EXC6B_HUMAN - dbPTM
EXC6B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EXC6B_HUMAN
UniProt AC Q9Y2D4
Protein Name Exocyst complex component 6B
Gene Name EXOC6B
Organism Homo sapiens (Human).
Sequence Length 811
Subcellular Localization
Protein Description Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane..
Protein Sequence MERGKMAEAESLETAAEHERILREIESTDTACIGPTLRSVYDGEEHGRFMEKLETRIRNHDREIEKMCNFHYQGFVDSITELLKVRGEAQKLKNQVTDTNRKLQHEGKELVIAMEELKQCRLQQRNISATVDKLMLCLPVLEMYSKLRDQMKTKRHYPALKTLEHLEHTYLPQVSHYRFCKVMVDNIPKLREEIKDVSMSDLKDFLESIRKHSDKIGETAMKQAQQQRNLDNIVLQQPRIGSKRKSKKDAYIIFDTEIESTSPKSEQDSGILDVEDEEDDEEVPGAQDLVDFSPVYRCLHIYSVLGARETFENYYRKQRRKQARLVLQPPSNMHETLDGYRKYFNQIVGFFVVEDHILHTTQGLVNRAYIDELWEMALSKTIAALRTHSSYCSDPNLVLDLKNLIVLFADTLQVYGFPVNQLFDMLLEIRDQYSETLLKKWAGIFRNILDSDNYSPIPVTSEEMYKKVVGQFPFQDIELEKQPFPKKFPFSEFVPKVYNQIKEFIYACLKFSEDLHLSSTEVDDMIRKSTNLLLTRTLSNSLQNVIKRKNIGLTELVQIIINTTHLEKSCKYLEEFITNITNVLPETVHTTKLYGTTTFKDARHAAEEEIYTNLNQKIDQFLQLADYDWMTGDLGNKASDYLVDLIAFLRSTFAVFTHLPGKVAQTACMSACKHLATSLMQLLLEAEVRQLTLGALQQFNLDVRECEQFARSGPVPGFQEDTLQLAFIDLRQLLDLFIQWDWSTYLADYGQPNCKYLRVNPVTALTLLEKMKDTSRKNNMFAQFRKNERDKQKLIDTVAKQLRGLISSHHS
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
39PhosphorylationCIGPTLRSVYDGEEH
EECCCHHCCCCCCCC		28.3028122231
52UbiquitinationEHGRFMEKLETRIRN
CCHHHHHHHHHHHHH		39.57-
93UbiquitinationRGEAQKLKNQVTDTN
HHHHHHHHHHHCHHC		52.98-
97PhosphorylationQKLKNQVTDTNRKLQ
HHHHHHHCHHCHHHH		27.6023403867
99PhosphorylationLKNQVTDTNRKLQHE
HHHHHCHHCHHHHHH		27.7923403867
102UbiquitinationQVTDTNRKLQHEGKE
HHCHHCHHHHHHHHH		55.35-
118UbiquitinationVIAMEELKQCRLQQR
HHHHHHHHHHHHHHC		51.11-
145PhosphorylationLPVLEMYSKLRDQMK
HHHHHHHHHHHHHHH		24.7324719451
162PhosphorylationRHYPALKTLEHLEHT
HCCCHHHHHHHHHHH		37.9222210691
181UbiquitinationVSHYRFCKVMVDNIP
CCCHHHHHHHHHCHH		30.56-
189MethylationVMVDNIPKLREEIKD
HHHHCHHHHHHHHHC		57.2723644510
195UbiquitinationPKLREEIKDVSMSDL
HHHHHHHHCCCHHHH		56.19-
198PhosphorylationREEIKDVSMSDLKDF
HHHHHCCCHHHHHHH		23.7823403867
200PhosphorylationEIKDVSMSDLKDFLE
HHHCCCHHHHHHHHH		32.0823403867
215UbiquitinationSIRKHSDKIGETAMK
HHHHHHHHHHHHHHH		56.47-
222UbiquitinationKIGETAMKQAQQQRN
HHHHHHHHHHHHHCC		39.76-
242PhosphorylationLQQPRIGSKRKSKKD
HCCCCCCCCCCCCCC		27.2429514088
251PhosphorylationRKSKKDAYIIFDTEI
CCCCCCEEEEEECEE		12.5127642862
256PhosphorylationDAYIIFDTEIESTSP
CEEEEEECEECCCCC		28.2826657352
260PhosphorylationIFDTEIESTSPKSEQ
EEECEECCCCCCCCC		39.5926657352
261PhosphorylationFDTEIESTSPKSEQD
EECEECCCCCCCCCC		35.9428122231
262PhosphorylationDTEIESTSPKSEQDS
ECEECCCCCCCCCCC		39.3426657352
265PhosphorylationIESTSPKSEQDSGIL
ECCCCCCCCCCCCCC		43.8229116813
269PhosphorylationSPKSEQDSGILDVED
CCCCCCCCCCCCCCC		27.6826657352
310PhosphorylationSVLGARETFENYYRK
HHHCHHHHHHHHHHH		30.60-
466UbiquitinationVTSEEMYKKVVGQFP
CCCHHHHHHHHCCCC		37.472190698
466 (in isoform 2)Ubiquitination-37.47-
467UbiquitinationTSEEMYKKVVGQFPF
CCHHHHHHHHCCCCC		25.35-
481UbiquitinationFQDIELEKQPFPKKF
CCCCCCCCCCCCCCC		75.73-
481 (in isoform 2)Ubiquitination-75.73-
528UbiquitinationEVDDMIRKSTNLLLT
HHHHHHHHHHHHHHH		51.19-
554PhosphorylationKRKNIGLTELVQIII
HHCCCCHHHHHHHHH		23.2827461979
563PhosphorylationLVQIIINTTHLEKSC
HHHHHHHCCCHHHHH		12.7527461979
564PhosphorylationVQIIINTTHLEKSCK
HHHHHHCCCHHHHHH		21.7027461979
594PhosphorylationTVHTTKLYGTTTFKD
CCCCCCCCCCCCHHH		17.6228152594
596PhosphorylationHTTKLYGTTTFKDAR
CCCCCCCCCCHHHHH		14.7628152594
597PhosphorylationTTKLYGTTTFKDARH
CCCCCCCCCHHHHHH		26.3528152594
600MalonylationLYGTTTFKDARHAAE
CCCCCCHHHHHHHHH		48.6826320211
600AcetylationLYGTTTFKDARHAAE
CCCCCCHHHHHHHHH		48.6825953088
600UbiquitinationLYGTTTFKDARHAAE
CCCCCCHHHHHHHHH		48.68-
627PhosphorylationQFLQLADYDWMTGDL
HHHHHCCCCCCCCCC		13.0927642862
639PhosphorylationGDLGNKASDYLVDLI
CCCCHHHHHHHHHHH		28.5320071362
651PhosphorylationDLIAFLRSTFAVFTH
HHHHHHHHHHHHHHC		29.98-
657PhosphorylationRSTFAVFTHLPGKVA
HHHHHHHHCCCHHHH		18.86-
793MalonylationKNERDKQKLIDTVAK
HCHHHHHHHHHHHHH		53.8226320211
800UbiquitinationKLIDTVAKQLRGLIS
HHHHHHHHHHHHHHH		45.59-
800MalonylationKLIDTVAKQLRGLIS
HHHHHHHHHHHHHHH		45.5926320211
807PhosphorylationKQLRGLISSHHS---
HHHHHHHHCCCC---		28.7629449344
808PhosphorylationQLRGLISSHHS----
HHHHHHHCCCC----		20.4429449344
811PhosphorylationGLISSHHS-------
HHHHCCCC-------		36.1729449344
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 EXC6B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EXC6B_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 EXC6B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EXOC8_HUMANEXOC8physical
26344197
EXOC5_HUMANEXOC5physical
27173435
EXOC7_HUMANEXOC7physical
27173435
EXOC8_HUMANEXOC8physical
27173435
EXOC4_HUMANEXOC4physical
27173435
EXOC1_HUMANEXOC1physical
27173435
EXOC2_HUMANEXOC2physical
27173435
EXOC6_HUMANEXOC6physical
27173435
EXOC3_HUMANEXOC3physical
27173435
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EXC6B_HUMAN

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Related Literatures of Post-Translational Modification

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