ICP27_HHV11 - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ICP27_HHV11
• UniProt AC: P10238
• Protein Name: mRNA export factor
• Gene Name: UL54
• Organism: Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
• Sequence Length: 512
• Subcellular Localization: Host cytoplasm . Host nucleus . Shuttles between the nucleus and the cytoplasm.
• Protein Description: Multifunctional regulator of the expression of viral genes that contributes to the shutoff of host protein synthesis and mediates nuclear export of viral intronless mRNAs. Early in infection, this immediate early (EI) protein mediates the inhibition of cellular splicing. This results in the accumulation of unprocessed 3'end pre-mRNAs which can't be exported from the nucleus. Cellular protein synthesis is thereby shut off early after virus infection. Later in the infection, it helps recruit cellular RNA polymerase II to viral replication sites and promotes the nuclear export of viral intronless mRNAs by interacting with mRNAs and host NXF1/TAP. ICP27 binds to NUP62 which may provide facilitated viral mRNA export and may indirectly compete with some host cell transport receptors for binding and inhibit cellular nucleocytoplasmic transport pathways. [PubMed: 22334672 Also stimulates translation of viral transcripts. Repression of host gene expression blocks the cell cycle at the G1 phase and prevents apoptosis. Seems to silence the 3' splice site of the promyelocytic leukemia (PML) intron 7a, thereby switching PML isoforms from PML-II to PML-V. This could be linked to the accelerated mRNA export induced by ICP27 which might not provide sufficient time for PML pre-mRNA to be spliced in the nucleus.]
• Protein Sequence: MATDIDMLIDLGLDLSDSDLDEDPPEPAESRRDDLESDSSGECSSSDEDMEDPHGEDGPEPILDAARPAVRPSRPEDPGVPSTQTPRPTERQGPNDPQPAPHSVWSRLGARRPSCSPEQHGGKVARLQPPPTKAQPARGGRRGRRRGRGRGGPGAADGLSDPRRRAPRTNRNPGGPRPGAGWTDGPGAPHGEAWRGSEQPDPPGGQRTRGVRQAPPPLMTLAIAPPPADPRAPAPERKAPAADTIDATTRLVLRSISERAAVDRISESFGRSAQVMHDPFGGQPFPAANSPWAPVLAGQGGPFDAETRRVSWETLVAHGPSLYRTFAGNPRAASTAKAMRDCVLRQENFIEALASADETLAWCKMCIHHNLPLRPQDPIIGTTAAVLDNLATRLRPFLQCYLKARGLCGLDELCSRRRLADIKDIASFVFVILARLANRVERGVAEIDYATLGVGVGEKMHFYLPGACMAGLIEILDTHRQECSSRVCELTASHIVAPPYVHGKYFYCNSLF

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
16	Phosphorylation	IDLGLDLSDSDLDED HHCCCCCCCCCCCCC	34.43	10074178
18	Phosphorylation	LGLDLSDSDLDEDPP CCCCCCCCCCCCCCC	36.38	10074178
114	Phosphorylation	RLGARRPSCSPEQHG HHCCCCCCCCHHHCC	25.97	10074178
138	Methylation	PTKAQPARGGRRGRR CCCCCCCCCCCCCCC	55.57	19321610
148	Methylation	RRGRRRGRGRGGPGA CCCCCCCCCCCCCCC	29.80	19321610
150	Methylation	GRRRGRGRGGPGAAD CCCCCCCCCCCCCCC	45.60	19321610

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
16	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
18	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
114	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ICP27_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 ICP27_HHV11 !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NXF1_HUMAN	NXF1	physical	15767397

Drug and Disease Associations

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