dbPTM

BORG4_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BORG4_MOUSE
UniProt AC	Q9JM96
Protein Name	Cdc42 effector protein 4
Gene Name	Cdc42ep4
Organism	Mus musculus (Mouse).
Sequence Length	349
Subcellular Localization	Endomembrane system Peripheral membrane protein. Cytoplasm, cytoskeleton.
Protein Description	Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation, when overexpressed in fibroblasts..
Protein Sequence	MPILKQLVSSSVNSKRRSRADLTAEMISAPLGDFRHTMHVGRAGDAFGDTSFLTSKAREADDESLDEQASASKLSLLSRKFRGSKRSQSVTRGDREQRDMLGSLRDSALFVKNAMSLPQLNEKEAAEKDSSKLPKSLSSSPVKKADARDGGPKSPHRNGATGPHSPDPLLDEQAFGDLMDLPIMPKVSYGLKHAESILSFHIDLGPSMLGDVLSIMDKDQWGSEEEEEAGGYRDKEGPSSIVQAPPVLEVVPPLGRQESKASWDQASMLPPHAVEDDGWAVVAPSPSSARSVGSHTTRDSSSLSSYTSGVLEERSPAFRGPDRVAAAPPRQPDKEFCFMDEEEEDEIRV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Methylation	---MPILKQLVSSSV ---CCHHHHHHHHCH	42.16	-
9	Phosphorylation	PILKQLVSSSVNSKR CHHHHHHHHCHHHHC	26.03	29899451
10	Phosphorylation	ILKQLVSSSVNSKRR HHHHHHHHCHHHHCC	30.72	29899451
11	Phosphorylation	LKQLVSSSVNSKRRS HHHHHHHCHHHHCCC	20.15	22324799
14	Phosphorylation	LVSSSVNSKRRSRAD HHHHCHHHHCCCHHH	25.94	21743459
15	Ubiquitination	VSSSVNSKRRSRADL HHHCHHHHCCCHHHH	46.78	-
18	Phosphorylation	SVNSKRRSRADLTAE CHHHHCCCHHHHHHH	35.53	25177544
23	Phosphorylation	RRSRADLTAEMISAP CCCHHHHHHHHHHCC	22.56	25177544
28	Phosphorylation	DLTAEMISAPLGDFR HHHHHHHHCCCCCCC	23.64	25159016
37	Phosphorylation	PLGDFRHTMHVGRAG CCCCCCCCEECCCCC	12.52	25159016
51	Phosphorylation	GDAFGDTSFLTSKAR CCCCCCHHHHCHHHH	24.01	29514104
56	Ubiquitination	DTSFLTSKAREADDE CHHHHCHHHHHCCCC	46.34	-
64	Phosphorylation	AREADDESLDEQASA HHHCCCCCHHHHHHH	48.38	25521595
70	Phosphorylation	ESLDEQASASKLSLL CCHHHHHHHHHHHHH	32.54	25619855
72	Phosphorylation	LDEQASASKLSLLSR HHHHHHHHHHHHHHH	31.47	25619855
75	Phosphorylation	QASASKLSLLSRKFR HHHHHHHHHHHHHHC	30.88	27841257
78	Phosphorylation	ASKLSLLSRKFRGSK HHHHHHHHHHHCCCC	38.42	29899451
87	Phosphorylation	KFRGSKRSQSVTRGD HHCCCCCCCCCCCCC	30.46	22324799
89	Phosphorylation	RGSKRSQSVTRGDRE CCCCCCCCCCCCCHH	27.05	19367708
91	Phosphorylation	SKRSQSVTRGDREQR CCCCCCCCCCCHHHH	33.89	22324799
103	Phosphorylation	EQRDMLGSLRDSALF HHHHHHHHHHHHHHH	19.10	26824392
107	Phosphorylation	MLGSLRDSALFVKNA HHHHHHHHHHHHHCC	22.04	25521595
112	Ubiquitination	RDSALFVKNAMSLPQ HHHHHHHHCCCCCCC	31.49	-
116	Phosphorylation	LFVKNAMSLPQLNEK HHHHCCCCCCCCCHH	34.19	25521595
123	Ubiquitination	SLPQLNEKEAAEKDS CCCCCCHHHHHHHHH	52.13	-
130	Phosphorylation	KEAAEKDSSKLPKSL HHHHHHHHHCCCHHH	40.20	25168779
136	Phosphorylation	DSSKLPKSLSSSPVK HHHCCCHHHCCCCCC	31.38	25521595
138	Phosphorylation	SKLPKSLSSSPVKKA HCCCHHHCCCCCCHH	35.54	25168779
139	Phosphorylation	KLPKSLSSSPVKKAD CCCHHHCCCCCCHHH	43.91	25521595
140	Phosphorylation	LPKSLSSSPVKKADA CCHHHCCCCCCHHHC	30.27	25521595
154	Phosphorylation	ARDGGPKSPHRNGAT CCCCCCCCCCCCCCC	29.13	19144319
161	Phosphorylation	SPHRNGATGPHSPDP CCCCCCCCCCCCCCC	53.28	26060331
165	Phosphorylation	NGATGPHSPDPLLDE CCCCCCCCCCCCCCC	33.85	23984901
196	Phosphorylation	YGLKHAESILSFHID CCCCCHHHHHHHEEE	29.61	24719451
199	Phosphorylation	KHAESILSFHIDLGP CCHHHHHHHEEECCH	17.07	24719451
214	Phosphorylation	SMLGDVLSIMDKDQW HHHHHHHHHHCHHHC	18.73	24719451
223	Phosphorylation	MDKDQWGSEEEEEAG HCHHHCCCHHHHHHC	38.59	25521595
239	Phosphorylation	YRDKEGPSSIVQAPP CCCCCCCCCCCCCCC	43.48	30352176
240	Phosphorylation	RDKEGPSSIVQAPPV CCCCCCCCCCCCCCE	29.88	30352176
259	Phosphorylation	PPLGRQESKASWDQA CCCCCCCCCCCCHHH	25.78	22324799
285	Phosphorylation	GWAVVAPSPSSARSV CEEEECCCCCCCCCC	27.90	27180971
288	Phosphorylation	VVAPSPSSARSVGSH EECCCCCCCCCCCCC	30.96	20531401
291	Phosphorylation	PSPSSARSVGSHTTR CCCCCCCCCCCCCCC	30.46	25293948
294	Phosphorylation	SSARSVGSHTTRDSS CCCCCCCCCCCCCCC	18.59	25293948
296	Phosphorylation	ARSVGSHTTRDSSSL CCCCCCCCCCCCCHH	25.81	25293948
297	Phosphorylation	RSVGSHTTRDSSSLS CCCCCCCCCCCCHHH	27.36	25293948
300	Phosphorylation	GSHTTRDSSSLSSYT CCCCCCCCCHHHHHH	20.66	26643407
301	Phosphorylation	SHTTRDSSSLSSYTS CCCCCCCCHHHHHHC	39.32	26643407
302	Phosphorylation	HTTRDSSSLSSYTSG CCCCCCCHHHHHHCC	35.90	25521595
304	Phosphorylation	TRDSSSLSSYTSGVL CCCCCHHHHHHCCCC	24.21	29472430
305	Phosphorylation	RDSSSLSSYTSGVLE CCCCHHHHHHCCCCC	37.41	25521595
306	Phosphorylation	DSSSLSSYTSGVLEE CCCHHHHHHCCCCCC	11.10	29514104
307	Phosphorylation	SSSLSSYTSGVLEER CCHHHHHHCCCCCCC	22.43	29472430
308	Phosphorylation	SSLSSYTSGVLEERS CHHHHHHCCCCCCCC	20.76	25293948
315	Phosphorylation	SGVLEERSPAFRGPD CCCCCCCCCCCCCCC	24.70	29899451

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
Oops, there are no upstream regulatory protein records of BORG4_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BORG4_MOUSE !!

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 BORG4_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of BORG4_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of BORG4_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-139 AND SER-154, ANDMASS SPECTROMETRY.	19144319 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-107 AND SER-223,AND MASS SPECTROMETRY.	19367708 [Abstract]
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, AND MASSSPECTROMETRY.	17114649 [Abstract]
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND SER-223, AND MASSSPECTROMETRY.	17203969 [Abstract]