Human cytomegalovirus infection (Homo sapiens)

From WikiPathways

Jump to: navigation, search
5, 6, 1042, 8, 15, 24, 3020172412, 23, 2922142, 13, 24, 309, 232027, 294endosome lumenplasma membranehost cell viral assembly compartmentendosome membranenucleoplasmMCP VPS37A DYNLL2 MCP NUP153 UL112/UL113MCP:pPR-AP:pAPComplexUL35UL83TRM3 HDAC3 CVC1 MCP NUP35 TRX1 HCMV VesicleFormation ComplexUS23HIST1H4 ELK1US26UL43UL84 UL79UL22ACore histone octamerAAAS UL88SEC13 SCP HCMVGenome:TerminaseComplexUL122UL111ACVC1 NUP214 pBREZH2 TR2:TR1gB HomodimerUL131A NUP153 gB ectodomain NUP160 UL23TRM2 NUP88 UL104 NUP133 US2UL94RANBP2 UL14NUP37 US14UL47 HIST3H2BB POM121 US34UL133UL35 AAAS UL95Histone HIST1H2B UL84NUP58-1 NEC2 UL99 UL97TRX1 UL132gH CHMP2A NUP107 RL8AHIST1H3A gH:gL:UL128:UL130:UL131AUL104 TRX2 MCPUL112/UL113 US22 TRX2 HIST1H3A CHMP4C UL32 UL147VPS4A pBR HIST3H2A Daxx:PMLAcK-histone HIST1H2A MCP UL70 MVB12 UL54UL146NUP107 Human herpesvirus 5 Genome - Merlin Strain CHMP3 RL1RL10RAE1 NUP210 UL27Histone HIST2H2A gB ectodomain RAE1 UL52 UL54 UL70 MCP SEC13 NUP50 MCP TRX2 US30NUP54 AcK(5,15,19,24)-HIST2H3A SCP NEC1 UL96 gH:gL:gO (gCIII)AcK(6,13,16,21)-HIST3H2BB RAE1 TSG101 TRX2 UL131A UL84 AcK(5,15,19,24)-HIST1H3A Ins(1,4,5,6)P4 HELI HIST2H3A AcK9-HIST1H4 US33AITGB1 DYNC1H1 UL34UL16NUP155 UL104 SCP Human herpesvirus 5 Genome - Merlin Strain Human herpesvirus 5 Genome - Merlin Strain UL44 TRX2 UL31NUPL2 US32UL87 SUZ12 MCP UL102 TRX2 UL71 UL96 Nuclear EgressComplex (NEC)AcK(6,13,16,21)-histone HIST1H2B HIST2H2BF gH:gL:UL128:UL130:UL131ACVC1 NUP205 HIST3H2A UL32 TRS1 UL102 SUZ12 UL122 UL96 CHMP1A MCP Human herpesvirus 5 Genome - Merlin Strain TRX1 pAP gN UL82UL32 HCMV Mature VirionUL102 gB ectodomain TRM1DYNC1I1 gM PRC2 (EZH2) CoreHELI UL120CVC2 UL32 UL44 NUP153 gB ectodomain HELINUP58-1 Histone HIST2H2A TRX2 NUP214 UL7UL5TRX1 UL148UL123MCP UL104 DYNLL1 UL104 US10UL32 gM MCP NCOR2 AcK(6,13,16,21)-histone HIST1H2B DYNC1LI1 TRX1 NUP205 gB transmembrane component NCOR1 HCMVTegmentedCapsid:Dynein:MicrotubuleUL17gH UL2NUP133 AcK-histone HIST2H2A NUP93 NEC2gM UL96EGFR UL15ANUP205 TRX2 US34AHuman herpesvirus 5 Genome - Merlin Strain US19TRX2 UL25CEBPDNUP160 VPS37D TRM1 gN UL104 gO AcK6-HIST1H4 gH VPS25 UL52US24TPR UL104 HCMV C CapsidProteinsSEH1L-2 NFKB1(1-433)TRX2 AcK(6,13,16,21)-HIST2H2BF CoA-SHTRX1 NUP43 UL47 AcK17-HIST1H4 HCMV TegumentedVirionUL26TRX1 TPR RANBP2 UL104 CHMP1AHIST3H2BB Histone HIST1H2A UL70 HIST2H3A MicrotubuleNUP85 AAAS POM121C UL104 gM:gNHuman herpesvirus 5 Genome - Merlin Strain UL24AcK(6,13,16,21)-HIST2H2BE gO US9UL25 UL104gB HomodimerCVC2 TRIM28POM121C UL76MCP gM CREB1US23 pBR NUP54 SCP HCMV C NucleocapsidCVC2 NEC2 NUP210 RIR1UL54 NUP98-3 UL32 UL131ARL11NUP188 UL117RBBP7 CVC1:CVC2UL18MCP ITGB1 NEC2NDC1 AcK6-HIST1H4 CHMP7 Human herpesvirus 5 Genome - Merlin Strain AcK-histone HIST2H2A NUP98-5 CVC2 HNRNPKUS17NUP50 IRS1 VPS28 UL36NUP62 UL119/UL118UL32RBBP4 HELI SEC13 HCMV CNucleocapsid:NEC2RL9ATRX2 UL32 UL37EED TRX1 HDAC3-containingcomplexMCP:pPR-AP:pAPComplexUL24 gB HomodimerUL32 DYNC1I2 pBR UL32 UL44 pAP UL83 UL104 UL71pBR NUP58-2 AcK17-HIST1H4 POM121 ppUL84:IE2-p86TRX1 Ac-CoAEnveloped HCMVVirion withoutPentameric ComplexBound to EntryMediatorCVC1 TRM2 HSPGUL97 HCMV B NucleocapsidSCP gB transmembrane component NUP62 gB ectodomain Human herpesvirus 5 Genome - Merlin Strain DBP TRX1 NEC2UL84 HCMV Mature Virionwithout pentamericcomplexUL98SCPNUP98-4 UL32 UL4HCMV TegumentedVirionUL11Microtubule protofilament SCP UL104 NUP98-3 CBX1 SCP UL138Human herpesvirus 5 Genome - Merlin Strain UL99HNRNPK US8US28HCMV Genome DNASynthesisInitiation ComplexgH:gL:gO (gCIII)AcK(6,13,16,21)-HIST2H2BE TRX2 SEH1L-2 UL44UL122 ESCRT RegulatorComplexUL102AcK-HIST3H2A NUP43 UL36 TRX1 SEH1L-2 HIST1H4 UL132NUP58-2 pBR HCMV TegumentProteinsUL102 GPS2 SEH1L-1 UL21ATBL1X Nuclear Pore Complex(NPC)NUPL2 pAP UL79 NUP58-2 RANBP2 pBRTRX2 pAPUL92NUP37 NUP133 TRS1TRX1 SCP gH UL104 UL44 NUP98-3 TRX1 NDC1 VPS37B pPR-AP:pAPUL112/UL113 UL48 SCP Enveloped HCMVVirion Bound toEntry MediatorSCPSEH1L-1 gH SCP TRX1 MCP HCMV Host CellReceptorsUL41AUL25pBRNUP93 CVC2UL96TRX2 UL79 VPS36 HCMV ReplisomeUL111ATRX2 VPS37C CVC1:CVC2HCMV Host CellReceptorsNUP54 EGFR HELI MCP HIST2H2BE gM:gNgL MCP UL32 UL138DBPUL103 UL23 UL147ASNF8 NUP155 DAXX US22RBBP4 CVC1 UL32 TRX2 Acetylated corehistone octamerNUP98-4 AcK(5,15,19,24)-HIST2H3A NUP188 Histone HIST1H2A CHMP2B DBP UL69 HIST2H2BE gO Human herpesvirus 5 Genome - Merlin Strain AcK9-HIST1H4 NUP35 AcK-HIST3H2A dNTPNUP85 UL13UL32 UL48UL95 MCP NUP98-4 CVC2 AcK(5,15,19,24)-HIST1H3A TRX2 NUPL2 NUP160 SEH1L-1 gL UL88 CBX1SCP TRX1 UL70 UL38 HeterotrimericHelicase-primaseAcK(6,13,16,21)-HIST2H2BF NUP98-5 UL32 Replicating HCMVGenome ComplexUL91CHMP4A NUP210 NUP85 VPS4ANUP35 Human herpesvirus 5 Genome - Merlin Strain TRM1NDC1 PML UL32 HCMV Capsid:NuclearPore ComplexUS16gB transmembrane component Human herpesvirus 5Genome - MerlinStrainPOM121C IRS1UL130 HCMV B CapsidNUP50 SCP UL32MCP UL32 UL38SCP UL48 TBL1XR1 UL130UL114US11DAXX UL112/UL113 TRX1 Human herpesvirus 5 Genome - Merlin Strain UL130 UBAP1 Histone HIST1H2B gM:gNTRX1 UL54 TR2:TR1UL32 UL9NUP107 TRX2 US28UL104 UL52 UL84 UL103RIR1 MCPUS13LatentTranscriptionallyRepressed HCMVGenomeUL112/UL113HCMV C CapsidNUP93 Nuclear Pore Complex(NPC)CHMP1A CEBPD NUP58-1 gN US3US18pBR gN CVC1pAPHuman herpesvirus 5 Genome - Merlin Strain HCMV BNucleocapsid:NEC2CHMP4B gB transmembrane component NUP188 RBBP7 VPS4A UL94 EED NUP155 PML UL32 EZH2 HIST2H2BF UL29SCP MCP Human herpesvirus 5 Genome - Merlin Strain DYNC1LI2 NUP62 UL104 AcK-histone HIST1H2A DBP NUP43 TranscriptionallyActive HCMV GenomegL US20NUP88 NUP88 Dynein complexAcK(6,13,16,21)-HIST3H2BB UL144US12UL82 Human herpesvirus 5 Genome - Merlin Strain TRX2 UL104 UL76 US27UL43 NEC1Human herpesvirus 5 Genome - Merlin Strain gL pBR UL47:UL48TRM3 UL124gH:gL:gO (gCIII)UL26 UL69DUTHuman herpesvirus 5 Genome - Merlin Strain UL104TRM1 NUP98-5 SCP RL11SCP TRX1 UL121TPR Terminase ComplexpPR-AP:pAPUL78CHMP6 SCP TRX1 Late Gene SpecificComplexMCP gB transmembrane component UL122 POM121 NUP214 UL123UL104 UL104 Human herpesvirus 5 Genome - Merlin Strain HCMV Pre-releaseViriongL NUP37 2018, 19, 26, 31, 323434201, 7, 11, 16, 21...41, 7, 11, 16, 21...3


Description

Herpesviruses have a unique four-layered structure: a core containing the large, double-stranded DNA genome is enclosed by an icosapentahedral capsid which is composed of capsomers. The capsid is surrounded by an amorphous protein coat called the tegument. It is encased in a glycoprotein-bearing lipid bilayer envelope.

Herpesviruses are divided into three groups: alpha-herpesviruses, beta-herpesviruses, and gamma-herpesviruses. The beta herpesviruses have a restricted host range. Their reproductive life cycle is long (days), with infection progressing slowly in cell culture systems. These viruses cause their host cells to enlarge, as exemplified by a human cytomegalovirus (HCMV) infection. These viruses can establish latent infection in secretory glands, cells of the reticuloendothelial system, and the kidneys.

Human Cytomegalovirus, or HCMV, is a common virus that infects people of all ages. In the United States, nearly one in three children are already infected with HCMV by age 5 years. Over half of adults by age 40 have been infected with HCMV. Once HCMV is in a person’s body, it stays there for life and can reactivate.

Cytomegalovirus causes three clinical syndromes:

(1) Congenital cytomegalovirus infection (when symptomatic) causes hepatosplenomegaly, retinitis, rash, and central nervous system involvement.

(2) In about 10 per cent of older children and adults, primary cytomegalovirus infection causes a mononucleosis syndrome with fever, malaise, atypical lymphocytosis, and pharyngitis.

(3) Immunocompromised hosts (transplant recipients and human immunodeficiency virus [HIV]-infected individuals) may develop life-threatening disseminated disease involving the lungs, gastrointestinal tract, liver, retina, and central nervous system.

Experimentally HCMV can be propagated in multiple cell lines. When propagated in human fibroblasts, HCMV clinical isolates acquire mutations in a manner that suggests a process of adaptation. Two strains of HCMV AD169 (grown from cultures of adenoid tissue taken from a 7-year-old girl) and Towne (developed as an attenuated vaccine by passaging 125 times in vitro) were initially used as the primary clinical strains. As only 26 % of HCMV canonical genes (45/171) are essential for viral replication in vitro it became important that a model strain be developed.

The Merlin BAC was derived for this use. Produced using a bacterial artificial chromosome (BAC) cloning system (to avoid adaptation/degradation of the genome with each passage) the Merlin strain contains a complete HCMV genome that is thought to accurately to represent the original clinical agent from which it was derived. It is also a reproducible source of clonal virus (via transfection) and is capable of reconstituting phenotypically wild-type virus.

The lifecycle represented here uses the Merlin strain where possible.Infectious Human Cytomegalovirus (HCMV) particles enter the cell through interaction with cellular receptors. Once in the cytoplasm capsid and tegument proteins are delivered to the cytosol. The capsid travels to the nucleus, where the genome is delivered and circularized. Tegument proteins regulate host cell responses and initiate the expression of viral I immediate early genes. This is followed by delayed early genes, which initiate viral genome replication, then late genes. Late gene expression initiates capsid assembly in the nucleus, followed by nuclear egress to the cytosol. Capsids associate with tegument proteins in the cytosol and are trafficked to the viral assembly complex that contains components from the endoplasmic reticulum, Golgi apparatus, and endosomal machinery. The capsids acquire additional tegument proteins and a viral envelope by budding into intracellular vesicles. These vesicles fuse with the plasma membrane to release enveloped infectious particles along with non-infectious dense bodies.

View original pathway at Reactome.

Comments

Reactome-Converter 
Pathway is converted from Reactome ID: 9609646
Reactome-version 
Reactome version: 75
Reactome Author 
Reactome Author: Gillespie, Marc E

Try the New WikiPathways

View approved pathways at the new wikipathways.org.

Quality Tags

Ontology Terms

 

Bibliography

View all...
  1. Cronshaw JM, Krutchinsky AN, Zhang W, Chait BT, Matunis MJ.; ''Proteomic analysis of the mammalian nuclear pore complex.''; PubMed Europe PMC Scholia
  2. Goodrum F.; ''Human Cytomegalovirus Latency: Approaching the Gordian Knot.''; PubMed Europe PMC Scholia
  3. Fontoura BM, Blobel G, Matunis MJ.; ''A conserved biogenesis pathway for nucleoporins: proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96.''; PubMed Europe PMC Scholia
  4. Kalejta RF.; ''Tegument proteins of human cytomegalovirus.''; PubMed Europe PMC Scholia
  5. Wilkinson GW, Davison AJ, Tomasec P, Fielding CA, Aicheler R, Murrell I, Seirafian S, Wang EC, Weekes M, Lehner PJ, Wilkie GS, Stanton RJ.; ''Human cytomegalovirus: taking the strain.''; PubMed Europe PMC Scholia
  6. Jean Beltran PM, Cristea IM.; ''The life cycle and pathogenesis of human cytomegalovirus infection: lessons from proteomics.''; PubMed Europe PMC Scholia
  7. Ori A, Banterle N, Iskar M, Iskar M, Andrés-Pons A, Escher C, Khanh Bui H, Sparks L, Solis-Mezarino V, Rinner O, Bork P, Lemke EA, Beck M.; ''Cell type-specific nuclear pores: a case in point for context-dependent stoichiometry of molecular machines.''; PubMed Europe PMC Scholia
  8. Elder E, Sinclair J.; ''HCMV latency: what regulates the regulators?''; PubMed Europe PMC Scholia
  9. Ogawa-Goto K, Tanaka K, Gibson W, Moriishi E, Miura Y, Kurata T, Irie S, Sata T.; ''Microtubule network facilitates nuclear targeting of human cytomegalovirus capsid.''; PubMed Europe PMC Scholia
  10. Schottstedt V, Blümel J, Burger R, Drosten C, Gröner A, Gürtler L, Heiden M, Hildebrandt M, Jansen B, Montag-Lessing T, Offergeld R, Pauli G, Seitz R, Schlenkrich U, Strobel J, Willkommen H, von König CH.; ''Human Cytomegalovirus (HCMV) - Revised.''; PubMed Europe PMC Scholia
  11. Rabut G, Doye V, Ellenberg J.; ''Mapping the dynamic organization of the nuclear pore complex inside single living cells.''; PubMed Europe PMC Scholia
  12. Gabaev I, Steinbrück L, Pokoyski C, Pich A, Stanton RJ, Schwinzer R, Schulz TF, Jacobs R, Messerle M, Kay-Fedorov PC.; ''The human cytomegalovirus UL11 protein interacts with the receptor tyrosine phosphatase CD45, resulting in functional paralysis of T cells.''; PubMed Europe PMC Scholia
  13. Diggins NL, Hancock MH.; ''HCMV miRNA Targets Reveal Important Cellular Pathways for Viral Replication, Latency, and Reactivation.''; PubMed Europe PMC Scholia
  14. Prichard MN, Jairath S, Penfold ME, St Jeor S, Bohlman MC, Pari GS.; ''Identification of persistent RNA-DNA hybrid structures within the origin of replication of human cytomegalovirus.''; PubMed Europe PMC Scholia
  15. Knipe DM, Raja P, Lee J.; ''Viral gene products actively promote latent infection by epigenetic silencing mechanisms.''; PubMed Europe PMC Scholia
  16. Kosinski J, Mosalaganti S, von Appen A, Teimer R, DiGuilio AL, Wan W, Bui KH, Hagen WJ, Briggs JA, Glavy JS, Hurt E, Beck M.; ''Molecular architecture of the inner ring scaffold of the human nuclear pore complex.''; PubMed Europe PMC Scholia
  17. Gibson W.; ''Structure and formation of the cytomegalovirus virion.''; PubMed Europe PMC Scholia
  18. Kuzmichev A, Jenuwein T, Tempst P, Reinberg D.; ''Different EZH2-containing complexes target methylation of histone H1 or nucleosomal histone H3.''; PubMed Europe PMC Scholia
  19. Cao R, Zhang Y.; ''SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex.''; PubMed Europe PMC Scholia
  20. Tandon R, AuCoin DP, Mocarski ES.; ''Human cytomegalovirus exploits ESCRT machinery in the process of virion maturation.''; PubMed Europe PMC Scholia
  21. Kabachinski G, Schwartz TU.; ''The nuclear pore complex--structure and function at a glance.''; PubMed Europe PMC Scholia
  22. Cannon MJ, Schmid DS, Hyde TB.; ''Review of cytomegalovirus seroprevalence and demographic characteristics associated with infection.''; PubMed Europe PMC Scholia
  23. Sinzger C.; ''Entry route of HCMV into endothelial cells.''; PubMed Europe PMC Scholia
  24. Sinclair J.; ''Chromatin structure regulates human cytomegalovirus gene expression during latency, reactivation and lytic infection.''; PubMed Europe PMC Scholia
  25. Suntharalingam M, Wente SR.; ''Peering through the pore: nuclear pore complex structure, assembly, and function.''; PubMed Europe PMC Scholia
  26. Kuzmichev A, Nishioka K, Erdjument-Bromage H, Tempst P, Reinberg D.; ''Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein.''; PubMed Europe PMC Scholia
  27. Spaderna S, Kropff B, Ködel Y, Shen S, Coley S, Lu S, Britt W, Mach M.; ''Deletion of gpUL132, a structural component of human cytomegalovirus, results in impaired virus replication in fibroblasts.''; PubMed Europe PMC Scholia
  28. Lin DH, Stuwe T, Schilbach S, Rundlet EJ, Perriches T, Mobbs G, Fan Y, Thierbach K, Huber FM, Collins LN, Davenport AM, Jeon YE, Hoelz A.; ''Architecture of the symmetric core of the nuclear pore.''; PubMed Europe PMC Scholia
  29. Sarrazin S, Lamanna WC, Esko JD.; ''Heparan sulfate proteoglycans.''; PubMed Europe PMC Scholia
  30. Dupont L, Reeves MB.; ''Cytomegalovirus latency and reactivation: recent insights into an age old problem.''; PubMed Europe PMC Scholia
  31. Ciferri C, Lander GC, Maiolica A, Herzog F, Aebersold R, Nogales E.; ''Molecular architecture of human polycomb repressive complex 2.''; PubMed Europe PMC Scholia
  32. Cao R, Wang L, Wang H, Xia L, Erdjument-Bromage H, Tempst P, Jones RS, Zhang Y.; ''Role of histone H3 lysine 27 methylation in Polycomb-group silencing.''; PubMed Europe PMC Scholia

History

View all...
CompareRevisionActionTimeUserComment
123626view08:25, 7 August 2022EgonwModified title
117747view12:46, 22 May 2021EweitzModified title
115069view17:01, 25 January 2021ReactomeTeamReactome version 75
113513view11:59, 2 November 2020ReactomeTeamReactome version 74
112835view18:41, 9 October 2020DeSlOntology Term : 'Herpes simplex virus infection pathway' added !
112780view16:18, 9 October 2020ReactomeTeamNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
Rna
AAAS ProteinQ9NRG9 (Uniprot-TrEMBL)
Ac-CoAMetaboliteCHEBI:15351 (ChEBI)
AcK(5,15,19,24)-HIST1H3A R-HSA-4568746 (Reactome)
AcK(5,15,19,24)-HIST2H3A R-HSA-4568757 (Reactome)
AcK(6,13,16,21)-HIST2H2BE R-HSA-4568576 (Reactome)
AcK(6,13,16,21)-HIST2H2BF R-HSA-4568574 (Reactome)
AcK(6,13,16,21)-HIST3H2BB R-HSA-4568597 (Reactome)
AcK(6,13,16,21)-histone HIST1H2B R-HSA-4568589 (Reactome)
AcK-HIST3H2A ProteinQ7L7L0 (Uniprot-TrEMBL)
AcK-histone HIST1H2A R-HSA-4551328 (Reactome)
AcK-histone HIST2H2A R-HSA-4551329 (Reactome)
AcK17-HIST1H4 ProteinP62805 (Uniprot-TrEMBL)
AcK6-HIST1H4 ProteinP62805 (Uniprot-TrEMBL)
AcK9-HIST1H4 ProteinP62805 (Uniprot-TrEMBL)
Acetylated core histone octamerComplexR-HSA-4663858 (Reactome) This acetlyated histone octamer represents any possible acetylation state of core histones
CBX1 ProteinP83916 (Uniprot-TrEMBL)
CBX1ProteinP83916 (Uniprot-TrEMBL)
CEBPD ProteinP49716 (Uniprot-TrEMBL)
CEBPDProteinP49716 (Uniprot-TrEMBL)
CHMP1A ProteinQ9HD42 (Uniprot-TrEMBL)
CHMP1AProteinQ9HD42 (Uniprot-TrEMBL)
CHMP2A ProteinO43633 (Uniprot-TrEMBL)
CHMP2B ProteinQ9UQN3 (Uniprot-TrEMBL)
CHMP3 ProteinQ9Y3E7 (Uniprot-TrEMBL)
CHMP4A ProteinQ9BY43 (Uniprot-TrEMBL)
CHMP4B ProteinQ9H444 (Uniprot-TrEMBL)
CHMP4C ProteinQ96CF2 (Uniprot-TrEMBL)
CHMP6 ProteinQ96FZ7 (Uniprot-TrEMBL)
CHMP7 ProteinQ8WUX9 (Uniprot-TrEMBL)
CREB1ProteinP16220 (Uniprot-TrEMBL)
CVC1 ProteinQ6SW50 (Uniprot-TrEMBL)
CVC1:CVC2ComplexR-HCY-9636120 (Reactome)
CVC1:CVC2ComplexR-HCY-9636130 (Reactome)
CVC1ProteinQ6SW50 (Uniprot-TrEMBL)
CVC2 ProteinQ6SW65 (Uniprot-TrEMBL)
CVC2ProteinQ6SW65 (Uniprot-TrEMBL)
CoA-SHMetaboliteCHEBI:15346 (ChEBI)
Core histone octamerComplexR-HSA-4657034 (Reactome)
DAXX ProteinQ9UER7 (Uniprot-TrEMBL)
DBP ProteinF5HDQ6 (Uniprot-TrEMBL)
DBPProteinF5HDQ6 (Uniprot-TrEMBL)
DUTProteinQ6SW70 (Uniprot-TrEMBL)
DYNC1H1 ProteinQ14204 (Uniprot-TrEMBL)
DYNC1I1 ProteinO14576 (Uniprot-TrEMBL)
DYNC1I2 ProteinQ13409 (Uniprot-TrEMBL)
DYNC1LI1 ProteinQ9Y6G9 (Uniprot-TrEMBL)
DYNC1LI2 ProteinO43237 (Uniprot-TrEMBL)
DYNLL1 ProteinP63167 (Uniprot-TrEMBL)
DYNLL2 ProteinQ96FJ2 (Uniprot-TrEMBL)
Daxx:PMLComplexR-HSA-9653635 (Reactome)
Dynein complexComplexR-HSA-2029145 (Reactome)
EED ProteinO75530 (Uniprot-TrEMBL)
EGFR ProteinP00533 (Uniprot-TrEMBL)
ELK1ProteinP19419 (Uniprot-TrEMBL)
ESCRT Regulator ComplexComplexR-HSA-9611816 (Reactome)
EZH2 ProteinQ15910 (Uniprot-TrEMBL)
Enveloped HCMV

Virion Bound to

Entry Mediator
ComplexR-HSA-9609688 (Reactome)
Enveloped HCMV

Virion without Pentameric Complex Bound to Entry

Mediator
ComplexR-HSA-9610977 (Reactome)
GPS2 ProteinQ13227 (Uniprot-TrEMBL)
HCMV

Genome:Terminase

Complex
ComplexR-HCY-9636169 (Reactome)
HCMV

Tegmented

Capsid:Dynein:Microtubule
ComplexR-HSA-9614365 (Reactome)
HCMV B Nucleocapsid:NEC2ComplexR-HCY-9636220 (Reactome)
HCMV B CapsidComplexR-HCY-9636172 (Reactome)
HCMV B NucleocapsidComplexR-HCY-9636216 (Reactome)
HCMV C Nucleocapsid:NEC2ComplexR-HCY-9636224 (Reactome)
HCMV C Capsid ProteinsComplexR-HCY-9653612 (Reactome)
HCMV C CapsidComplexR-HCY-9605898 (Reactome)
HCMV C NucleocapsidComplexR-HCY-9636208 (Reactome)
HCMV Capsid:Nuclear Pore ComplexComplexR-HSA-9614366 (Reactome)
HCMV Genome DNA

Synthesis

Initiation Complex
ComplexR-HCY-9624028 (Reactome)
HCMV Host Cell ReceptorsComplexR-HSA-9610864 (Reactome)
HCMV Host Cell ReceptorsComplexR-HSA-9611144 (Reactome)
HCMV Mature Virion

without pentameric

complex
ComplexR-HCY-9610868 (Reactome)
HCMV Mature VirionComplexR-HCY-9609479 (Reactome)
HCMV Pre-release VirionComplexR-HCY-9610395 (Reactome)
HCMV ReplisomeComplexR-HCY-9624040 (Reactome)
HCMV Tegument ProteinsComplexR-HCY-9653613 (Reactome)
HCMV Tegumented VirionComplexR-HCY-9606777 (Reactome)
HCMV Vesicle Formation ComplexComplexR-HSA-9610921 (Reactome)
HDAC3 ProteinO15379 (Uniprot-TrEMBL)
HDAC3-containing complexComplexR-HSA-4663830 (Reactome)
HELI ProteinF5HEN8 (Uniprot-TrEMBL)
HELIProteinF5HEN8 (Uniprot-TrEMBL)
HIST1H3A ProteinP68431 (Uniprot-TrEMBL)
HIST1H4 ProteinP62805 (Uniprot-TrEMBL)
HIST2H2BE ProteinQ16778 (Uniprot-TrEMBL)
HIST2H2BF ProteinQ5QNW6 (Uniprot-TrEMBL)
HIST2H3A ProteinQ71DI3 (Uniprot-TrEMBL)
HIST3H2A ProteinQ7L7L0 (Uniprot-TrEMBL)
HIST3H2BB ProteinQ8N257 (Uniprot-TrEMBL)
HNRNPK ProteinP61978 (Uniprot-TrEMBL)
HNRNPKProteinP61978 (Uniprot-TrEMBL)
HSPGMetaboliteCHEBI:24499 (ChEBI)
Heterotrimeric Helicase-primaseComplexR-HCY-9624041 (Reactome)
Histone HIST1H2A R-HSA-4549214 (Reactome)
Histone HIST1H2B R-HSA-4549207 (Reactome)
Histone HIST2H2A R-HSA-4549206 (Reactome)
Human herpesvirus 5

Genome - Merlin

Strain
GeneProductAY446894 (EMBL)
Human herpesvirus 5 Genome - Merlin Strain ProteinAY446894 (EMBL)
IRS1 ProteinQ6SW04 (Uniprot-TrEMBL)
IRS1ProteinQ6SW04 (Uniprot-TrEMBL)
ITGB1 ProteinP05556 (Uniprot-TrEMBL)
Ins(1,4,5,6)P4 MetaboliteCHEBI:57627 (ChEBI)
Late Gene Specific ComplexComplexR-HCY-9625993 (Reactome)
Latent

Transcriptionally Repressed HCMV

Genome
ComplexR-HSA-9614812 (Reactome)
MCP ProteinF5HGT1 (Uniprot-TrEMBL)
MCP:pPR-AP:pAP ComplexComplexR-HCY-9629013 (Reactome)
MCP:pPR-AP:pAP ComplexComplexR-HCY-9629024 (Reactome)
MCPProteinF5HGT1 (Uniprot-TrEMBL)
MVB12 R-HSA-8959998 (Reactome)
Microtubule protofilament R-HSA-8982424 (Reactome)
MicrotubuleComplexR-HSA-190599 (Reactome)
NCOR1 ProteinO75376 (Uniprot-TrEMBL)
NCOR2 ProteinQ9Y618 (Uniprot-TrEMBL)
NDC1 ProteinQ9BTX1 (Uniprot-TrEMBL)
NEC1 ProteinF5HFZ4 (Uniprot-TrEMBL)
NEC1ProteinF5HFZ4 (Uniprot-TrEMBL)
NEC2 ProteinQ6SW81 (Uniprot-TrEMBL)
NEC2ProteinQ6SW81 (Uniprot-TrEMBL)
NFKB1(1-433)ProteinP19838 (Uniprot-TrEMBL)
NUP107 ProteinP57740 (Uniprot-TrEMBL)
NUP133 ProteinQ8WUM0 (Uniprot-TrEMBL)
NUP153 ProteinP49790 (Uniprot-TrEMBL)
NUP155 ProteinO75694 (Uniprot-TrEMBL)
NUP160 ProteinQ12769 (Uniprot-TrEMBL)
NUP188 ProteinQ5SRE5 (Uniprot-TrEMBL)
NUP205 ProteinQ92621 (Uniprot-TrEMBL)
NUP210 ProteinQ8TEM1 (Uniprot-TrEMBL)
NUP214 ProteinP35658 (Uniprot-TrEMBL)
NUP35 ProteinQ8NFH5 (Uniprot-TrEMBL)
NUP37 ProteinQ8NFH4 (Uniprot-TrEMBL)
NUP43 ProteinQ8NFH3 (Uniprot-TrEMBL)
NUP50 ProteinQ9UKX7 (Uniprot-TrEMBL)
NUP54 ProteinQ7Z3B4 (Uniprot-TrEMBL)
NUP58-1 ProteinQ9BVL2-1 (Uniprot-TrEMBL)
NUP58-2 ProteinQ9BVL2-2 (Uniprot-TrEMBL)
NUP62 ProteinP37198 (Uniprot-TrEMBL)
NUP85 ProteinQ9BW27 (Uniprot-TrEMBL)
NUP88 ProteinQ99567 (Uniprot-TrEMBL)
NUP93 ProteinQ8N1F7 (Uniprot-TrEMBL)
NUP98-3 ProteinP52948-3 (Uniprot-TrEMBL)
NUP98-4 ProteinP52948-4 (Uniprot-TrEMBL)
NUP98-5 ProteinP52948-5 (Uniprot-TrEMBL)
NUPL2 ProteinO15504 (Uniprot-TrEMBL)
Nuclear Egress Complex (NEC)ComplexR-HCY-9636214 (Reactome)
Nuclear Pore Complex (NPC)ComplexR-HSA-157689 (Reactome)
PML ProteinP29590 (Uniprot-TrEMBL)
POM121 ProteinQ96HA1 (Uniprot-TrEMBL)
POM121C ProteinA8CG34 (Uniprot-TrEMBL)
PRC2 (EZH2) CoreComplexR-HSA-212285 (Reactome) The human Polycomb Repressive Complex 2 (PRC2) is homologous to the Drosophila PRC2. The core PRC2 contains EZH2, a histone methyltransferase specific for lysine 27 and lysine 9 of histone H3. The methyltransferase activity of EZH2 is dependent on its association with PRC2. The complex contains other uncharacterized proteins, its composition may vary in different tissues and developmental stages, and the order of assembly of the complex is presently unknown.
RAE1 ProteinP78406 (Uniprot-TrEMBL)
RANBP2 ProteinP49792 (Uniprot-TrEMBL)
RBBP4 ProteinQ09028 (Uniprot-TrEMBL)
RBBP7 ProteinQ16576 (Uniprot-TrEMBL)
RIR1 ProteinQ6SW87 (Uniprot-TrEMBL)
RIR1ProteinQ6SW87 (Uniprot-TrEMBL)
RL10ProteinF5HI32 (Uniprot-TrEMBL)
RL11ProteinQ6SWD1 (Uniprot-TrEMBL)
RL1ProteinQ6SWD5 (Uniprot-TrEMBL)
RL8AProteinF7V995 (Uniprot-TrEMBL)
RL9AProteinF7V996 (Uniprot-TrEMBL)
Replicating HCMV Genome ComplexComplexR-HSA-9624037 (Reactome)
SCP ProteinF5HEN7 (Uniprot-TrEMBL)
SCPProteinF5HEN7 (Uniprot-TrEMBL)
SEC13 ProteinP55735 (Uniprot-TrEMBL)
SEH1L-1 ProteinQ96EE3-1 (Uniprot-TrEMBL)
SEH1L-2 ProteinQ96EE3-2 (Uniprot-TrEMBL)
SNF8 ProteinQ96H20 (Uniprot-TrEMBL)
SUZ12 ProteinQ15022 (Uniprot-TrEMBL)
TBL1X ProteinO60907 (Uniprot-TrEMBL)
TBL1XR1 ProteinQ9BZK7 (Uniprot-TrEMBL)
TPR ProteinP12270 (Uniprot-TrEMBL)
TR2:TR1ComplexR-HCY-9636119 (Reactome)
TR2:TR1ComplexR-HCY-9636125 (Reactome)
TRIM28ProteinQ13263 (Uniprot-TrEMBL)
TRM1 ProteinF5HC79 (Uniprot-TrEMBL)
TRM1ProteinF5HC79 (Uniprot-TrEMBL)
TRM2 ProteinF5HGI9 (Uniprot-TrEMBL)
TRM3 ProteinF5HCU8 (Uniprot-TrEMBL)
TRS1 ProteinQ6SVX2 (Uniprot-TrEMBL)
TRS1ProteinQ6SVX2 (Uniprot-TrEMBL)
TRX1 ProteinF5HA93 (Uniprot-TrEMBL)
TRX2 ProteinF5HIN9 (Uniprot-TrEMBL)
TSG101 ProteinQ99816 (Uniprot-TrEMBL)
Terminase ComplexComplexR-HCY-9636162 (Reactome)
Transcriptionally Active HCMV GenomeComplexR-HSA-9614809 (Reactome)
UBAP1 ProteinQ9NZ09 (Uniprot-TrEMBL)
UL102 ProteinF5HIG1 (Uniprot-TrEMBL)
UL102ProteinF5HIG1 (Uniprot-TrEMBL)
UL103 ProteinF5HA10 (Uniprot-TrEMBL)
UL103ProteinF5HA10 (Uniprot-TrEMBL)
UL104 ProteinF5HBR4 (Uniprot-TrEMBL)
UL104ProteinF5HBR4 (Uniprot-TrEMBL)
UL111AProteinF5HC71 (Uniprot-TrEMBL)
UL112/UL113 ProteinQ6SW37 (Uniprot-TrEMBL)
UL112/UL113ProteinQ6SW37 (Uniprot-TrEMBL)
UL114ProteinF5HI85 (Uniprot-TrEMBL)
UL117ProteinF5HFA5 (Uniprot-TrEMBL)
UL119/UL118ProteinF5HC14 (Uniprot-TrEMBL)
UL11ProteinQ6SWB9 (Uniprot-TrEMBL)
UL120ProteinQ6SW31 (Uniprot-TrEMBL)
UL121ProteinF5HD27 (Uniprot-TrEMBL)
UL122 ProteinQ6SW29 (Uniprot-TrEMBL)
UL122ProteinQ6SW29 (Uniprot-TrEMBL)
UL123ProteinF5HCM1 (Uniprot-TrEMBL)
UL124ProteinF5HHS3 (Uniprot-TrEMBL)
UL130 ProteinF5HCP3 (Uniprot-TrEMBL)
UL130ProteinF5HCP3 (Uniprot-TrEMBL)
UL131A ProteinF5HET4 (Uniprot-TrEMBL)
UL131AProteinF5HET4 (Uniprot-TrEMBL)
UL132ProteinF5HGU6 (Uniprot-TrEMBL)
UL133ProteinQ6SW10 (Uniprot-TrEMBL)
UL138ProteinF5HGQ8 (Uniprot-TrEMBL)
UL13ProteinQ6SWB8 (Uniprot-TrEMBL)
UL144ProteinF5HAM0 (Uniprot-TrEMBL)
UL146ProteinF5HBX1 (Uniprot-TrEMBL)
UL147AProteinF5H8R0 (Uniprot-TrEMBL)
UL147ProteinF5HA06 (Uniprot-TrEMBL)
UL148ProteinF5H8Q3 (Uniprot-TrEMBL)
UL14ProteinQ6SWB7 (Uniprot-TrEMBL)
UL15AProteinF5HAE6 (Uniprot-TrEMBL)
UL16ProteinF5HG68 (Uniprot-TrEMBL)
UL17ProteinF5HHT4 (Uniprot-TrEMBL)
UL18ProteinF5HFB4 (Uniprot-TrEMBL)
UL21AProteinF5HH39 (Uniprot-TrEMBL)
UL22AProteinF5HF90 (Uniprot-TrEMBL)
UL23 ProteinF5HDM3 (Uniprot-TrEMBL)
UL23ProteinF5HDM3 (Uniprot-TrEMBL)
UL24 ProteinF5H9N4 (Uniprot-TrEMBL)
UL24ProteinF5H9N4 (Uniprot-TrEMBL)
UL25 ProteinF5HGJ4 (Uniprot-TrEMBL)
UL25ProteinF5HGJ4 (Uniprot-TrEMBL)
UL26 ProteinF5HGG3 (Uniprot-TrEMBL)
UL26ProteinF5HGG3 (Uniprot-TrEMBL)
UL27ProteinQ6SWA4 (Uniprot-TrEMBL)
UL29ProteinQ6SWA3 (Uniprot-TrEMBL)
UL2ProteinQ6SWC7 (Uniprot-TrEMBL)
UL31ProteinQ6SWA0 (Uniprot-TrEMBL)
UL32 ProteinQ6SW99 (Uniprot-TrEMBL)
UL32ProteinQ6SW99 (Uniprot-TrEMBL)
UL34ProteinF5HC16 (Uniprot-TrEMBL)
UL35 ProteinF5HE12 (Uniprot-TrEMBL)
UL35ProteinF5HE12 (Uniprot-TrEMBL)
UL36 ProteinF5HAY6 (Uniprot-TrEMBL)
UL36ProteinF5HAY6 (Uniprot-TrEMBL)
UL37ProteinQ6SW94 (Uniprot-TrEMBL)
UL38 ProteinF5HG98 (Uniprot-TrEMBL)
UL38ProteinF5HG98 (Uniprot-TrEMBL)
UL41AProteinF5HFG3 (Uniprot-TrEMBL)
UL43 ProteinQ6SW89 (Uniprot-TrEMBL)
UL43ProteinQ6SW89 (Uniprot-TrEMBL)
UL44 ProteinF5HC97 (Uniprot-TrEMBL)
UL44ProteinF5HC97 (Uniprot-TrEMBL)
UL47 ProteinQ6SW85 (Uniprot-TrEMBL)
UL47:UL48ComplexR-HCY-9640354 (Reactome)
UL48 ProteinQ6SW84 (Uniprot-TrEMBL)
UL48ProteinQ6SW84 (Uniprot-TrEMBL)
UL4ProteinQ6SWC6 (Uniprot-TrEMBL)
UL52 ProteinQ6SW79 (Uniprot-TrEMBL)
UL52ProteinQ6SW79 (Uniprot-TrEMBL)
UL54 ProteinQ6SW77 (Uniprot-TrEMBL)
UL54ProteinQ6SW77 (Uniprot-TrEMBL)
UL5ProteinQ6SWC5 (Uniprot-TrEMBL)
UL69 ProteinQ6SW73 (Uniprot-TrEMBL)
UL69ProteinQ6SW73 (Uniprot-TrEMBL)
UL70 ProteinF5HG51 (Uniprot-TrEMBL)
UL71 ProteinF5HEA3 (Uniprot-TrEMBL)
UL71ProteinF5HEA3 (Uniprot-TrEMBL)
UL76 ProteinQ6SW66 (Uniprot-TrEMBL)
UL76ProteinQ6SW66 (Uniprot-TrEMBL)
UL78ProteinF5HET1 (Uniprot-TrEMBL)
UL79 ProteinQ6SW63 (Uniprot-TrEMBL)
UL79ProteinQ6SW63 (Uniprot-TrEMBL)
UL7ProteinQ6SWC3 (Uniprot-TrEMBL)
UL82 ProteinF5HBC6 (Uniprot-TrEMBL)
UL82ProteinF5HBC6 (Uniprot-TrEMBL)
UL83 ProteinQ6SW59 (Uniprot-TrEMBL)
UL83ProteinQ6SW59 (Uniprot-TrEMBL)
UL84 ProteinF5HB40 (Uniprot-TrEMBL)
UL84ProteinF5HB40 (Uniprot-TrEMBL)
UL87 ProteinQ6SW55 (Uniprot-TrEMBL)
UL88 ProteinF5H9F9 (Uniprot-TrEMBL)
UL88ProteinF5H9F9 (Uniprot-TrEMBL)
UL91ProteinF5HFJ8 (Uniprot-TrEMBL)
UL92ProteinF5HAS7 (Uniprot-TrEMBL)
UL94 ProteinF5HAC7 (Uniprot-TrEMBL)
UL94ProteinF5HAC7 (Uniprot-TrEMBL)
UL95 ProteinQ6SW48 (Uniprot-TrEMBL)
UL95ProteinQ6SW48 (Uniprot-TrEMBL)
UL96 ProteinF5H8R6 (Uniprot-TrEMBL)
UL96ProteinF5H8R6 (Uniprot-TrEMBL)
UL97 ProteinQ6SW46 (Uniprot-TrEMBL)
UL97ProteinQ6SW46 (Uniprot-TrEMBL)
UL98ProteinF5HF49 (Uniprot-TrEMBL)
UL99 ProteinF5HI87 (Uniprot-TrEMBL)
UL99ProteinF5HI87 (Uniprot-TrEMBL)
UL9ProteinF5H9T4 (Uniprot-TrEMBL)
US10ProteinF5HFJ7 (Uniprot-TrEMBL)
US11ProteinQ6SVZ5 (Uniprot-TrEMBL)
US12ProteinF5HE44 (Uniprot-TrEMBL)
US13ProteinF5H9I4 (Uniprot-TrEMBL)
US14ProteinF5HD92 (Uniprot-TrEMBL)
US16ProteinQ6SVZ0 (Uniprot-TrEMBL)
US17ProteinF5H9N9 (Uniprot-TrEMBL)
US18ProteinF5HE69 (Uniprot-TrEMBL)
US19ProteinF5HAR3 (Uniprot-TrEMBL)
US20ProteinF5HGH8 (Uniprot-TrEMBL)
US22 ProteinF5HDC7 (Uniprot-TrEMBL)
US22ProteinF5HDC7 (Uniprot-TrEMBL)
US23 ProteinF5HAZ3 (Uniprot-TrEMBL)
US23ProteinF5HAZ3 (Uniprot-TrEMBL)
US24ProteinF5H8S6 (Uniprot-TrEMBL)
US26ProteinF5H991 (Uniprot-TrEMBL)
US27ProteinF5HDK1 (Uniprot-TrEMBL)
US28ProteinF5HF62 (Uniprot-TrEMBL)
US2ProteinF5HE05 (Uniprot-TrEMBL)
US30ProteinF5HB41 (Uniprot-TrEMBL)
US32ProteinF5HD03 (Uniprot-TrEMBL)
US33AProteinF7V999 (Uniprot-TrEMBL)
US34AProteinQ6SVX3 (Uniprot-TrEMBL)
US34ProteinF5HEF3 (Uniprot-TrEMBL)
US3ProteinF5HEU0 (Uniprot-TrEMBL)
US8ProteinF5HB52 (Uniprot-TrEMBL)
US9ProteinF5HC33 (Uniprot-TrEMBL)
VPS25 ProteinQ9BRG1 (Uniprot-TrEMBL)
VPS28 ProteinQ9UK41 (Uniprot-TrEMBL)
VPS36 ProteinQ86VN1 (Uniprot-TrEMBL)
VPS37A ProteinQ8NEZ2 (Uniprot-TrEMBL)
VPS37B ProteinQ9H9H4 (Uniprot-TrEMBL)
VPS37C ProteinA5D8V6 (Uniprot-TrEMBL)
VPS37D ProteinQ86XT2 (Uniprot-TrEMBL)
VPS4A ProteinQ9UN37 (Uniprot-TrEMBL)
VPS4AProteinQ9UN37 (Uniprot-TrEMBL)
dNTPMetaboliteCHEBI:16516 (ChEBI)
gB HomodimerComplexR-HCY-9610957 (Reactome)
gB HomodimerComplexR-HCY-9611153 (Reactome)
gB ectodomain ProteinF5HB53 (Uniprot-TrEMBL)
gB transmembrane component ProteinF5HB53 (Uniprot-TrEMBL)
gH ProteinQ6SW67 (Uniprot-TrEMBL)
gH:gL:UL128:UL130:UL131AComplexR-HCY-9610958 (Reactome)
gH:gL:gO (gCIII)ComplexR-HCY-9610959 (Reactome)
gH:gL:gO (gCIII)ComplexR-HCY-9611162 (Reactome)
gL ProteinF5HCH8 (Uniprot-TrEMBL)
gM ProteinQ6SW43 (Uniprot-TrEMBL)
gM:gNComplexR-HCY-9610912 (Reactome)
gM:gNComplexR-HCY-9611145 (Reactome)
gN ProteinF5HHQ0 (Uniprot-TrEMBL)
gO ProteinF5HGP1 (Uniprot-TrEMBL)
pAP ProteinQ6SW62 (Uniprot-TrEMBL)
pAPProteinQ6SW62 (Uniprot-TrEMBL)
pBR ProteinQ6SW62 (Uniprot-TrEMBL)
pBRProteinQ6SW62 (Uniprot-TrEMBL)
pPR-AP:pAPComplexR-HCY-9629008 (Reactome)
pPR-AP:pAPComplexR-HCY-9629011 (Reactome)
ppUL84:IE2-p86ComplexR-HCY-9624036 (Reactome)
vRNA-1 Protein

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
Ac-CoAR-HSA-9614810 (Reactome)
Acetylated core histone octamerR-HSA-9614811 (Reactome)
CBX1ArrowR-HSA-9614810 (Reactome)
CBX1R-HSA-9614816 (Reactome)
CEBPDArrowR-HSA-9698926 (Reactome)
CEBPDR-HSA-9624033 (Reactome)
CHMP1AArrowR-HSA-9610954 (Reactome)
CHMP1AR-HSA-9610942 (Reactome)
CREB1ArrowR-HSA-9621073 (Reactome)
CREB1ArrowR-HSA-9623096 (Reactome)
CVC1:CVC2ArrowR-HSA-9636128 (Reactome)
CVC1:CVC2R-HSA-9636128 (Reactome)
CVC1:CVC2R-HSA-9698924 (Reactome)
CVC1:CVC2R-HSA-9698931 (Reactome)
CVC1ArrowR-HSA-9698928 (Reactome)
CVC2ArrowR-HSA-9623096 (Reactome)
CoA-SHArrowR-HSA-9614810 (Reactome)
Core histone octamerR-HSA-9614816 (Reactome)
DBPArrowR-HSA-9623096 (Reactome)
DUTArrowR-HSA-9623096 (Reactome)
Daxx:PMLArrowR-HSA-9614810 (Reactome)
Daxx:PMLR-HSA-9614816 (Reactome)
Dynein complexArrowR-HSA-9614367 (Reactome)
Dynein complexR-HSA-9614343 (Reactome)
ELK1ArrowR-HSA-9623096 (Reactome)
ESCRT Regulator ComplexArrowR-HSA-9610942 (Reactome)
ESCRT Regulator ComplexArrowR-HSA-9610954 (Reactome)
Enveloped HCMV

Virion Bound to

Entry Mediator
ArrowR-HSA-9610867 (Reactome)
Enveloped HCMV

Virion Bound to

Entry Mediator
R-HSA-9611147 (Reactome)
Enveloped HCMV

Virion without Pentameric Complex Bound to Entry

Mediator
ArrowR-HSA-9609689 (Reactome)
Enveloped HCMV

Virion without Pentameric Complex Bound to Entry

Mediator
R-HSA-9611158 (Reactome)
HCMV

Genome:Terminase

Complex
ArrowR-HSA-9698926 (Reactome)
HCMV

Genome:Terminase

Complex
R-HSA-9698925 (Reactome)
HCMV

Tegmented

Capsid:Dynein:Microtubule
ArrowR-HSA-9614343 (Reactome)
HCMV

Tegmented

Capsid:Dynein:Microtubule
R-HSA-9614367 (Reactome)
HCMV B Nucleocapsid:NEC2ArrowR-HSA-9698933 (Reactome)
HCMV B CapsidArrowR-HSA-9698932 (Reactome)
HCMV B CapsidR-HSA-9698924 (Reactome)
HCMV B CapsidR-HSA-9698925 (Reactome)
HCMV B NucleocapsidArrowR-HSA-9698924 (Reactome)
HCMV B NucleocapsidR-HSA-9698933 (Reactome)
HCMV C Nucleocapsid:NEC2ArrowR-HSA-9698930 (Reactome)
HCMV C Nucleocapsid:NEC2R-HSA-9640368 (Reactome)
HCMV C Capsid ProteinsArrowR-HSA-9614369 (Reactome)
HCMV C CapsidArrowR-HSA-9698925 (Reactome)
HCMV C CapsidR-HSA-9698931 (Reactome)
HCMV C NucleocapsidArrowR-HSA-9698931 (Reactome)
HCMV C NucleocapsidR-HSA-9698930 (Reactome)
HCMV Capsid:Nuclear Pore ComplexArrowR-HSA-9614367 (Reactome)
HCMV Capsid:Nuclear Pore ComplexR-HSA-9614369 (Reactome)
HCMV Genome DNA

Synthesis

Initiation Complex
ArrowR-HSA-9698926 (Reactome)
HCMV Genome DNA

Synthesis

Initiation Complex
ArrowR-HSA-9698927 (Reactome)
HCMV Genome DNA

Synthesis

Initiation Complex
R-HSA-9624033 (Reactome)
HCMV Host Cell ReceptorsArrowR-HSA-9611147 (Reactome)
HCMV Host Cell ReceptorsArrowR-HSA-9611158 (Reactome)
HCMV Host Cell ReceptorsR-HSA-9609689 (Reactome)
HCMV Host Cell ReceptorsR-HSA-9610867 (Reactome)
HCMV Mature Virion

without pentameric

complex
R-HSA-9609689 (Reactome)
HCMV Mature VirionArrowR-HSA-9610388 (Reactome)
HCMV Mature VirionR-HSA-9610867 (Reactome)
HCMV Pre-release VirionArrowR-HSA-9610954 (Reactome)
HCMV Pre-release VirionR-HSA-9610388 (Reactome)
HCMV ReplisomeArrowR-HSA-9698926 (Reactome)
HCMV ReplisomeR-HSA-9624033 (Reactome)
HCMV Tegument ProteinsArrowR-HSA-9614367 (Reactome)
HCMV Tegumented VirionArrowR-HSA-9611147 (Reactome)
HCMV Tegumented VirionArrowR-HSA-9611158 (Reactome)
HCMV Tegumented VirionArrowR-HSA-9640368 (Reactome)
HCMV Tegumented VirionR-HSA-9610942 (Reactome)
HCMV Tegumented VirionR-HSA-9614343 (Reactome)
HCMV Tegumented Virionmim-catalysisR-HSA-9614343 (Reactome)
HCMV Vesicle Formation ComplexArrowR-HSA-9610942 (Reactome)
HCMV Vesicle Formation ComplexR-HSA-9610954 (Reactome)
HDAC3-containing complexArrowR-HSA-9614816 (Reactome)
HELIArrowR-HSA-9623096 (Reactome)
HNRNPKArrowR-HSA-9698926 (Reactome)
HNRNPKR-HSA-9624033 (Reactome)
HSPGArrowR-HSA-9611147 (Reactome)
HSPGArrowR-HSA-9611158 (Reactome)
HSPGR-HSA-9609689 (Reactome)
HSPGR-HSA-9610867 (Reactome)
Heterotrimeric Helicase-primaseR-HSA-9698927 (Reactome)
Human herpesvirus 5

Genome - Merlin

Strain
ArrowR-HSA-9614369 (Reactome)
Human herpesvirus 5

Genome - Merlin

Strain
R-HSA-9614811 (Reactome)
Human herpesvirus 5

Genome - Merlin

Strain
R-HSA-9614816 (Reactome)
Human herpesvirus 5

Genome - Merlin

Strain
R-HSA-9698927 (Reactome)
IRS1ArrowR-HSA-9621073 (Reactome)
IRS1R-HSA-9640368 (Reactome)
Late Gene Specific ComplexArrowR-HSA-9698928 (Reactome)
Latent

Transcriptionally Repressed HCMV

Genome
ArrowR-HSA-9614816 (Reactome)
Latent

Transcriptionally Repressed HCMV

Genome
R-HSA-9614810 (Reactome)
MCP:pPR-AP:pAP ComplexArrowR-HSA-9629004 (Reactome)
MCP:pPR-AP:pAP ComplexArrowR-HSA-9698923 (Reactome)
MCP:pPR-AP:pAP ComplexR-HSA-9629004 (Reactome)
MCP:pPR-AP:pAP ComplexR-HSA-9698929 (Reactome)
MCPArrowR-HSA-9698928 (Reactome)
MCPArrowR-HSA-9698929 (Reactome)
MCPR-HSA-9698923 (Reactome)
MCPR-HSA-9698932 (Reactome)
MicrotubuleArrowR-HSA-9614367 (Reactome)
MicrotubuleR-HSA-9614343 (Reactome)
NEC1ArrowR-HSA-9623096 (Reactome)
NEC2ArrowR-HSA-9623096 (Reactome)
NEC2ArrowR-HSA-9640368 (Reactome)
NEC2R-HSA-9698930 (Reactome)
NEC2R-HSA-9698933 (Reactome)
NFKB1(1-433)ArrowR-HSA-9621073 (Reactome)
Nuclear Egress Complex (NEC)ArrowR-HSA-9698930 (Reactome)
Nuclear Egress Complex (NEC)ArrowR-HSA-9698933 (Reactome)
Nuclear Egress Complex (NEC)mim-catalysisR-HSA-9698930 (Reactome)
Nuclear Egress Complex (NEC)mim-catalysisR-HSA-9698933 (Reactome)
Nuclear Pore Complex (NPC)ArrowR-HSA-9614369 (Reactome)
Nuclear Pore Complex (NPC)ArrowR-HSA-9629004 (Reactome)
Nuclear Pore Complex (NPC)ArrowR-HSA-9636128 (Reactome)
Nuclear Pore Complex (NPC)R-HSA-9614367 (Reactome)
PRC2 (EZH2) CoreArrowR-HSA-9614810 (Reactome)
PRC2 (EZH2) CoreR-HSA-9614816 (Reactome)
R-HSA-9609689 (Reactome) Viral attachment and penetration of Human Cytomegalovirus (HCMV) occurs either via direct HCMV fusion with the cell membrane or via endocytosis. The endocytic mechanism occurs with cell types including endothelial and epithelial cells, where the pentameric viral protein complex, gH:gL:p128:p130:p131A, facilitates entry.
R-HSA-9610388 (Reactome) The enveloped virion is carried in a vesicle which will be released through exocytosis. This step carries virus particles as well as dense bodies to the extracellular space. The host cellular exocytic pathway carries out this process.
R-HSA-9610867 (Reactome) Viral attachment and penetration of Human Cytomegalovirus (HCMV) occurs either via direct HCMV fusion with the cell membrane or via endocytosis. The endocytic mechanism occurs with cell types including endothelial and epithelial cells, where the pentameric viral protein complex, gH:gL:p128:p130:p131A, facilitates entry.
R-HSA-9610942 (Reactome) VPS4A and CHMP1A components localize within the assembly compartment (AC), with a striking colocalization of the chromatin modifying protein 1A (CHMP1A) and assembled gM:gN. Both the Vps4A and CHMP1A localized in the vicinity of viral cytoplasmic assembly compartments are sites of viral maturation that develop in human cytomeglovirus (HCMV)-infected cells. The accumulation of viral tegument also occurs during this step of viral maturation.
R-HSA-9610954 (Reactome) As part of the HCMV Vesicle Formation Complex, Vps4 controls the release of ESCRT complexes from membranes. Upstream ESCRT complexes ESCRT-I and ESCRT-II are believed to work in parallel to recruit the cargo, whereas Vps4 and ESCRT-III work in series. Virus envelopment occurs by budding into endosomal vesicles, which fuse with the plasma membrane to release virions to the extracellular space. Accumulation of viral glycoproteins gM-gN and ESCRT proteins at the periphery of AC support this model of viral egress, where these proteins provide essential functions such as envelopment and endosomal budding before viral exit.
R-HSA-9611147 (Reactome) Once the pentameric viral protein complex, gH:gL:p128:p130:p131A, facilitates attchment of the Human Cytomegalovirus (HCMV) endocytic uptake allows the virion to enter epithelial and endothelial cells. The virion is released from the endocytic vesicle by low-pH-dependent fusion of the virion coat with endosomes membrane.
R-HSA-9611158 (Reactome) Once Human cytomegalovirus (HCMV) initial attachs to cell surface heparan sulfate proteoglycans (HSPGs), the virus fuses with thecell membrane.
R-HSA-9614343 (Reactome) Tegument proteins help deliver the Human Cytomegalovirus (HCMV) genome-containing capsid to the nucleus during the viral entry process. Signals initiated upon receptor binding induce cellular antiviral responses but may also prime the cell for subsequent events during viral entry. The Capsid-associated tegument proteins UL47 and UL48 (and perhaps pp150) direct capsids along microtubules (MTs) toward nuclear pore complexes driven by cellular motor proteins such as dynein.
R-HSA-9614367 (Reactome) Virion capsids eventually dissociate from microtubules, dock at nuclear pores, and release their DNA into the nucleus. The role of tegument proteins in this process is implicated but has not been described in detail.
R-HSA-9614369 (Reactome) After the Human Cytomegalovirus (HCMV) capsid docks at the nuclear pore complex the HCMV genome containing capsid is transported into the nucleus.
R-HSA-9614810 (Reactome) A cell containing a repressed or latent Human Cytomegalovirus (HCMV) genome sits quietly carrying on its normal cellular functions. The HCMV silenced HCMV geneome can be activated by a number of celluar events or state changes. Reactivation of HCMV lytic infection is correlated to changes in histone modifications around the MIEP promoter resulting in a new chromatin structure conducive to transcriptional activity. These changes are intimately linked with cell differentiation, a phenomenon known to reactivate latent virus in vivo.
R-HSA-9614811 (Reactome) Cells infected by with the human cytomegalovirus (HCMV) have two potential fates once the HCMV genome enters the nucleus. In an active infection there is extensive viral gene expression, viral DNA replication and release of progeny virus. In contrast, in a latent infection the lytic transcription programme of HCMV is effectively suppressed and the cells undergo latent infection. The suppression of viral lytic gene expression observed during latency is the result from the cells inability to support robust viral immediate early (IE) gene expression; crucial genes responsible for driving the lytic cycle. The repression of IE gene expression results from specific post-translational modifications of histones associated with the viral major immediate early promoter (MIEP). The histone modifications present on the MIEP impart a repressive chromatin structure preventing transcriptional activity.
R-HSA-9614816 (Reactome) Cells infected by with the Human Cytomegalovirus (HCMV) have two potential fates once the HCMV genome enters the nucleus. In contrast, in a latent infection the lytic transcription programme of HCMV is effectively suppressed and the cells undergo latent infection. The suppression of viral lytic gene expression observed during latency is the result from the cells inability to support robust viral immediate early (IE) gene expression; crucial genes responsible for driving the lytic cycle. The repression of IE gene expression results from specific post-translational modifications of histones associated with the viral major immediate early promoter (MIEP). The histone modifications present on the MIEP impart a repressive chromatin structure preventing transcriptional activity.
In an active infection there is extensive viral gene expression, viral DNA replication and release of progeny virus.
R-HSA-9621073 (Reactome) Once the HCMV genome is delivered to the nucleus, IE gene expression ensues. RNA pol II transcription machinery transcribes IE as well as all other protein-coding and noncoding RNAs made from the HCMV genome. Regulation of viral gene expression occurs via two broad strategies: (1) viral as well as cellular factors that directly influence the transcription machinery by binding to promoter/enhancer elements directly (transcription factors) or through interactions with other proteins (adaptors) (2) viral factors that alter chromatin remodeling by regulating the opposing activities of histone acetyl transferases (HATs) acting together with demethylases and histone deacetylases (HDACs) and methylases. HDAC-dependent repression of viral IE gene expression, in particular, is a cell-intrinsic host defense mechanism that must be defused before productive replication can ensue. Epigenetic regulation is important in permissive cells, even though the viral genome does not take on a recognizable chromatin structure, and also during latency, where viral genomes take on an organized chromatin arrangement and viral HDAC inhibitors can drive reactivation.
R-HSA-9623096 (Reactome) Following peak expression of major immediate early (MIE) regulatory proteins, the second class of early genes, delayed early (DE), become transcriptionally active independent of the host cell type. Although some DE gene products are produced in abundance from the start, most of the proteins and assorted miRNAs accumulate gradually. The DE period of viral replication continues until viral DNA synthesis initiates. DE genes are crucial for viral DNA synthesis and include several functions that become important later in infection for maturation and egress. Many DE genes have a substantial impact on replication when disrupted. DE gene products dispensable for replication in fibroblasts may contribute to modulation of the host cell and host animal response to infection. Several HCMV DE genes switch or add transcriptional start sites later in infection, which means that transcript levels represent the combined products of different kinetic classes of gene expression.
R-HSA-9624033 (Reactome) DNA synthesis occurs in the nucleus and relies on a core set of virus-coded proteins composed of replication fork machinery that work together to promote replication initiation on the oriLyt region. DNA synthesis initiates in the vicinity of oriLyt as soon as essential virus encoded proteins appear, producing high molecular weight replication intermediates. Onset of viral DNA synthesis licenses transcription of a subset of the late class (L) of viral genes, many of which encode proteins that take part in virion assembly.
R-HSA-9629004 (Reactome) The process of capsid continues with the rranslocation of SCP, Triplex (TRI) complex, CVC complex, and accessory proteins from the cytoplasm into the nucleous, joing MCP and the maturational protease precursor complex (pPR-AP:pAP). Together these are the structural foundation of the Procapsid.
R-HSA-9636128 (Reactome) The process of capsid continues with the rranslocation of SCP, Triplex (TRI) complex, CVC complex, and accessory proteins from the cytoplasm into the nucleous, joing MCP and the maturational protease precursor complex (pPR-AP:pAP). Together these are the structural foundation of the Procapsid.
R-HSA-9640368 (Reactome) Nucleocapsids most likely reach the cytoplasm by obtaining a temporary envelope at the inner nuclear membrane passage through the perinuclear space and de-envelopment at the outer nuclear membrane. Once delivered to the cytoplasm, further assembly occurs within the cytoplasmic viral assembly compartment (AC) composed of cellular membranes and organelles that support the final steps in maturation and release. Subsequently transport is directed to sites where tegumented nucleocapsids obtain a second, final envelope to become virions.
R-HSA-9698923 (Reactome) The process of capsid formation gets underway when the newly translated major capsid protein (MCP) associates with the maturational protease precursor complex (pPR-AP:pAP). Once the complex is formed it is transported into the nucleus.
R-HSA-9698924 (Reactome) A non-infectious B capsid aquires both tegument and transport protein in the nucleus. A putative capsid vertex capping complex (CVC), composed of UL77 (CVC1) and UL93 (CVC2) proteins, decorates penton tips, and the UL51 and UL52 proteins are added to provide capsid stability. The order of addition of capsid vertex and stabilizing proteins (UL77, UL93, UL51, and UL52) remains to be established. It is not yet resolved whether these proteins are to be considered components of the capsid or tegument. The most capsid-proximal major tegument protein in HCMV is the UL32 protein, pp150, added to nucleocapsids in the nucleus and accompanying maturing particles to the cytoplasm. The pp150 and ppUL96 proteins stabilize nucleocapsids in a common pathway of translocation to cytoplasmic sites of envelopment.
R-HSA-9698925 (Reactome)
R-HSA-9698926 (Reactome) Human Cytomegalovirus (HCMV) DNA synthesis may start replication using a theta form initiating at an origin and generating a replication bubble before switching to a rolling circle mode of replication. The architecture of replicating DNA is consistent with concatemeric structures generated by rolling circle form of replication, and this is the likely template for the genome encapsidation. Replication ends with the association of the Terminase complex and the threading of the completed genome into the procapsid
R-HSA-9698927 (Reactome) During late stages of Human Cytomegalovirus (HCMV) infection viral DNA replication is established. Viral Proteins, UL36, UL49, UL80, UL100, UL117, UL112-UL113, and TRS1 all play a role in DNA replication. UL76 was found to modulate the expression of the essential protein UL77 possibly as part of a mechanism to modulate UL77 levels required for efficient viral replication. Furthermore UL55 and UL76 were found to inhibit DNA replication suggesting that these viral factors are likely key proteins to fine-tune the replication process.
R-HSA-9698928 (Reactome) Once Human Cytomegalovirus (HCMV) viral DNA synthesis is underway transcription of a subset of the late class (L) of viral genes, many of which encode proteins that take part in virion assembly ensues.
R-HSA-9698929 (Reactome) The maturational protease (PR) processes both pPR-AP and pPR in a pathway that releases PR, pAP, and AP. Although pAP is sufficient for procapsid assembly, self-cleavage of pPR-AP to PR and release of a number of pAP and pPR-AP products are required for proper DNA encapsidation and production of nucleocapsids. Precise protease cleavage steps lead to the release of major capsid protein (MCP), inactivation of the protease, and orchestration of the replacement of the scaffold in procapsids with viral DNA. PR and AP, as well as pAP forms, are completely removed from nucleocapsids into which DNA has been packaged.
R-HSA-9698930 (Reactome) Nucleocapsid C transport from the nucleus to the cytoplasm is carried out by a herpesvirus-conserved nuclear egress complex (NEC). The NEC is located at the inner nuclear membrane. This is probably one quality control step where preference is afforded to DNA-containing C capsids (nucleocapsids) over B capsids, possibly mediated by tegument proteins that associate with C capsids.The NEC is composed of a type II membrane-spanning component (NEC1, UL50 gene product) together with a nuclear lamina-interacting component (NEC2, UL53 gene product). This complex facilitates egress from the nucleus by recruiting cellular and viral protein kinases to phosphorylate and disrupt the nuclear lamina cage and allow nucleocapsid passage. Consistent with this, NEC1 or NEC2 mutant viruses in many herpesviruses including MCMV and HCMV accumulate nucleocapsids (C capsids) in the nucleus. In HCMV, host protein kinase C functions interchangeably with viral ppUL97/VPK, cellular p32, and the lamin B receptor in the NEC to phosphorylate lamins. Nucleocapsids are delivered to the cytoplasm with pp53/NEC2 remaining attached. ppUL53 accompanies the nucleocapsid as it is transported through the cytoplasm and becomes part of the tegument in mature virions. ppUL50/NEC1 remains in the nucleus and apparently cycles ppUL53.
R-HSA-9698931 (Reactome) An infectious C capsid aquires both tegument and transport protein in the nucleus. A putative capsid vertex capping complex (CVC), composed of UL77 (CVC1) and UL93 (CVC2) proteins, decorates penton tips, and the UL51 and UL52 proteins are added to provide capsid stability. The order of addition of capsid vertex and stabilizing proteins (UL77, UL93, UL51, and UL52) remains to be established. It is not yet resolved whether these proteins are to be considered components of the capsid or tegument. The most capsid-proximal major tegument protein in HCMV is the UL32 protein, pp150, added to nucleocapsids in the nucleus and accompanying maturing particles to the cytoplasm. The pp150 and ppUL96 proteins stabilize nucleocapsids in a common pathway of translocation to cytoplasmic sites of envelopment.
R-HSA-9698932 (Reactome) The procapsid shell is made up of major capsid proteins (MCP)-containing capsomeres, with six copies of MCP per hexon and five copies of MCP per penton. One of the 12 pentons in each capsid is composed entirely of portal protein (PORT), the UL104 protein, a self-assembling homododecamer. The PORT penton provides a channel for viral DNA encapsidation. Triplex (TRI) complex TRI1:TRI2 is added to stabilize hexons and pentons, and small capsid protein (SCP )decorates the outer capsid surface, interacting with MCP at hexon tips.
Before the capsid has aquired the genome, it is designated a B capsid. Three capsid forms accumulate in the nucleus of herpesvirus-infected cells: A capsids that lack both scaffold and packaged viral DNA, B capsids that contain scaffold but lack viral DNA, and C capsids, contains viral DNA in place of scaffold and probably represents nucleocapsids in the process of maturation.
R-HSA-9698933 (Reactome) Nucleocapsid B transport from the nucleus to the cytoplasm is carried out by a herpesvirus-conserved nuclear egress complex (NEC). The NEC is located at the inner nuclear membrane. This is probably one quality control step where preference is afforded to DNA-containing C capsids (nucleocapsids) over B capsids, possibly mediated by tegument proteins that associate with C capsids.The NEC is composed of a type II membrane-spanning component (NEC1, UL50 gene product) together with a nuclear lamina-interacting component (NEC2, UL53 gene product). This complex facilitates egress from the nucleus by recruiting cellular and viral protein kinases to phosphorylate and disrupt the nuclear lamina cage and allow nucleocapsid passage. Consistent with this, NEC1 or NEC2 mutant viruses in many herpesviruses including MCMV and HCMV accumulate nucleocapsids (C capsids) in the nucleus. In HCMV, host protein kinase C functions interchangeably with viral ppUL97/VPK, cellular p32, and the lamin B receptor in the NEC to phosphorylate lamins. Nucleocapsids are delivered to the cytoplasm with pp53/NEC2 remaining attached. ppUL53 accompanies the nucleocapsid as it is transported through the cytoplasm and becomes part of the tegument in mature virions. ppUL50/NEC1 remains in the nucleus and apparently cycles ppUL53.
R-HSA-9698962 (Reactome) The process of capsid formation begins with the formation of the maturational protease precursor complex (pPR-AP:pAP).
RIR1ArrowR-HSA-9623096 (Reactome)
RIR1R-HSA-9640368 (Reactome)
RL10ArrowR-HSA-9611158 (Reactome)
RL11ArrowR-HSA-9611158 (Reactome)
RL11ArrowR-HSA-9698928 (Reactome)
RL1ArrowR-HSA-9623096 (Reactome)
RL8AArrowR-HSA-9698928 (Reactome)
RL9AArrowR-HSA-9698928 (Reactome)
Replicating HCMV Genome ComplexArrowR-HSA-9624033 (Reactome)
Replicating HCMV Genome ComplexR-HSA-9698926 (Reactome)
SCPArrowR-HSA-9623096 (Reactome)
SCPArrowR-HSA-9636128 (Reactome)
SCPR-HSA-9636128 (Reactome)
SCPR-HSA-9698932 (Reactome)
TBarR-HSA-9614816 (Reactome)
TR2:TR1ArrowR-HSA-9636128 (Reactome)
TR2:TR1R-HSA-9636128 (Reactome)
TR2:TR1R-HSA-9698932 (Reactome)
TRIM28TBarR-HSA-9614816 (Reactome)
TRM1ArrowR-HSA-9636128 (Reactome)
TRM1R-HSA-9636128 (Reactome)
TRS1ArrowR-HSA-9621073 (Reactome)
TRS1R-HSA-9640368 (Reactome)
Terminase ComplexArrowR-HSA-9698925 (Reactome)
Terminase ComplexR-HSA-9698926 (Reactome)
Transcriptionally Active HCMV GenomeArrowR-HSA-9614810 (Reactome)
Transcriptionally Active HCMV GenomeArrowR-HSA-9614811 (Reactome)
Transcriptionally Active HCMV GenomeR-HSA-9621073 (Reactome)
Transcriptionally Active HCMV GenomeR-HSA-9623096 (Reactome)
Transcriptionally Active HCMV GenomeR-HSA-9698928 (Reactome)
UL102ArrowR-HSA-9623096 (Reactome)
UL103ArrowR-HSA-9698928 (Reactome)
UL103R-HSA-9640368 (Reactome)
UL104ArrowR-HSA-9623096 (Reactome)
UL104ArrowR-HSA-9636128 (Reactome)
UL104R-HSA-9636128 (Reactome)
UL104R-HSA-9698932 (Reactome)
UL111AArrowR-HSA-9698928 (Reactome)
UL111ATBarR-HSA-9614816 (Reactome)
UL112/UL113ArrowR-HSA-9623096 (Reactome)
UL112/UL113R-HSA-9640368 (Reactome)
UL112/UL113R-HSA-9698927 (Reactome)
UL114ArrowR-HSA-9623096 (Reactome)
UL117ArrowR-HSA-9698928 (Reactome)
UL119/UL118ArrowR-HSA-9623096 (Reactome)
UL11ArrowR-HSA-9623096 (Reactome)
UL120ArrowR-HSA-9698928 (Reactome)
UL121ArrowR-HSA-9698928 (Reactome)
UL122ArrowR-HSA-9621073 (Reactome)
UL122ArrowR-HSA-9623096 (Reactome)
UL123ArrowR-HSA-9621073 (Reactome)
UL124ArrowR-HSA-9623096 (Reactome)
UL130ArrowR-HSA-9698928 (Reactome)
UL131AArrowR-HSA-9698928 (Reactome)
UL132ArrowR-HSA-9611158 (Reactome)
UL132R-HSA-9698932 (Reactome)
UL133TBarR-HSA-9614816 (Reactome)
UL138ArrowR-HSA-9623096 (Reactome)
UL138TBarR-HSA-9614816 (Reactome)
UL13ArrowR-HSA-9623096 (Reactome)
UL144ArrowR-HSA-9698928 (Reactome)
UL146ArrowR-HSA-9698928 (Reactome)
UL147AArrowR-HSA-9698928 (Reactome)
UL147ArrowR-HSA-9698928 (Reactome)
UL148ArrowR-HSA-9698928 (Reactome)
UL14ArrowR-HSA-9698928 (Reactome)
UL15AArrowR-HSA-9698928 (Reactome)
UL16ArrowR-HSA-9623096 (Reactome)
UL17ArrowR-HSA-9623096 (Reactome)
UL18ArrowR-HSA-9698928 (Reactome)
UL21AArrowR-HSA-9623096 (Reactome)
UL22AArrowR-HSA-9698928 (Reactome)
UL23R-HSA-9640368 (Reactome)
UL24R-HSA-9640368 (Reactome)
UL25ArrowR-HSA-9698928 (Reactome)
UL25R-HSA-9640368 (Reactome)
UL26ArrowR-HSA-9623096 (Reactome)
UL26R-HSA-9640368 (Reactome)
UL27ArrowR-HSA-9623096 (Reactome)
UL29ArrowR-HSA-9698928 (Reactome)
UL2ArrowR-HSA-9698928 (Reactome)
UL31ArrowR-HSA-9698928 (Reactome)
UL32ArrowR-HSA-9623096 (Reactome)
UL32ArrowR-HSA-9636128 (Reactome)
UL32R-HSA-9636128 (Reactome)
UL32R-HSA-9698924 (Reactome)
UL32R-HSA-9698931 (Reactome)
UL34ArrowR-HSA-9623096 (Reactome)
UL35ArrowR-HSA-9623096 (Reactome)
UL35R-HSA-9640368 (Reactome)
UL36ArrowR-HSA-9621073 (Reactome)
UL36R-HSA-9640368 (Reactome)
UL37ArrowR-HSA-9621073 (Reactome)
UL38ArrowR-HSA-9623096 (Reactome)
UL38R-HSA-9640368 (Reactome)
UL41AArrowR-HSA-9698928 (Reactome)
UL43ArrowR-HSA-9698928 (Reactome)
UL43R-HSA-9640368 (Reactome)
UL44ArrowR-HSA-9623096 (Reactome)
UL44R-HSA-9640368 (Reactome)
UL47:UL48R-HSA-9640368 (Reactome)
UL48ArrowR-HSA-9623096 (Reactome)
UL4ArrowR-HSA-9623096 (Reactome)
UL52R-HSA-9698924 (Reactome)
UL52R-HSA-9698925 (Reactome)
UL54ArrowR-HSA-9623096 (Reactome)
UL54R-HSA-9640368 (Reactome)
UL5ArrowR-HSA-9623096 (Reactome)
UL69R-HSA-9640368 (Reactome)
UL71R-HSA-9640368 (Reactome)
UL76R-HSA-9640368 (Reactome)
UL78ArrowR-HSA-9623096 (Reactome)
UL79R-HSA-9640368 (Reactome)
UL7ArrowR-HSA-9698928 (Reactome)
UL82ArrowR-HSA-9698928 (Reactome)
UL82R-HSA-9640368 (Reactome)
UL83R-HSA-9640368 (Reactome)
UL84ArrowR-HSA-9623096 (Reactome)
UL84R-HSA-9640368 (Reactome)
UL88R-HSA-9640368 (Reactome)
UL91ArrowR-HSA-9698928 (Reactome)
UL92ArrowR-HSA-9698928 (Reactome)
UL94R-HSA-9640368 (Reactome)
UL95ArrowR-HSA-9623096 (Reactome)
UL96ArrowR-HSA-9623096 (Reactome)
UL96ArrowR-HSA-9636128 (Reactome)
UL96R-HSA-9636128 (Reactome)
UL96R-HSA-9640368 (Reactome)
UL96R-HSA-9698924 (Reactome)
UL96R-HSA-9698931 (Reactome)
UL97ArrowR-HSA-9623096 (Reactome)
UL97R-HSA-9640368 (Reactome)
UL98ArrowR-HSA-9623096 (Reactome)
UL99R-HSA-9640368 (Reactome)
UL9ArrowR-HSA-9698928 (Reactome)
US10ArrowR-HSA-9623096 (Reactome)
US11ArrowR-HSA-9623096 (Reactome)
US12ArrowR-HSA-9623096 (Reactome)
US13ArrowR-HSA-9623096 (Reactome)
US14ArrowR-HSA-9623096 (Reactome)
US16ArrowR-HSA-9623096 (Reactome)
US17ArrowR-HSA-9623096 (Reactome)
US18ArrowR-HSA-9623096 (Reactome)
US19ArrowR-HSA-9623096 (Reactome)
US20ArrowR-HSA-9623096 (Reactome)
US22ArrowR-HSA-9623096 (Reactome)
US22R-HSA-9640368 (Reactome)
US23ArrowR-HSA-9623096 (Reactome)
US23R-HSA-9640368 (Reactome)
US24ArrowR-HSA-9623096 (Reactome)
US26ArrowR-HSA-9623096 (Reactome)
US27ArrowR-HSA-9623096 (Reactome)
US28ArrowR-HSA-9623096 (Reactome)
US28TBarR-HSA-9614816 (Reactome)
US2ArrowR-HSA-9623096 (Reactome)
US30ArrowR-HSA-9623096 (Reactome)
US32ArrowR-HSA-9698928 (Reactome)
US33AArrowR-HSA-9623096 (Reactome)
US34AArrowR-HSA-9623096 (Reactome)
US34ArrowR-HSA-9623096 (Reactome)
US3ArrowR-HSA-9621073 (Reactome)
US8ArrowR-HSA-9623096 (Reactome)
US9ArrowR-HSA-9623096 (Reactome)
VPS4AArrowR-HSA-9610954 (Reactome)
VPS4AR-HSA-9610942 (Reactome)
dNTPR-HSA-9624033 (Reactome)
gB HomodimerArrowR-HSA-9611147 (Reactome)
gB HomodimerArrowR-HSA-9611158 (Reactome)
gB HomodimerR-HSA-9610954 (Reactome)
gH:gL:UL128:UL130:UL131AArrowR-HSA-9611147 (Reactome)
gH:gL:UL128:UL130:UL131AR-HSA-9610954 (Reactome)
gH:gL:gO (gCIII)ArrowR-HSA-9611147 (Reactome)
gH:gL:gO (gCIII)ArrowR-HSA-9611158 (Reactome)
gH:gL:gO (gCIII)R-HSA-9610954 (Reactome)
gM:gNArrowR-HSA-9611147 (Reactome)
gM:gNArrowR-HSA-9611158 (Reactome)
gM:gNR-HSA-9610942 (Reactome)
pAPArrowR-HSA-9698925 (Reactome)
pAPArrowR-HSA-9698929 (Reactome)
pAPR-HSA-9698932 (Reactome)
pBRArrowR-HSA-9698925 (Reactome)
pBRArrowR-HSA-9698928 (Reactome)
pBRArrowR-HSA-9698929 (Reactome)
pBRR-HSA-9698932 (Reactome)
pBRR-HSA-9698962 (Reactome)
pPR-AP:pAPArrowR-HSA-9698962 (Reactome)
pPR-AP:pAPR-HSA-9698923 (Reactome)
pPR-AP:pAPmim-catalysisR-HSA-9698929 (Reactome)
ppUL84:IE2-p86R-HSA-9698927 (Reactome)
Personal tools