BST2_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BST2_RAT
• UniProt AC: Q811A2
• Protein Name: Bone marrow stromal antigen 2
• Gene Name: Bst2
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 172
• Subcellular Localization: Golgi apparatus, trans-Golgi network. Cell membrane; Single-pass type II membrane protein. Cell membrane; Lipid-anchor, GPI-anchor. Late endosome. Membrane raft. Cytoplasm. Apical cell membrane. Shuttles between the cell membrane, where it is present
• Protein Description: IFN-induced antiviral host restriction factor which efficiently blocks the release of diverse mammalian enveloped viruses by directly tethering nascent virions to the membranes of infected cells. Acts as a direct physical tether, holding virions to the cell membrane and linking virions to each other. The tethered virions can be internalized by endocytosis and subsequently degraded or they can remain on the cell surface. In either case, their spread as cell-free virions is restricted. Its target viruses belong to diverse families, including retroviridae: human immunodeficiency virus type 1 (HIV-1), mouse mammary tumor virus (MMTV) and murine leukemia virus (MLV), filoviridae: ebola virus (EBOV), arenaviridae: lassa virus (LASV), and rhabdoviridae: vesicular stomatitis virus (VSV). Can inhibit cell surface proteolytic activity of MMP14 causing decreased activation of MMP15 which results in inhibition of cell growth and migration. Can stimulate signaling by LILRA4/ILT7 and consequently provide negative feedback to the production of IFN by plasmacytoid dendritic cells in response to viral infection (By similarity). Plays a role in the organization of the subapical actin cytoskeleton in polarized epithelial cells..
• Protein Sequence: MAPSFYHYLPVAMDERWEPKGWSIRRWWLVAAILVVLIGVVLVCLIVYFANAAHSEACKNGLRLQDECRNTTHLLKHQLTRAQDSLLQTEMQANSCNQTVMDLRDSLKKKVSQTQEQQARIKELENKIERLNQELENLRTQKEISTTVQVNSGGSVVVSSLLVLVAVLFLHF

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
4	Phosphorylation	----MAPSFYHYLPV ----CCCCCHHHCCC	28.97	25575281
6	Phosphorylation	--MAPSFYHYLPVAM --CCCCCHHHCCCCC	8.22	25575281
8	Phosphorylation	MAPSFYHYLPVAMDE CCCCCHHHCCCCCCC	11.00	25575281
70	N-linked_Glycosylation	RLQDECRNTTHLLKH CHHHHHHCHHHHHHH	62.07	-
97	N-linked_Glycosylation	EMQANSCNQTVMDLR HHHHHCCCCHHHHHH	40.14	-
106	Phosphorylation	TVMDLRDSLKKKVSQ HHHHHHHHHHHHHCH	35.34	29779826
122	Acetylation	QEQQARIKELENKIE HHHHHHHHHHHHHHH	51.17	22902405
127	Acetylation	RIKELENKIERLNQE HHHHHHHHHHHHHHH	36.25	22902405
152	GPI-anchor	STTVQVNSGGSVVVS CCEEEECCCCCHHHH	45.75	-

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

Oops, there are no upstream regulatory protein records of BST2_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BST2_RAT !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of BST2_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of BST2_RAT !!

Drug and Disease Associations

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