EXOC5_HUMAN - dbPTM
EXOC5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EXOC5_HUMAN
UniProt AC O00471
Protein Name Exocyst complex component 5
Gene Name EXOC5
Organism Homo sapiens (Human).
Sequence Length 708
Subcellular Localization Cytoplasm . Midbody . Localization at the midbody requires the presence of RALA, EXOC2 and EXOC3.
Protein Description Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane..
Protein Sequence MATTAELFEEPFVADEYIERLVWRTPGGGSRGGPEAFDPKRLLEEFVNHIQELQIMDERIQRKVEKLEQQCQKEAKEFAKKVQELQKSNQVAFQHFQELDEHISYVATKVCHLGDQLEGVNTPRQRAVEAQKLMKYFNEFLDGELKSDVFTNSEKIKEAADIIQKLHLIAQELPFDRFSEVKSKIASKYHDLECQLIQEFTSAQRRGEISRMREVAAVLLHFKGYSHCVDVYIKQCQEGAYLRNDIFEDAGILCQRVNKQVGDIFSNPETVLAKLIQNVFEIKLQSFVKEQLEECRKSDAEQYLKNLYDLYTRTTNLSSKLMEFNLGTDKQTFLSKLIKSIFISYLENYIEVETGYLKSRSAMILQRYYDSKNHQKRSIGTGGIQDLKERIRQRTNLPLGPSIDTHGETFLSQEVVVNLLQETKQAFERCHRLSDPSDLPRNAFRIFTILVEFLCIEHIDYALETGLAGIPSSDSRNANLYFLDVVQQANTIFHLFDKQFNDHLMPLISSSPKLSECLQKKKEIIEQMEMKLDTGIDRTLNCMIGQMKHILAAEQKKTDFKPEDENNVLIQYTNACVKVCAYVRKQVEKIKNSMDGKNVDTVLMELGVRFHRLIYEHLQQYSYSCMGGMLAICDVAEYRKCAKDFKIPMVLHLFDTLHALCNLLVVAPDNLKQVCSGEQLANLDKNILHSFVQLRADYRSARLARHFS
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
2Acetylation------MATTAELFE
------CCCHHHHHC		17.4122814378
3Phosphorylation-----MATTAELFEE
-----CCCHHHHHCC		25.8218491316
4Phosphorylation----MATTAELFEEP
----CCCHHHHHCCC		14.4818491316
40UbiquitinationGPEAFDPKRLLEEFV
CCCCCCHHHHHHHHH		58.4824816145
63AcetylationMDERIQRKVEKLEQQ
HHHHHHHHHHHHHHH		38.0725953088
78UbiquitinationCQKEAKEFAKKVQEL
HHHHHHHHHHHHHHH		13.7224816145
87UbiquitinationKKVQELQKSNQVAFQ
HHHHHHHHHCCHHHH		65.0929967540
122PhosphorylationDQLEGVNTPRQRAVE
HHCCCCCCHHHHHHH		19.9025159151
132AcetylationQRAVEAQKLMKYFNE
HHHHHHHHHHHHHHH		58.5625953088
132UbiquitinationQRAVEAQKLMKYFNE
HHHHHHHHHHHHHHH		58.5629967540
135UbiquitinationVEAQKLMKYFNEFLD
HHHHHHHHHHHHHHC		58.0629967540
146UbiquitinationEFLDGELKSDVFTNS
HHHCCCCCCCCCCCH		40.0629967540
147PhosphorylationFLDGELKSDVFTNSE
HHCCCCCCCCCCCHH		52.19-
155UbiquitinationDVFTNSEKIKEAADI
CCCCCHHHHHHHHHH		59.9229967540
157UbiquitinationFTNSEKIKEAADIIQ
CCCHHHHHHHHHHHH		52.9829967540
165UbiquitinationEAADIIQKLHLIAQE
HHHHHHHHHHHHHHH		27.7129967540
177MethylationAQELPFDRFSEVKSK
HHHCCCCCHHHHHHH		37.05-
179PhosphorylationELPFDRFSEVKSKIA
HCCCCCHHHHHHHHH		42.2328122231
187PhosphorylationEVKSKIASKYHDLEC
HHHHHHHHHHHHHHH		36.9028122231
189PhosphorylationKSKIASKYHDLECQL
HHHHHHHHHHHHHHH		9.7027690223
194GlutathionylationSKYHDLECQLIQEFT
HHHHHHHHHHHHHHH		5.3322555962
210PhosphorylationAQRRGEISRMREVAA
HHHHCCHHHHHHHHH		18.74-
225PhosphorylationVLLHFKGYSHCVDVY
HHHHHCCCCCHHHHH		8.88-
259UbiquitinationILCQRVNKQVGDIFS
HHHHHHHHHHHHHHC		43.4329967540
266PhosphorylationKQVGDIFSNPETVLA
HHHHHHHCCHHHHHH		52.3823403867
270PhosphorylationDIFSNPETVLAKLIQ
HHHCCHHHHHHHHHH		23.2923403867
289UbiquitinationIKLQSFVKEQLEECR
HHHHHHHHHHHHHHH		37.4229967540
297UbiquitinationEQLEECRKSDAEQYL
HHHHHHHHCHHHHHH		65.4329967540
328PhosphorylationLMEFNLGTDKQTFLS
HHHCCCCCCHHHHHH		43.0921406692
332PhosphorylationNLGTDKQTFLSKLIK
CCCCCHHHHHHHHHH		32.08-
335PhosphorylationTDKQTFLSKLIKSIF
CCHHHHHHHHHHHHH		22.6430576142
378PhosphorylationSKNHQKRSIGTGGIQ
CCCCCCCCCCCCCHH		32.1928857561
388UbiquitinationTGGIQDLKERIRQRT
CCCHHHHHHHHHHHC		53.9233845483
388MalonylationTGGIQDLKERIRQRT
CCCHHHHHHHHHHHC		53.9226320211
395PhosphorylationKERIRQRTNLPLGPS
HHHHHHHCCCCCCCC		32.54-
405PhosphorylationPLGPSIDTHGETFLS
CCCCCCCCCCCCCCC		30.06-
412PhosphorylationTHGETFLSQEVVVNL
CCCCCCCCHHHHHHH		21.80-
426UbiquitinationLLQETKQAFERCHRL
HHHHHHHHHHHHHHC		15.1524816145
556UbiquitinationHILAAEQKKTDFKPE
HHHHHHHCCCCCCCC		49.5022505724
557UbiquitinationILAAEQKKTDFKPED
HHHHHHCCCCCCCCC		53.6829967540
561AcetylationEQKKTDFKPEDENNV
HHCCCCCCCCCCCCE		50.7519413330
593PhosphorylationQVEKIKNSMDGKNVD
HHHHHHHCCCCCCHH		17.1629978859
594UbiquitinationVEKIKNSMDGKNVDT
HHHHHHCCCCCCHHH		12.6122505724
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 EXOC5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EXOC5_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 EXOC5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARF6_HUMANARF6physical
14662749
EXOC8_HUMANEXOC8physical
22939629
EXOC7_HUMANEXOC7physical
22939629
SOX10_HUMANSOX10physical
21988832
ICA69_HUMANICA1physical
21988832
TBX21_HUMANTBX21physical
21988832
EXOC5_HUMANEXOC5physical
25416956
TXN4A_HUMANTXNL4Aphysical
25416956
SACA9_HUMANC9orf9physical
25416956
EDRF1_HUMANEDRF1physical
25416956
ASC_HUMANPYCARDphysical
25416956
TNPO2_HUMANTNPO2physical
25416956
RAB14_HUMANRAB14physical
25416956
RAB4B_HUMANRAB4Bphysical
25416956
KXDL1_HUMANKXD1physical
25416956
C102B_HUMANCCDC102Bphysical
25416956
BRM1L_HUMANBRMS1Lphysical
25416956
FRMD6_HUMANFRMD6physical
25416956
TT23L_HUMANTTC23Lphysical
25416956
DEUP1_HUMANCCDC67physical
25416956
TXLNB_HUMANTXLNBphysical
25416956
MESH1_HUMANHDDC3physical
25416956
EXOC4_HUMANEXOC4physical
23037926
SC61B_HUMANSEC61Bphysical
23037926
EXOC2_HUMANEXOC2physical
26344197
EXOC3_HUMANEXOC3physical
26344197
EXOC4_HUMANEXOC4physical
26344197
EXOC6_HUMANEXOC6physical
26344197
EXC6B_HUMANEXOC6Bphysical
26344197
EXOC7_HUMANEXOC7physical
26344197
EXOC8_HUMANEXOC8physical
26344197
EDRF1_HUMANEDRF1physical
21516116
TNPO2_HUMANTNPO2physical
21516116
EXOC8_HUMANEXOC8physical
27173435
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 EXOC5_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-122, AND MASSSPECTROMETRY.

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