EXOC6_HUMAN - dbPTM
EXOC6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EXOC6_HUMAN
UniProt AC Q8TAG9
Protein Name Exocyst complex component 6
Gene Name EXOC6
Organism Homo sapiens (Human).
Sequence Length 804
Subcellular Localization Cytoplasm . Cytoplasm, perinuclear region . Cell projection, growth cone . Midbody, Midbody ring . Perinuclear in undifferentiated cells. Redistributes to growing neurites and growth cones during neuronal differentiation. Colocalizes with CNTRL/centr
Protein Description Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. Together with RAB11A, RAB3IP, RAB8A, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis (By similarity)..
Protein Sequence MAENSESLGTVPEHERILQEIESTDTACVGPTLRSVYDDQPNAHKKFMEKLDACIRNHDKEIEKMCNFHHQGFVDAITELLKVRTDAEKLKVQVTDTNRRFQDAGKEVIVHTEDIIRCRIQQRNITTVVEKLQLCLPVLEMYSKLKEQMSAKRYYSALKTMEQLENVYFPWVSQYRFCQLMIENLPKLREDIKEISMSDLKDFLESIRKHSDKIGETAMKQAQHQKTFSVSLQKQNKMKFGKNMYINRDRIPEERNETVLKHSLEEEDENEEEILTVQDLVDFSPVYRCLHIYSVLGDEETFENYYRKQRKKQARLVLQPQSNMHETVDGYRRYFTQIVGFFVVEDHILHVTQGLVTRAYTDELWNMALSKIIAVLRAHSSYCTDPDLVLELKNLTVIFADTLQGYGFPVNRLFDLLFEIRDQYNETLLKKWAGVFRDIFEEDNYSPIPVVNEEEYKIVISKFPFQDPDLEKQSFPKKFPMSQSVPHIYIQVKEFIYASLKFSESLHRSSTEIDDMLRKSTNLLLTRTLSSCLLNLIRKPHIGLTELVQIIINTTHLEQACKYLEDFITNITNISQETVHTTRLYGLSTFKDARHAAEGEIYTKLNQKIDEFVQLADYDWTMSEPDGRASGYLMDLINFLRSIFQVFTHLPGKVAQTACMSACQHLSTSLMQMLLDSELKQISMGAVQQFNLDVIQCELFASSEPVPGFQGDTLQLAFIDLRQLLDLFMVWDWSTYLADYGQPASKYLRVNPNTALTLLEKMKDTSKKNNIFAQFRKNDRDKQKLIETVVKQLRSLVNGMSQHM
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
5Phosphorylation---MAENSESLGTVP
---CCCCCCCCCCCC		21.7730108239
7Phosphorylation-MAENSESLGTVPEH
-CCCCCCCCCCCCHH		31.7427251275
10PhosphorylationENSESLGTVPEHERI
CCCCCCCCCCHHHHH		37.8727251275
35PhosphorylationCVGPTLRSVYDDQPN
CCCHHHHHHHCCCCC		28.3028122231
91UbiquitinationRTDAEKLKVQVTDTN
CCCHHHCCEEEECCC		41.51-
106UbiquitinationRRFQDAGKEVIVHTE
HHHHHCCCEEEEEHH		50.99-
143PhosphorylationLPVLEMYSKLKEQMS
HHHHHHHHHHHHHHC		30.1524719451
155PhosphorylationQMSAKRYYSALKTME
HHCHHHHHHHHHHHH		7.47-
156PhosphorylationMSAKRYYSALKTMEQ
HCHHHHHHHHHHHHH		20.4224719451
175PhosphorylationYFPWVSQYRFCQLMI
CCHHHHHHHHHHHHH		9.73-
193UbiquitinationPKLREDIKEISMSDL
HHHHHHHHHCCHHHH		62.41-
196PhosphorylationREDIKEISMSDLKDF
HHHHHHCCHHHHHHH		17.2127251275
198PhosphorylationDIKEISMSDLKDFLE
HHHHCCHHHHHHHHH		32.7627251275
201UbiquitinationEISMSDLKDFLESIR
HCCHHHHHHHHHHHH		51.96-
213UbiquitinationSIRKHSDKIGETAMK
HHHHHHHHHHHHHHH		56.47-
220MethylationKIGETAMKQAQHQKT
HHHHHHHHHHHHHCC		39.76-
226UbiquitinationMKQAQHQKTFSVSLQ
HHHHHHHCCEEEEEH		49.79-
231PhosphorylationHQKTFSVSLQKQNKM
HHCCEEEEEHHHHCC		24.7228857561
234UbiquitinationTFSVSLQKQNKMKFG
CEEEEEHHHHCCCCC		62.22-
242UbiquitinationQNKMKFGKNMYINRD
HHCCCCCCCCEECCC		41.49-
301PhosphorylationSVLGDEETFENYYRK
HHHCCHHHHHHHHHH		33.91-
445PhosphorylationDIFEEDNYSPIPVVN
HHHCCCCCCCCCCCC		28.3126657352
446PhosphorylationIFEEDNYSPIPVVNE
HHCCCCCCCCCCCCH		23.7026852163
462UbiquitinationEYKIVISKFPFQDPD
HEEEEEEECCCCCCC		46.0321890473
472UbiquitinationFQDPDLEKQSFPKKF
CCCCCHHCCCCCCCC		59.55-
478UbiquitinationEKQSFPKKFPMSQSV
HCCCCCCCCCCCCCC		55.74-
503PhosphorylationIYASLKFSESLHRSS
HHHHHCCCHHHHCCC		25.3720860994
505PhosphorylationASLKFSESLHRSSTE
HHHCCCHHHHCCCCH		28.4220860994
519UbiquitinationEIDDMLRKSTNLLLT
HHHHHHHHHHHHHHH		58.64-
591UbiquitinationLYGLSTFKDARHAAE
CCCCCCHHCHHHHHC		51.03-
591AcetylationLYGLSTFKDARHAAE
CCCCCCHHCHHHHHC		51.0325953088
604UbiquitinationAEGEIYTKLNQKIDE
HCCHHHHHHHHHHHH		28.5921890473
608UbiquitinationIYTKLNQKIDEFVQL
HHHHHHHHHHHHHHH		51.5621890473
791UbiquitinationKLIETVVKQLRSLVN
HHHHHHHHHHHHHHH		39.00-
801PhosphorylationRSLVNGMSQHM----
HHHHHHHHHCC----		20.5223917254
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 EXOC6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EXOC6_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 EXOC6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYO5A_HUMANMYO5Aphysical
22172676
NOS3_HUMANNOS3physical
21163940
A4_HUMANAPPphysical
21163940
EXOS1_HUMANEXOSC1physical
21163940
GCDH_HUMANGCDHphysical
21163940
LOXL4_HUMANLOXL4physical
21163940
PRDX2_HUMANPRDX2physical
21163940
EXOC6_HUMANEXOC6physical
21163940
EXOC8_HUMANEXOC8physical
26344197
ULA1_HUMANNAE1physical
26344197
EXOC3_HUMANEXOC3physical
28514442
EXOC1_HUMANEXOC1physical
28514442
EXOC7_HUMANEXOC7physical
28514442
EXOC5_HUMANEXOC5physical
28514442
EXOC2_HUMANEXOC2physical
28514442
CAR19_HUMANC9orf89physical
28514442
RAP1A_HUMANRAP1Aphysical
28514442
EXOC4_HUMANEXOC4physical
28514442
VPS53_HUMANVPS53physical
28514442
GNAQ_HUMANGNAQphysical
28514442
EXOC8_HUMANEXOC8physical
27173435
EXOC7_HUMANEXOC7physical
27173435
EXOC5_HUMANEXOC5physical
27173435
EXOC4_HUMANEXOC4physical
27173435
MIC60_HUMANIMMTphysical
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 EXOC6_HUMAN

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Related Literatures of Post-Translational Modification

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