GAG_HV2BE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GAG_HV2BE
• UniProt AC: P18095
• Protein Name: Gag polyprotein
• Gene Name: gag
• Organism: Human immunodeficiency virus type 2 subtype A (isolate BEN) (HIV-2).
• Sequence Length: 521
• Subcellular Localization: Gag polyprotein: Host cell membrane ; Lipid-anchor . Host endosome, host multivesicular body . These locations are probably linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartme
• Protein Description: Gag polyprotein: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi).; Matrix protein p17: Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus (By similarity). Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA (By similarity).; Capsid protein p24: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (By similarity). Host restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species. Host PIN1 apparently facilitates the virion uncoating (By similarity). On the other hand, interactions with PDZD8 or CYPA stabilize the capsid (By similarity).; Nucleocapsid protein p7: Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly.; p6-gag: Plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1..
• Protein Sequence: MGARNSVLRGKKADELEKVRLRPGGKKKYRLKHIVWAANELDKFGLAESLLESKEGCQKILRVLDPLVPTGSENLKSLFNTVCVIWCLHAEEKVKDTEEAKKLAQRHLVAETGTAEKMPNTSRPTAPPSGKRGNYPVQQAGGNYVHVPLSPRTLNAWVKLVEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINEEAADWDSQHPIPGPLPAGQLRDPRGSDIAGTTSTVDEQIQWMYRPQNPVPVGNIYRRWIQIGLQKCVRKYNPTNILDIKQGPKEPFQSYVDRFYKSLRAEQTDPAVKNWMTQTLLIQNANPDCKLVLKGLGMNPTLEEMLTACQGVGGPGQKARLMAEALKEAMGPSPIPFAAAQQRKAIRYWNCGKEGHSARQCRAPRRQGCWKCGKPGHIMANCPERQAGFLGLGPRGKKPRNFPVTQAPQGLIPTAPPADPAAELLERYMQQGRKQREQRERPYKEVTEDLLHLEQRETPHREETEDLLHLNSLFGKDQ

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
2	Myristoylation	------MGARNSVLR ------CCCCCHHHC	32.99	-
150	Phosphorylation	NYVHVPLSPRTLNAW CEEECCCCHHHHHHH	13.28	-

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
150	S	Phosphorylation	Kinase	MAPK1	-	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of GAG_HV2BE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of GAG_HV2BE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TS101_HUMAN	TSG101	physical	12388682
UBC_HUMAN	UBC	physical	12388682
EF1A1_HUMAN	EEF1A1	physical	15452250
TS101_HUMAN	TSG101	physical	15452250
PRP4_HUMAN	PRPF4	physical	15452250

Drug and Disease Associations

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