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Protein

Gag polyprotein

Gene

gag

Organism
Human immunodeficiency virus type 1 group M subtype B (isolate NY5) (HIV-1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Gag polyprotein: Mediates, with Gag-Pol polyrotein, 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).By similarity
Matrix protein p17: Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus (PubMed:16840558). Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA (PubMed:23552424).By similarity2 Publications
Capsid protein p24: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. 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 (By similarity). Host restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species. Host PIN1 apparently facilitates the virion uncoating (PubMed:24509437). On the other hand, interactions with PDZD8 or CYPA stabilize the capsid.By similarity1 Publication
Nucleocapsid protein p7: Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates to gRNA dimerization, packaging, tRNA incorporation and virion assembly.By similarity
p6-gag: Plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri390 – 40718CCHC-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri411 – 42818CCHC-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Viral budding, Viral budding via the host ESCRT complexes, Virus exit from host cell

Keywords - Ligandi

Metal-binding, RNA-binding, Viral nucleoprotein, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.

Names & Taxonomyi

Protein namesi
Recommended name:
Gag polyprotein
Alternative name(s):
Pr55Gag
Cleaved into the following 6 chains:
Matrix protein p17
Short name:
MA
Capsid protein p24
Short name:
CA
Spacer peptide 11 Publication
Short name:
SP1
Alternative name(s):
p2
Spacer peptide 21 Publication
Short name:
SP2
Alternative name(s):
p1
Gene namesi
Name:gag
OrganismiHuman immunodeficiency virus type 1 group M subtype B (isolate NY5) (HIV-1)
Taxonomic identifieri11698 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostiHomo sapiens (Human) [TaxID: 9606]

Subcellular locationi

Gag polyprotein :
  • Host cell membrane; Lipid-anchor 1 Publication
  • Host endosomehost multivesicular body

  • Note: These locations are probably linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly.1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host cell membrane, Host cytoplasm, Host endosome, Host membrane, Host nucleus, Membrane, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi9 – 91S → A: Loss of ability to fuse with target cell membranes and infect host cell. 1 Publication
Mutagenesisi67 – 671S → A: Loss of ability to fuse with target cell membranes and infect host cell. 1 Publication
Mutagenesisi72 – 721S → A: Loss of ability to fuse with target cell membranes and infect host cell. 1 Publication
Mutagenesisi77 – 771S → A: Loss of ability to fuse with target cell membranes and infect host cell. 1 Publication

Keywords - Diseasei

AIDS

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved; by hostBy similarity
Chaini2 – 500499Gag polyproteinPRO_0000261226Add
BLAST
Chaini2 – 132131Matrix protein p17By similarityPRO_0000038559Add
BLAST
Chaini133 – 363231Capsid protein p24By similarityPRO_0000038560Add
BLAST
Peptidei364 – 37714Spacer peptide 1By similarityPRO_0000038561Add
BLAST
Chaini378 – 43255Nucleocapsid protein p7By similarityPRO_0000038562Add
BLAST
Peptidei433 – 44816Spacer peptide 2By similarityPRO_0000038563Add
BLAST
Chaini449 – 50052p6-gagBy similarityPRO_0000038564Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
Modified residuei148 – 1481Phosphoserine; by host MAPK11 Publication
Modified residuei387 – 3871Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6By similarity
Modified residuei409 – 4091Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6By similarity

Post-translational modificationi

Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins.1 Publication
Matrix protein p17: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association.By similarity
Capsid protein p24: Phosphorylated possibly by host MAPK1; this phosphorylation is necessary for Pin1-mediated virion uncoating.1 Publication
Nucleocapsid protein p7: Methylated by host PRMT6, impairing its function by reducing RNA annealing and the initiation of reverse transcription.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei132 – 1332Cleavage; by viral proteaseBy similarity
Sitei363 – 3642Cleavage; by viral proteaseBy similarity
Sitei377 – 3782Cleavage; by viral proteaseBy similarity
Sitei432 – 4332Cleavage; by viral proteaseBy similarity
Sitei448 – 4492Cleavage; by viral proteaseBy similarity

Keywords - PTMi

Lipoprotein, Methylation, Myristate, Phosphoprotein

PTM databases

iPTMnetiP12493.

Interactioni

Subunit structurei

Gag polyprotein: Homotrimer; further assembles as hexamers of trimers (By similarity). Oligomerization possibly creates a central hole into which the cytoplasmic tail of the gp41 envelope protein may be inserted. Gag polyprotein: Interacts with host TRIM22; this interaction seems to disrupt proper trafficking of Gag polyprotein and may interfere with budding (By similarity). Gag polyprotein: Interacts with host PDZD8 (By similarity). Matrix protein p17: Homotrimer; further assembles as hexamers of trimers (By similarity). Matrix protein p17: Interacts with gp41 (via C-terminus) (PubMed:8918455). Matrix protein p17: Interacts with host CALM1; this interaction induces a conformational change in the Matrix protein, triggering exposure of the myristate group (PubMed:21799007). Matrix protein p17: Interacts with host AP3D1; this interaction allows the polyprotein trafficking to multivesicular bodies during virus assembly (PubMed:15766529). Matrix protein p17: Part of the pre-integration complex (PIC) which is composed of viral genome, matrix protein, Vpr and integrase (By similarity). Capsid protein p24: Homodimer; the homodimer further multimerizes as homohexamers or homopentamers (PubMed:24066695). Capsid protein p24: Interacts with human PPIA/CYPA; this interaction stabilizes the capsid (PubMed:8980234). Capsid protein p24: Interacts with human NUP153 (PubMed:24130490). Capsid protein p24: Interacts with host PDZD8; this interaction stabilizes the capsid (By similarity). Capsid protein p24: Interacts with monkey TRIM5; this interaction destabilizes the capsid (By similarity). p6-gag interacts with Vpr; this interaction allows Vpr incorporation into the virion (By similarity). p6-gag interacts with host TSG101 (PubMed:11427703, PubMed:11595185). p6-gag interacts with host PDCD6IP/AIP1(PubMed:19282983).By similarity9 Publications

Structurei

Secondary structure

1
500
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi134 – 1363Combined sources
Beta strandi138 – 1403Combined sources
Beta strandi142 – 1443Combined sources
Helixi149 – 16214Combined sources
Helixi168 – 1758Combined sources
Turni176 – 1783Combined sources
Helixi181 – 1899Combined sources
Helixi195 – 21521Combined sources
Beta strandi225 – 2273Combined sources
Helixi233 – 2364Combined sources
Beta strandi239 – 2413Combined sources
Helixi243 – 2508Combined sources
Beta strandi252 – 2543Combined sources
Helixi258 – 27619Combined sources
Helixi282 – 2843Combined sources
Helixi293 – 30715Combined sources
Turni308 – 3103Combined sources
Turni311 – 3133Combined sources
Helixi321 – 3244Combined sources
Helixi328 – 33710Combined sources
Helixi343 – 3497Combined sources
Turni463 – 4653Combined sources
Helixi466 – 4683Combined sources
Beta strandi474 – 4763Combined sources
Beta strandi480 – 4845Combined sources
Helixi487 – 4904Combined sources
Helixi492 – 4943Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GWPNMR-A133-283[»]
2C55NMR-A449-500[»]
4U0AX-ray2.05A133-363[»]
4U0BX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L133-363[»]
4U0CX-ray1.77A133-363[»]
4U0DX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L133-363[»]
4U0EX-ray2.04A133-363[»]
4U0FX-ray2.22A133-363[»]
4XFXX-ray2.43A133-363[»]
4XFYX-ray2.80A133-363[»]
4XFZX-ray2.70A133-363[»]
4XROX-ray2.01A133-363[»]
4XRQX-ray1.95A133-363[»]
DisProtiDP00101.
ProteinModelPortaliP12493.
SMRiP12493. Positions 2-432, 449-500.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12493.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7 – 3125Interaction with Gp411 PublicationAdd
BLAST
Regioni8 – 4336Interaction with host CALM1By similarityAdd
BLAST
Regioni12 – 198Interaction with host AP3D11 Publication
Regioni14 – 3320Interaction with membrane phosphatidylinositol 4,5-bisphosphate and RNA1 PublicationAdd
BLAST
Regioni73 – 775Interaction with membrane phosphatidylinositol 4,5-bisphosphate1 Publication
Regioni189 – 22739Interaction with host PPIA/CYPA and NUP153By similarityAdd
BLAST
Regioni189 – 22739Interaction with human PPIA/CYPA and NUP1532 PublicationsAdd
BLAST
Regioni217 – 2259PPIA/CYPA-binding loopBy similarity
Regioni277 – 36387Dimerization/Multimerization of capsid protein p24By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi16 – 227Nuclear export signalBy similarity
Motifi26 – 327Nuclear localization signalBy similarity
Motifi455 – 4584PTAP/PSAP motif
Motifi483 – 49210LYPX(n)L motif

Domaini

Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. p6-gag contains two L domains: a PTAP/PSAP motif, which interacts with the UEV domain of TSG101 and a LYPX(n)L motif which interacts with PDCD6IP/AIP1.1 Publication

Sequence similaritiesi

Contains 2 CCHC-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri390 – 40718CCHC-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri411 – 42818CCHC-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Family and domain databases

Gene3Di1.10.1200.30. 1 hit.
1.10.150.90. 1 hit.
1.10.375.10. 1 hit.
4.10.60.10. 1 hit.
InterProiIPR000721. Gag_p24.
IPR014817. Gag_p6.
IPR000071. Lentvrl_matrix_N.
IPR012344. Matrix_HIV/RSV.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF00540. Gag_p17. 1 hit.
PF00607. Gag_p24. 1 hit.
PF08705. Gag_p6. 1 hit.
PF00098. zf-CCHC. 2 hits.
[Graphical view]
PRINTSiPR00234. HIV1MATRIX.
SMARTiSM00343. ZnF_C2HC. 2 hits.
[Graphical view]
SUPFAMiSSF47353. SSF47353. 1 hit.
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF57756. SSF57756. 1 hit.
PROSITEiPS50158. ZF_CCHC. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by ribosomal frameshifting. AlignAdd to basket

Note: Translation results in the formation of the Gag polyprotein most of the time. Ribosomal frameshifting at the gag-pol genes boundary occurs at low frequency and produces the Gag-Pol polyprotein. This strategy of translation probably allows the virus to modulate the quantity of each viral protein. Maintenance of a correct Gag to Gag-Pol ratio is essential for RNA dimerization and viral infectivity.

Isoform Gag polyprotein (identifier: P12493-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGARASVLSG GELDKWEKIR LRPGGKKQYK LKHIVWASRE LERFAVNPGL
60 70 80 90 100
LETSEGCRQI LGQLQPSLQT GSEELRSLYN TIAVLYCVHQ RIDVKDTKEA
110 120 130 140 150
LDKIEEEQNK SKKKAQQAAA DTGNNSQVSQ NYPIVQNLQG QMVHQAISPR
160 170 180 190 200
TLNAWVKVVE EKAFSPEVIP MFSALSEGAT PQDLNTMLNT VGGHQAAMQM
210 220 230 240 250
LKETINEEAA EWDRLHPVHA GPIAPGQMRE PRGSDIAGTT STLQEQIGWM
260 270 280 290 300
THNPPIPVGE IYKRWIILGL NKIVRMYSPT SILDIRQGPK EPFRDYVDRF
310 320 330 340 350
YKTLRAEQAS QEVKNWMTET LLVQNANPDC KTILKALGPG ATLEEMMTAC
360 370 380 390 400
QGVGGPGHKA RVLAEAMSQV TNPATIMIQK GNFRNQRKTV KCFNCGKEGH
410 420 430 440 450
IAKNCRAPRK KGCWKCGKEG HQMKDCTERQ ANFLGKIWPS HKGRPGNFLQ
460 470 480 490 500
SRPEPTAPPE ESFRFGEETT TPSQKQEPID KELYPLASLR SLFGSDPSSQ
Note: Produced by conventional translation.
Length:500
Mass (Da):55,819
Last modified:January 23, 2007 - v3
Checksum:i08ECC125834088C6
GO
Isoform Gag-Pol polyprotein (identifier: P12497-1) [UniParc]FASTAAdd to basket

The sequence of this isoform can be found in the external entry P12497.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by -1 ribosomal frameshifting.
Length:1,435
Mass (Da):161,789
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19921 Genomic RNA. Translation: AAA44987.1.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19921 Genomic RNA. Translation: AAA44987.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GWPNMR-A133-283[»]
2C55NMR-A449-500[»]
4U0AX-ray2.05A133-363[»]
4U0BX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L133-363[»]
4U0CX-ray1.77A133-363[»]
4U0DX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L133-363[»]
4U0EX-ray2.04A133-363[»]
4U0FX-ray2.22A133-363[»]
4XFXX-ray2.43A133-363[»]
4XFYX-ray2.80A133-363[»]
4XFZX-ray2.70A133-363[»]
4XROX-ray2.01A133-363[»]
4XRQX-ray1.95A133-363[»]
DisProtiDP00101.
ProteinModelPortaliP12493.
SMRiP12493. Positions 2-432, 449-500.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiP12493.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.

Miscellaneous databases

EvolutionaryTraceiP12493.

Family and domain databases

Gene3Di1.10.1200.30. 1 hit.
1.10.150.90. 1 hit.
1.10.375.10. 1 hit.
4.10.60.10. 1 hit.
InterProiIPR000721. Gag_p24.
IPR014817. Gag_p6.
IPR000071. Lentvrl_matrix_N.
IPR012344. Matrix_HIV/RSV.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF00540. Gag_p17. 1 hit.
PF00607. Gag_p24. 1 hit.
PF08705. Gag_p6. 1 hit.
PF00098. zf-CCHC. 2 hits.
[Graphical view]
PRINTSiPR00234. HIV1MATRIX.
SMARTiSM00343. ZnF_C2HC. 2 hits.
[Graphical view]
SUPFAMiSSF47353. SSF47353. 1 hit.
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF57756. SSF57756. 1 hit.
PROSITEiPS50158. ZF_CCHC. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Buckler C.E., Buckler-White A.J., Willey R.L., McCoy J.
    Submitted (JUN-1988) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Clone pNL4-3.
  2. "Direct interaction between the envelope and matrix proteins of HIV-1."
    Cosson P.
    EMBO J. 15:5783-5788(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF MATRIX PROTEIN P17 WITH GP41.
  3. "Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid."
    Gamble T.R., Vajdos F.F., Yoo S., Worthylake D.K., Houseweart M., Sundquist W.I., Hill C.P.
    Cell 87:1285-1294(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF CAPSID PROTEIN WITH HUMAN PPIA/CYPA.
  4. "Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55(Gag)."
    VerPlank L., Bouamr F., LaGrassa T.J., Agresta B., Kikonyogo A., Leis J., Carter C.A.
    Proc. Natl. Acad. Sci. U.S.A. 98:7724-7729(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF P6-GAG WITH HUMAN TSG101, FUNCTION (P6-GAG).
  5. Cited for: INTERACTION OF P6-GAG WITH HUMAN TSG101, FUNCTION (P6-GAG).
  6. "Cell-type-dependent targeting of human immunodeficiency virus type 1 assembly to the plasma membrane and the multivesicular body."
    Ono A., Freed E.O.
    J. Virol. 78:1552-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION OF GAG POLYPROTEIN.
  7. "AP-3 directs the intracellular trafficking of HIV-1 Gag and plays a key role in particle assembly."
    Dong X., Li H., Derdowski A., Ding L., Burnett A., Chen X., Peters T.R., Dermody T.S., Woodruff E., Wang J.J., Spearman P.
    Cell 120:663-674(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF MATRIX PROTEIN P17 WITH HUMAN AP3D1.
  8. "Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly."
    Saad J.S., Miller J., Tai J., Kim A., Ghanam R.H., Summers M.F.
    Proc. Natl. Acad. Sci. U.S.A. 103:11364-11369(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF MATRIX PROTEIN P17 WITH PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE, FUNCTION (MATRIX PROTEIN P17).
  9. "Mutation of critical serine residues in HIV-1 matrix result in an envelope incorporation defect which can be rescued by truncation of the gp41 cytoplasmic tail."
    Bhatia A.K., Kaushik R., Campbell N.A., Pontow S.E., Ratner L.
    Virology 384:233-241(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-9; SER-67; SER-72 AND SER-77.
  10. "The nucleocapsid region of HIV-1 Gag cooperates with the PTAP and LYPXnL late domains to recruit the cellular machinery necessary for viral budding."
    Dussupt V., Javid M.P., Abou-Jaoude G., Jadwin J.A., de La Cruz J., Nagashima K., Bouamr F.
    PLoS Pathog. 5:E1000339-E1000339(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: LATE-BUDDING DOMAINS, INTERACTION OF P6-GAG WITH HOST TSG101, INTERACTION OF P6-GAG WITH HOST PDCD6IP/AIP1, FUNCTION (P6-GAG).
  11. "NMR, biophysical, and biochemical studies reveal the minimal Calmodulin binding domain of the HIV-1 matrix protein."
    Samal A.B., Ghanam R.H., Fernandez T.F., Monroe E.B., Saad J.S.
    J. Biol. Chem. 286:33533-33543(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF MATRIX PROTEIN P17 WITH RAT CALM1.
  12. "Context surrounding processing sites is crucial in determining cleavage rate of a subset of processing sites in HIV-1 Gag and Gag-Pro-Pol polyprotein precursors by viral protease."
    Lee S.K., Potempa M., Kolli M., Ozen A., Schiffer C.A., Swanstrom R.
    J. Biol. Chem. 287:13279-13290(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF GAG POLYPROTEIN.
  13. "Nucleoporin NUP153 phenylalanine-glycine motifs engage a common binding pocket within the HIV-1 capsid protein to mediate lentiviral infectivity."
    Matreyek K.A., Yucel S.S., Li X., Engelman A.
    PLoS Pathog. 9:E1003693-E1003693(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF CAPSID WITH HUMAN NUP153.
    Strain: Clone pNL4-3.
  14. "Structure and dynamics of full-length HIV-1 capsid protein in solution."
    Deshmukh L., Schwieters C.D., Grishaev A., Ghirlando R., Baber J.L., Clore G.M.
    J. Am. Chem. Soc. 135:16133-16147(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT (CAPSID PROTEIN P24).
  15. "Evidence in support of RNA-mediated inhibition of phosphatidylserine-dependent HIV-1 Gag membrane binding in cells."
    Chukkapalli V., Inlora J., Todd G.C., Ono A.
    J. Virol. 87:7155-7159(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF MATRIX PROTEIN P17 WITH RNA, FUNCTION (MATRIX PROTEIN P17).
  16. "Phosphorylation of human immunodeficiency virus type 1 capsid protein at serine 16, required for peptidyl-prolyl isomerase-dependent uncoating, is mediated by virion-incorporated extracellular signal-regulated kinase 2."
    Dochi T., Nakano T., Inoue M., Takamune N., Shoji S., Sano K., Misumi S.
    J. Gen. Virol. 95:1156-1166(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-148 (CAPSID PROTEIN P24), FUNCTION (CAPSID PROTEIN P24).
  17. "Role of HIV-1 Gag domains in viral assembly."
    Scarlata S., Carter C.
    Biochim. Biophys. Acta 1614:62-72(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  18. "Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein."
    Tang C., Ndassa Y., Summers M.F.
    Nat. Struct. Biol. 9:537-543(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 133-283.
  19. "Solution structure of the human immunodeficiency virus type 1 p6 protein."
    Fossen T., Wray V., Bruns K., Rachmat J., Henklein P., Tessmer U., Maczurek A., Klinger P., Schubert U.
    J. Biol. Chem. 280:42515-42527(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 449-500.

Entry informationi

Entry nameiGAG_HV1N5
AccessioniPrimary (citable) accession number: P12493
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

The infectious clone pNL4-3 is a chimeric provirus that consists of DNA from HIV isolates NY5 (5' half) and BRU (3' half).
HIV-1 lineages are divided in three main groups, M (for Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast majority of strains found worldwide belong to the group M. Group O seems to be endemic to and largely confined to Cameroon and neighboring countries in West Central Africa, where these viruses represent a small minority of HIV-1 strains. The group N is represented by a limited number of isolates from Cameroonian persons. The group M is further subdivided in 9 clades or subtypes (A to D, F to H, J and K).

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.