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P03070 (LT_SV40) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Large T antigen

Short name=LT
Short name=LT-AG
EC=3.6.4.-
OrganismSimian virus 40 (SV40) [Reference proteome]
Taxonomic identifier10633 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stagePolyomaviridaePolyomavirus
Virus hostMacaca (macaques) [TaxID: 9539]

Protein attributes

Sequence length708 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Isoform largeT antigen is a key early protein essential for both driving viral replication and inducing cellular transformation. Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle and by autoregulating the synthesis of viral early mRNA. Displays highly oncogenic activities by corrupting the host cellular checkpoint mechanisms that guard cell division and the transcription, replication, and repair of DNA. Participates in the modulation of cellular gene expression preceeding viral DNA replication. This step involves binding to host key cell cycle regulators retinoblastoma protein RB1/pRb and TP53. Induces the disassembly of host E2F1 transcription factors from RB1, thus promoting transcriptional activation of E2F1-regulated S-phase genes. Inhibits host TP53 binding to DNA, abrogating the ability of TP53 to stimulate gene expression. Plays the role of a TFIID-associated factor (TAF) in transcription initiation for all three RNA polymerases, by stabilizing the TBP-TFIIA complex on promoters. Initiates viral DNA replication and unwinding via interactions with the viral origin of replication. Binds two adjacent sites in the SV40 origin. The replication fork movement is facilitated by Large T antigen helicase activity. Activates the transcription of viral late mRNA, through host TBP and TFIIA stabilization. Interferes with histone deacetylation mediated by HDAC1, leading to activation of transcription. May inactivate the growth-suppressing properties of the E3 ubiquitin ligase CUL7. Ref.21 Ref.22 Ref.26 Ref.27 Ref.29 Ref.31

Isoform 17kTantigen targets host RBL2 for degradation and promotes cell proliferation. Transactivates host cyclin A promoter through its J domain. Ref.21 Ref.22 Ref.26 Ref.27 Ref.29 Ref.31

Subunit structure

Isoform largeT antigen forms homohexamers in the presence of ATP. Interacts with host HDAC1. Interacts (via LXCXE domain) with host RB1; the interaction induces the aberrant dissociation of RB1-E2F1 complex thereby disrupting RB1's activity. Interacts (via LXCXE domain) with host pRB-related proteins RBL1 and RBL2. Interacts (via C-terminus) with host TOP1 and POLA1 allowing DNA replication. Interacts with host TP53, inhibiting TP53 binding to DNA. Interacts with host preinitiation complex components TBP, TFIIA and TFIID to regulate transcription initiation. LT interacts (via CPD region) with host FBW7gamma isoform (viaWD repeats); seems to function as a competitive inhibitor of FBW7gamma function for physiologic substrates. LT interacts with host E3 ubiquitin ligase CUL7; this interaction seems to inhibit CUL7. Component of a SCF(CUL7)-like complex composed of SV40 Lt and host proteins CUL7, SKP1, RBX1, and FBXW8. LT interacts with host BUB1; this interaction induces activation of a DNA damage response and promotes p53 stabilization and phosphorylation Probable. Interacts with host FAM111A and this interaction is required for efficient viral replication and sustained viral gene expression in restrictive cell types. Ref.5 Ref.8 Ref.10 Ref.13 Ref.19 Ref.21 Ref.22 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32

Subcellular location

Host nucleus Ref.9.

Domain

The J domain is essential for multiple viral activities, including virion assembly, viral DNA replication, transformation and transcriptional activation (Ref.23). Ref.23

The LXCXE motif specifically binds to host pRB, RBL1, and RBL2. Ref.23

The origin-binding domain (T-ag OBD) interacts specifically with several pentameric sequences 5'-GAGGC-3' in the SV40 origin of DNA replication. Ref.23

The zinc finger region contributes to protein-protein interactions essential for the assembly of stable T-antigen hexamers at the origin of replication. The hexamers are required for subsequent alterations in the structure of origin DNA (Ref.15, Ref.16). Ref.23

The C-terminal region is involved in interaction with host FAM111A. It is also required for the host range and adenovirus helper functions of the virus (Ref.32). Ref.23

The ATP binding/ATPase domain is required for proper hexamer assembly and helicase activity (Ref.24). Ref.23

Cdc4 phospho-degron (CPD) region is involved in interaction with host FBW7gamma isoform. Ref.23

Post-translational modification

Phosphorylated on both serine and threonine residues. Phosphorylation on Ser-120 and Ser-123 inhibits viral replication, while phosphorylation on Thr-124 enhances replication by activating the DNA-binding domain. Phosphorylation on Thr-701 is required for binding to host FBW7gamma isoform. Dephosphorylated preferentially by PP2A on Ser-120, Ser-123, Ser-677 and perhaps Ser-679. Small t antigen inhibits the dephosphorylation by the AC form of PP2A. Ref.4 Ref.11 Ref.14 Ref.17 Ref.18 Ref.20

O-Glycosylated near the C-terminal region. Ref.9

Acetylated by CBP in a TP53-dependent manner. Ref.2 Ref.25

Sequence similarities

Contains 1 J domain.

Contains 1 SF3 helicase domain.

Contains 1 T-ag D1-type zinc finger.

Contains 1 T-ag OBD DNA-binding domain.

Ontologies

Keywords
   Biological processDNA replication
G1/S host cell cycle checkpoint dysregulation by virus
Host-virus interaction
Inhibition of host innate immune response by virus
Inhibition of host interferon signaling pathway by virus
Inhibition of host JAK1 by virus
Modulation of host cell cycle by virus
Modulation of host E3 ubiquitin ligases by virus
Modulation of host ubiquitin pathway by virus
Transcription
Transcription regulation
Viral immunoevasion
   Cellular componentHost nucleus
   Coding sequence diversityAlternative initiation
Alternative splicing
   Developmental stageEarly protein
   DiseaseOncogene
   DomainZinc-finger
   LigandATP-binding
DNA-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionActivator
Helicase
Hydrolase
   PTMAcetylation
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

modulation by virus of host G1/S transition checkpoint

Inferred from electronic annotation. Source: UniProtKB-KW

modulation by virus of host ubiquitin-protein ligase activity

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host JAK1 activity

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host type I interferon-mediated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA replication origin binding

Inferred from electronic annotation. Source: InterPro

helicase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 1311258Ref.32. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BUB1O436832EBI-617698,EBI-748936From a different organism.
CCNA2P202482EBI-617698,EBI-457097From a different organism.
CDC28P005463EBI-617698,EBI-4253From a different organism.
CDK1P064932EBI-617698,EBI-444308From a different organism.
CREBBPQ927932EBI-617698,EBI-81215From a different organism.
EP300Q094722EBI-617698,EBI-447295From a different organism.
IRS1P355682EBI-617698,EBI-517592From a different organism.
Kpna2P522933EBI-617698,EBI-3043908From a different organism.
MYCP011062EBI-617698,EBI-447544From a different organism.
POLA1P098846EBI-617698,EBI-850026From a different organism.
PURAQ005772EBI-617698,EBI-1045860From a different organism.
RB1P064006EBI-617698,EBI-491274From a different organism.
RPA1P276943EBI-617698,EBI-621389From a different organism.
TP53P0463718EBI-617698,EBI-366083From a different organism.
Tp53P0234011EBI-617698,EBI-474016From a different organism.

Alternative products

This entry describes 4 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]
Isoform Large T antigen (identifier: P03070-1)

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.
Isoform Small t antigen (identifier: P03081-1)

The sequence of this isoform can be found in the external entry P03081.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by alternative splicing.
Isoform 17kT antigen (identifier: P03070-2)

The sequence of this isoform differs from the canonical sequence as follows:
     132-135: VEDP → ALLT
     136-708: Missing.
Note: Produced by alternative splicing.
Isoform SELP (identifier: P0C6L2-1)

The sequence of this isoform can be found in the external entry P0C6L2.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by alternative initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 708708Large T antigen
PRO_0000115046

Regions

Domain12 – 7564J
Domain400 – 560161SF3 helicase
DNA binding139 – 254116T-ag OBD Ref.6
Zinc finger265 – 35793T-ag D1-type
Nucleotide binding426 – 4338ATP Potential
Region63 – 8927Binding of LT to the CUL7 complex
Region337 – 672336Binding to host TP53 protein
Region418 – 616199ATPase activity
Region627 – 70882C-terminal region
Region699 – 70810CPD
Motif103 – 1075LXCXE motif
Motif125 – 1328Nuclear localization signal Ref.7
Compositional bias633 – 6386Poly-Asp

Amino acid modifications

Modified residue11N-acetylmethionine; by host Ref.2
Modified residue1061Phosphoserine; by host
Modified residue1121Phosphoserine; by host
Modified residue1201Phosphoserine; by host
Modified residue1231Phosphoserine; by host
Modified residue1241Phosphothreonine; by host Ref.4 Ref.20
Modified residue6391Phosphoserine; by host
Modified residue6761Phosphoserine; by host
Modified residue6771Phosphoserine; by host
Modified residue6791Phosphoserine; by host
Modified residue6971N6-acetyllysine; by host
Modified residue7011Phosphothreonine; by host

Natural variations

Alternative sequence132 – 1354VEDP → ALLT in isoform 17kT antigen.
VSP_035893
Alternative sequence136 – 708573Missing in isoform 17kT antigen.
VSP_035894
Natural variant5311F → Y in strain: 776.
Natural variant5491A → P in strain: 776.
Natural variant5521Y → P in strain: 776.

Experimental info

Mutagenesis981F → A: Complete loss of interaction with host CUL7. Ref.28
Mutagenesis1241T → A: 200-fold reduction in phosphorylation by CDC2. No DNA replication activation. Ref.20
Mutagenesis6791S → A: Enhanced DNA replication.
Mutagenesis7011T → A: Complete loss of interaction with host FBW7gamma isoform. Ref.27

Secondary structure

............................................................................................................. 708
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Large T antigen [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: CB81306EF9E4E2C0

FASTA70881,582
        10         20         30         40         50         60 
MDKVLNREES LQLMDLLGLE RSAWGNIPLM RKAYLKKCKE FHPDKGGDEE KMKKMNTLYK 

        70         80         90        100        110        120 
KMEDGVKYAH QPDFGGFWDA TEIPTYGTDE WEQWWNAFNE ENLFCSEEMP SSDDEATADS 

       130        140        150        160        170        180 
QHSTPPKKKR KVEDPKDFPS ELLSFLSHAV FSNRTLACFA IYTTKEKAAL LYKKIMEKYS 

       190        200        210        220        230        240 
VTFISRHNSY NHNILFFLTP HRHRVSAINN YAQKLCTFSF LICKGVNKEY LMYSALTRDP 

       250        260        270        280        290        300 
FSVIEESLPG GLKEHDFNPE EAEETKQVSW KLVTEYAMET KCDDVLLLLG MYLEFQYSFE 

       310        320        330        340        350        360 
MCLKCIKKEQ PSHYKYHEKH YANAAIFADS KNQKTICQQA VDTVLAKKRV DSLQLTREQM 

       370        380        390        400        410        420 
LTNRFNDLLD RMDIMFGSTG SADIEEWMAG VAWLHCLLPK MDSVVYDFLK CMVYNIPKKR 

       430        440        450        460        470        480 
YWLFKGPIDS GKTTLAAALL ELCGGKALNV NLPLDRLNFE LGVAIDQFLV VFEDVKGTGG 

       490        500        510        520        530        540 
ESRDLPSGQG INNLDNLRDY LDGSVKVNLE KKHLNKRTQI FPPGIVTMNE FSVPKTLQAR 

       550        560        570        580        590        600 
FVKQIDFRAK DYLKHCLERS EFLLEKRIIQ SGIALLLMLI WYRPVAEFAQ SIQSRIVEWK 

       610        620        630        640        650        660 
ERLDKEFSLS VYQKMKFNVA MGIGVLDWLR NSDDDDEDSQ ENADKNEDGG EKNMEDSGHE 

       670        680        690        700 
TGIDSQSQGS FQAPQSSQSV HDHNQPYHIC RGFTCFKKPP TPPPEPET 

« Hide

Isoform Small t antigen [UniParc].

See P03081.

Isoform 17kT antigen [UniParc].

Checksum: 34517296D3E87E4F
Show »

FASTA13515,754
Isoform SELP [UniParc].

See P0C6L2.

References

[1]"The genome of simian virus 40."
Reddy V.B., Thimmappaya B., Dhar R., Subramanian K.N., Zain B.S., Pan J., Ghosh P.K., Celma M.L., Weissman S.M.
Science 200:494-502(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete nucleotide sequence of SV40 DNA."
Fiers W., Contreras R., Haegeman G., Rogiers R., van de Voorde A., van Heuverswyn H., van Herreweghe J., Volckaert G., Ysebaert M.
Nature 273:113-120(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ACETYLATION AT MET-1.
Strain: 776.
[3]"Independent expression of the transforming amino-terminal domain of SV40 large I antigen from an alternatively spliced third SV40 early mRNA."
Zerrahn J., Knippschild U., Winkler T., Deppert W.
EMBO J. 12:4739-4746(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE (ISOFORM 17KT ANTIGEN), ALTERNATIVE SPLICING.
[4]"Phosphorylation of large tumour antigen by cdc2 stimulates SV40 DNA replication."
McVey D., Brizuela L., Mohr I., Marshak D.R., Gluzman Y., Beach D.
Nature 341:503-507(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 102-118, PHOSPHORYLATION AT THR-124 BY CDC2.
[5]"T antigen is bound to a host protein in SV40-transformed cells."
Lane D.P., Crawford L.V.
Nature 278:261-263(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HOST TP53.
[6]"Topography of simian virus 40 A protein-DNA complexes: arrangement of pentanucleotide interaction sites at the origin of replication."
DeLucia A.L., Lewton B.A., Tjian R., Tegtmeyer P.
J. Virol. 46:143-150(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING.
[7]"A short amino acid sequence able to specify nuclear location."
Kalderon D., Roberts B.L., Richardson W.D., Smith A.E.
Cell 39:499-509(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEAR LOCALIZATION SIGNAL.
[8]"T-antigen-DNA polymerase alpha complex implicated in simian virus 40 DNA replication."
Smale S.T., Tjian R.
Mol. Cell. Biol. 6:4077-4087(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HOST POLA1.
[9]"Glycosylation of simian virus 40 T antigen and localization of glycosylated T antigen in the nuclear matrix."
Schmitt M.K., Mann K.
Virology 156:268-281(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, SUBCELLULAR LOCATION.
[10]"SV40 large tumor antigen forms a specific complex with the product of the retinoblastoma susceptibility gene."
Decaprio J.A., Ludlow J.W., Figge J., Shew J.-Y., Huang C.-M., Lee W.-H., Marsilio E., Paucha E., Livingston D.M.
Cell 54:275-283(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HOST RB PROTEIN.
[11]"In vitro phosphorylation of SV40 large T antigen."
Graesser F.A., Scheidmann K.H., Tuazon P.T., Traugh J.A., Walter G.
Virology 165:13-22(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[12]"Activation of SV40 DNA replication in vitro by cellular protein phosphatase 2A."
Virshup D.M., Kauffman M.G., Kelly T.J.
EMBO J. 8:3891-3898(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVATION OF DNA REPLICATION BY HOST PP2A.
[13]"The cellular 107K protein that binds to adenovirus E1A also associates with the large T antigens of SV40 and JC virus."
Dyson N., Buchkovich K., Whyte P., Harlow E.
Cell 58:249-255(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HOST RBL1.
[14]"The replication functions of SV40 T antigen are regulated by phosphorylation."
Prives C.
Cell 61:735-738(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[15]"The finger domain of simian virus 40 large T antigen controls DNA-binding specificity."
Hoess A., Moarefi I.F., Fanning E., Arthur A.K.
J. Virol. 64:6291-6296(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: ZINC-FINGER.
[16]"The zinc finger region of simian virus 40 large T antigen is needed for hexamer assembly and origin melting."
Loeber G., Stenger J.E., Ray S., Parsons R.E., Anderson M.E., Tegtmeyer P.
J. Virol. 65:3167-3174(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: ZINC-FINGER.
[17]"Dephosphorylation of simian virus 40 large-T antigen and p53 protein by protein phosphatase 2A: inhibition by small-t antigen."
Scheidtmann K.H., Mumby M.C., Rundell K., Walter G.
Mol. Cell. Biol. 11:1996-2003(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: DEPHOSPHORYLATION BY HOST PP2A.
[18]"Protein phosphatase 2A dephosphorylates simian virus 40 large T antigen specifically at residues involved in regulation of DNA-binding activity."
Scheidtmann K.H., Virshup D.M., Kelly T.J.
J. Virol. 65:2098-2101(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: DEPHOSPHORYLATION BY HOST PP2A.
[19]"Adenovirus E1A, simian virus 40 tumor antigen, and human papillomavirus E7 protein share the capacity to disrupt the interaction between transcription factor E2F and the retinoblastoma gene product."
Chellappan S., Kraus V.B., Kroger B., Munger K., Howley P.M., Phelps W.C., Nevins J.R.
Proc. Natl. Acad. Sci. U.S.A. 89:4549-4553(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HOST RB1.
[20]"Mechanisms of simian virus 40 T-antigen activation by phosphorylation of threonine 124."
McVey D., Woelker B., Tegtmeyer P.
J. Virol. 70:3887-3893(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-124, MUTAGENESIS OF THR-124.
[21]"TAF-like function of SV40 large T antigen."
Damania B., Alwine J.C.
Genes Dev. 10:1369-1381(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HOST TBP AND TFIID.
[22]"Simian virus 40 large T antigen stabilizes the TATA-binding protein-TFIIA complex on the TATA element."
Damania B., Lieberman P., Alwine J.C.
Mol. Cell. Biol. 18:3926-3935(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRANSCRIPTION INITIATION, INTERACTION WITH HOST TFIIA.
[23]"The J domain of simian virus 40 large T antigen is required to functionally inactivate RB family proteins."
Zalvide J., Stubdal H., DeCaprio J.A.
Mol. Cell. Biol. 18:1408-1415(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: J DOMAIN.
[24]"SV40 large T antigen hexamer structure: domain organization and DNA-induced conformational changes."
VanLoock M.S., Alexandrov A., Yu X., Cozzarelli N.R., Egelman E.H.
Curr. Biol. 12:472-476(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ATPASE REGION.
[25]"p53 targets simian virus 40 large T antigen for acetylation by CBP."
Poulin D.L., Kung A.L., DeCaprio J.A.
J. Virol. 78:8245-8253(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION.
[26]"PP2A-dependent transactivation of the cyclin A promoter by SV40 ST is mediated by a cell cycle-regulated E2F site."
Skoczylas C., Henglein B., Rundell K.
Virology 332:596-601(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF ISOFORM 17KT.
[27]"The SV40 large T antigen contains a decoy phosphodegron that mediates its interactions with Fbw7/hCdc4."
Welcker M., Clurman B.E.
J. Biol. Chem. 280:7654-7658(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HUMAN FBW7GAMMA ISOFORM, MUTAGENESIS OF THR-701.
[28]"Simian virus 40 large T antigen's association with the CUL7 SCF complex contributes to cellular transformation."
Kasper J.S., Kuwabara H., Arai T., Ali S.H., DeCaprio J.A.
J. Virol. 79:11685-11692(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN CUL7, IDENTIFICATION IN A SCF(CUL7)-LIKE COMPLEX, MUTAGENESIS OF PHE-98.
[29]"Involvement of chromatin and histone deacetylation in SV40 T antigen transcription regulation."
Valls E., Blanco-Garcia N., Aquizu N., Piedra D., Estaras C., de la Cruz X., Martinez-Balbas M.A.
Nucleic Acids Res. 35:1958-1968(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HOST HDAC1.
[30]"Simian virus 40 DNA replication is dependent on an interaction between topoisomerase I and the C-terminal end of T antigen."
Khopde S., Simmons D.T.
J. Virol. 82:1136-1145(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HOST TOP1.
[31]"Simian virus 40 large T antigen disrupts genome integrity and activates a DNA damage response via Bub1 binding."
Hein J., Boichuk S., Wu J., Cheng Y., Freire R., Jat P.S., Roberts T.M., Gjoerup O.V.
J. Virol. 83:117-127(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HUMAN BUB1.
[32]"Identification of FAM111A as an SV40 host range restriction and adenovirus helper factor."
Fine D.A., Rozenblatt-Rosen O., Padi M., Korkhin A., James R.L., Adelmant G., Yoon R., Guo L., Berrios C., Zhang Y., Calderwood M.A., Velmurgan S., Cheng J., Marto J.A., Hill D.E., Cusick M.E., Vidal M., Florens L. expand/collapse author list , Washburn M.P., Litovchick L., DeCaprio J.A.
PLoS Pathog. 8:E1002949-E1002949(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HOST FAM111A, C-TERMINAL REGION.
[33]"Structural basis for the inactivation of retinoblastoma tumor suppressor by SV40 large T antigen."
Kim H.-Y., Ahn B.-Y., Cho Y.
EMBO J. 20:295-304(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 7-117.
[34]"Structure of the replicative helicase of the oncoprotein SV40 large tumour antigen."
Li D., Zhao R., Lilyestrom W., Gai D., Zhang R., DeCaprio J.A., Fanning E., Jochimiak A., Szakonyi G., Chen X.S.
Nature 423:512-518(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 260-627.
[35]"Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen."
Gai D., Zhao R., Li D., Finkielstein C.V., Chen X.S.
Cell 119:47-60(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 251-627.
[36]"Crystal structure of SV40 large T-antigen bound to p53: interplay between a viral oncoprotein and a cellular tumor suppressor."
Lilyestrom W., Klein M.G., Zhang R., Joachimiak A., Chen X.S.
Genes Dev. 20:2373-2382(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.16 ANGSTROMS) OF 251-627.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02400 Genomic DNA. Translation: AAB59924.1.
RefSeqYP_003708382.1. NC_001669.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EJLX-ray2.80A/B126-132[»]
1GH6X-ray3.20A7-117[»]
1N25X-ray2.80A/B260-627[»]
1Q1SX-ray2.30A/B110-133[»]
1Q1TX-ray2.50A/B110-134[»]
1SVLX-ray1.95A/B/C251-627[»]
1SVMX-ray1.94A/B/C/D/E/F251-627[»]
1SVOX-ray2.60A/B251-627[»]
1TBDNMR-A131-260[»]
1Z1DNMR-B131-259[»]
2FUFX-ray1.45A131-259[»]
2H1LX-ray3.16A/B/C/D/E/F/G/H/I/J/K/L260-627[»]
2IF9X-ray2.59A/B131-260[»]
2IPRX-ray1.50A/B131-259[»]
2ITJX-ray2.50A/B131-259[»]
2ITLX-ray1.65A/B131-259[»]
2NL8X-ray2.30A131-259[»]
2NTCX-ray2.40A/B131-260[»]
2TBDNMR-A131-260[»]
3QK2X-ray1.64A131-260[»]
3QN2X-ray1.66A131-260[»]
4E2IX-ray5.00A/B/C/D/E/F/G/H/I/J/K/L266-627[»]
4FGNX-ray3.20A/B131-260[»]
4GDFX-ray2.80A/B/E/F131-627[»]
ProteinModelPortalP03070.
SMRP03070. Positions 7-117, 131-260, 265-627.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-24251N.
IntActP03070. 36 interactions.
MINTMINT-91005.

Chemistry

ChEMBLCHEMBL1075257.

PTM databases

UniCarbKBP03070.

Proteomic databases

PRIDEP03070.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1489531.

Family and domain databases

Gene3D1.10.10.510. 1 hit.
1.10.287.110. 1 hit.
3.40.50.300. 1 hit.
InterProIPR001623. DnaJ_domain.
IPR014015. Helicase_SF3_DNA-vir.
IPR016392. Lg_T_Ag_polyomavir.
IPR010932. Lg_T_Ag_Polyomavir_C.
IPR027417. P-loop_NTPase.
IPR003133. T_Ag_DNA-bd.
IPR017910. Znf_lg_T-Ag_D1-typ.
[Graphical view]
PfamPF00226. DnaJ. 1 hit.
PF06431. Polyoma_lg_T_C. 1 hit.
PF02217. T_Ag_DNA_bind. 1 hit.
[Graphical view]
PIRSFPIRSF003368. Large_T_antigen_polyomaV. 1 hit.
SMARTSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMSSF46565. SSF46565. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS50076. DNAJ_2. 1 hit.
PS51206. SF3_HELICASE_1. 1 hit.
PS51287. T_AG_OBD. 1 hit.
PS51341. ZF_LTAG_D1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP03070.

Entry information

Entry nameLT_SV40
AccessionPrimary (citable) accession number: P03070
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references