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Protein

Protein Tat

Gene

tat

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

Nuclear transcriptional activator of viral gene expression, that is essential for viral transcription from the LTR promoter and replication. Acts as a sequence-specific molecular adapter, directing components of the cellular transcription machinery to the viral RNA to promote processive transcription elongation by the RNA polymerase II (RNA pol II) complex, thereby increasing the level of full-length transcripts (PubMed:1756726). In the absence of Tat, the RNA Pol II generates short or non-processive transcripts that terminate at approximately 60 bp from the initiation site. Tat associates with the CCNT1/cyclin-T1 component of the P-TEFb complex (CDK9 and CCNT1), which promotes RNA chain elongation. This binding increases Tat's affinity for a hairpin structure at the 5'-end of all nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR RNA) and allows Tat/P-TEFb complex to bind cooperatively to TAR RNA (PubMed:9491887). The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin (PubMed:16687403). This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA (PubMed:22187158). Through its interaction with host TBP, Tat may also modulate transcription initiation (PubMed:7608968). Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs.6 Publications
Extracellular circulating Tat can be endocytosed by surrounding uninfected cells via the binding to several surface receptors such as CD26, CXCR4, heparan sulfate proteoglycans (HSPG) or LDLR. Neurons are rarely infected, but they internalize Tat via their LDLR. Through its interaction with nuclear HATs, Tat is potentially able to control the acetylation-dependent cellular gene expression. Modulates the expression of many cellular genes involved in cell survival, proliferation or in coding for cytokines or cytokine receptors. Tat plays a role in T-cell and neurons apoptosis. Tat induced neurotoxicity and apoptosis probably contribute to neuroAIDS (PubMed:17360663). Circulating Tat also acts as a chemokine-like and/or growth factor-like molecule that binds to specific receptors on the surface of the cells, affecting many cellular pathways. In the vascular system, Tat binds to ITGAV/ITGB3 and ITGA5/ITGB1 integrins dimers at the surface of endothelial cells and competes with bFGF for heparin-binding sites, leading to an excess of soluble bFGF.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei11 – 111Essential for Tat translocation through the endosomal membraneBy similarity
Metal bindingi22 – 221Zinc 12 Publications
Metal bindingi25 – 251Zinc 22 Publications
Metal bindingi27 – 271Zinc 22 Publications
Metal bindingi30 – 301Zinc 22 Publications
Metal bindingi33 – 331Zinc 1; via pros nitrogen2 Publications
Metal bindingi34 – 341Zinc 12 Publications
Metal bindingi37 – 371Zinc 12 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Apoptosis, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Modulation of host chromatin by virus, Modulation of host PP1 activity by virus, Transcription, Transcription regulation, Viral immunoevasion

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation.
R-HSA-167243. Tat-mediated HIV elongation arrest and recovery.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-176034. Interactions of Tat with host cellular proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein Tat
Alternative name(s):
Transactivating regulatory protein
Gene namesi
Name:tat
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

  • Host nucleushost nucleolus 1 Publication
  • Host cytoplasm 1 Publication
  • Secreted 1 Publication

  • Note: Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear localization signal with importin KPNB1. Secretion occurs through a Golgi-independent pathway. Tat is released from infected cells to the extracellular space where it remains associated to the cell membrane, or is secreted into the cerebrospinal fluid and sera. Extracellular Tat can be endocytosed by surrounding uninfected cells via binding to several receptors depending on the cell type.

GO - Cellular componenti

  • extracellular region Source: UniProtKB-SubCell
  • host cell cytoplasm Source: UniProtKB-SubCell
  • host cell nucleolus Source: UniProtKB-SubCell
  • host cell nucleus Source: BHF-UCL
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Host nucleus, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi50 – 512KK → AA: Reduced virus production. 1 Publication

Keywords - Diseasei

AIDS

Chemistry

ChEMBLiCHEMBL4011.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8686Protein TatPRO_0000085364Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei28 – 281N6-acetyllysine; by host PCAFBy similarity
Modified residuei50 – 501N6-acetyllysine; by host EP300 and GCN5L21 Publication
Modified residuei51 – 511N6-acetyllysine; by host EP300 and GCN5L21 Publication
Modified residuei52 – 521Asymmetric dimethylarginine; by host PRMT61 Publication
Modified residuei53 – 531Asymmetric dimethylarginine; by host PRMT61 Publication
Cross-linki71 – 71Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Post-translational modificationi

Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of Lys-50 promotes dissociation of Tat from the TAR RNA through the competitive binding to PCAF's bromodomain. In addition, the non-acetylated Tat's N-terminus can also interact with PCAF. PCAF-mediated acetylation of Lys-28 enhances Tat's binding to CCNT1. Lys-50 is deacetylated by SIRT1.1 Publication
Phosphorylated by EIF2AK2 on serine and threonine residues adjacent to the basic region important for TAR RNA binding and function. Phosphorylation of Tat by EIF2AK2 is dependent on the prior activation of EIF2AK2 by dsRNA.1 Publication
Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1.1 Publication
Polyubiquitination by host MDM2 does not target Tat to degradation, but activates its transactivation function and fosters interaction with CCNT1 and TAR RNA.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Interactioni

Subunit structurei

Interacts with host CCNT1. Associates with the P-TEFb complex composed at least of Tat, P-TEFb (CDK9 and CCNT1), TAR RNA, RNA Pol II. Recruits the HATs CREBBP, TAF1/TFIID, EP300, PCAF and GCN5L2. Interacts with host KAT5/Tip60; this interaction targets the latter to degradation. Interacts with the host deacetylase SIRT1. Interacts with host capping enzyme RNGTT; this interaction stimulates RNGTT. Binds to host KDR, and to the host integrins ITGAV/ITGB3 and ITGA5/ITGB1. Interacts with host KPNB1/importin beta-1 without previous binding to KPNA1/importin alpha-1. Interacts with EIF2AK2. Interacts with host nucleosome assembly protein NAP1L1; this interaction may be required for the transport of Tat within the nucleus, since the two proteins interact at the nuclear rim. Interacts with host C1QBP/SF2P32; this interaction involves lysine-acetylated Tat. Interacts with the host chemokine receptors CCR2, CCR3 and CXCR4. Interacts with host DPP4/CD26; this interaction may trigger an anti-proliferative effect. Interacts with host LDLR. Interacts with the host extracellular matrix metalloproteinase MMP1. Interacts with host PRMT6; this interaction mediates Tat's methylation. Interacts with, and is ubiquitinated by MDM2/Hdm2. Interacts with host PSMC3 and HTATIP2. Interacts with STAB1; this interaction may overcome SATB1-mediated repression of IL2 and IL2RA (interleukin) in T cells by binding to the same domain than HDAC1 (By similarity). Interacts (when acetylated on Lys-50 and Lys-51) with human CDK13, thereby increasing HIV-1 mRNA splicing and promoting the production of the doubly spliced HIV-1 protein Nef.Interacts with host TBP; this interaction modulates the activity of transcriptional pre-initiation complex. Interacts with host RELA.By similarity11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AFF1P518253EBI-6164389,EBI-2610180From a different organism.
AFF4Q9UHB74EBI-6164389,EBI-395282From a different organism.
AHCYL1O438655EBI-6164389,EBI-2371423From a different organism.
CCNT1O605635EBI-6164389,EBI-2479671From a different organism.
CDK9P507505EBI-6164389,EBI-1383449From a different organism.
CREBBPQ927932EBI-6164389,EBI-81215From a different organism.
DCAF16Q9NXF72EBI-6164389,EBI-2559096From a different organism.
DDX3XO005714EBI-6164389,EBI-353779From a different organism.
envP045784EBI-6164389,EBI-6163496
EP300Q094723EBI-6164389,EBI-447295From a different organism.
FBXO3Q9UK993EBI-6164389,EBI-2509901From a different organism.
NAP1L1P552096EBI-6164389,EBI-356392From a different organism.
NAP1L4Q997333EBI-6164389,EBI-2255116From a different organism.
NPM3O756072EBI-6164389,EBI-721544From a different organism.
PPM1GO153553EBI-6164389,EBI-725702From a different organism.
SIRT1Q96EB63EBI-6164389,EBI-1802965From a different organism.
USP11P517843EBI-6164389,EBI-306876From a different organism.

GO - Molecular functioni

  • actinin binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi1205541. 314 interactions.
IntActiP04608. 31 interactions.

Chemistry

BindingDBiP04608.

Structurei

Secondary structure

1
86
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 123Combined sources
Helixi30 – 323Combined sources
Helixi35 – 406Combined sources
Turni41 – 433Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MI9X-ray2.10C1-86[»]
3MIAX-ray3.00C1-86[»]
4OR5X-ray2.90C/H1-48[»]
ProteinModelPortaliP04608.
SMRiP04608. Positions 1-86.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04608.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 4848TransactivationBy similarityAdd
BLAST
Regioni1 – 2424Interaction with human CREBBPAdd
BLAST
Regioni22 – 3716Cysteine-richBy similarityAdd
BLAST
Regioni38 – 4811CoreBy similarityAdd
BLAST
Regioni49 – 8638Interaction with the host capping enzyme RNGTTBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi49 – 579Nuclear localization signal, RNA-binding (TAR), and protein transductionBy similarity
Motifi78 – 803Cell attachment siteSequence analysis

Domaini

The transactivation domain mediates the interaction with CCNT1, GCN5L2, and MDM2.By similarity
The Arg-rich RNA-binding region binds the TAR RNA. This region also mediates the nuclear localization through direct binding to KPNB1 and is involved in Tat's transfer across cell membranes (protein transduction). The same region is required for the interaction with EP300, PCAF, EIF2AK2 and KDR.By similarity
The Cys-rich region may bind 2 zinc ions. This region is involved in binding to KAT5.By similarity
The cell attachment site mediates the interaction with ITGAV/ITGB3 and ITGA5/ITGB1 integrins, leading to vascular cell migration and invasion. This interaction also provides endothelial cells with the adhesion signal they require to grow in response to mitogens.By similarity

Sequence similaritiesi

Belongs to the lentiviruses Tat family.Curated

Phylogenomic databases

KOiK19258.

Family and domain databases

Gene3Di4.10.20.10. 1 hit.
InterProiIPR001831. IV_Tat.
[Graphical view]
PfamiPF00539. Tat. 1 hit.
[Graphical view]
PRINTSiPR00055. HIVTATDOMAIN.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: P04608-1) [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
MEPVDPRLEP WKHPGSQPKT ACTNCYCKKC CFHCQVCFIT KALGISYGRK
60 70 80
KRRQRRRAHQ NSQTHQASLS KQPTSQPRGD PTGPKE
Length:86
Mass (Da):9,837
Last modified:July 15, 1999 - v2
Checksum:i4DDC56D979769115
GO
Isoform Short (identifier: P04608-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     73-86: Missing.

Note: No experimental confirmation available. Expressed in the late stage of the infection cycle, when unspliced viral RNAs are exported to the cytoplasm by the viral Rev protein.
Show »
Length:72
Mass (Da):8,389
Checksum:iBA65366648F48150
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei73 – 8614Missing in isoform Short. CuratedVSP_022300Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03455 Genomic RNA. Translation: AAB50256.1.
AF033819 Genomic RNA. Translation: AAC82591.1.
RefSeqiNP_057853.1. NC_001802.1.

Genome annotation databases

GeneIDi155871.
KEGGivg:155871.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

BioAfrica HIV proteomics resource

Tat entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03455 Genomic RNA. Translation: AAB50256.1.
AF033819 Genomic RNA. Translation: AAC82591.1.
RefSeqiNP_057853.1. NC_001802.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MI9X-ray2.10C1-86[»]
3MIAX-ray3.00C1-86[»]
4OR5X-ray2.90C/H1-48[»]
ProteinModelPortaliP04608.
SMRiP04608. Positions 1-86.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1205541. 314 interactions.
IntActiP04608. 31 interactions.

Chemistry

BindingDBiP04608.
ChEMBLiCHEMBL4011.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi155871.
KEGGivg:155871.

Phylogenomic databases

KOiK19258.

Enzyme and pathway databases

ReactomeiR-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation.
R-HSA-167243. Tat-mediated HIV elongation arrest and recovery.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-176034. Interactions of Tat with host cellular proteins.

Miscellaneous databases

EvolutionaryTraceiP04608.

Family and domain databases

Gene3Di4.10.20.10. 1 hit.
InterProiIPR001831. IV_Tat.
[Graphical view]
PfamiPF00539. Tat. 1 hit.
[Graphical view]
PRINTSiPR00055. HIVTATDOMAIN.
ProtoNetiSearch...

Publicationsi

  1. "Location of the trans-activating region on the genome of human T-cell lymphotropic virus type III."
    Sodroski J., Patarca R., Rosen C., Wong-Staal F., Haseltine W.
    Science 229:74-77(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  3. Ratner L., Fisher A., Jagodzinski L.L., Mitsuya H., Liou R.-S., Gallo R.C., Wong-Staal F.
    Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  4. Chappey C.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  5. "HIV-1 Tat protein promotes formation of more-processive elongation complexes."
    Marciniak R.A., Sharp P.A.
    EMBO J. 10:4189-4196(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Evidence for functional interaction between the HIV-1 Tat transactivator and the TATA box binding protein in vivo."
    Veschambre P., Simard P., Jalinot P.
    J. Mol. Biol. 250:169-180(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HOST TBP.
  7. "The Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKR."
    Brand S.R., Kobayashi R., Mathews M.B.
    J. Biol. Chem. 272:8388-8395(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, INTERACTION WITH HOST EIF2AK2, FUNCTION.
  8. "A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA."
    Wei P., Garber M.E., Fang S.-M., Fischer W.H., Jones K.A.
    Cell 92:451-462(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HOST CCNT1.
  9. "HIV-1 tat transactivator recruits p300 and CREB-binding protein histone acetyltransferases to the viral promoter."
    Marzio G., Tyagi M., Gutierrez M.I., Giacca M.
    Proc. Natl. Acad. Sci. U.S.A. 95:13519-13524(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOST CREBBP AND EP300.
  10. "The Tat protein of human immunodeficiency virus type-1 promotes vascular cell growth and locomotion by engaging the alpha5beta1 and alphavbeta3 integrins and by mobilizing sequestered basic fibroblast growth factor."
    Barillari G., Sgadari C., Fiorelli V., Samaniego F., Colombini S., Manzari V., Modesti A., Nair B.C., Cafaro A., Stuerzl M., Ensoli B.
    Blood 94:663-672(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Uptake of HIV-1 tat protein mediated by low-density lipoprotein receptor-related protein disrupts the neuronal metabolic balance of the receptor ligands."
    Liu Y., Jones M., Hingtgen C.M., Bu G., Laribee N., Tanzi R.E., Moir R.D., Nath A., He J.J.
    Nat. Med. 6:1380-1387(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN LDLR.
  12. Cited for: UBIQUITINATION BY HOST MDM2.
  13. "Decoding Tat: the biology of HIV Tat posttranslational modifications."
    Hetzer C., Dormeyer W., Schnolzer M., Ott M.
    Microbes Infect. 7:1364-1369(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW, ALTERNATIVE SPLICING.
  14. "The multiple functions of HIV-1 Tat: proliferation versus apoptosis."
    Peruzzi F.
    Front. Biosci. 11:708-717(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  15. "The SWI/SNF chromatin-remodeling complex is a cofactor for Tat transactivation of the HIV promoter."
    Mahmoudi T., Parra M., Vries R.G., Kauder S.E., Verrijzer C.P., Ott M., Verdin E.
    J. Biol. Chem. 281:19960-19968(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. Cited for: REVIEW.
  17. "Acetylated Tat regulates human immunodeficiency virus type 1 splicing through its interaction with the splicing regulator p32."
    Berro R., Kehn K., de la Fuente C., Pumfery A., Adair R., Wade J., Colberg-Poley A.M., Hiscott J., Kashanchi F.
    J. Virol. 80:3189-3204(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN C1QBP.
  18. "Arginine methylation of the human immunodeficiency virus type 1 Tat protein by PRMT6 negatively affects Tat Interactions with both cyclin T1 and the Tat transactivation region."
    Xie B., Invernizzi C.F., Richard S., Wainberg M.A.
    J. Virol. 81:4226-4234(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, METHYLATION AT ARG-52 AND ARG-53.
  19. "HIV-tat induces formation of an LRP-PSD-95- NMDAR-nNOS complex that promotes apoptosis in neurons and astrocytes."
    Eugenin E.A., King J.E., Nath A., Calderon T.M., Zukin R.S., Bennett M.V., Berman J.W.
    Proc. Natl. Acad. Sci. U.S.A. 104:3438-3443(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. "CDK13, a new potential human immunodeficiency virus type 1 inhibitory factor regulating viral mRNA splicing."
    Berro R., Pedati C., Kehn-Hall K., Wu W., Klase Z., Even Y., Geneviere A.M., Ammosova T., Nekhai S., Kashanchi F.
    J. Virol. 82:7155-7166(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HUMAN CDK13, ACETYLATION AT LYS-50 AND LYS-51, MUTAGENESIS OF 50-LYS-LYS-51.
  21. "The histone chaperone protein Nucleosome Assembly Protein-1 (hNAP-1) binds HIV-1 Tat and promotes viral transcription."
    Vardabasso C., Manganaro L., Lusic M., Marcello A., Giacca M.
    Retrovirology 5:8-8(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN NAP1L1.
  22. "Subcellular localization of the interaction between the human immunodeficiency virus transactivator Tat and the nucleosome assembly protein 1."
    De Marco A., Dans P.D., Knezevich A., Maiuri P., Pantano S., Marcello A.
    Amino Acids 38:1583-1593(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH HUMAN NAP1L1.
  23. "Human immunodeficiency virus-1 Tat activates NF-kappaB via physical interaction with IkappaB-alpha and p65."
    Fiume G., Vecchio E., De Laurentiis A., Trimboli F., Palmieri C., Pisano A., Falcone C., Pontoriero M., Rossi A., Scialdone A., Fasanella Masci F., Scala G., Quinto I.
    Nucleic Acids Res. 40:3548-3562(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HOST RELA.
  24. "NMR mapping of the HIV-1 Tat interaction surface of the KIX domain of the human coactivator CBP."
    Vendel A.C., Lumb K.J.
    Biochemistry 43:904-908(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-24 IN COMPLEX WITH CREBBP KIX DOMAIN.
  25. "Crystal structure of HIV-1 Tat complexed with human P-TEFb."
    Tahirov T.H., Babayeva N.D., Varzavand K., Cooper J.J., Sedore S.C., Price D.H.
    Nature 465:747-751(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH ZINC.
  26. "Crystal structure of HIV-1 Tat complexed with human P-TEFb and AFF4."
    Gu J., Babayeva N.D., Suwa Y., Baranovskiy A.G., Price D.H., Tahirov T.H.
    Cell Cycle 13:1788-1797(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-48 IN COMPLEX WITH ZINC.

Entry informationi

Entry nameiTAT_HV1H2
AccessioniPrimary (citable) accession number: P04608
Secondary accession number(s): O09778
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: July 15, 1999
Last modified: June 8, 2016
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

This truncated variant has a premature stop codon. It may have arose as a consequence of tissue culture passaging.
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.