BST2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BST2_HUMAN
• UniProt AC: Q10589
• Protein Name: Bone marrow stromal antigen 2
• Gene Name: BST2
• Organism: Homo sapiens (Human).
• Sequence Length: 180
• 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 pre
• 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), human immunodeficiency virus type 2 (HIV-2), simian immunodeficiency viruses (SIVs), equine infectious anemia virus (EIAV), feline immunodeficiency virus (FIV), prototype foamy virus (PFV), Mason-Pfizer monkey virus (MPMV), human T-cell leukemia virus type 1 (HTLV-1), Rous sarcoma virus (RSV) and murine leukemia virus (MLV), flavivirideae: hepatitis C virus (HCV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), arenaviridae: lassa virus (LASV) and machupo virus (MACV), herpesviridae: kaposis sarcoma-associated herpesvirus (KSHV), rhabdoviridae: vesicular stomatitis virus (VSV), orthomyxoviridae: influenza A virus, and paramyxoviridae: nipah virus. 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. [PubMed: 19564354]
• Protein Sequence: MASTSYDYCRVPMEDGDKRCKLLLGIGILVLLIIVILGVPLIIFTIKANSEACRDGLRAVMECRNVTHLLQQELTEAQKGFQDVEAQAATCNHTVMALMASLDAEKAQGQKKVEELEGEITTLNHKLQDASAEVERLRRENQVLSVRIADKKYYPSSQDSSSAAAPQLLIVLLGLSALLQ

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
3	Phosphorylation	-----MASTSYDYCR -----CCCCCCCEEC	19.31	21815630
4	Phosphorylation	----MASTSYDYCRV ----CCCCCCCEECC	23.05	28796482
5	Phosphorylation	---MASTSYDYCRVP ---CCCCCCCEECCC	17.32	28796482
6	Phosphorylation	--MASTSYDYCRVPM --CCCCCCCEECCCC	15.83	28796482
8	Phosphorylation	MASTSYDYCRVPMED CCCCCCCEECCCCCC	3.64	28796482
18	Ubiquitination	VPMEDGDKRCKLLLG CCCCCCCHHHHHHHH	66.29	20419159
65	N-linked_Glycosylation	RAVMECRNVTHLLQQ HHHHHHHCHHHHHHH	55.48	19737401
65	N-linked_Glycosylation	RAVMECRNVTHLLQQ HHHHHHHCHHHHHHH	55.48	19349973
92	N-linked_Glycosylation	EAQAATCNHTVMALM HHHHHCCCHHHHHHH	29.52	19737401
112	Sumoylation	EKAQGQKKVEELEGE HHHHCCHHHHHHHHH	47.17	-
112	Sumoylation	EKAQGQKKVEELEGE HHHHCCHHHHHHHHH	47.17	-
112	Ubiquitination	EKAQGQKKVEELEGE HHHHCCHHHHHHHHH	47.17	-
121	O-linked_Glycosylation	EELEGEITTLNHKLQ HHHHHHHHHHHHHHH	22.41	55831799
122	O-linked_Glycosylation	ELEGEITTLNHKLQD HHHHHHHHHHHHHHH	31.09	55831803
126	Ubiquitination	EITTLNHKLQDASAE HHHHHHHHHHHHHHH	46.93	-
131	Phosphorylation	NHKLQDASAEVERLR HHHHHHHHHHHHHHH	33.00	26657352
131	O-linked_Glycosylation	NHKLQDASAEVERLR HHHHHHHHHHHHHHH	33.00	63752265
151	Ubiquitination	LSVRIADKKYYPSSQ EEEEECCCCCCCCCC	33.38	-
161	GPI-anchor	YPSSQDSSSAAAPQL CCCCCCCCCCHHHHH	32.08	-

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
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:24658274
-	K	Ubiquitination	E3 ubiquitin ligase	K5	P90489	PMID:22199232

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BST2_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FBW1A_HUMAN	BTRC	physical	20980512
TFR1_HUMAN	TFRC	physical	20980512
FBW1A_HUMAN	BTRC	physical	19730691
GLO2_HUMAN	HAGH	physical	21988832
SYHM_HUMAN	HARS2	physical	21988832

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-65, AND MASS SPECTROMETRY.
PubMed: 19349973

"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-65, AND MASS SPECTROMETRY.
PubMed: 19159218

"Tetherin inhibits HIV-1 release by directly tethering virions tocells.";
Perez-Caballero D., Zang T., Ebrahimi A., McNatt M.W., Gregory D.A.,Johnson M.C., Bieniasz P.D.;
Cell 139:499-511(2009).
Cited for: FUNCTION IN HIV-1 INFECTION, GLYCOSYLATION AT ASN-65 AND ASN-92,SUBCELLULAR LOCATION, DISULFIDE BONDS, SUBUNIT, TOPOLOGY, GPI-ANCHOR,AND MUTAGENESIS OF ASN-65 AND ASN-92.
PubMed: 19879838

Ubiquitylation

"The RING-CH ligase K5 antagonizes restriction of KSHV and HIV-1particle release by mediating ubiquitin-dependent endosomaldegradation of tetherin.";
Pardieu C., Vigan R., Wilson S.J., Calvi A., Zang T., Bieniasz P.,Kellam P., Towers G.J., Neil S.J.;
PLoS Pathog. 6:E1000843-E1000843(2010).
Cited for: FUNCTION IN KSHV AND HIV-1 INFECTION, SUBCELLULAR LOCATION,MUTAGENESIS OF LYS-18 AND LYS-21, AND UBIQUITINATION AT LYS-18 BY KSHVIRUS E3 UBIQUITIN-PROTEIN LIGASE K5.
PubMed: 20419159