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Protein

Large T antigen

Gene
N/A
Organism
Simian virus 40 (SV40)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Isoform large T 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 CUL7.5 Publications
Isoform 17kT antigen targets host RBL2 for degradation and promotes cell proliferation. Transactivates host cyclin A promoter through its J domain.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi139 – 254T-ag OBDPROSITE-ProRule annotationAdd BLAST116
<p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri265 – 357T-ag D1-typePROSITE-ProRule annotationAdd BLAST93
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi426 – 433ATPPROSITE-ProRule annotation8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • DNA replication origin binding Source: InterPro
  • double-stranded DNA binding Source: UniProtKB
  • helicase activity Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW
  • single-stranded DNA binding Source: UniProtKB

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, DNA-binding, Helicase, Hydrolase
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
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Large T antigen (EC:3.6.4.-)
Short name:
LT
Short name:
LT-AG
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSimian virus 40 (SV40)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1891767 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiVirusesdsDNA viruses, no RNA stagePolyomaviridae
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiMacaca (macaques) [TaxID: 9539]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000007705 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Host nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi98F → A: Complete loss of interaction with host CUL7. 1 Publication1
Mutagenesisi124T → A: 200-fold reduction in phosphorylation by CDC2. No DNA replication activation. 1 Publication1
Mutagenesisi679S → A: Enhanced DNA replication. 1
Mutagenesisi701T → A: Complete loss of interaction with host FBW7gamma isoform. 1 Publication1

Keywords - Diseasei

Oncogene

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1075257

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001150461 – 708Large T antigenAdd BLAST708

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionine; by host1 Publication1
Modified residuei106Phosphoserine; by host2 Publications1
Modified residuei112Phosphoserine; by host2 Publications1
Modified residuei120Phosphoserine; by host1 Publication1
Modified residuei123Phosphoserine; by host2 Publications1
Modified residuei124Phosphothreonine; by host4 Publications1
Modified residuei639Phosphoserine; by host1 Publication1
Modified residuei676Phosphoserine; by host1 Publication1
Modified residuei677Phosphoserine; by host2 Publications1
Modified residuei679Phosphoserine; by host2 Publications1
Modified residuei697N6-acetyllysine; by host1 Publication1
Modified residuei701Phosphothreonine; by host2 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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.4 Publications
O-Glycosylated near the C-terminal region.1 Publication
Acetylated by CBP in a TP53-dependent manner.2 Publications

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P03070

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
326

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P03070

UniCarbKB; an annotated and curated database of glycan structures

More...
UniCarbKBi
P03070

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Keywords - Developmental stagei

Early protein

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Isoform large T 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 (via WD 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.Curated14 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
3509198, 5 interactors

Database of interacting proteins

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DIPi
DIP-24251N

Protein interaction database and analysis system

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IntActi
P03070, 60 interactors

Molecular INTeraction database

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MINTi
P03070

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P03070

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1708
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P03070

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P03070

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P03070

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini12 – 75JPROSITE-ProRule annotationAdd BLAST64
Domaini400 – 560SF3 helicasePROSITE-ProRule annotationAdd BLAST161

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni63 – 89Binding of LT to the CUL7 complexAdd BLAST27
Regioni337 – 672Binding to host TP53 proteinAdd BLAST336
Regioni418 – 616ATPase activityAdd BLAST199
Regioni627 – 708C-terminal regionAdd BLAST82
Regioni699 – 708CPD10

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi103 – 107LXCXE motif1 Publication5
Motifi125 – 132Nuclear localization signal1 Publication8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi633 – 638Poly-Asp6

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The J domain is essential for multiple viral activities, including virion assembly, viral DNA replication, transformation and transcriptional activation.1 Publication
The LXCXE motif specifically binds to host pRB, RBL1, and RBL2.1 Publication
The origin-binding domain (T-ag OBD) interacts specifically with several pentameric sequences 5'-GAGGC-3' in the SV40 origin of DNA replication.1 Publication
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 (PubMed:2173794, PubMed:1851875).2 Publications
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 (PubMed:23093934).1 Publication
The ATP binding/ATPase domain is required for proper hexamer assembly and helicase activity.1 Publication
Cdc4 phospho-degron (CPD) region is involved in interaction with host FBW7gamma isoform.

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri265 – 357T-ag D1-typePROSITE-ProRule annotationAdd BLAST93

Keywords - Domaini

Zinc-finger

Family and domain databases

Conserved Domains Database

More...
CDDi
cd06257 DnaJ, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.287.110, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001623 DnaJ_domain
IPR014015 Helicase_SF3_DNA-vir
IPR036869 J_dom_sf
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

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF06431 Polyoma_lg_T_C, 1 hit
PF02217 T_Ag_DNA_bind, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF003368 Large_T_antigen_polyomaV, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00271 DnaJ, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF46565 SSF46565, 1 hit
SSF52540 SSF52540, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50076 DNAJ_2, 1 hit
PS51206 SF3_HELICASE_1, 1 hit
PS51287 T_AG_OBD, 1 hit
PS51341 ZF_LTAG_D1, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket
Isoform Large T antigen (identifier: P03070-1) [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
MDKVLNREES LQLMDLLGLE RSAWGNIPLM RKAYLKKCKE FHPDKGGDEE
60 70 80 90 100
KMKKMNTLYK KMEDGVKYAH QPDFGGFWDA TEIPTYGTDE WEQWWNAFNE
110 120 130 140 150
ENLFCSEEMP SSDDEATADS QHSTPPKKKR KVEDPKDFPS ELLSFLSHAV
160 170 180 190 200
FSNRTLACFA IYTTKEKAAL LYKKIMEKYS VTFISRHNSY NHNILFFLTP
210 220 230 240 250
HRHRVSAINN YAQKLCTFSF LICKGVNKEY LMYSALTRDP FSVIEESLPG
260 270 280 290 300
GLKEHDFNPE EAEETKQVSW KLVTEYAMET KCDDVLLLLG MYLEFQYSFE
310 320 330 340 350
MCLKCIKKEQ PSHYKYHEKH YANAAIFADS KNQKTICQQA VDTVLAKKRV
360 370 380 390 400
DSLQLTREQM LTNRFNDLLD RMDIMFGSTG SADIEEWMAG VAWLHCLLPK
410 420 430 440 450
MDSVVYDFLK CMVYNIPKKR YWLFKGPIDS GKTTLAAALL ELCGGKALNV
460 470 480 490 500
NLPLDRLNFE LGVAIDQFLV VFEDVKGTGG ESRDLPSGQG INNLDNLRDY
510 520 530 540 550
LDGSVKVNLE KKHLNKRTQI FPPGIVTMNE FSVPKTLQAR FVKQIDFRAK
560 570 580 590 600
DYLKHCLERS EFLLEKRIIQ SGIALLLMLI WYRPVAEFAQ SIQSRIVEWK
610 620 630 640 650
ERLDKEFSLS VYQKMKFNVA MGIGVLDWLR NSDDDDEDSQ ENADKNEDGG
660 670 680 690 700
EKNMEDSGHE TGIDSQSQGS FQAPQSSQSV HDHNQPYHIC RGFTCFKKPP

TPPPEPET
Length:708
Mass (Da):81,582
Last modified:February 1, 1996 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iCB81306EF9E4E2C0
GO
Isoform Small t antigen (identifier: P03081-1) [UniParc]FASTAAdd to basket
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.
Length:174
Mass (Da):20,449
GO
Isoform 17kT antigen (identifier: P03070-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     132-135: VEDP → ALLT
     136-708: Missing.

Note: Produced by alternative splicing.
Show »
Length:135
Mass (Da):15,754
Checksum:i34517296D3E87E4F
GO
Isoform SELP (identifier: P0C6L2-1) [UniParc]FASTAAdd to basket
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.
Length:23
Mass (Da):2,705
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti531F → Y in strain: 776. 1
Natural varianti549A → P in strain: 776. 1
Natural varianti552Y → P in strain: 776. 1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_035893132 – 135VEDP → ALLT in isoform 17kT antigen. 1 Publication4
Alternative sequenceiVSP_035894136 – 708Missing in isoform 17kT antigen. 1 PublicationAdd BLAST573

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
J02400 Genomic DNA Translation: AAB59924.1

NCBI Reference Sequences

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RefSeqi
YP_003708382.1, NC_001669.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
29031019

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
vg:29031019

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02400 Genomic DNA Translation: AAB59924.1
RefSeqiYP_003708382.1, NC_001669.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB 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[»]
4RXHX-ray1.76A/C125-132[»]
5D9IX-ray1.70A/B131-260[»]
5TCTX-ray2.90A/B/C/D/E/F266-627[»]
ProteinModelPortaliP03070
SMRiP03070
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi3509198, 5 interactors
DIPiDIP-24251N
IntActiP03070, 60 interactors
MINTiP03070

Chemistry databases

BindingDBiP03070
ChEMBLiCHEMBL1075257

PTM databases

GlyConnecti326
iPTMnetiP03070
UniCarbKBiP03070

Proteomic databases

PRIDEiP03070

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29031019
KEGGivg:29031019

Miscellaneous databases

EvolutionaryTraceiP03070

Family and domain databases

CDDicd06257 DnaJ, 1 hit
Gene3Di1.10.287.110, 1 hit
InterProiView protein in InterPro
IPR001623 DnaJ_domain
IPR014015 Helicase_SF3_DNA-vir
IPR036869 J_dom_sf
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
PfamiView protein in Pfam
PF06431 Polyoma_lg_T_C, 1 hit
PF02217 T_Ag_DNA_bind, 1 hit
PIRSFiPIRSF003368 Large_T_antigen_polyomaV, 1 hit
SMARTiView protein in SMART
SM00271 DnaJ, 1 hit
SUPFAMiSSF46565 SSF46565, 1 hit
SSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS50076 DNAJ_2, 1 hit
PS51206 SF3_HELICASE_1, 1 hit
PS51287 T_AG_OBD, 1 hit
PS51341 ZF_LTAG_D1, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLT_SV40
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P03070
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1996
Last modified: November 7, 2018
This is version 167 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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