GH_HHV11 - dbPTM
GH_HHV11 - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GH_HHV11
UniProt AC P06477
Protein Name Envelope glycoprotein H {ECO:0000255|HAMAP-Rule:MF_04033}
Gene Name gH {ECO:0000255|HAMAP-Rule:MF_04033}
Organism Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
Sequence Length 838
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 . During virion morphogenesis, this protein probably accumulates in the en
Protein Description The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Following initial binding to host receptor, membrane fusion is mediated by the fusion machinery composed of gB and the heterodimer gH/gL. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion morphogenesis..
Protein Sequence MGNGLWFVGVIILGVAWGQVHDWTEQTDPWFLDGLGMDRMYWRDTNTGRLWLPNTPDPQKPPRGFLAPPDELNLTTASLPLLRWYEERFCFVLVTTAEFPRDPGQLLYIPKTYLLGRPPNASLPAPTTVEPTAQPPPSVAPLKGLLHNPAASVLLRSRAWVTFSAVPDPEALTFPRGDNVATASHPSGPRDTPPPRPPVGARRHPTTELDITHLHNASTTWLATRGLLRSPGRYVYFSPSASTWPVGIWTTGELVLGCDAALVRARYGREFMGLVISMHDSPPVEVMVVPAGQTLDRVGDPADENPPGALPGPPGGPRYRVFVLGSLTRADNGSALDALRRVGGYPEEGTNYAQFLSRAYAEFFSGDAGAEQGPRPPLFWRLTGLLATSGFAFVNAAHANGAVCLSDLLGFLAHSRALAGLAARGAAGCAADSVFFNVSVLDPTARLQLEARLQHLVAEILEREQSLALHALGYQLAFVLDSPSAYDAVAPSAAHLIDALYAEFLGGRVLTTPVVHRALFYASAVLRQPFLAGVPSAVQRERARRSLLIASALCTSDVAAATNADLRTALARADHQKTLFWLPDHFSPCAASLRFDLDESVFILDALAQATRSETPVEVLAQQTHGLASTLTRWAHYNALIRAFVPEASHRCGGQSANVEPRILVPITHNASYVVTHSPLPRGIGYKLTGVDVRRPLFLTYLTATCEGSTRDIESKRLVRTQNQRDLGLVGAVFMRYTPAGEVMSVLLVDTDNTQQQIAAGPTEGAPSVFSSDVPSTALLLFPNGTVIHLLAFDTQPVAAIAPGFLAASALGVVMITAALAGILKVLRTSVPFFWRRE
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
73N-linked_GlycosylationLAPPDELNLTTASLP
CCCHHHCCCCCCCCH
33.04UniProtKB CARBOHYD
120N-linked_GlycosylationYLLGRPPNASLPAPT
EECCCCCCCCCCCCC
44.86UniProtKB CARBOHYD
216N-linked_GlycosylationLDITHLHNASTTWLA
EECEEECCCCHHHHE
41.78UniProtKB CARBOHYD
332N-linked_GlycosylationGSLTRADNGSALDAL
ECCEECCCCCHHHHH
45.38UniProtKB CARBOHYD
437N-linked_GlycosylationAADSVFFNVSVLDPT
CCCCEEEEHHCCCCC
17.43UniProtKB CARBOHYD
670N-linked_GlycosylationILVPITHNASYVVTH
EEEEECCCCCEEEEC
23.18UniProtKB CARBOHYD
784N-linked_GlycosylationTALLLFPNGTVIHLL
CEEEECCCCEEEEEE
51.97UniProtKB CARBOHYD

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 GH_HHV11 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GH_HHV11 !!

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 GH_HHV11 !!

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

Oops, there are no PPI records of GH_HHV11 !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GH_HHV11

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Related Literatures of Post-Translational Modification

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