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P03079

- MT_POVHA

UniProt

P03079 - MT_POVHA

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Protein

Middle T antigen

Gene
N/A
Organism
Hamster polyomavirus (HaPyV)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Plays a role in transformation by modulating the activities of cellular proteins involved in control of cell proliferation and by acting as a functional homolog of an activated tyrosine kinase-associated growth-factor receptor. Recruits upon association with Ppp2/PP2A the Src tyrosine kinase component Fyn, thereby activating its kinase activity. In turn, MT becomes phosphorylated and mediates signal transduction pathways leading to cell cycle progression and cell division. MT plays also a role in regulation of early and late gene expression as well as viral DNA replication (By similarity).By similarity

GO - Biological processi

  1. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Names & Taxonomyi

Protein namesi
Recommended name:
Middle T antigen
Short name:
MT
Short name:
MT-AG
OrganismiHamster polyomavirus (HaPyV)
Taxonomic identifieri10626 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stagePolyomaviridaePolyomavirus
Virus hostiMesocricetus auratus (Golden hamster) [TaxID: 10036]
ProteomesiUP000008477: Genome

Subcellular locationi

GO - Cellular componenti

  1. host cell membrane Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi324 – 3241Y → F: 70% loss of interaction with host Fyn. 1 Publication

Keywords - Diseasei

Oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 401401Middle T antigenPRO_0000115047Add
BLAST

Keywords - PTMi

Phosphoprotein

Expressioni

Keywords - Developmental stagei

Early protein

Interactioni

Subunit structurei

Interacts with host Ppp2/PP2A A and C subunits; this interaction alters PP2A substrate specificity and localization (By similarity). Interacts with host Fyn.By similarity1 Publication

Protein-protein interaction databases

IntActiP03079. 1 interaction.
MINTiMINT-8019810.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOTNMR-P321-331[»]
1AOUNMR-P321-331[»]
1LCJX-ray1.80B321-331[»]
1SPSX-ray2.70D/E/F321-331[»]
ProteinModelPortaliP03079.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03079.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 374374CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini396 – 4016ExtracellularSequence Analysis

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei375 – 39521HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 7564JPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 J domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
InterProiIPR001623. DnaJ_domain.
IPR003354. Papo_T_antigen.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF02380. Papo_T_antigen. 1 hit.
[Graphical view]
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
PROSITEiPS50076. DNAJ_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform Middle T antigen (identifier: P03079-1) [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
MDRILTKEEK QALISLLDLE PQYWGDYGRM QKCYKKKCLQ LHPDKGGNEE
60 70 80 90 100
LMQQLNTLWT KLKDGLYRVR LLLGPSQVRR LGKDQWNLSL QQTFSGTYFR
110 120 130 140 150
RLCRLPITCL RNKGISTCNC ILCLLRKQHF LLKKSWRVPC LVLGECYCID
160 170 180 190 200
CFALWFGLPV TNMLVPLYAQ FLAPIPVDWL DLNVHEVYNP ASGMTLMLPP
210 220 230 240 250
PPADPESSTI LTQEDTGPTL MGQQDTLTSR RNTGKSFSLS GMLMRTSPAK
260 270 280 290 300
KSYHHQKMNS PPGIPIPPPP LFLFPVTAPV PPVTRNTQET QAERENEYMP
310 320 330 340 350
MAPQIHLYSQ IREPTHQEEE EPQYEEIPIY LELLPENPNQ HLALTSTARR
360 370 380 390 400
SLRRKYHKHN SHIITQRQRN RLRRLVLMIF LLSLGGFFLT LFFLIKRKMH

L
Length:401
Mass (Da):46,562
Last modified:July 21, 1986 - v1
Checksum:i91B6172F4293F448
GO
Isoform Small t antigen (identifier: P03080-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform can be found in the external entry P03080.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:194
Mass (Da):22,625
GO
Isoform Large T antigen (identifier: P03075-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform can be found in the external entry P03075.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:751
Mass (Da):85,988
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M26281 Genomic DNA. Translation: AAA67117.1.
X02449 Genomic DNA. Translation: CAB59362.1.
PIRiA03615. TVVPMH.
RefSeqiNP_056731.1. NC_001663.1. [P03079-1]

Genome annotation databases

GeneIDi1489030.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M26281 Genomic DNA. Translation: AAA67117.1 .
X02449 Genomic DNA. Translation: CAB59362.1 .
PIRi A03615. TVVPMH.
RefSeqi NP_056731.1. NC_001663.1. [P03079-1 ]

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AOT NMR - P 321-331 [» ]
1AOU NMR - P 321-331 [» ]
1LCJ X-ray 1.80 B 321-331 [» ]
1SPS X-ray 2.70 D/E/F 321-331 [» ]
ProteinModelPortali P03079.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P03079. 1 interaction.
MINTi MINT-8019810.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 1489030.

Miscellaneous databases

EvolutionaryTracei P03079.

Family and domain databases

Gene3Di 1.10.287.110. 1 hit.
InterProi IPR001623. DnaJ_domain.
IPR003354. Papo_T_antigen.
[Graphical view ]
Pfami PF00226. DnaJ. 1 hit.
PF02380. Papo_T_antigen. 1 hit.
[Graphical view ]
SMARTi SM00271. DnaJ. 1 hit.
[Graphical view ]
SUPFAMi SSF46565. SSF46565. 1 hit.
PROSITEi PS50076. DNAJ_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "A new member of the polyomavirus family: the hamster papovavirus. Complete nucleotide sequence and transformation properties."
    Delmas V., Bastien C., Scherneck S., Feunteun J.
    EMBO J. 4:1279-1286(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Functional interaction between the SH2 domain of Fyn and tyrosine 324 of hamster polyomavirus middle-T antigen."
    Dunant N.M., Messerschmitt A.S., Ballmer-Hofer K.
    J. Virol. 71:199-206(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-324, INTERACTION WITH HOST FYN.
  3. "The SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity."
    Mulhern T.D., Shaw G.L., Morton C.J., Day A.J., Campbell I.D.
    Structure 5:1313-1323(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 321-331.
  4. "Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck."
    Eck M.J., Shoelson S.E., Harrison S.C.
    Nature 362:87-91(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 321-331.
  5. "Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms."
    Waksman G., Shoelson S.E., Pant N., Cowburn D., Kuriyan J.
    Cell 72:779-790(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 321-331.

Entry informationi

Entry nameiMT_POVHA
AccessioniPrimary (citable) accession number: P03079
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 29, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

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

External Data

Dasty 3