WASL_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: WASL_MOUSE
• UniProt AC: Q91YD9
• Protein Name: Neural Wiskott-Aldrich syndrome protein
• Gene Name: Wasl
• Organism: Mus musculus (Mouse).
• Sequence Length: 501
• Subcellular Localization: Nucleus . Cytoplasm . Cytoplasm, cytoskeleton . Preferentially localized in the cytoplasm when phosphorylated and in the nucleus when unphosphorylated (PubMed:12871950, PubMed:14676198). Exported from the nucleus by an nuclear export signal (NES)-dep
• Protein Description: Involved in mitosis and cytokinesis, via its role in the regulation of actin polymerization (By similarity). Regulates actin polymerization by stimulating the actin-nucleating activity of the Arp2/3 complex. Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression. Plays a role in dendrite spine morphogenesis. [PubMed: 25851601]
• Protein Sequence: MSSGQQPPRRVTNVGSLLLTPQENESLFSFLGKKCVTMSSAVVQLYAADRNCMWAKKCSGVACLVKDNPQRSYFLRIFDIKDGKLLWEQELYNNFVYNSPRGYFHTFAGDTCQVALNFANEEEAKKFRKAVTDLLGRRQRKSEKRRDAPNGPNLPMATVDIKNPEITTNRFYGSQVNNISHTKEKKKGKAKKKRLTKADIGTPSNFQHIGHVGWDPNTGFDLNNLDPELKNLFDMCGISEAQLKDRETSKVIYDFIEKTGGVEAVKNELRRQAPPPPPPSRGGPPPPPPPPHSSGPPPPPARGRGAPPPPPSRAPTAAPPPPPPSRPGVVVPPPPPNRMYPPPPPALPSSAPSGPPPPPPPSMAGSTAPPPPPPPPPPPGPPPPPGLPSDGDHQVPAPSGNKAALLDQIREGAQLKKVEQNSRPVSCSGRDALLDQIRQGIQLKSVSDGQESTPPTPAPTSGIVGALMEVMQKRSKAIHSSDEDEDDDDEEDFEDDDEWED

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
2	Acetylation	------MSSGQQPPR ------CCCCCCCCC	43.08	-
46	Phosphorylation	SSAVVQLYAADRNCM HHHHHHHHHHCCCCC	5.22	28576409
132	Phosphorylation	KKFRKAVTDLLGRRQ HHHHHHHHHHHHHHH	26.28	25159016
141	Acetylation	LLGRRQRKSEKRRDA HHHHHHHHHHHHCCC	55.41	15630825
144	Acetylation	RRQRKSEKRRDAPNG HHHHHHHHHCCCCCC	60.88	15630835
172	Phosphorylation	EITTNRFYGSQVNNI CCCCCCCCHHHCCCC	16.78	25159016
174	Phosphorylation	TTNRFYGSQVNNISH CCCCCCHHHCCCCCC	21.41	25159016
183	Ubiquitination	VNNISHTKEKKKGKA CCCCCCCCHHHCCCC	63.21	-
239	Phosphorylation	LFDMCGISEAQLKDR HHHHHCCCHHHHCCC	16.50	-
253	Phosphorylation	RETSKVIYDFIEKTG CCHHHHHHHHHHHHC	14.05	25521595
304	Methylation	PPPPARGRGAPPPPP CCCCCCCCCCCCCCC	32.33	16186577
422	Phosphorylation	LKKVEQNSRPVSCSG HHCHHHCCCCCCCCC	37.34	26824392
426	Phosphorylation	EQNSRPVSCSGRDAL HHCCCCCCCCCHHHH	12.78	27087446
428	Phosphorylation	NSRPVSCSGRDALLD CCCCCCCCCHHHHHH	29.38	29233185
445	Phosphorylation	RQGIQLKSVSDGQES HHCCEEEECCCCCCC	35.13	26643407
447	Phosphorylation	GIQLKSVSDGQESTP CCEEEECCCCCCCCC	43.01	26643407
452	Phosphorylation	SVSDGQESTPPTPAP ECCCCCCCCCCCCCC	38.02	26643407
453	Phosphorylation	VSDGQESTPPTPAPT CCCCCCCCCCCCCCC	32.32	26643407
456	Phosphorylation	GQESTPPTPAPTSGI CCCCCCCCCCCCCHH	33.03	26643407
460	Phosphorylation	TPPTPAPTSGIVGAL CCCCCCCCCHHHHHH	41.51	29899451
475	Phosphorylation	MEVMQKRSKAIHSSD HHHHHHHHHHHHCCC	33.21	26160508
480	Phosphorylation	KRSKAIHSSDEDEDD HHHHHHHCCCCCCCC	33.11	23684622
481	Phosphorylation	RSKAIHSSDEDEDDD HHHHHHCCCCCCCCC	30.75	23684622

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
239	S	Phosphorylation	Kinase	TNK2	O54967	Uniprot
253	Y	Phosphorylation	Kinase	TNK2	O54967	Uniprot
253	Y	Phosphorylation	Kinase	FAK1	P34152	Uniprot
253	Y	Phosphorylation	Kinase	PTK2	P34152-2	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
239	S	Phosphorylation	Phosphorylation at Ser-239, Tyr-253, Ser-480 and Ser-481 enhances actin polymerization activity.	-
480	S	Phosphorylation	Phosphorylation at Ser-239, Tyr-253, Ser-480 and Ser-481 enhances actin polymerization activity.	21183079
481	S	Phosphorylation	Phosphorylation at Ser-239, Tyr-253, Ser-480 and Ser-481 enhances actin polymerization activity.	-

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BIN1_MOUSE	Bin1	physical	25262827

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-253, AND MASSSPECTROMETRY.
PubMed: 19131326

"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-253, AND MASSSPECTROMETRY.
PubMed: 19144319

"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-253, AND MASSSPECTROMETRY.
PubMed: 18034455

"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-253, AND MASSSPECTROMETRY.
PubMed: 15592455

"Focal adhesion kinase regulation of N-WASP subcellular localizationand function.";
Wu X., Suetsugu S., Cooper L.A., Takenawa T., Guan J.L.;
J. Biol. Chem. 279:9565-9576(2004).
Cited for: INTERACTION WITH PTK2/FAK1, SUBCELLULAR LOCATION, AND PHOSPHORYLATIONAT TYR-253.
PubMed: 14676198