EXOC8_HUMAN - dbPTM
EXOC8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EXOC8_HUMAN
UniProt AC Q8IYI6
Protein Name Exocyst complex component 8
Gene Name EXOC8
Organism Homo sapiens (Human).
Sequence Length 725
Subcellular Localization Cytoplasm . Cytoplasm, perinuclear region . Cell projection, growth cone . Cell projection . Perinuclear in undifferentiated PC12 cells. Redistributes to growing neurites and growth cones during neuronal differentiation (By similarity). Binds lipids
Protein Description Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane..
Protein Sequence MAMAMSDSGASRLRRQLESGGFEARLYVKQLSQQSDGDRDLQEHRQRIQALAEETAQNLKRNVYQNYRQFIETAREISYLESEMYQLSHLLTEQKSSLESIPLTLLPAAAAAGAAAASGGEEGVGGAGGRDHLRGQAGFFSTPGGASRDGSGPGEEGKQRTLTTLLEKVEGCRHLLETPGQYLVYNGDLVEYDADHMAQLQRVHGFLMNDCLLVATWLPQRRGMYRYNALYSLDGLAVVNVKDNPPMKDMFKLLMFPESRIFQAENAKIKREWLEVLEDTKRALSEKRRREQEEAAAPRGPPQVTSKATNPFEDDEEEEPAVPEVEEEKVDLSMEWIQELPEDLDVCIAQRDFEGAVDLLDKLNHYLEDKPSPPPVKELRAKVEERVRQLTEVLVFELSPDRSLRGGPKATRRAVSQLIRLGQCTKACELFLRNRAAAVHTAIRQLRIEGATLLYIHKLCHVFFTSLLETAREFEIDFAGTDSGCYSAFVVWARSAMGMFVDAFSKQVFDSKESLSTAAECVKVAKEHCQQLGDIGLDLTFIIHALLVKDIQGALHSYKEIIIEATKHRNSEEMWRRMNLMTPEALGKLKEEMKSCGVSNFEQYTGDDCWVNLSYTVVAFTKQTMGFLEEALKLYFPELHMVLLESLVEIILVAVQHVDYSLRCEQDPEKKAFIRQNASFLYETVLPVVEKRFEEGVGKPAKQLQDLRNASRLIRVNPESTTSVV
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
6Phosphorylation--MAMAMSDSGASRL
--CCCCCCCHHHHHH		21.0623401153
8PhosphorylationMAMAMSDSGASRLRR
CCCCCCCHHHHHHHH		29.0223401153
11PhosphorylationAMSDSGASRLRRQLE
CCCCHHHHHHHHHHH		35.0628857561
19PhosphorylationRLRRQLESGGFEARL
HHHHHHHHCCEEEEE		53.4630266825
29UbiquitinationFEARLYVKQLSQQSD
EEEEEHHHHHHHCCC		31.7822817900
32PhosphorylationRLYVKQLSQQSDGDR
EEHHHHHHHCCCCCH		24.5524275569
35PhosphorylationVKQLSQQSDGDRDLQ
HHHHHHCCCCCHHHH		35.6023312004
60MethylationEETAQNLKRNVYQNY
HHHHHHHHHHHHHHH		49.85-
60UbiquitinationEETAQNLKRNVYQNY
HHHHHHHHHHHHHHH		49.8521906983
64PhosphorylationQNLKRNVYQNYRQFI
HHHHHHHHHHHHHHH		8.4527642862
67PhosphorylationKRNVYQNYRQFIETA
HHHHHHHHHHHHHHH		7.1128348404
73PhosphorylationNYRQFIETAREISYL
HHHHHHHHHHHHHHH		26.6327251275
78PhosphorylationIETAREISYLESEMY
HHHHHHHHHHHHHHH		20.9327251275
79PhosphorylationETAREISYLESEMYQ
HHHHHHHHHHHHHHH		21.8327251275
82PhosphorylationREISYLESEMYQLSH
HHHHHHHHHHHHHHH		25.6827251275
118PhosphorylationAAGAAAASGGEEGVG
HHHHHHHHCCCCCCC		42.4728348404
141PhosphorylationRGQAGFFSTPGGASR
CCCCCCCCCCCCCCC		31.2822199227
142PhosphorylationGQAGFFSTPGGASRD
CCCCCCCCCCCCCCC		22.3125159151
147PhosphorylationFSTPGGASRDGSGPG
CCCCCCCCCCCCCCC		33.8929978859
151PhosphorylationGGASRDGSGPGEEGK
CCCCCCCCCCCHHHC		46.2122985185
161PhosphorylationGEEGKQRTLTTLLEK
CHHHCHHCHHHHHHH		26.4330622161
163PhosphorylationEGKQRTLTTLLEKVE
HHCHHCHHHHHHHCC		18.1328122231
164PhosphorylationGKQRTLTTLLEKVEG
HCHHCHHHHHHHCCC		32.2427067055
168UbiquitinationTLTTLLEKVEGCRHL
CHHHHHHHCCCCHHH		45.62-
227PhosphorylationQRRGMYRYNALYSLD
CCCCCCCCCCEEECC		6.3132142685
231PhosphorylationMYRYNALYSLDGLAV
CCCCCCEEECCCEEE		12.5532142685
232PhosphorylationYRYNALYSLDGLAVV
CCCCCEEECCCEEEE		22.3428122231
248UbiquitinationVKDNPPMKDMFKLLM
CCCCCCHHHHHHHHH		52.3829967540
268UbiquitinationIFQAENAKIKREWLE
HCCCHHHHHCHHHHH		61.4124816145
270UbiquitinationQAENAKIKREWLEVL
CCHHHHHCHHHHHHH		43.49-
280PhosphorylationWLEVLEDTKRALSEK
HHHHHHHHHHHHHHH		17.0420860994
281UbiquitinationLEVLEDTKRALSEKR
HHHHHHHHHHHHHHH		48.2529967540
305PhosphorylationPRGPPQVTSKATNPF
CCCCCCCCCCCCCCC		21.1827251275
306PhosphorylationRGPPQVTSKATNPFE
CCCCCCCCCCCCCCC		22.8027251275
307UbiquitinationGPPQVTSKATNPFED
CCCCCCCCCCCCCCC		50.2729967540
309PhosphorylationPQVTSKATNPFEDDE
CCCCCCCCCCCCCCC		47.3527251275
329SumoylationVPEVEEEKVDLSMEW
CCCCHHHHCCCCHHH		44.31-
362UbiquitinationGAVDLLDKLNHYLED
HHHHHHHHHHHHHCC		51.6729967540
370UbiquitinationLNHYLEDKPSPPPVK
HHHHHCCCCCCCCHH		37.7129967540
372PhosphorylationHYLEDKPSPPPVKEL
HHHCCCCCCCCHHHH		56.6428985074
377UbiquitinationKPSPPPVKELRAKVE
CCCCCCHHHHHHHHH		57.7329967540
399PhosphorylationEVLVFELSPDRSLRG
HHEEEECCCCCCCCC		19.9824719451
416PhosphorylationKATRRAVSQLIRLGQ
HHHHHHHHHHHHHCH		20.4818452278
426UbiquitinationIRLGQCTKACELFLR
HHHCHHHHHHHHHHH		59.68-
441PhosphorylationNRAAAVHTAIRQLRI
CHHHHHHHHHHHHHH		19.7223403867
455PhosphorylationIEGATLLYIHKLCHV
HCHHHHHHHHHHHHH		12.23-
481PhosphorylationFEIDFAGTDSGCYSA
HCCCEECCCCCCHHH		24.4622210691
483PhosphorylationIDFAGTDSGCYSAFV
CCEECCCCCCHHHHH		30.5122210691
511PhosphorylationFSKQVFDSKESLSTA
HHHHHHCCHHHHHHH		27.19-
512UbiquitinationSKQVFDSKESLSTAA
HHHHHCCHHHHHHHH		53.8429967540
514PhosphorylationQVFDSKESLSTAAEC
HHHCCHHHHHHHHHH		31.21-
516PhosphorylationFDSKESLSTAAECVK
HCCHHHHHHHHHHHH		25.86-
517PhosphorylationDSKESLSTAAECVKV
CCHHHHHHHHHHHHH		34.87-
523UbiquitinationSTAAECVKVAKEHCQ
HHHHHHHHHHHHHHH		48.4033845483
567UbiquitinationEIIIEATKHRNSEEM
HHHHHHHCCCCHHHH		47.8429967540
661PhosphorylationAVQHVDYSLRCEQDP
HHHHCCHHHCCCCCH		12.6024719451
679PhosphorylationAFIRQNASFLYETVL
HHHHHCHHHHHHHHH		24.2728348404
699UbiquitinationRFEEGVGKPAKQLQD
HHHCCCCCCHHHHHH		39.1229967540
702UbiquitinationEGVGKPAKQLQDLRN
CCCCCCHHHHHHHHH		61.1324816145
711PhosphorylationLQDLRNASRLIRVNP
HHHHHHCHHCEECCC		31.0430631047
720PhosphorylationLIRVNPESTTSVV--
CEECCCCCCCCCC--		37.9430631047
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 EXOC8_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EXOC8_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 EXOC8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RALA_HUMANRALAphysical
14525976
EXOC2_HUMANEXOC2physical
14525976
RALB_HUMANRALBphysical
14525976
TLN2_HUMANTLN2physical
22939629
EFHC2_HUMANEFHC2physical
19060904
R3GEF_HUMANRAB3IL1physical
19060904
MBIP1_HUMANMBIPphysical
19060904
RUBIC_HUMANKIAA0226physical
21241894
BAKOR_HUMANATG14physical
21241894
BECN1_HUMANBECN1physical
21241894
RALB_HUMANRALBphysical
21241894
EXOC4_HUMANEXOC4physical
21241894
PK3C3_HUMANPIK3C3physical
21241894
ULK1_HUMANULK1physical
21241894
CE57L_HUMANCEP57L1physical
25416956
EXOC4_HUMANEXOC4physical
26344197
EXOC6_HUMANEXOC6physical
28514442
EXC6B_HUMANEXOC6Bphysical
28514442
3BP1_HUMANSH3BP1physical
28514442
EXOC7_HUMANEXOC7physical
28514442
EXOC3_HUMANEXOC3physical
28514442
EXOC5_HUMANEXOC5physical
28514442
RALB_HUMANRALBphysical
28514442
EXOC1_HUMANEXOC1physical
28514442
LRC41_HUMANLRRC41physical
28514442
EXOC2_HUMANEXOC2physical
28514442
EHD4_HUMANEHD4physical
28514442
LIPA1_HUMANPPFIA1physical
28514442
S27A2_HUMANSLC27A2physical
28514442
SEC20_HUMANBNIP1physical
28514442
EHD1_HUMANEHD1physical
28514442
OCAD1_HUMANOCIAD1physical
28514442
EXOC4_HUMANEXOC4physical
28514442
RAB8A_HUMANRAB8Aphysical
27173435
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 EXOC8_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-19, AND MASSSPECTROMETRY.
"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-142, AND MASSSPECTROMETRY.

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