dbPTM

BORG4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BORG4_HUMAN
UniProt AC	Q9H3Q1
Protein Name	Cdc42 effector protein 4
Gene Name	CDC42EP4
Organism	Homo sapiens (Human).
Sequence Length	356
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	MPILKQLVSSSVHSKRRSRADLTAEMISAPLGDFRHTMHVGRAGDAFGDTSFLNSKAGEPDGESLDEQPSSSSSKRSLLSRKFRGSKRSQSVTRGEREQRDMLGSLRDSALFVKNAMSLPQLNEKEAAEKGTSKLPKSLSSSPVKKANDGEGGDEEAGTEEAVPRRNGAAGPHSPDPLLDEQAFGDLTDLPVVPKATYGLKHAESIMSFHIDLGPSMLGDVLSIMDKEEWDPEEGEGGYHGDEGAAGTITQAPPYAVAAPPLARQEGKAGPDLPSLPSHALEDEGWAAAAPSPGSARSMGSHTTRDSSSLSSCTSGILEERSPAFRGPDRARAAVSRQPDKEFSFMDEEEEDEIRV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Methylation	---MPILKQLVSSSV ---CCHHHHHHHCCH	42.16	24129315
5	Ubiquitination	---MPILKQLVSSSV ---CCHHHHHHHCCH	42.16	-
9	Phosphorylation	PILKQLVSSSVHSKR CHHHHHHHCCHHHCC	26.03	30266825
10	Phosphorylation	ILKQLVSSSVHSKRR HHHHHHHCCHHHCCC	28.97	30266825
11	Phosphorylation	LKQLVSSSVHSKRRS HHHHHHCCHHHCCCC	19.15	23401153
14	Phosphorylation	LVSSSVHSKRRSRAD HHHCCHHHCCCCHHH	26.21	30266825
15	Ubiquitination	VSSSVHSKRRSRADL HHCCHHHCCCCHHHH	36.63	-
18	Phosphorylation	SVHSKRRSRADLTAE CHHHCCCCHHHHHHH	35.53	30266825
23	Phosphorylation	RRSRADLTAEMISAP CCCHHHHHHHHHHCC	22.56	30266825
28	Phosphorylation	DLTAEMISAPLGDFR HHHHHHHHCCCCCCC	23.64	23927012
42	Methylation	RHTMHVGRAGDAFGD CCCEECCCCCCCCCC	34.02	-
50	Phosphorylation	AGDAFGDTSFLNSKA CCCCCCCCHHHCCCC	23.04	29396449
51	Phosphorylation	GDAFGDTSFLNSKAG CCCCCCCHHHCCCCC	32.26	21815630
56	Ubiquitination	DTSFLNSKAGEPDGE CCHHHCCCCCCCCCC	60.38	-
64	Phosphorylation	AGEPDGESLDEQPSS CCCCCCCCCCCCCCC	46.80	19664994
68 (in isoform 2)	Phosphorylation	-	42.73	29743597
70	Phosphorylation	ESLDEQPSSSSSKRS CCCCCCCCCCHHHHH	42.41	22167270
71	Phosphorylation	SLDEQPSSSSSKRSL CCCCCCCCCHHHHHH	40.71	22167270
72	Phosphorylation	LDEQPSSSSSKRSLL CCCCCCCCHHHHHHH	42.86	22167270
73	Phosphorylation	DEQPSSSSSKRSLLS CCCCCCCHHHHHHHH	41.65	22167270
74	Phosphorylation	EQPSSSSSKRSLLSR CCCCCCHHHHHHHHH	33.75	23927012
75	Ubiquitination	QPSSSSSKRSLLSRK CCCCCHHHHHHHHHH	48.21	21906983
76	Ubiquitination	PSSSSSKRSLLSRKF CCCCHHHHHHHHHHH	34.19	-
77	Phosphorylation	SSSSSKRSLLSRKFR CCCHHHHHHHHHHHC	37.08	29496963
80	Phosphorylation	SSKRSLLSRKFRGSK HHHHHHHHHHHCCCH	38.42	25137130
86	O-linked_Glycosylation	LSRKFRGSKRSQSVT HHHHHCCCHHHCCCC	22.19	30379171
89	Phosphorylation	KFRGSKRSQSVTRGE HHCCCHHHCCCCCHH	30.46	22617229
91	Phosphorylation	RGSKRSQSVTRGERE CCCHHHCCCCCHHHH	27.05	26329039
93	Phosphorylation	SKRSQSVTRGEREQR CHHHCCCCCHHHHHH	37.90	26434776
105	Phosphorylation	EQRDMLGSLRDSALF HHHHHHHHHHHHHHH	19.10	25463755
109	Phosphorylation	MLGSLRDSALFVKNA HHHHHHHHHHHHHCC	22.04	29255136
114	Ubiquitination	RDSALFVKNAMSLPQ HHHHHHHHCCCCCCC	31.49	21906983
118	Phosphorylation	LFVKNAMSLPQLNEK HHHHCCCCCCCCCHH	34.19	19664994
125	Ubiquitination	SLPQLNEKEAAEKGT CCCCCCHHHHHHHCC	52.13	21906983
138	Phosphorylation	GTSKLPKSLSSSPVK CCCCCCHHHCCCCCE	31.38	23927012
140	Phosphorylation	SKLPKSLSSSPVKKA CCCCHHHCCCCCEEC	35.54	22167270
141	Phosphorylation	KLPKSLSSSPVKKAN CCCHHHCCCCCEECC	43.91	30266825
142	Phosphorylation	LPKSLSSSPVKKAND CCHHHCCCCCEECCC	30.27	22167270
146	Ubiquitination	LSSSPVKKANDGEGG HCCCCCEECCCCCCC	53.29	21906983
159	Phosphorylation	GGDEEAGTEEAVPRR CCCCCCCCCCCCCCC	37.39	23312004
174	Phosphorylation	NGAAGPHSPDPLLDE CCCCCCCCCCCCCCC	33.85	25159151
188	Phosphorylation	EQAFGDLTDLPVVPK CHHCCCCCCCCCCCC	39.98	23927012
255	Phosphorylation	TITQAPPYAVAAPPL CCCCCCCCEEECCCH	16.79	22817900
275	Phosphorylation	KAGPDLPSLPSHALE CCCCCCCCCCHHHHC	61.28	23927012
278	Phosphorylation	PDLPSLPSHALEDEG CCCCCCCHHHHCCCC	27.04	23927012
292	Phosphorylation	GWAAAAPSPGSARSM CCCCCCCCCCCCCCC	36.85	22167270
295	Phosphorylation	AAAPSPGSARSMGSH CCCCCCCCCCCCCCC	24.72	22167270
298	Phosphorylation	PSPGSARSMGSHTTR CCCCCCCCCCCCCCC	27.49	20363803
301	Phosphorylation	GSARSMGSHTTRDSS CCCCCCCCCCCCCCC	14.71	20363803
303	Phosphorylation	ARSMGSHTTRDSSSL CCCCCCCCCCCCCHH	25.81	28857561
304	Phosphorylation	RSMGSHTTRDSSSLS CCCCCCCCCCCCHHC	27.36	23403867
307	Phosphorylation	GSHTTRDSSSLSSCT CCCCCCCCCHHCCCC	20.66	29507054
308	Phosphorylation	SHTTRDSSSLSSCTS CCCCCCCCHHCCCCC	39.32	30266825
309	Phosphorylation	HTTRDSSSLSSCTSG CCCCCCCHHCCCCCH	35.90	26657352
311	Phosphorylation	TRDSSSLSSCTSGIL CCCCCHHCCCCCHHH	25.89	30266825
312	Phosphorylation	RDSSSLSSCTSGILE CCCCHHCCCCCHHHH	27.06	29978859
314	Phosphorylation	SSSLSSCTSGILEER CCHHCCCCCHHHHCC	31.75	29978859
315	Phosphorylation	SSLSSCTSGILEERS CHHCCCCCHHHHCCC	28.32	29978859
322	Phosphorylation	SGILEERSPAFRGPD CHHHHCCCHHHCCCH	24.70	30266825
344	Phosphorylation	RQPDKEFSFMDEEEE CCCCCCCCCCCHHHH	22.28	22617229

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
18	S	Phosphorylation	Kinase	PKCA	P17252	PSP
80	S	Phosphorylation	Kinase	PKCA	P17252	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BORG4_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 BORG4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
FAM9B_HUMAN	FAM9B	physical	25416956
SEPT4_HUMAN	SEPT4	physical	26186194
SEPT2_HUMAN	SEPT2	physical	26186194
SEPT7_HUMAN	SEPT7	physical	26186194
SEPT5_HUMAN	SEPT5	physical	26186194
SEPT6_HUMAN	SEPT6	physical	26186194
SEPT8_HUMAN	SEPT8	physical	26186194
SEP11_HUMAN	SEPT11	physical	26186194
SEPT9_HUMAN	SEPT9	physical	26186194
SEPT3_HUMAN	SEPT3	physical	26186194
KLH15_HUMAN	KLHL15	physical	26186194
SEP10_HUMAN	SEPT10	physical	26186194
YBEY_HUMAN	YBEY	physical	26186194
FHL2_HUMAN	FHL2	physical	26186194
SEP10_HUMAN	SEPT10	physical	28514442
SEPT3_HUMAN	SEPT3	physical	28514442
SEPT8_HUMAN	SEPT8	physical	28514442
SEPT5_HUMAN	SEPT5	physical	28514442
SEPT2_HUMAN	SEPT2	physical	28514442
SEPT6_HUMAN	SEPT6	physical	28514442
SEPT7_HUMAN	SEPT7	physical	28514442
SEP11_HUMAN	SEPT11	physical	28514442
SEPT9_HUMAN	SEPT9	physical	28514442
SEPT4_HUMAN	SEPT4	physical	28514442
SEP14_HUMAN	SEPT14	physical	28514442
FHL2_HUMAN	FHL2	physical	28514442
KLH15_HUMAN	KLHL15	physical	28514442

Drug and Disease Associations

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

Regulatory Network of BORG4_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND MASSSPECTROMETRY.	19413330 [Abstract]
"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 SER-64; SER-138; SER-142;SER-174; SER-292 AND SER-295, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292 AND SER-295, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"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-292 AND SER-295, ANDMASS SPECTROMETRY.	18220336 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174; SER-292 ANDSER-295, AND MASS SPECTROMETRY.	17081983 [Abstract]