WIPF1_HUMAN - dbPTM
WIPF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WIPF1_HUMAN
UniProt AC O43516
Protein Name WAS/WASL-interacting protein family member 1
Gene Name WIPF1
Organism Homo sapiens (Human).
Sequence Length 503
Subcellular Localization Cytoplasmic vesicle. Cytoplasm, cytoskeleton. Cell projection, ruffle . 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
Protein Description 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..
Protein Sequence MPVPPPPAPPPPPTFALANTEKPTLNKTEQAGRNALLSDISKGKKLKKTVTNDRSAPILDKPKGAGAGGGGGGFGGGGGFGGGGGGGGGGSFGGGGPPGLGGLFQAGMPKLRSTANRDNDSGGSRPPLLPPGGRSTSAKPFSPPSGPGRFPVPSPGHRSGPPEPQRNRMPPPRPDVGSKPDSIPPPVPSTPRPIQSSPHNRGSPPVPGGPRQPSPGPTPPPFPGNRGTALGGGSIRQSPLSSSSPFSNRPPLPPTPSRALDDKPPPPPPPVGNRPSIHREAVPPPPPQNNKPPVPSTPRPSASSQAPPPPPPPSRPGPPPLPPSSSGNDETPRLPQRNLSLSSSTPPLPSPGRSGPLPPPPSERPPPPVRDPPGRSGPLPPPPPVSRNGSTSRALPATPQLPSRSGVDSPRSGPRPPLPPDRPSAGAPPPPPPSTSIRNGFQDSPCEDEWESRFYFHPISDLPPPEPYVQTTKSYPSKLARNESRSGSNRRERGAPPLPPIPR
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
33MethylationNKTEQAGRNALLSDI
CHHHHHHHHHHHHHH
28.4180702493
33Asymmetric dimethylarginineNKTEQAGRNALLSDI
CHHHHHHHHHHHHHH
28.41-
49PhosphorylationKGKKLKKTVTNDRSA
HCCCCCCCCCCCCCC
30.8626437602
91PhosphorylationGGGGGGGSFGGGGPP
CCCCCCCCCCCCCCC
24.8027251275
125MethylationDNDSGGSRPPLLPPG
CCCCCCCCCCCCCCC
39.8858860295
125DimethylationDNDSGGSRPPLLPPG
CCCCCCCCCCCCCCC
39.88-
134MethylationPLLPPGGRSTSAKPF
CCCCCCCCCCCCCCC
42.5516287957
134DimethylationPLLPPGGRSTSAKPF
CCCCCCCCCCCCCCC
42.55-
135PhosphorylationLLPPGGRSTSAKPFS
CCCCCCCCCCCCCCC
29.9529978859
136PhosphorylationLPPGGRSTSAKPFSP
CCCCCCCCCCCCCCC
31.2029978859
137PhosphorylationPPGGRSTSAKPFSPP
CCCCCCCCCCCCCCC
35.2329978859
142PhosphorylationSTSAKPFSPPSGPGR
CCCCCCCCCCCCCCC
44.4129978859
145PhosphorylationAKPFSPPSGPGRFPV
CCCCCCCCCCCCCCC
62.0929978859
149DimethylationSPPSGPGRFPVPSPG
CCCCCCCCCCCCCCC
35.51-
149MethylationSPPSGPGRFPVPSPG
CCCCCCCCCCCCCCC
35.51115391861
154PhosphorylationPGRFPVPSPGHRSGP
CCCCCCCCCCCCCCC
43.6929978859
203PhosphorylationSSPHNRGSPPVPGGP
CCCCCCCCCCCCCCC
23.8523401153
211DimethylationPPVPGGPRQPSPGPT
CCCCCCCCCCCCCCC
65.40-
211MethylationPPVPGGPRQPSPGPT
CCCCCCCCCCCCCCC
65.4080702477
214PhosphorylationPGGPRQPSPGPTPPP
CCCCCCCCCCCCCCC
33.8623401153
218PhosphorylationRQPSPGPTPPPFPGN
CCCCCCCCCCCCCCC
55.1028450419
226MethylationPPPFPGNRGTALGGG
CCCCCCCCCCCCCCC
50.1652723719
228PhosphorylationPFPGNRGTALGGGSI
CCCCCCCCCCCCCCC
18.5723403867
234PhosphorylationGTALGGGSIRQSPLS
CCCCCCCCCCCCCCC
20.2023401153
236MethylationALGGGSIRQSPLSSS
CCCCCCCCCCCCCCC
32.4080702485
238PhosphorylationGGGSIRQSPLSSSSP
CCCCCCCCCCCCCCC
20.2626055452
241PhosphorylationSIRQSPLSSSSPFSN
CCCCCCCCCCCCCCC
31.4021712546
242PhosphorylationIRQSPLSSSSPFSNR
CCCCCCCCCCCCCCC
42.3826425664
243PhosphorylationRQSPLSSSSPFSNRP
CCCCCCCCCCCCCCC
38.3621712546
244PhosphorylationQSPLSSSSPFSNRPP
CCCCCCCCCCCCCCC
31.7321712546
247PhosphorylationLSSSSPFSNRPPLPP
CCCCCCCCCCCCCCC
35.0021712546
249MethylationSSSPFSNRPPLPPTP
CCCCCCCCCCCCCCC
32.7780702501
255PhosphorylationNRPPLPPTPSRALDD
CCCCCCCCCCCCCCC
31.7726055452
257PhosphorylationPPLPPTPSRALDDKP
CCCCCCCCCCCCCCC
32.4421712546
258MethylationPLPPTPSRALDDKPP
CCCCCCCCCCCCCCC
40.13115383587
276PhosphorylationPPVGNRPSIHREAVP
CCCCCCCCCCCCCCC
27.9923401153
296PhosphorylationNNKPPVPSTPRPSAS
CCCCCCCCCCCCCCC
51.8022210691
301PhosphorylationVPSTPRPSASSQAPP
CCCCCCCCCCCCCCC
41.9022210691
331PhosphorylationSSSGNDETPRLPQRN
CCCCCCCCCCCCCCC
19.3026074081
340PhosphorylationRLPQRNLSLSSSTPP
CCCCCCCCCCCCCCC
29.7428674151
342PhosphorylationPQRNLSLSSSTPPLP
CCCCCCCCCCCCCCC
20.9022115753
343PhosphorylationQRNLSLSSSTPPLPS
CCCCCCCCCCCCCCC
43.4529255136
344PhosphorylationRNLSLSSSTPPLPSP
CCCCCCCCCCCCCCC
41.3729255136
345PhosphorylationNLSLSSSTPPLPSPG
CCCCCCCCCCCCCCC
30.7623401153
350PhosphorylationSSTPPLPSPGRSGPL
CCCCCCCCCCCCCCC
47.9029255136
354PhosphorylationPLPSPGRSGPLPPPP
CCCCCCCCCCCCCCC
51.1526074081
362PhosphorylationGPLPPPPSERPPPPV
CCCCCCCCCCCCCCC
52.6026074081
376PhosphorylationVRDPPGRSGPLPPPP
CCCCCCCCCCCCCCC
51.1528555341
386O-linked_GlycosylationLPPPPPVSRNGSTSR
CCCCCCCCCCCCCCC
26.2929485866
386PhosphorylationLPPPPPVSRNGSTSR
CCCCCCCCCCCCCCC
26.2929978859
390PhosphorylationPPVSRNGSTSRALPA
CCCCCCCCCCCCCCC
27.1029978859
391PhosphorylationPVSRNGSTSRALPAT
CCCCCCCCCCCCCCC
24.5129978859
392PhosphorylationVSRNGSTSRALPATP
CCCCCCCCCCCCCCC
19.7729978859
398PhosphorylationTSRALPATPQLPSRS
CCCCCCCCCCCCCCC
15.0423401153
403PhosphorylationPATPQLPSRSGVDSP
CCCCCCCCCCCCCCC
47.9022199227
404MethylationATPQLPSRSGVDSPR
CCCCCCCCCCCCCCC
35.17115383595
405PhosphorylationTPQLPSRSGVDSPRS
CCCCCCCCCCCCCCC
47.7222199227
409PhosphorylationPSRSGVDSPRSGPRP
CCCCCCCCCCCCCCC
21.5822199227
412PhosphorylationSGVDSPRSGPRPPLP
CCCCCCCCCCCCCCC
57.4422210691
415MethylationDSPRSGPRPPLPPDR
CCCCCCCCCCCCCCC
49.33115383603
422MethylationRPPLPPDRPSAGAPP
CCCCCCCCCCCCCCC
32.61115383611
424PhosphorylationPLPPDRPSAGAPPPP
CCCCCCCCCCCCCCC
39.9827080861
434PhosphorylationAPPPPPPSTSIRNGF
CCCCCCCCCCCCCCC
40.3329052541
435PhosphorylationPPPPPPSTSIRNGFQ
CCCCCCCCCCCCCCC
33.6729052541
436PhosphorylationPPPPPSTSIRNGFQD
CCCCCCCCCCCCCCC
24.7229052541
444PhosphorylationIRNGFQDSPCEDEWE
CCCCCCCCCCCCHHH
22.2223401153
452PhosphorylationPCEDEWESRFYFHPI
CCCCHHHHCCEEEEH
28.8529449344
455PhosphorylationDEWESRFYFHPISDL
CHHHHCCEEEEHHHC
10.4028674419
468PhosphorylationDLPPPEPYVQTTKSY
HCCCCCCCCCCCCCC
11.9728555341
488PhosphorylationRNESRSGSNRRERGA
CCCCCCCCCCCCCCC
28.5412504004
493MethylationSGSNRRERGAPPLPP
CCCCCCCCCCCCCCC
44.77115383619

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
154SPhosphorylationKinaseAKT2P31751
PSP
398TPhosphorylationKinaseAKT2P31751
PSP
488SPhosphorylationKinasePRKCQQ04759
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WIPF1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of WIPF1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NCK1_HUMANNCK1physical
9694849
WASP_HUMANWASphysical
9694849
WASL_HUMANWASLphysical
11331876
ACTG_HUMANACTG1physical
11331876
WASL_HUMANWASLphysical
25416956
HOME3_HUMANHOMER3physical
25416956
SC24C_HUMANSEC24Cphysical
25416956
ABI2_HUMANABI2physical
25416956
FASTK_HUMANFASTKphysical
25416956
WWP2_HUMANWWP2physical
25416956
HOME3_HUMANHOMER3physical
21516116

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614493Wiskott-Aldrich syndrome 2 (WAS2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of WIPF1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340 AND SER-350, ANDMASS SPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-345 AND SER-350, ANDMASS SPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND MASSSPECTROMETRY.

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