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Protein

Gag polyprotein

Gene

gag

Organism
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (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).1 Publication
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).By similarity
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 (PubMed:12660176). Host restriction factors such as monkey 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 (PubMed:23785198). Host PIN1 apparently facilitates the virion uncoating (By similarity). On the other hand, interactions with PDZD8 or CYPA stabilize the capsid (PubMed:24554657).By similarity5 Publications
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.6 Publications
p6-gag: Plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1.By similarity

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-162585. Uncoating of the HIV Virion.
R-HSA-162588. Budding and maturation of HIV virion.
R-HSA-162592. Integration of provirus.
R-HSA-162594. Early Phase of HIV Life Cycle.
R-HSA-164516. Minus-strand DNA synthesis.
R-HSA-164525. Plus-strand DNA synthesis.
R-HSA-164843. 2-LTR circle formation.
R-HSA-173107. Binding and entry of HIV virion.
R-HSA-174490. Membrane binding and targetting of GAG proteins.
R-HSA-174495. Synthesis And Processing Of GAG, GAGPOL Polyproteins.
R-HSA-175474. Assembly Of The HIV Virion.
R-HSA-175567. Integration of viral DNA into host genomic DNA.
R-HSA-177539. Autointegration results in viral DNA circles.
R-HSA-180689. APOBEC3G mediated resistance to HIV-1 infection.
R-HSA-180910. Vpr-mediated nuclear import of PICs.

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 1By similarity
Short name:
SP1
Alternative name(s):
p2
Spacer peptide 2By similarity
Short name:
SP2
Alternative name(s):
p1
Gene namesi
Name:gag
OrganismiHuman immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1)
Taxonomic identifieri11706 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000002241 Componenti: Genome

Subcellular locationi

Gag polyprotein :
  • Host cell membrane; Lipid-anchor
  • Host endosomehost multivesicular body By similarity

  • 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.By similarity

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
Mutagenesisi6 – 61S → D: No influence on the PIP2- or concentration-dependent myristyl switch mechanism. 1 Publication
Mutagenesisi9 – 91S → D: No influence on the PIP2- or concentration-dependent myristyl switch mechanism. 1 Publication
Mutagenesisi18 – 181K → A: Replication-defective, induces nuclear mislocalization of matrix protein; when associated with G-22. 1 Publication
Mutagenesisi22 – 221R → G: Replication-defective, induces nuclear mislocalization of matrix protein; when associated with A-18. 1 Publication
Mutagenesisi27 – 271K → A: No effect on subcellular localization of matrix protein; when associated with A-18 and G-22. 1 Publication
Mutagenesisi67 – 671S → D: No influence on the PIP2- or concentration-dependent myristyl switch mechanism. 1 Publication
Mutagenesisi72 – 721S → D: No influence on the PIP2- or concentration-dependent myristyl switch mechanism. 1 Publication
Mutagenesisi217 – 2171P → A: 3-fold decrease of PPIA-binding affinity. 1 Publication
Mutagenesisi218 – 2181V → A: 2.7-fold decrease of PPIA-binding affinity. 1 Publication
Mutagenesisi219 – 2191H → A or Q: 8-fold decrease of PPIA-binding affinity. 1 Publication
Mutagenesisi220 – 2201A → G: 44-fold decrease of PPIA-binding affinity. 1 Publication
Mutagenesisi220 – 2201A → V: 3.4-fold decrease of PPIA-binding affinity. 1 Publication
Mutagenesisi221 – 2211G → A: 31-fold decrease of PPIA-binding affinity. 1 Publication
Mutagenesisi221 – 2211G → V: 154-fold decrease of PPIA-binding affinity. 1 Publication
Mutagenesisi222 – 2221P → A: 36-fold decrease of PPIA-binding affinity. 1 Publication
Mutagenesisi222 – 2221P → V: More than 150-fold decrease of PPIA-binding affinity. 1 Publication
Mutagenesisi223 – 2231I → A: 1.2-fold decrease of PPIA-binding affinity. 1 Publication
Mutagenesisi223 – 2231I → V: 1.0-fold decrease of PPIA-binding affinity. 1 Publication
Mutagenesisi224 – 2241A → G: 2.3-fold decrease of PPIA-binding affinity. 1 Publication
Mutagenesisi224 – 2241A → V: 1.7-fold decrease of PPIA-binding affinity. 1 Publication
Mutagenesisi225 – 2251P → A: 1.6-fold decrease of PPIA-binding affinity. 1 Publication
Mutagenesisi394 – 3941N → F or G: Decreases infectivity and replication. 1 Publication
Mutagenesisi400 – 4001H → C: Complete loss of infectivity and in vitro chaperone activity. 1 Publication
Mutagenesisi405 – 4051C → H: Complete loss of infectivity and DNA synthesis. 1 Publication
Mutagenesisi421 – 4211H → C: Partial loss of infectivity. Complete loss of in vitro chaperone activity. 1 Publication
Mutagenesisi426 – 4261C → H: Partial loss of infectivity. 1 Publication

Keywords - Diseasei

AIDS

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved; by hostBy similarity
Chaini2 – 500499Gag polyproteinPRO_0000261216Add
BLAST
Chaini2 – 132131Matrix protein p17By similarityPRO_0000038593Add
BLAST
Chaini133 – 363231Capsid protein p24By similarityPRO_0000038594Add
BLAST
Peptidei364 – 37714Spacer peptide 1By similarityPRO_0000038595Add
BLAST
Chaini378 – 43255Nucleocapsid protein p7By similarityPRO_0000038596Add
BLAST
Peptidei433 – 44816Spacer peptide 2By similarityPRO_0000038597Add
BLAST
Chaini449 – 50052p6-gagBy similarityPRO_0000038598Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
Modified residuei148 – 1481Phosphoserine; by host MAPK1By similarity
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.By similarity
Matrix protein p17: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association (PubMed:17656588).1 Publication
Capsid protein p24: Phosphorylated possibly by host MAPK1; this phosphorylation is necessary for Pin1-mediated virion uncoating.By similarity
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

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 (PubMed:18389079). Gag polyprotein: Interacts with host PDZD8 (By similarity). Matrix protein p17: Homotrimer; further assembles as hexamers of trimers (PubMed:19327811). Matrix protein p17: Interacts with gp41 (via C-terminus) (By similarity). Matrix protein p17: Interacts with host CALM1; this interaction induces a conformational change in the Matrix protein, triggering exposure of the myristate group (PubMed:24500712). Matrix protein p17: Interacts with host AP3D1; this interaction allows the polyprotein trafficking to multivesicular bodies during virus assembly (By similarity). 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:19914170). Capsid protein p24: Interacts with human PPIA/CYPA;this interaction stabilizes the capsid (PubMed:9223641). Capsid protein p24: Interacts with human NUP153 (By similarity). Capsid protein p24: Interacts with host PDZD8; this interaction stabilizes the capsid (PubMed:20573829). Capsid protein p24: Interacts with monkey TRIM5; this interaction destabilizes the capsid (PubMed:23785198). p6-gag interacts with Vpr; this interaction allows Vpr incorporation into the virion (By similarity). p6-gag interacts with host TSG101 (By similarity). p6-gag interacts with host PDCD6IP/AIP1 (By similarity).By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AIMP1Q129043EBI-6179719,EBI-1045802From a different organism.
AIMP2Q131553EBI-6179719,EBI-745226From a different organism.
Cct3P803183EBI-10634977,EBI-772361From a different organism.
CTNNA3Q9UI472EBI-6179727,EBI-3937546From a different organism.
EEF1E1O433244EBI-6179719,EBI-1048486From a different organism.
LRRC47Q8N1G42EBI-6179727,EBI-2509921From a different organism.
MRPL11Q9Y3B73EBI-6179727,EBI-5453723From a different organism.
NOLC1Q149782EBI-6179719,EBI-396155From a different organism.
OLA1Q9NTK54EBI-6179719,EBI-766468From a different organism.
PRMT1Q998732EBI-6179727,EBI-78738From a different organism.
SDCCAG8Q86SQ72EBI-6179719,EBI-1047850From a different organism.
SEPSECSQ9HD403EBI-6163428,EBI-6163446From a different organism.
SNU13P557692EBI-6179727,EBI-712228From a different organism.
STAU1O95793-24EBI-6163428,EBI-358189From a different organism.
YTHDF3Q7Z7392EBI-6179727,EBI-2849837From a different organism.

Protein-protein interaction databases

BioGridi1205537. 184 interactions.
IntActiP04591. 46 interactions.

Structurei

Secondary structure

1
500
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni5 – 62
Beta strandi7 – 104
Helixi11 – 188
Beta strandi19 – 213
Beta strandi23 – 253
Helixi31 – 4515
Beta strandi46 – 483
Turni50 – 523
Helixi54 – 6714
Turni68 – 703
Helixi72 – 9019
Helixi97 – 11216
Beta strandi116 – 1183
Helixi149 – 16214
Turni163 – 1642
Turni166 – 1672
Helixi168 – 1758
Turni176 – 1783
Helixi181 – 1899
Turni190 – 1901
Helixi195 – 21521
Turni218 – 2192
Helixi233 – 2364
Turni237 – 2404
Helixi243 – 2508
Beta strandi251 – 2544
Helixi258 – 27720
Helixi282 – 2843
Turni289 – 2902
Helixi293 – 30513
Turni306 – 3061
Helixi311 – 32414
Turni325 – 3251
Helixi328 – 33710
Turni339 – 3402
Helixi343 – 3497
Turni350 – 3501
Beta strandi393 – 3953
Turni399 – 3991
Turni402 – 4043
Beta strandi414 – 4163
Turni423 – 4253

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TSQX-ray2.00P429-438[»]
1TSUX-ray2.10P429-436[»]
5FJBelectron microscopy9.00A/B133-350[»]
5I1ROther-A378-432[»]
ProteinModelPortaliP04591.
SMRiP04591. Positions 1-432, 449-500.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04591.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7 – 3125Interaction with Gp41By similarityAdd
BLAST
Regioni8 – 4336Interaction with host CALM11 PublicationAdd
BLAST
Regioni12 – 198Interaction with host AP3D1By similarity
Regioni14 – 3320Interaction with membrane phosphatidylinositol 4,5-bisphosphate and RNABy similarityAdd
BLAST
Regioni73 – 775Interaction with membrane phosphatidylinositol 4,5-bisphosphateBy similarity
Regioni189 – 22739Interaction with host PPIA/CYPA and NUP153By similarityAdd
BLAST
Regioni217 – 2259PPIA/CYPA-binding loop
Regioni277 – 36387Dimerization/Multimerization of capsid protein p24Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi16 – 227Nuclear export signal
Motifi26 – 327Nuclear localization signal
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.By similarity

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: P04591-1) [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 GELDRWEKIR LRPGGKKKYK LKHIVWASRE LERFAVNPGL
60 70 80 90 100
LETSEGCRQI LGQLQPSLQT GSEELRSLYN TVATLYCVHQ RIEIKDTKEA
110 120 130 140 150
LDKIEEEQNK SKKKAQQAAA DTGHSNQVSQ NYPIVQNIQG QMVHQAISPR
160 170 180 190 200
TLNAWVKVVE EKAFSPEVIP MFSALSEGAT PQDLNTMLNT VGGHQAAMQM
210 220 230 240 250
LKETINEEAA EWDRVHPVHA GPIAPGQMRE PRGSDIAGTT STLQEQIGWM
260 270 280 290 300
TNNPPIPVGE IYKRWIILGL NKIVRMYSPT SILDIRQGPK EPFRDYVDRF
310 320 330 340 350
YKTLRAEQAS QEVKNWMTET LLVQNANPDC KTILKALGPA ATLEEMMTAC
360 370 380 390 400
QGVGGPGHKA RVLAEAMSQV TNSATIMMQR GNFRNQRKIV KCFNCGKEGH
410 420 430 440 450
TARNCRAPRK KGCWKCGKEG HQMKDCTERQ ANFLGKIWPS YKGRPGNFLQ
460 470 480 490 500
SRPEPTAPPE ESFRSGVETT TPPQKQEPID KELYPLTSLR SLFGNDPSSQ
Note: Produced by conventional translation.
Length:500
Mass (Da):55,930
Last modified:January 23, 2007 - v3
Checksum:iB74C3858C20EF82C
GO
Isoform Gag-Pol polyprotein (identifier: P04585-1) [UniParc]FASTAAdd to basket

The sequence of this isoform can be found in the external entry P04585.
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):162,042
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03455 Genomic RNA. Translation: AAB50258.1.
RefSeqiNP_057850.1. NC_001802.1.

Genome annotation databases

GeneIDi155030.
KEGGivg:155030.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Web resourcesi

BioAfrica HIV proteomics resource

Gag entry

BioAfrica HIV proteomics resource

MA (p17) entry

BioAfrica HIV proteomics resource

CA (p24) entry

BioAfrica HIV proteomics resource

p2 entry

BioAfrica HIV proteomics resource

NC (p7) entry

BioAfrica HIV proteomics resource

p1 entry

BioAfrica HIV proteomics resource

p6 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03455 Genomic RNA. Translation: AAB50258.1.
RefSeqiNP_057850.1. NC_001802.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TSQX-ray2.00P429-438[»]
1TSUX-ray2.10P429-436[»]
5FJBelectron microscopy9.00A/B133-350[»]
5I1ROther-A378-432[»]
ProteinModelPortaliP04591.
SMRiP04591. Positions 1-432, 449-500.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1205537. 184 interactions.
IntActiP04591. 46 interactions.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi155030.
KEGGivg:155030.

Enzyme and pathway databases

ReactomeiR-HSA-162585. Uncoating of the HIV Virion.
R-HSA-162588. Budding and maturation of HIV virion.
R-HSA-162592. Integration of provirus.
R-HSA-162594. Early Phase of HIV Life Cycle.
R-HSA-164516. Minus-strand DNA synthesis.
R-HSA-164525. Plus-strand DNA synthesis.
R-HSA-164843. 2-LTR circle formation.
R-HSA-173107. Binding and entry of HIV virion.
R-HSA-174490. Membrane binding and targetting of GAG proteins.
R-HSA-174495. Synthesis And Processing Of GAG, GAGPOL Polyproteins.
R-HSA-175474. Assembly Of The HIV Virion.
R-HSA-175567. Integration of viral DNA into host genomic DNA.
R-HSA-177539. Autointegration results in viral DNA circles.
R-HSA-180689. APOBEC3G mediated resistance to HIV-1 infection.
R-HSA-180910. Vpr-mediated nuclear import of PICs.

Miscellaneous databases

EvolutionaryTraceiP04591.

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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Cyclophilin A is required for an early step in the life cycle of human immunodeficiency virus type 1 before the initiation of reverse transcription."
    Braaten D., Franke E.K., Luban J.
    J. Virol. 70:3551-3560(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (CAPSID PROTEIN P24).
  3. "Molecular recognition in the HIV-1 capsid/cyclophilin A complex."
    Yoo S., Myszka D.G., Yeh C., McMurray M., Hill C.P., Sundquist W.I.
    J. Mol. Biol. 269:780-795(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF PRO-217; VAL-218; HIS-219; ALA-220; GLY-221; PRO-222; ILE-223; ALA-224 AND PRO-225, INTERACTION WITH HUMAN CYPA.
  4. "A novel nuclear export activity in HIV-1 matrix protein required for viral replication."
    Dupont S., Sharova N., DeHoratius C., Virbasius C.M., Zhu X., Bukrinskaya A.G., Stevenson M., Green M.R.
    Nature 402:681-685(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LYS-18; ARG-22 AND LYS-27.
  5. "Recombination during reverse transcription: an evaluation of the role of the nucleocapsid protein."
    Negroni M., Buc H.
    J. Mol. Biol. 286:15-31(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (NUCLEOCAPSID PROTEIN P7).
  6. "Roles of Pr55(gag) and NCp7 in tRNA(3)(Lys) genomic placement and the initiation step of reverse transcription in human immunodeficiency virus type 1."
    Cen S., Khorchid A., Gabor J., Rong L., Wainberg M.A., Kleiman L.
    J. Virol. 74:10796-10800(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (NUCLEOCAPSID PROTEIN P7).
  7. "Maintenance of the Gag/Gag-Pol ratio is important for human immunodeficiency virus type 1 RNA dimerization and viral infectivity."
    Shehu-Xhilaga M., Crowe S.M., Mak J.
    J. Virol. 75:1834-1841(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: GAG/GAG-POL RATIO.
  8. "Catalysis of cis/trans isomerization in native HIV-1 capsid by human cyclophilin A."
    Bosco D.A., Eisenmesser E.Z., Pochapsky S., Sundquist W.I., Kern D.
    Proc. Natl. Acad. Sci. U.S.A. 99:5247-5252(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CIS/TRANS ISOMERIZATION (CAPSID PROTEIN P24).
  9. "Subtle alterations of the native zinc finger structures have dramatic effects on the nucleic acid chaperone activity of human immunodeficiency virus type 1 nucleocapsid protein."
    Guo J., Wu T., Kane B.F., Johnson D.G., Henderson L.E., Gorelick R.J., Levin J.G.
    J. Virol. 76:4370-4378(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (NUCLEOCAPSID PROTEIN P7), MUTAGENESIS OF HIS-400; CYS-405; HIS-421 AND CYS-426.
  10. "Structural organization of authentic, mature HIV-1 virions and cores."
    Briggs J.A., Wilk T., Welker R., Krausslich H.G., Fuller S.D.
    EMBO J. 22:1707-1715(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (CAPSID PROTEIN P24), QUARTERNARY STRUCTURE (CAPSID PROTEIN P24).
  11. "In vitro processing of HIV-1 nucleocapsid protein by the viral proteinase: effects of amino acid substitutions at the scissile bond in the proximal zinc finger sequence."
    Tozser J., Shulenin S., Louis J.M., Copeland T.D., Oroszlan S.
    Biochemistry 43:4304-4312(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE (NUCLEOCAPSID PROTEIN P7).
  12. "Characterization of human immunodeficiency virus type 1 (HIV-1) containing mutations in the nucleocapsid protein at a putative HIV-1 protease cleavage site."
    Thomas J.A., Shulenin S., Coren L.V., Bosche W.J., Gagliardi T.D., Gorelick R.J., Oroszlan S.
    Virology 354:261-270(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASN-394.
  13. "Dissecting the protein-RNA and RNA-RNA interactions in the nucleocapsid-mediated dimerization and isomerization of HIV-1 stemloop 1."
    Hagan N.A., Fabris D.
    J. Mol. Biol. 365:396-410(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (NUCLEOCAPSID PROTEIN P7).
  14. "Mutations that mimic phosphorylation of the HIV-1 matrix protein do not perturb the myristyl switch."
    Saad J.S., Kim A., Ghanam R.H., Dalton A.K., Vogt V.M., Wu Z., Lu W., Summers M.F.
    Protein Sci. 16:1793-1797(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-6; SER-9; SER-67 AND SER-72, PHOSPHORYLATION.
  15. "Human immunodeficiency virus type 1 matrix protein assembles on membranes as a hexamer."
    Alfadhli A., Huseby D., Kapit E., Colman D., Barklis E.
    J. Virol. 81:1472-1478(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT (MATRIX PROTEIN P17).
  16. "Mapping of nucleocapsid residues important for HIV-1 genomic RNA dimerization and packaging."
    Kafaie J., Song R., Abrahamyan L., Mouland A.J., Laughrea M.
    Virology 375:592-610(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (NUCLEOCAPSID PROTEIN P7).
  17. "The interferon response inhibits HIV particle production by induction of TRIM22."
    Barr S.D., Smiley J.R., Bushman F.D.
    PLoS Pathog. 4:E1000007-E1000007(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN TRIM22.
  18. "Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function."
    Byeon I.J., Meng X., Jung J., Zhao G., Yang R., Ahn J., Shi J., Concel J., Aiken C., Zhang P., Gronenborn A.M.
    Cell 139:780-790(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT (CAPSID PROTEIN P24), FUNCTION (CAPSID PROTEIN P24).
  19. "HIV-1 matrix organizes as a hexamer of trimers on membranes containing phosphatidylinositol-(4,5)-bisphosphate."
    Alfadhli A., Barklis R.L., Barklis E.
    Virology 387:466-472(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT (MATRIX PROTEIN P17).
  20. "Formation of immature and mature genomic RNA dimers in wild-type and protease-inactive HIV-1: differential roles of the Gag polyprotein, nucleocapsid proteins NCp15, NCp9, NCp7, and the dimerization initiation site."
    Jalalirad M., Laughrea M.
    Virology 407:225-236(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (NUCLEOCAPSID PROTEIN P7), FUNCTION (GAG POLYPROTEIN).
  21. "PDZD8 is a novel Gag-interacting factor that promotes retroviral infection."
    Henning M.S., Morham S.G., Goff S.P., Naghavi M.H.
    J. Virol. 84:8990-8995(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF GAG POLYPROTEIN WITH PDZD8.
  22. "Solution structure of calmodulin bound to the binding domain of the HIV-1 matrix protein."
    Vlach J., Samal A.B., Saad J.S.
    J. Biol. Chem. 289:8697-8705(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF MATRIX PROTEIN P17 WITH RAT CALM1.
  23. "Retrovirus restriction by TRIM5 proteins requires recognition of only a small fraction of viral capsid subunits."
    Shi J., Friedman D.B., Aiken C.
    J. Virol. 87:9271-9278(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MONKEY TRIM5 (CAPSID PROTEIN P24).
  24. "Contribution of PDZD8 to stabilization of the human immunodeficiency virus type 1 capsid."
    Guth C.A., Sodroski J.
    J. Virol. 88:4612-4623(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF CAPSID-NUCLEOCAPSID COMPLEX WITH HUMAN PDZD8, FUNCTION (CAPSID PROTEIN P24).
  25. Cited for: REVIEW.
  26. "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.
  27. "Cyclophilin, TRIM5, and innate immunity to HIV-1."
    Sokolskaja E., Luban J.
    Curr. Opin. Microbiol. 9:404-408(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  28. "Molecular determinants that regulate plasma membrane association of HIV-1 Gag."
    Chukkapalli V., Ono A.
    J. Mol. Biol. 410:512-524(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  29. "Retrospective on the all-in-one retroviral nucleocapsid protein."
    Darlix J.L., de Rocquigny H., Mauffret O., Mely Y.
    Virus Res. 193:2-15(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  30. "The role of matrix in HIV-1 envelope glycoprotein incorporation."
    Tedbury P.R., Freed E.O.
    Trends Microbiol. 22:372-378(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiGAG_HV1H2
AccessioniPrimary (citable) accession number: P04591
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

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, Complete proteome, Reference proteome

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.