothreonine Ref.10 Ref.13

Modified residue

350

1

Phosphoserine Ref.10 Ref.11 Ref.13

Natural variations

Alternative sequence

220 – 364

145

Missing in isoform 4.

VSP_012964

Alternative sequence

487 – 503

17

GSNRR…PPIPR → EYFCQGF in isoform 2.

VSP_012965

Alternative sequence

503

1

R → RPPKQAAE in isoform 3.

VSP_012966

Natural variant

198

1

P → L. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 Ref.7
Corresponds to variant rs4972450 [ dbSNP | Ensembl ].

VAR_046526

Natural variant

495

1

A → G. Ref.1 Ref.2

VAR_010295

Experimental info

Sequence conflict

119

1

N → D in CAE45928. Ref.3

Sequence conflict

120

1

D → H in AAH02914. Ref.6

Sequence conflict

360

1

P → PV in CAA60014. Ref.2

Secondary structure

1

.

.

.

503

Helix Strand Turn

Details...

Helix

33 – 42

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 30, 2010. Version 3. Checksum: 09B7A95E6808A46D	FASTA	503	51,258
	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
	Isoform 2 [UniParc]. Checksum: E6BD4D77F6F2B6F4	FASTA	493	50,281
	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 RNESRSEYFC QGF
	Isoform 3 [UniParc]. Checksum: 9AEF92B15E4FE7F9	FASTA	510	51,980
	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 490 500 510 RNESRSGSNR RERGAPPLPP IPRPPKQAAE
	Isoform 4 [UniParc]. Checksum: 0473FF11AFC330B4	FASTA	358	36,426
	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 PPPVRDPPGR SGPLPPPPPV 250 260 270 280 290 300 SRNGSTSRAL PATPQLPSRS GVDSPRSGPR PPLPPDRPSA GAPPPPPPST SIRNGFQDSP 310 320 330 340 350 CEDEWESRFY FHPISDLPPP EPYVQTTKSY PSKLARNESR SGSNRRERGA PPLPPIPR

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.

CCDS

CCDS2260.1. [O43516-1]

RefSeq

NP_001070737.1. NM_001077269.1. [O43516-1]
NP_003378.3. NM_003387.4. [O43516-1]
XP_006712790.1. XM_006712727.1. [O43516-1]

UniGene

Hs.128067.

3D structure databases

PDBe
RCSB-PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2A41	X-ray	2.60	C	29-60	[»]

ProteinModelPortal

O43516.

SMR

O43516. Positions 29-60, 461-488.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

113295. 21 interactions.

DIP

DIP-17015N.

IntAct

O43516. 17 interactions.

MINT

MINT-238480.

STRING

9606.ENSP00000352802.

PTM databases

PhosphoSite

O43516.

Proteomic databases

MaxQB

O43516.

PaxDb

O43516.

PRIDE

O43516.

Protocols and materials databases

DNASU

7456.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

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]

GeneID

7456.

KEGG

hsa:7456.

UCSC

uc002uiz.3. human. [O43516-1]
uc002ujb.2. human. [O43516-2]
uc010fqt.1. human. [O43516-3]

Organism-specific databases

CTD

7456.

GeneCards

GC02M175424.

H-InvDB

HIX0034792.

HGNC

HGNC:12736. WIPF1.

HPA

CAB009737.
HPA003739.

MIM

602357. gene.
614493. phenotype.

neXtProt

NX_O43516.

Orphanet

906. Wiskott-Aldrich syndrome.

PharmGKB

PA162409189.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG149184.

HOVERGEN

HBG054157.

InParanoid

O43516.

OMA

QSSLHNR.

OrthoDB

EOG7PS1GQ.

PhylomeDB

O43516.

TreeFam

TF332135.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

O43516.

Bgee

O43516.

CleanEx

HS_WIPF1.

Genevestigator

O43516.

Family and domain databases

InterPro

IPR003124. WH2_dom.
IPR028295. WIP.
[Graphical view]

PANTHER

PTHR23202:SF30. PTHR23202:SF30. 1 hit.

Pfam

PF02205. WH2. 1 hit.
[Graphical view]

SMART

SM00246. WH2. 1 hit.
[Graphical view]

PROSITE

PS51082. WH2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O43516.

GeneWiki

WIPF1.

GenomeRNAi

7456.

NextBio

29198.

PRO

O43516.

SOURCE

Search...

Entry information

Entry name

WIPF1_HUMAN

Accession

Primary (citable) accession number: O43516
Secondary accession number(s): B8ZZM1 , D3DPE4, Q15220, Q53TA9, Q6MZU9, Q9BU37, Q9UNP1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	November 30, 2010
Last modified:	July 9, 2014
This is version 133 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.