GB_HHV8P - dbPTM
GB_HHV8P - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GB_HHV8P
UniProt AC F5HB81
Protein Name Envelope glycoprotein B {ECO:0000255|HAMAP-Rule:MF_04032}
Gene Name gB {ECO:0000255|HAMAP-Rule:MF_04032}
Organism Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus).
Sequence Length 845
Subcellular Localization Virion membrane
Single-pass type I membrane protein . Host cell membrane
Single-pass type I membrane protein . Host endosome membrane
Single-pass type I membrane protein . Host Golgi apparatus membrane
Single-pass type I membrane protein . Du
Protein Description Envelope glycoprotein that forms spikes at the surface of the virion envelope. Participates in viral entry through an RGD motif that binds ITGAV-ITGB3. Membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress..
Protein Sequence MTPRSRLATLGTVILLVCFCAGAAHSRGDTFQTSSSPTPPGSSSKAPTKPGEEASGPKSVDFYQFRVCSASITGELFRFNLEQTCPDTKDKYHQEGILLVYKKNIVPHIFKVRRYRKIATSVTVYRGLTESAITNKYELPRPVPLYEISHMDSTYQCFSSMKVNVNGVENTFTDRDDVNTTVFLQPVEGLTDNIQRYFSQPVIYAEPGWFPGIYRVRTTVNCEIVDMIARSAEPYNYFVTSLGDTVEVSPFCYNESSCSTTPSNKNGLSVQVVLNHTVVTYSDRGTSPTPQNRIFVETGAYTLSWASESKTTAVCPLALWKTFPRSIQTTHEDSFHFVANEITATFTAPLTPVANFTDTYSCLTSDINTTLNASKAKLASTHVPNGTVQYFHTTGGLYLVWQPMSAINLTHAQGDSGNPTSSPPPSASPMTTSASRRKRRSASTAAAGGGGSTDNLSYTQLQFAYDKLRDGINQVLEELSRAWCREQVRDNLMWYELSKINPTSVMTAIYGRPVSAKFVGDAISVTECINVDQSSVNIHKSLRTNSKDVCYARPLVTFKFLNSSNLFTGQLGARNEIILTNNQVETCKDTCEHYFITRNETLVYKDYAYLRTINTTDISTLNTFIALNLSFIQNIDFKAIELYSSAEKRLASSVFDLETMFREYNYYTHRLAGLREDLDNTIDMNKERFVRDLSEIVADLGGIGKTVVNVASSVVTLCGSLVTGFINFIKHPLGGMLMIIIVIAIILIIFMLSRRTNTIAQAPVKMIYPDVDRRAPPSGGAPTREEIKNILLGMHQLQQEERQKADDLKKSTPSVFQRTANGLRQRLRGYKPLTQSLDISPETGE
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
179N-linked_GlycosylationFTDRDDVNTTVFLQP
CCCCCCCCEEEEEEE
-
254N-linked_GlycosylationEVSPFCYNESSCSTT
EECCCCCCCCCCCCC
-
275N-linked_GlycosylationLSVQVVLNHTVVTYS
EEEEEEEECEEEECC
-
355N-linked_GlycosylationAPLTPVANFTDTYSC
CCCCCCCCEECCHHH
-
368N-linked_GlycosylationSCLTSDINTTLNASK
HHHHCCHHHHCCHHH
-
372N-linked_GlycosylationSDINTTLNASKAKLA
CCHHHHCCHHHCHHH
-
385N-linked_GlycosylationLASTHVPNGTVQYFH
HHCCCCCCCEEEEEE
-
408N-linked_GlycosylationWQPMSAINLTHAQGD
EEECCEEECCCCCCC
-
455N-linked_GlycosylationGGGGSTDNLSYTQLQ
CCCCCCCCCCHHHHH
-
562N-linked_GlycosylationLVTFKFLNSSNLFTG
EEEEEECCCCCCCCC
UniProtKB CARBOHYD
599N-linked_GlycosylationEHYFITRNETLVYKD
CEEEEECCCEEEECC
UniProtKB CARBOHYD
614N-linked_GlycosylationYAYLRTINTTDISTL
EEEEEECCCCCHHHH
-
628N-linked_GlycosylationLNTFIALNLSFIQNI
HHHHHHHCCHHHHCC
-

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 GB_HHV8P !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GB_HHV8P !!

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 GB_HHV8P !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
B3GA3_HUMANB3GAT3physical
25544563

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GB_HHV8P

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Related Literatures of Post-Translational Modification

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