GB_HHV11 - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GB_HHV11
• UniProt AC: P10211
• Protein Name: Envelope glycoprotein B {ECO:0000255|HAMAP-Rule:MF_04032}
• Gene Name: gB {ECO:0000255|HAMAP-Rule:MF_04032}
• Organism: Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
• Sequence Length: 904
• 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 virion envelope. Essential for the initial attachment to heparan sulfate moities of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding to its host receptors, 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 (By similarity). Also plays a role, together with gK, in virus-induced cell-to-cell fusion (syncytia formation)..
• Protein Sequence: MRQGAPARGRRWFVVWALLGLTLGVLVASAAPSSPGTPGVAAATQAANGGPATPAPPAPGAPPTGDPKPKKNRKPKPPKPPRPAGDNATVAAGHATLREHLRDIKAENTDANFYVCPPPTGATVVQFEQPRRCPTRPEGQNYTEGIAVVFKENIAPYKFKATMYYKDVTVSQVWFGHRYSQFMGIFEDRAPVPFEEVIDKINAKGVCRSTAKYVRNNLETTAFHRDDHETDMELKPANAATRTSRGWHTTDLKYNPSRVEAFHRYGTTVNCIVEEVDARSVYPYDEFVLATGDFVYMSPFYGYREGSHTEHTSYAADRFKQVDGFYARDLTTKARATAPTTRNLLTTPKFTVAWDWVPKRPSVCTMTKWQEVDEMLRSEYGGSFRFSSDAISTTFTTNLTEYPLSRVDLGDCIGKDARDAMDRIFARRYNATHIKVGQPQYYLANGGFLIAYQPLLSNTLAELYVREHLREQSRKPPNPTPPPPGASANASVERIKTTSSIEFARLQFTYNHIQRHVNDMLGRVAIAWCELQNHELTLWNEARKLNPNAIASATVGRRVSARMLGDVMAVSTCVPVAADNVIVQNSMRISSRPGACYSRPLVSFRYEDQGPLVEGQLGENNELRLTRDAIEPCTVGHRRYFTFGGGYVYFEEYAYSHQLSRADITTVSTFIDLNITMLEDHEFVPLEVYTRHEIKDSGLLDYTEVQRRNQLHDLRFADIDTVIHADANAAMFAGLGAFFEGMGDLGRAVGKVVMGIVGGVVSAVSGVSSFMSNPFGALAVGLLVLAGLAAAFFAFRYVMRLQSNPMKALYPLTTKELKNPTNPDASGEGEEGGDFDEAKLAEAREMIRYMALVSAMERTEHKAKKKGTSALLSAKVTDMVMRKRRNTNYTQVPNKDGDADEDDL

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
87	N-linked_Glycosylation	PPRPAGDNATVAAGH CCCCCCCCCCCCCCH	36.27	UniProtKB CARBOHYD
141	N-linked_Glycosylation	PTRPEGQNYTEGIAV CCCCCCCCCCCCEEE	57.46	UniProtKB CARBOHYD
398	N-linked_Glycosylation	ISTTFTTNLTEYPLS EECEEECCCCCCCCC	41.74	UniProtKB CARBOHYD
430	N-linked_Glycosylation	RIFARRYNATHIKVG HHHHHHCCCCEEECC	36.23	UniProtKB CARBOHYD
489	N-linked_Glycosylation	PPPGASANASVERIK CCCCCCCCCCEEEEE	30.19	UniProtKB CARBOHYD
674	N-linked_Glycosylation	VSTFIDLNITMLEDH EEHHEECCEEECCCC	24.76	UniProtKB CARBOHYD

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of GB_HHV11 !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of GB_HHV11 !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of GB_HHV11 !!

Protein-Protein Interaction

Oops, there are no PPI records of GB_HHV11 !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.