dbPTM

PVR_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PVR_HUMAN
UniProt AC	P15151
Protein Name	Poliovirus receptor
Gene Name	PVR
Organism	Homo sapiens (Human).
Sequence Length	417
Subcellular Localization	Isoform Alpha: Cell membrane Single-pass type I membrane protein. Isoform Delta: Cell membrane Single-pass type I membrane protein. Isoform Beta: Secreted. Isoform Gamma: Secreted.
Protein Description	Mediates NK cell adhesion and triggers NK cell effector functions. Binds two different NK cell receptors: CD96 and CD226. These interactions accumulates at the cell-cell contact site, leading to the formation of a mature immunological synapse between NK cell and target cell. This may trigger adhesion and secretion of lytic granules and IFN-gamma and activate cytoxicity of activated NK cells. May also promote NK cell-target cell modular exchange, and PVR transfer to the NK cell. This transfer is more important in some tumor cells expressing a lot of PVR, and may trigger fratricide NK cell activation, providing tumors with a mechanism of immunoevasion. Plays a role in mediating tumor cell invasion and migration.; (Microbial infection) Acts as a receptor for poliovirus. May play a role in axonal transport of poliovirus, by targeting virion-PVR-containing endocytic vesicles to the microtubular network through interaction with DYNLT1. This interaction would drive the virus-containing vesicle to the axonal retrograde transport.; (Microbial infection) Acts as a receptor for Pseudorabies virus.; (Microbial infection) Is prevented to reach cell surface upon infection by Human cytomegalovirus /HHV-5, presumably to escape immune recognition of infected cell by NK cells..
Protein Sequence	MARAMAAAWPLLLVALLVLSWPPPGTGDVVVQAPTQVPGFLGDSVTLPCYLQVPNMEVTHVSQLTWARHGESGSMAVFHQTQGPSYSESKRLEFVAARLGAELRNASLRMFGLRVEDEGNYTCLFVTFPQGSRSVDIWLRVLAKPQNTAEVQKVQLTGEPVPMARCVSTGGRPPAQITWHSDLGGMPNTSQVPGFLSGTVTVTSLWILVPSSQVDGKNVTCKVEHESFEKPQLLTVNLTVYYPPEVSISGYDNNWYLGQNEATLTCDARSNPEPTGYNWSTTMGPLPPFAVAQGAQLLIRPVDKPINTTLICNVTNALGARQAELTVQVKEGPPSEHSGISRNAIIFLVLGILVFLILLGIGIYFYWSKCSREVLWHCHLCPSSTEHASASANGHVSYSAVSRENSSSQDPQTEGTR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
90	Ubiquitination	GPSYSESKRLEFVAA CCCCCHHHHHHHHHH	57.88	2190698
90 (in isoform 4)	Ubiquitination	-	57.88	21906983
90 (in isoform 3)	Ubiquitination	-	57.88	21906983
90 (in isoform 2)	Ubiquitination	-	57.88	21906983
90 (in isoform 1)	Ubiquitination	-	57.88	21906983
105	N-linked_Glycosylation	RLGAELRNASLRMFG HHHHHHHHCEEEECC	46.64	10618374
105	N-linked_Glycosylation	RLGAELRNASLRMFG HHHHHHHHCEEEECC	46.64	7914388
120	N-linked_Glycosylation	LRVEDEGNYTCLFVT EEEEECCCEEEEEEE	27.22	7914388
120	N-linked_Glycosylation	LRVEDEGNYTCLFVT EEEEECCCEEEEEEE	27.22	7914388
153	Ubiquitination	QNTAEVQKVQLTGEP CCCCCEEEEEECCCC	36.80	-
188	N-linked_Glycosylation	SDLGGMPNTSQVPGF CCCCCCCCCCCCCCC	43.39	UniProtKB CARBOHYD
218	N-linked_Glycosylation	SSQVDGKNVTCKVEH HHHCCCCCCEEEEEC	39.60	UniProtKB CARBOHYD
227	Phosphorylation	TCKVEHESFEKPQLL EEEEECCCCCCCEEE	40.38	27794612
237	N-linked_Glycosylation	KPQLLTVNLTVYYPP CCEEEEEEEEEECCC	25.43	UniProtKB CARBOHYD
278	N-linked_Glycosylation	NPEPTGYNWSTTMGP CCCCCCCCCCCCCCC	27.80	16335952
307	N-linked_Glycosylation	RPVDKPINTTLICNV EECCCCCCEEEEEEE	35.22	19159218
313	N-linked_Glycosylation	INTTLICNVTNALGA CCEEEEEEECCCCCC	36.33	UniProtKB CARBOHYD
352 (in isoform 3)	N-linked_Glycosylation	-	2.31	16335952
360 (in isoform 2)	N-linked_Glycosylation	-	16.78	16335952
398	Phosphorylation	SANGHVSYSAVSREN HCCCCCCEEEEECCC	10.28	22171320
402	Phosphorylation	HVSYSAVSRENSSSQ CCCEEEEECCCCCCC	33.33	25137130
405	N-linked_Glycosylation	YSAVSRENSSSQDPQ EEEEECCCCCCCCCC	46.19	16335952
406	Phosphorylation	SAVSRENSSSQDPQT EEEECCCCCCCCCCC	26.98	23401153
407	Phosphorylation	AVSRENSSSQDPQTE EEECCCCCCCCCCCC	43.53	30266825
408	Phosphorylation	VSRENSSSQDPQTEG EECCCCCCCCCCCCC	38.12	30266825
413	Phosphorylation	SSSQDPQTEGTR--- CCCCCCCCCCCC---	41.59	29396449
416	Phosphorylation	QDPQTEGTR------ CCCCCCCCC------	27.29	-

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	MARCHF9	Q86YJ5	PMID:19457934

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PVR_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of PVR_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NECT3_HUMAN	PVRL3	physical	12759359
DYLT1_HUMAN	DYNLT1	physical	11751937
AP1M2_HUMAN	AP1M2	physical	11573956
ZCCHV_HUMAN	ZC3HAV1	physical	22939629
WNK1_HUMAN	WNK1	physical	21988832
ZNT2_HUMAN	SLC30A2	physical	25416956
KR107_HUMAN	KRTAP10-7	physical	25416956
KR109_HUMAN	KRTAP10-9	physical	25416956
KR108_HUMAN	KRTAP10-8	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
NT2NL_HUMAN	NOTCH2NL	physical	25416956
NLRX1_HUMAN	NLRX1	physical	28514442
CO4A_HUMAN	C4A	physical	28514442
UBE2C_HUMAN	UBE2C	physical	28514442
RYK_HUMAN	RYK	physical	28514442
CDON_HUMAN	CDON	physical	28514442
P4K2A_HUMAN	PI4K2A	physical	28514442
RAB5B_HUMAN	RAB5B	physical	28514442
LRBA_HUMAN	LRBA	physical	28514442
FXL20_HUMAN	FBXL20	physical	28514442
GNPAT_HUMAN	GNPAT	physical	28514442
MMS22_HUMAN	MMS22L	physical	28514442
MTCH2_HUMAN	MTCH2	physical	28514442
XPO6_HUMAN	XPO6	physical	28514442
QSOX1_HUMAN	QSOX1	physical	28514442
ATR_HUMAN	ATR	physical	28514442
XYLK_HUMAN	FAM20B	physical	28514442
GPDM_HUMAN	GPD2	physical	28514442
PPM1B_HUMAN	PPM1B	physical	28514442
LANC2_HUMAN	LANCL2	physical	28514442
ALG5_HUMAN	ALG5	physical	28514442
UBP30_HUMAN	USP30	physical	28514442
ARV1_HUMAN	ARV1	physical	28514442
GNA13_HUMAN	GNA13	physical	28514442
CISD2_HUMAN	CISD2	physical	28514442
MAP2_HUMAN	METAP2	physical	28514442
XPO5_HUMAN	XPO5	physical	28514442
TNFL9_HUMAN	TNFSF9	physical	28514442
HELLS_HUMAN	HELLS	physical	28514442
ALG11_HUMAN	ALG11	physical	28514442
ULBP3_HUMAN	ULBP3	physical	28514442
STAT3_HUMAN	STAT3	physical	28514442
RFC3_HUMAN	RFC3	physical	28514442
EFNB1_HUMAN	EFNB1	physical	28514442
RETR2_HUMAN	FAM134A	physical	28514442

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.

Regulatory Network of PVR_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD."; Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; Mol. Cell. Proteomics 0:0-0(2011). Cited for: GLYCOSYLATION AT ASN-120, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY.	22171320 [Abstract]
"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-307, AND MASSSPECTROMETRY.	19159218 [Abstract]
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-278, GLYCOSYLATION [LARGESCALE ANALYSIS] AT ASN-360 (ISOFORM BETA), AND MASS SPECTROMETRY.	16335952 [Abstract]