POL_HV1H2 - dbPTM
POL_HV1H2 - PTM Information in dbPTM
Basic Information of Protein
UniProt ID POL_HV1H2
UniProt AC P04585
Protein Name Gag-Pol polyprotein
Gene Name gag-pol
Organism Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1).
Sequence Length 1435
Subcellular Localization Gag-Pol polyprotein: Host cell membrane
Lipid-anchor . Host endosome, host multivesicular body . These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments ca
Protein Description Gag-Pol polyprotein: Mediates, with Gag 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). Gag-Pol polyprotein may regulate its own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, the polyprotein would promote translation, whereas at high concentration, the polyprotein would encapsidate genomic RNA and then shut off translation.; 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. [PubMed: 8648689 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]
Protein Sequence MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAADTGHSNQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVTNSATIMMQRGNFRNQRKIVKCFNCGKEGHTARNCRAPRKKGCWKCGKEGHQMKDCTERQANFLREDLAFLQGKAREFSSEQTRANSPTRRELQVWGRDNNSPSEAGADRQGTVSFNFPQVTLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPGRWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNFPISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFRKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGLTTPDKKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEEAELELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWEFVNTPPLVKLWYQLEKEPIVGAETFYVDGAANRETKLGKAGYVTNRGRQKVVTLTDTTNQKTELQAIYLALQDSGLEVNIVTDSQYALGIIQAQPDQSESELVNQIIEQLIKKEKVYLAWVPAHKGIGGNEQVDKLVSAGIRKVLFLDGIDKAQDEHEKYHSNWRAMASDFNLPPVVAKEIVASCDKCQLKGEAMHGQVDCSPGIWQLDCTHLEGKVILVAVHVASGYIEAEVIPAETGQETAYFLLKLAGRWPVKTIHTDNGSNFTGATVRAACWWAGIKQEFGIPYNPQSQGVVESMNKELKKIIGQVRDQAEHLKTAVQMAVFIHNFKRKGGIGGYSAGERIVDIIATDIQTKELQKQITKIQNFRVYYRDSRNPLWKGPAKLLWKGEGAVVIQDNSDIKVVPRRKAKIIRDYGKQMAGDDCVASRQDED
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 Orthologous
Protein Cluster
2Myristoylation------MGARASVLS
------CCCCEECCC
34.77-
132PhosphorylationSNQVSQNYPIVQNIQ
CCHHHCCCCEEECCC
6.16-
1405AcetylationIQDNSDIKVVPRRKA
ECCCCCCEEEECHHH
42.0220226045
1411AcetylationIKVVPRRKAKIIRDY
CEEEECHHHHHHHHH
56.1420226045
1413AcetylationVVPRRKAKIIRDYGK
EEECHHHHHHHHHHH
41.5220226045
1420AcetylationKIIRDYGKQMAGDDC
HHHHHHHHHHCCCCC
30.5820226045

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 POL_HV1H2 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of POL_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 POL_HV1H2 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
POL_HV1H2gag-polphysical
7542140
PSIP1_HUMANPSIP1physical
12407101
PSIP1_HUMANPSIP1physical
15895093
SNF5_HUMANSMARCB1physical
14963118
XRCC6_HUMANXRCC6physical
21454661
POL_HV1H2gag-polphysical
21454548
NFKB1_HUMANNFKB1physical
2017258
BCL2_HUMANBCL2physical
8790371
RAD18_HUMANRAD18physical
12016221
NEF_HV1H2nefphysical
15137387
PFD3_HUMANVBP1physical
17698809
VHL_HUMANVHLphysical
17698809
CUL2_HUMANCUL2physical
17698809
EED_HUMANEEDphysical
14610174
EP300_HUMANEP300physical
16096645
PSIP1_HUMANPSIP1physical
20016921
BTF3_HUMANBTF3physical
20016921
TR150_HUMANTHRAP3physical
20016921
HMGN2_HUMANHMGN2physical
20016921
RANB9_HUMANRANBP9physical
20016921
EIF3H_HUMANEIF3Hphysical
20016921
EF1A1_HUMANEEF1A1physical
20016921
ROA2_HUMANHNRNPA2B1physical
20016921
STMN1_HUMANSTMN1physical
20016921
RL23_HUMANRPL23physical
20016921
CCD32_HUMANC15orf57physical
20016921
EIF3D_HUMANEIF3Dphysical
22190034
VIME_HUMANVIMphysical
22944692
DAXX_HUMANDAXXphysical
21556766
EIF3F_HUMANEIF3Fphysical
22190034
EIF3C_HUMANEIF3Cphysical
22190034
EIF3A_HUMANEIF3Aphysical
22190034
EIF3L_HUMANEIF3Lphysical
22190034
EIF3K_HUMANEIF3Kphysical
22190034
UBR4_HUMANUBR4physical
22190034
OSBL3_HUMANOSBPL3physical
22190034
EIF3H_HUMANEIF3Hphysical
22190034
EIF3E_HUMANEIF3Ephysical
22190034
EIF3B_HUMANEIF3Bphysical
22190034
RUVB1_HUMANRUVBL1physical
22190034
PDIA4_HUMANPDIA4physical
22190034
NFU1_HUMANNFU1physical
22190034
SUCB1_HUMANSUCLA2physical
22190034
PDIA6_HUMANPDIA6physical
22190034
MCM7_HUMANMCM7physical
22190034
PELO_HUMANPELOphysical
22190034
RCN1_HUMANRCN1physical
22190034
CCAR2_HUMANCCAR2physical
22190034
TYSD1_HUMANTYSND1physical
22190034
EIF3I_HUMANEIF3Iphysical
22190034
HEMH_HUMANFECHphysical
22190034
RECQ1_HUMANRECQLphysical
22190034
LG3BP_HUMANLGALS3BPphysical
22190034
LIMD1_HUMANLIMD1physical
22190034
EIF3G_HUMANEIF3Gphysical
22190034
CATB_HUMANCTSBphysical
22190034
RIR2_HUMANRRM2physical
22190034
PSIP1_HUMANPSIP1physical
22190034
MCM4_HUMANMCM4physical
22190034
GRB2_HUMANGRB2physical
22190034
PP2AB_HUMANPPP2CBphysical
22190034
MCM6_HUMANMCM6physical
22190034
ANC2_HUMANANAPC2physical
22190034
NUDC_HUMANNUDCphysical
22190034
IDH3A_HUMANIDH3Aphysical
22190034
ARRB2_HUMANARRB2physical
22190034
POL_HV1H2gag-polphysical
22190034
SSA27_HUMANSSSCA1physical
22190034
GOGA1_HUMANGOLGA1physical
22190034
DPOE3_HUMANPOLE3physical
22190034
DPOE1_HUMANPOLEphysical
22190034
HGH1_HUMANHGH1physical
22190034
SF3A3_HUMANSF3A3physical
22190034
HERC2_HUMANHERC2physical
22190034
FNIP1_HUMANFNIP1physical
22190034
DIAP1_HUMANDIAPH1physical
22190034
FLCN_HUMANFLCNphysical
22190034
DPOE4_HUMANPOLE4physical
22190034
EIF3M_HUMANEIF3Mphysical
22190034
IF122_HUMANIFT122physical
22190034
ARHGC_HUMANARHGEF12physical
22190034
DOHH_HUMANDOHHphysical
22190034
EPIPL_HUMANEPPK1physical
22190034
TRPS1_HUMANTRPS1physical
22190034
PFD3_HUMANVBP1physical
22190034
FOXC1_HUMANFOXC1physical
22190034
ALMS1_HUMANALMS1physical
22190034
OSBL6_HUMANOSBPL6physical
22190034
SYSC_HUMANSARSphysical
22190034
CARM1_HUMANCARM1physical
22190034
EST1A_HUMANSMG6physical
22190034
PUM2_HUMANPUM2physical
22190034
APC1_HUMANANAPC1physical
22190034
MSH2_HUMANMSH2physical
22190034
PARP4_HUMANPARP4physical
22190034
AKAP9_HUMANAKAP9physical
22190034
DOK1_HUMANDOK1physical
22190034
MCL1_HUMANMCL1physical
22190034
FAD1_HUMANFLAD1physical
22190034
SAHH_HUMANAHCYphysical
22190034
BICD2_HUMANBICD2physical
22190034
FKBP4_HUMANFKBP4physical
22190034
GAK_HUMANGAKphysical
22190034
NFAT5_HUMANNFAT5physical
22190034
EMAL3_HUMANEML3physical
22190034
NHRF1_HUMANSLC9A3R1physical
22190034
VIR_HUMANKIAA1429physical
22190034
KCRU_HUMANCKMT1Bphysical
22190034
UN45A_HUMANUNC45Aphysical
22190034
PLOD1_HUMANPLOD1physical
22190034
MIP18_HUMANFAM96Bphysical
22190034
CAND2_HUMANCAND2physical
22190034
UBA1_HUMANUBA1physical
22190034
HDDC2_HUMANHDDC2physical
22190034
WDR61_HUMANWDR61physical
22190034
PLAP_HUMANPLAAphysical
22190034
HEAT1_HUMANHEATR1physical
22190034
RNBP6_HUMANRANBP6physical
22190034
1433E_HUMANYWHAEphysical
22190034
CIAO1_HUMANCIAO1physical
22190034
1433B_HUMANYWHABphysical
22190034
ZNT7_HUMANSLC30A7physical
22190034
IPO4_HUMANIPO4physical
22190034
PLOD2_HUMANPLOD2physical
22190034
1433Z_HUMANYWHAZphysical
22190034
1433G_HUMANYWHAGphysical
22190034
DESP_HUMANDSPphysical
22190034
KAT2A_HUMANKAT2Aphysical
20226045

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of POL_HV1H2

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Related Literatures of Post-Translational Modification

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