EXOC3_HUMAN - dbPTM
EXOC3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EXOC3_HUMAN
UniProt AC O60645
Protein Name Exocyst complex component 3
Gene Name EXOC3
Organism Homo sapiens (Human).
Sequence Length 756
Subcellular Localization Cytoplasm . Cytoplasm, perinuclear region . Cell projection, growth cone . Midbody . Golgi apparatus . Perinuclear in undifferentiated cells. Redistributes to growing neurites and growth cones during neuronal differentiation (By similarity). During m
Protein Description Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane..
Protein Sequence MQCEDSTSFFTMKETDREAVATAVQRVAGMLQRPDQLDKVEQYRRREARKKASVEARLKAAIQSQLDGVRTGLSQLHNALNDVKDIQQSLADVSKDWRQSINTIESLKDVKDAVVQHSQLAAAVENLKNIFSVPEIVRETQDLIEQGALLQAHRKLMDLECSRDGLMYEQYRMDSGNTRDMTLIHGYFGSTQGLSDELAKQLWMVLQRSLVTVRRDPTLLVSVVRIIEREEKIDRRILDRKKQTGFVPPGRPKNWKEKMFTILERTVTTRIEGTQADTRESDKMWLVRHLEIIRKYVLDDLIVAKNLMVQCFPPHYEIFKNLLNMYHQALSTRMQDLASEDLEANEIVSLLTWVLNTYTSTEMMRNVELAPEVDVGTLEPLLSPHVVSELLDTYMSTLTSNIIAWLRKALETDKKDWVKETEPEADQDGYYQTTLPAIVFQMFEQNLQVAAQISEDLKTKVLVLCLQQMNSFLSRYKDEAQLYKEEHLRNRQHPHCYVQYMIAIINNCQTFKESIVSLKRKYLKNEVEEGVSPSQPSMDGILDAIAKEGCSGLLEEVFLDLEQHLNELMTKKWLLGSNAVDIICVTVEDYFNDFAKIKKPYKKRMTAEAHRRVVVEYLRAVMQKRISFRSPEERKEGAEKMVREAEQLRFLFRKLASGFGEDVDGYCDTIVAVAEVIKLTDPSLLYLEVSTLVSKYPDIRDDHIGALLAVRGDASRDMKQTIMETLEQGPAQASPSYVPLFKDIVVPSLNVAKLLK
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
28AcetylationATAVQRVAGMLQRPD
HHHHHHHHHHHCCHH		10.4019608861
28UbiquitinationATAVQRVAGMLQRPD
HHHHHHHHHHHCCHH		10.4019608861
39AcetylationQRPDQLDKVEQYRRR
CCHHHHHHHHHHHHH		57.1519608861
48MethylationEQYRRREARKKASVE
HHHHHHHHHHHCCHH		27.12-
48UbiquitinationEQYRRREARKKASVE
HHHHHHHHHHHCCHH		27.12-
59MalonylationASVEARLKAAIQSQL
CCHHHHHHHHHHHHH		30.1626320211
59MethylationASVEARLKAAIQSQL
CCHHHHHHHHHHHHH		30.16115977651
73UbiquitinationLDGVRTGLSQLHNAL
HHHHHHHHHHHHHHH		2.66-
84UbiquitinationHNALNDVKDIQQSLA
HHHHHHHHHHHHHHH		52.56-
89PhosphorylationDVKDIQQSLADVSKD
HHHHHHHHHHHHCHH		14.7821406692
94PhosphorylationQQSLADVSKDWRQSI
HHHHHHHCHHHHHHH		25.9921406692
97UbiquitinationLADVSKDWRQSINTI
HHHHCHHHHHHHHHH		12.16-
100UbiquitinationVSKDWRQSINTIESL
HCHHHHHHHHHHHHH		14.83-
106PhosphorylationQSINTIESLKDVKDA
HHHHHHHHHHCHHHH		36.5520860994
128UbiquitinationAAAVENLKNIFSVPE
HHHHHHHHHHCCHHH		60.63-
132PhosphorylationENLKNIFSVPEIVRE
HHHHHHCCHHHHHHH		32.72-
144UbiquitinationVRETQDLIEQGALLQ
HHHHHHHHHHHHHHH		5.10-
155UbiquitinationALLQAHRKLMDLECS
HHHHHHHHHHCCCCC		37.99-
182PhosphorylationSGNTRDMTLIHGYFG
CCCCCCCEEEEHHCC		27.1830175587
191PhosphorylationIHGYFGSTQGLSDEL
EEHHCCCCCCCCHHH		27.3430175587
195PhosphorylationFGSTQGLSDELAKQL
CCCCCCCCHHHHHHH		35.54-
201PhosphorylationLSDELAKQLWMVLQR
CCHHHHHHHHHHHHH		34.4519664995
209PhosphorylationLWMVLQRSLVTVRRD
HHHHHHHHHHHCCCC		17.77-
212PhosphorylationVLQRSLVTVRRDPTL
HHHHHHHHCCCCCHH		17.3719664995
218PhosphorylationVTVRRDPTLLVSVVR
HHCCCCCHHHEEHHH		36.6926074081
221AcetylationRRDPTLLVSVVRIIE
CCCCHHHEEHHHHHH		4.61-
222PhosphorylationRDPTLLVSVVRIIER
CCCHHHEEHHHHHHC		18.1826074081
231UbiquitinationVRIIEREEKIDRRIL
HHHHHCHHHHCHHHH		62.63-
232AcetylationRIIEREEKIDRRILD
HHHHCHHHHCHHHHH		45.1920167786
278PhosphorylationIEGTQADTRESDKMW
EECCCCCCCHHHHCH		39.07-
474PhosphorylationQQMNSFLSRYKDEAQ
HHHHHHHHHHHHHHH		31.3924719451
476PhosphorylationMNSFLSRYKDEAQLY
HHHHHHHHHHHHHHH		21.2926657352
477UbiquitinationNSFLSRYKDEAQLYK
HHHHHHHHHHHHHHH		48.24-
483PhosphorylationYKDEAQLYKEEHLRN
HHHHHHHHHHHHHHC		12.3126657352
508UbiquitinationMIAIINNCQTFKESI
HHHHHHCCHHHHHHH		3.31-
513UbiquitinationNNCQTFKESIVSLKR
HCCHHHHHHHHHHHH		41.32-
521PhosphorylationSIVSLKRKYLKNEVE
HHHHHHHHHHHHHHH		54.04-
532PhosphorylationNEVEEGVSPSQPSMD
HHHHCCCCCCCCCHH		29.6822199227
534PhosphorylationVEEGVSPSQPSMDGI
HHCCCCCCCCCHHHH		47.4122199227
537PhosphorylationGVSPSQPSMDGILDA
CCCCCCCCHHHHHHH		23.1322199227
606PhosphorylationKPYKKRMTAEAHRRV
CCCHHCCCHHHHHHH		25.9422210691
624UbiquitinationYLRAVMQKRISFRSP
HHHHHHHHCCCCCCH		33.34-
627PhosphorylationAVMQKRISFRSPEER
HHHHHCCCCCCHHHH		20.7423403867
630PhosphorylationQKRISFRSPEERKEG
HHCCCCCCHHHHHHH		34.3523403867
657PhosphorylationFLFRKLASGFGEDVD
HHHHHHHCCCCCCCC		45.1228122231
708UbiquitinationDDHIGALLAVRGDAS
CCCHHHHHHHCCCCC		4.03-
723PhosphorylationRDMKQTIMETLEQGP
HHHHHHHHHHHHHCC		3.5024719451
734PhosphorylationEQGPAQASPSYVPLF
HHCCCCCCCCCHHCC		11.4226657352
736PhosphorylationGPAQASPSYVPLFKD
CCCCCCCCCHHCCCC		35.9528857561
737PhosphorylationPAQASPSYVPLFKDI
CCCCCCCCHHCCCCC		14.9628102081
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 EXOC3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EXOC3_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 EXOC3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EXOC5_HUMANEXOC5physical
14525976
EXOC4_HUMANEXOC4physical
12738960
DLG3_HUMANDLG3physical
12738960
A4_HUMANAPPphysical
21832049
EXOC4_HUMANEXOC4physical
22939629
EXOC5_HUMANEXOC5physical
22939629
EXOC8_HUMANEXOC8physical
22939629
EXOC6_HUMANEXOC6physical
22939629
EXOC4_HUMANEXOC4physical
26344197
EXOC6_HUMANEXOC6physical
26344197
EXOC7_HUMANEXOC7physical
26344197
EXOC8_HUMANEXOC8physical
26344197
MAP11_HUMANMETAP1physical
26344197
TRM2A_HUMANTRMT2Aphysical
26344197
EXOC1_HUMANEXOC1physical
28514442
GCC2_HUMANGCC2physical
28514442
TRIPB_HUMANTRIP11physical
28514442
EXOC2_HUMANEXOC2physical
28514442
SCLT1_HUMANSCLT1physical
28514442
EXC6B_HUMANEXOC6Bphysical
28514442
KIZ_HUMANKIZphysical
28514442
EXOC4_HUMANEXOC4physical
28514442
EXOC5_HUMANEXOC5physical
28514442
KLC2_HUMANKLC2physical
28514442
EXOC7_HUMANEXOC7physical
28514442
IFT20_HUMANIFT20physical
28514442
KIF3A_HUMANKIF3Aphysical
28514442
CC136_HUMANCCDC136physical
28514442
PIBF1_HUMANPIBF1physical
28514442
PKD2_HUMANPKD2physical
28514442
KXDL1_HUMANKXD1physical
28514442
KLC1_HUMANKLC1physical
28514442
RGPD2_HUMANRGPD2physical
28514442
MACD1_HUMANMACROD1physical
28514442
RGPD5_HUMANRGPD5physical
28514442
EXOC1_HUMANEXOC1physical
27173435
EXOC4_HUMANEXOC4physical
27173435
EXOC5_HUMANEXOC5physical
27173435
TMED1_HUMANTMED1physical
27173435
EXOC6_HUMANEXOC6physical
27173435
EXOC7_HUMANEXOC7physical
27173435
EXOC8_HUMANEXOC8physical
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 EXOC3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-39, AND MASS SPECTROMETRY.

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