BORG5_HUMAN - dbPTM
BORG5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BORG5_HUMAN
UniProt AC Q00587
Protein Name Cdc42 effector protein 1
Gene Name CDC42EP1
Organism Homo sapiens (Human).
Sequence Length 391
Subcellular Localization Endomembrane system
Peripheral membrane protein . Cytoplasm, cytoskeleton .
Protein Description Probably involved in the organization of the actin cytoskeleton. Induced membrane extensions in fibroblasts..
Protein Sequence MPGPQGGRGAATMSLGKLSPVGWVSSSQGKRRLTADMISHPLGDFRHTMHVGRGGDVFGDTSFLSNHGGSSGSTHRSPRSFLAKKLQLVRRVGAPPRRMASPPAPSPAPPAISPIIKNAISLPQLNQAAYDSLVVGKLSFDSSPTSSTDGHSSYGLDSGFCTISRLPRSEKPHDRDRDGSFPSEPGLRRSDSLLSFRLDLDLGPSLLSELLGVMSLPEAPAAETPAPAANPPAPTANPTGPAANPPATTANPPAPAANPSAPAATPTGPAANPPAPAASSTPHGHCPNGVTAGLGPVAEVKSSPVGGGPRGPAGPALGRHWGAGWDGGHHYPEMDARQERVEVLPQARASWESLDEEWRAPQAGSRTPVPSTVQANTFEFADAEEDDEVKV
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
8MethylationMPGPQGGRGAATMSL
CCCCCCCCCCCEECC		38.10-
12PhosphorylationQGGRGAATMSLGKLS
CCCCCCCEECCCCCC		13.5220068231
14PhosphorylationGRGAATMSLGKLSPV
CCCCCEECCCCCCCC		29.6120068231
17MethylationAATMSLGKLSPVGWV
CCEECCCCCCCCCEE		51.60-
19PhosphorylationTMSLGKLSPVGWVSS
EECCCCCCCCCEECC		22.4825159151
25PhosphorylationLSPVGWVSSSQGKRR
CCCCCEECCCCCCCE		20.1220068231
26PhosphorylationSPVGWVSSSQGKRRL
CCCCEECCCCCCCEE		19.6425159151
27PhosphorylationPVGWVSSSQGKRRLT
CCCEECCCCCCCEEE		35.1325159151
30 (in isoform 2)Ubiquitination-27.0621890473
30 (in isoform 1)Ubiquitination-27.0621890473
30UbiquitinationWVSSSQGKRRLTADM
EECCCCCCCEEEHHH		27.0623000965
34PhosphorylationSQGKRRLTADMISHP
CCCCCEEEHHHHCCC		20.8523927012
39PhosphorylationRLTADMISHPLGDFR
EEEHHHHCCCCCCCC		16.6523927012
53MethylationRHTMHVGRGGDVFGD
CCEEECCCCCCCCCC		44.8524129315
61PhosphorylationGGDVFGDTSFLSNHG
CCCCCCCCHHHCCCC		23.0423927012
62PhosphorylationGDVFGDTSFLSNHGG
CCCCCCCHHHCCCCC		29.0020873877
65PhosphorylationFGDTSFLSNHGGSSG
CCCCHHHCCCCCCCC		25.4423927012
70PhosphorylationFLSNHGGSSGSTHRS
HHCCCCCCCCCCCCC		35.8023927012
71PhosphorylationLSNHGGSSGSTHRSP
HCCCCCCCCCCCCCH		39.7823927012
73PhosphorylationNHGGSSGSTHRSPRS
CCCCCCCCCCCCHHH		24.0023927012
74PhosphorylationHGGSSGSTHRSPRSF
CCCCCCCCCCCHHHH		25.4923927012
76MethylationGSSGSTHRSPRSFLA
CCCCCCCCCHHHHHH		48.74-
77PhosphorylationSSGSTHRSPRSFLAK
CCCCCCCCHHHHHHH		19.6323927012
79MethylationGSTHRSPRSFLAKKL
CCCCCCHHHHHHHHH		41.09-
80PhosphorylationSTHRSPRSFLAKKLQ
CCCCCHHHHHHHHHH		28.1722617229
98MethylationRVGAPPRRMASPPAP
HHCCCCCCCCCCCCC		30.69-
101PhosphorylationAPPRRMASPPAPSPA
CCCCCCCCCCCCCCC		23.2929255136
106PhosphorylationMASPPAPSPAPPAIS
CCCCCCCCCCCCCCH		35.4829255136
113PhosphorylationSPAPPAISPIIKNAI
CCCCCCCHHHHHHHC		16.5022167270
117UbiquitinationPAISPIIKNAISLPQ
CCCHHHHHHHCCCHH		40.83-
121PhosphorylationPIIKNAISLPQLNQA
HHHHHHCCCHHHCHH		31.4229255136
130PhosphorylationPQLNQAAYDSLVVGK
HHHCHHHHHHEEEEE		14.7421945579
132O-linked_GlycosylationLNQAAYDSLVVGKLS
HCHHHHHHEEEEEEE		15.4730379171
132PhosphorylationLNQAAYDSLVVGKLS
HCHHHHHHEEEEEEE		15.4721945579
139PhosphorylationSLVVGKLSFDSSPTS
HEEEEEEECCCCCCC		30.4123663014
142PhosphorylationVGKLSFDSSPTSSTD
EEEEECCCCCCCCCC		35.8925159151
143PhosphorylationGKLSFDSSPTSSTDG
EEEECCCCCCCCCCC		33.7625159151
145PhosphorylationLSFDSSPTSSTDGHS
EECCCCCCCCCCCCC		36.9422617229
146PhosphorylationSFDSSPTSSTDGHSS
ECCCCCCCCCCCCCC		34.3322617229
147PhosphorylationFDSSPTSSTDGHSSY
CCCCCCCCCCCCCCC		32.7530183078
148PhosphorylationDSSPTSSTDGHSSYG
CCCCCCCCCCCCCCC		45.8521712546
152PhosphorylationTSSTDGHSSYGLDSG
CCCCCCCCCCCCCCC		30.6823663014
153PhosphorylationSSTDGHSSYGLDSGF
CCCCCCCCCCCCCCC		19.9723663014
154PhosphorylationSTDGHSSYGLDSGFC
CCCCCCCCCCCCCCE		25.4020007894
158PhosphorylationHSSYGLDSGFCTISR
CCCCCCCCCCEEEEC		38.5223663014
162PhosphorylationGLDSGFCTISRLPRS
CCCCCCEEEECCCCC		21.5230576142
164PhosphorylationDSGFCTISRLPRSEK
CCCCEEEECCCCCCC		15.0423186163
180PhosphorylationHDRDRDGSFPSEPGL
CCCCCCCCCCCCCCC		37.9730266825
183PhosphorylationDRDGSFPSEPGLRRS
CCCCCCCCCCCCCCC		55.1826657352
190PhosphorylationSEPGLRRSDSLLSFR
CCCCCCCCCCCEEEE		25.7230266825
192PhosphorylationPGLRRSDSLLSFRLD
CCCCCCCCCEEEEEC		32.2419664994
195PhosphorylationRRSDSLLSFRLDLDL
CCCCCCEEEEECCCC		17.3919664994
302PhosphorylationGPVAEVKSSPVGGGP
CCCEEEECCCCCCCC		45.0830266825
303PhosphorylationPVAEVKSSPVGGGPR
CCEEEECCCCCCCCC		20.2130266825
310MethylationSPVGGGPRGPAGPAL
CCCCCCCCCCCCCCC		67.98-
331PhosphorylationGWDGGHHYPEMDARQ
CCCCCCCCCCCCHHH		8.6721945579
350PhosphorylationVLPQARASWESLDEE
HHHHHHHHHHHCCHH		26.3122167270
353PhosphorylationQARASWESLDEEWRA
HHHHHHHHCCHHHCC		34.5622167270
365PhosphorylationWRAPQAGSRTPVPST
HCCCCCCCCCCCCCC		35.6826657352
367PhosphorylationAPQAGSRTPVPSTVQ
CCCCCCCCCCCCCEE		30.2726657352
371PhosphorylationGSRTPVPSTVQANTF
CCCCCCCCCEECCEE		41.2529523821
372PhosphorylationSRTPVPSTVQANTFE
CCCCCCCCEECCEEE		15.5729523821
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 BORG5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BORG5_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 BORG5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KR412_HUMANKRTAP4-12physical
16189514
SIN1_HUMANMAPKAP1physical
16189514
MDFI_HUMANMDFIphysical
19060904
DEFI6_HUMANDEF6physical
25416956
RHOJ_HUMANRHOJphysical
25416956
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 BORG5_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND MASSSPECTROMETRY.
"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-19; SER-27; SER-101;SER-113; SER-143; THR-145 AND SER-192, AND MASS 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 SER-101; SER-106; SER-113;SER-121; SER-190; SER-192; SER-195; SER-350 AND SER-353, AND MASSSPECTROMETRY.
"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-19; SER-101; SER-113;SER-121; SER-190; SER-192 AND SER-350, AND MASS SPECTROMETRY.
"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-192, AND MASSSPECTROMETRY.
"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-192, AND MASSSPECTROMETRY.
"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-192; SER-350 ANDSER-353, AND MASS SPECTROMETRY.

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