dbPTM

ENV_HV1H2 - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ENV_HV1H2
UniProt AC	P04578
Protein Name	Envelope glycoprotein gp160 {ECO:0000255\|HAMAP-Rule:MF_04083}
Gene Name	env {ECO:0000255\|HAMAP-Rule:MF_04083}
Organism	Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1).
Sequence Length	856
Subcellular Localization	Surface protein gp120: Virion membrane Peripheral membrane protein . Host cell membrane Peripheral membrane protein . Host endosome membrane Single-pass type I membrane protein . The surface protein is not anchored to the viral envelope, but as
Protein Description	Envelope glycoprotein gp160: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41.; Surface protein gp120: Attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. Acts as a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. HIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells.; Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm..
Protein Sequence	MRVKEKYQHLWRWGWRWGTMLLGMLMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYKLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSVNFTDNAKTIIVQLNTSVEINCTRPNNNTRKRIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWNNTLKQIASKLREQFGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTITLPCRIKQIINMWQKVGKAMYAPPISGQIRCSSNITGLLLTRDGGNSNNESEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEQIWNHTTWMEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWFNITNWLWYIKLFIMIVGGLVGLRIVFAVLSIVNRVRQGYSPLSFQTHLPTPRGPDRPEGIEEEGGERDRDRSIRLVNGSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQGACRAIRHIPRRIRQGLERILL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
88	N-linked_Glycosylation	PQEVVLVNVTENFNM CCCEEEEEEECCCCH	30.72	26972002
136	N-linked_Glycosylation	LKCTDLKNDTNTNSS EEECCCCCCCCCCCH	69.50	UniProtKB CARBOHYD
141	N-linked_Glycosylation	LKNDTNTNSSSGRMI CCCCCCCCCHHCCEE	41.80	UniProtKB CARBOHYD
156	N-linked_Glycosylation	MEKGEIKNCSFNIST EECCCEEEEEEEEEH	32.12	26972002
160	N-linked_Glycosylation	EIKNCSFNISTSIRG CEEEEEEEEEHHHCC	15.82	26972002
186	N-linked_Glycosylation	LDIIPIDNDTTSYKL EEEEEECCCCCCEEE	49.61	UniProtKB CARBOHYD
197	N-linked_Glycosylation	SYKLTSCNTSVITQA CEEEECCCCHHHCCC	34.85	14981267
230	N-linked_Glycosylation	FAILKCNNKTFNGTG EEEEEECCEEECCCC	54.97	UniProtKB CARBOHYD
234	N-linked_Glycosylation	KCNNKTFNGTGPCTN EECCEEECCCCCCCC	52.96	26972002
241	N-linked_Glycosylation	NGTGPCTNVSTVQCT CCCCCCCCCCEEECC	32.24	UniProtKB CARBOHYD
262	N-linked_Glycosylation	VSTQLLLNGSLAEEE EEEEEEECCCCCCCE	37.67	14981267
276	N-linked_Glycosylation	EVVIRSVNFTDNAKT EEEEEEEECCCCCEE	35.03	14981267
289	N-linked_Glycosylation	KTIIVQLNTSVEINC EEEEEEECCEEEEEE	17.14	9641677
295	N-linked_Glycosylation	LNTSVEINCTRPNNN ECCEEEEEECCCCCC	13.96	14981267
301	N-linked_Glycosylation	INCTRPNNNTRKRIR EEECCCCCCCCCEEE	54.66	UniProtKB CARBOHYD
332	N-linked_Glycosylation	NMRQAHCNISRAKWN CCCHHHCCCCHHHHH	25.96	9641677
339	N-linked_Glycosylation	NISRAKWNNTLKQIA CCCHHHHHHHHHHHH	30.79	9641677
356	N-linked_Glycosylation	LREQFGNNKTIIFKQ HHHHHCCCCEEEEEC	43.13	19965434
386	N-linked_Glycosylation	GGEFFYCNSTQLFNS CCEEEEECCCCCCCC	36.39	9641677
392	N-linked_Glycosylation	CNSTQLFNSTWFNST ECCCCCCCCCCCCCC	47.31	14981267
397	N-linked_Glycosylation	LFNSTWFNSTWSTEG CCCCCCCCCCCCCCC	30.05	UniProtKB CARBOHYD
406	N-linked_Glycosylation	TWSTEGSNNTEGSDT CCCCCCCCCCCCCCE	71.01	UniProtKB CARBOHYD
448	N-linked_Glycosylation	GQIRCSSNITGLLLT CEEEECCCCCEEEEE	21.39	14981267
463	N-linked_Glycosylation	RDGGNSNNESEIFRP CCCCCCCCCCCCCCC	54.73	11188697
611	N-linked_Glycosylation	CTTAVPWNASWSNKS EEECCCCCCCCCCCC	20.30	26972002
616	N-linked_Glycosylation	PWNASWSNKSLEQIW CCCCCCCCCCHHHHH	31.51	UniProtKB CARBOHYD
624	N-linked_Glycosylation	KSLEQIWNHTTWMEW CCHHHHHCCCCHHHH	25.02	UniProtKB CARBOHYD
637	N-linked_Glycosylation	EWDREINNYTSLIHS HHHHHHHHHHHHHHH	47.31	26972002
674	N-linked_Glycosylation	ASLWNWFNITNWLWY HHHHHHHHHHHHHHH	31.61	UniProtKB CARBOHYD
764	S-palmitoylation	WDDLRSLCLFSYHRL HHCHHHHHHHCHHHH	3.67	7568235
837	S-palmitoylation	IEVVQGACRAIRHIP HHHHHHHHHHHHHHH	3.74	7568235

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
Oops, there are no upstream regulatory protein records of ENV_HV1H2 !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ENV_HV1H2 !!

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 ENV_HV1H2 !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CD4_HUMAN	CD4	physical	1605591
CD4_HUMAN	CD4	physical	2076345
FINC_HUMAN	FN1	physical	8173552
CD4_HUMAN	CD4	physical	15321703
CD4_HUMAN	CD4	physical	2461565
M3K7_HUMAN	MAP3K7	physical	22341466
CD4_HUMAN	CD4	physical	12218052
GANAB_HUMAN	GANAB	physical	22190034
DJB11_HUMAN	DNAJB11	physical	22190034
ERLEC_HUMAN	ERLEC1	physical	22190034
LMAN1_HUMAN	LMAN1	physical	22190034
SDF2L_HUMAN	SDF2L1	physical	22190034
SE1L1_HUMAN	SEL1L	physical	22190034
GLU2B_HUMAN	PRKCSH	physical	22190034
SDF2_HUMAN	SDF2	physical	22190034
CALR_HUMAN	CALR	physical	22190034
CKAP4_HUMAN	CKAP4	physical	22190034
SUN1_HUMAN	SUN1	physical	22190034
UGGG1_HUMAN	UGGT1	physical	22190034
ITM2B_HUMAN	ITM2B	physical	22190034
CALX_HUMAN	CANX	physical	22190034
VDAC2_HUMAN	VDAC2	physical	22190034
PSA1_HUMAN	PSMA1	physical	22190034
PHB_HUMAN	PHB	physical	22190034
COX41_HUMAN	COX4I1	physical	22190034
RPN1_HUMAN	RPN1	physical	22190034
AT2A2_HUMAN	ATP2A2	physical	22190034
PDIA1_HUMAN	P4HB	physical	22190034
PGRC1_HUMAN	PGRMC1	physical	22190034
PON2_HUMAN	PON2	physical	22190034
OS9_HUMAN	OS9	physical	22190034
ATLA3_HUMAN	ATL3	physical	22190034
SEH1_HUMAN	SEH1L	physical	22190034
CAF1B_HUMAN	CHAF1B	physical	22190034
DSC3_HUMAN	DSC3	physical	22190034
GCP60_HUMAN	ACBD3	physical	22190034
PDIA3_HUMAN	PDIA3	physical	22190034
SSRD_HUMAN	SSR4	physical	22190034
A4_HUMAN	APP	physical	22190034
CAN1_HUMAN	CAPN1	physical	22190034
LMAN2_HUMAN	LMAN2	physical	22190034
FUT8_HUMAN	FUT8	physical	22190034
NGLY1_HUMAN	NGLY1	physical	22190034
ITB2_HUMAN	ITGB2	physical	22190034
ITAL_HUMAN	ITGAL	physical	22190034
1C07_HUMAN	HLA-C	physical	22190034
S61A1_HUMAN	SEC61A1	physical	22190034
1A02_HUMAN	HLA-A	physical	22190034
1A03_HUMAN	HLA-A	physical	22190034
1A01_HUMAN	HLA-A	physical	22190034
1A26_HUMAN	HLA-A	physical	22190034
CLGN_HUMAN	CLGN	physical	22190034
DHC24_HUMAN	DHCR24	physical	22190034
CATD_HUMAN	CTSD	physical	22190034
LDLR_HUMAN	LDLR	physical	22190034
TM38B_HUMAN	TMEM38B	physical	22190034
RHOC_HUMAN	RHOC	physical	22190034
HS105_HUMAN	HSPH1	physical	22190034
CLN6_HUMAN	CLN6	physical	22190034
ERGI2_HUMAN	ERGIC2	physical	22190034
AP1M1_HUMAN	AP1M1	physical	22190034
CH3L2_HUMAN	CHI3L2	physical	22190034
KI3L2_HUMAN	KIR3DL2	physical	22190034
HM13_HUMAN	HM13	physical	22190034
CT024_HUMAN	C20orf24	physical	22190034
RNF5_HUMAN	RNF5	physical	22190034
FLOT1_HUMAN	FLOT1	physical	22190034
AT2A3_HUMAN	ATP2A3	physical	22190034
MESD_HUMAN	MESDC2	physical	22190034
ERGI3_HUMAN	ERGIC3	physical	22190034
KI3L1_HUMAN	KIR3DL1	physical	22190034
VDAC1_HUMAN	VDAC1	physical	22190034
PSB6_HUMAN	PSMB6	physical	22190034
1B07_HUMAN	HLA-B	physical	22190034
1B18_HUMAN	HLA-B	physical	22190034
HYOU1_HUMAN	HYOU1	physical	22190034
CAB45_HUMAN	SDF4	physical	22190034
CALU_HUMAN	CALU	physical	22190034
ENPL_HUMAN	HSP90B1	physical	22190034
RCN2_HUMAN	RCN2	physical	22190034
LSM12_HUMAN	LSM12	physical	22190034
SUMF2_HUMAN	SUMF2	physical	22190034
TXND5_HUMAN	TXNDC5	physical	22190034
SERPH_HUMAN	SERPINH1	physical	22190034
GT251_HUMAN	COLGALT1	physical	22190034
MAGT1_HUMAN	MAGT1	physical	22190034
EDEM3_HUMAN	EDEM3	physical	22190034
HSP76_HUMAN	HSPA6	physical	22190034
DNJC3_HUMAN	DNAJC3	physical	22190034
ITA4_HUMAN	ITGA4	physical	22190034
MOGS_HUMAN	MOGS	physical	22190034
RN126_HUMAN	RNF126	physical	22190034
PDIA5_HUMAN	PDIA5	physical	22190034
TMM43_HUMAN	TMEM43	physical	22190034
TOR1A_HUMAN	TOR1A	physical	22190034
HSP13_HUMAN	HSPA13	physical	22190034
DDX6_HUMAN	DDX6	physical	22190034
CASC3_HUMAN	CASC3	physical	22190034
FBLN3_HUMAN	EFEMP1	physical	22190034
MCRI2_HUMAN	FAM195A	physical	22190034
TAB2_HUMAN	TAB2	physical	22190034
G3BP2_HUMAN	G3BP2	physical	22190034
TOIP2_HUMAN	TOR1AIP2	physical	22190034
IFG15_HUMAN	TOR1AIP2	physical	22190034
ERP44_HUMAN	ERP44	physical	22190034
PSMD7_HUMAN	PSMD7	physical	22190034
F133B_HUMAN	FAM133B	physical	22190034
P4HA2_HUMAN	P4HA2	physical	22190034
G3BP1_HUMAN	G3BP1	physical	22190034
PSD11_HUMAN	PSMD11	physical	22190034
H31_HUMAN	HIST1H3A	physical	22190034
EVL_HUMAN	EVL	physical	22190034
TIM13_HUMAN	TIMM13	physical	22190034
PHB2_HUMAN	PHB2	physical	22190034
ENDD1_HUMAN	ENDOD1	physical	22190034
HACD3_HUMAN	PTPLAD1	physical	22190034
TERA_HUMAN	VCP	physical	22190034
STML2_HUMAN	STOML2	physical	22190034
VDAC3_HUMAN	VDAC3	physical	22190034
SPAG5_HUMAN	SPAG5	physical	22190034
TIM8A_HUMAN	TIMM8A	physical	22190034
CX6B1_HUMAN	COX6B1	physical	22190034
VAPA_HUMAN	VAPA	physical	22190034
SPCS3_HUMAN	SPCS3	physical	22190034
SURF4_HUMAN	SURF4	physical	22190034
TIM8B_HUMAN	TIMM8B	physical	22190034
PI42A_HUMAN	PIP4K2A	physical	22190034
EMC1_HUMAN	EMC1	physical	22190034
PLS1_HUMAN	PLSCR1	physical	22190034
MMGT1_HUMAN	MMGT1	physical	22190034
PRDX4_HUMAN	PRDX4	physical	22190034
RBGP1_HUMAN	RABGAP1	physical	22190034
BAP31_HUMAN	BCAP31	physical	22190034
SPCS2_HUMAN	SPCS2	physical	22190034
K2013_HUMAN	KIAA2013	physical	22190034
NDUBA_HUMAN	NDUFB10	physical	22190034
COX5A_HUMAN	COX5A	physical	22190034
FBX6_HUMAN	FBXO6	physical	22190034
VTI1A_HUMAN	VTI1A	physical	22190034
TOM40_HUMAN	TOMM40	physical	22190034
GSLG1_HUMAN	GLG1	physical	22190034
SEC62_HUMAN	SEC62	physical	22190034
RER1_HUMAN	RER1	physical	22190034
PDIA1_HUMAN	P4HB	physical	14592831
LCK_HUMAN	LCK	physical	14592831
TFR1_HUMAN	TFRC	physical	14592831
SQSTM_HUMAN	SQSTM1	physical	11563677
PRS8_HUMAN	PSMC5	physical	10776788
SQSTM_HUMAN	SQSTM1	physical	10776788
CD4_HUMAN	CD4	physical	24156545
CH60_HUMAN	HSPD1	physical	10499815
SQSTM_HUMAN	SQSTM1	physical	10397530
TLR2_HUMAN	TLR2	physical	26347747
TLR1_HUMAN	TLR1	physical	26347747

Drug and Disease Associations

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

Regulatory Network of ENV_HV1H2

Related Literatures of Post-Translational Modification

Palmitoylation
Reference	PubMed
"The human and simian immunodeficiency virus envelope glycoproteintransmembrane subunits are palmitoylated."; Yang C., Spies C.P., Compans R.W.; Proc. Natl. Acad. Sci. U.S.A. 92:9871-9875(1995). Cited for: PALMITOYLATION, AND MUTAGENESIS OF CYS-764 AND CYS-837.	7568235 [Abstract]