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O54857

- O54857_RAT

UniProt

O54857 - O54857_RAT

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Protein
Submitted name:

Phosphatase and tensin homolog, isoform CRA_a

Gene

Pten

Organism
Rattus norvegicus (Rat)
Status
Unreviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity Source: Ensembl
  2. magnesium ion binding Source: InterPro
  3. PDZ domain binding Source: RGD
  4. phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity Source: RGD
  5. phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity Source: InterPro
  6. phosphatidylinositol-3-phosphatase activity Source: Ensembl
  7. platelet-derived growth factor receptor binding Source: RGD
  8. protein serine/threonine phosphatase activity Source: Ensembl
  9. protein tyrosine/serine/threonine phosphatase activity Source: RGD
  10. protein tyrosine phosphatase activity Source: InterPro

GO - Biological processi

  1. activation of mitotic anaphase-promoting complex activity Source: Ensembl
  2. aging Source: RGD
  3. angiogenesis Source: Ensembl
  4. canonical Wnt signaling pathway Source: Ensembl
  5. cardiac muscle tissue development Source: Ensembl
  6. central nervous system myelin maintenance Source: Ensembl
  7. central nervous system neuron axonogenesis Source: Ensembl
  8. dendritic spine morphogenesis Source: Ensembl
  9. dentate gyrus development Source: Ensembl
  10. endothelial cell migration Source: Ensembl
  11. forebrain morphogenesis Source: Ensembl
  12. inositol phosphate dephosphorylation Source: InterPro
  13. locomotor rhythm Source: Ensembl
  14. long term synaptic depression Source: RGD
  15. long-term synaptic potentiation Source: Ensembl
  16. male mating behavior Source: Ensembl
  17. maternal behavior Source: Ensembl
  18. memory Source: RGD
  19. multicellular organismal response to stress Source: Ensembl
  20. negative regulation of apoptotic process Source: Ensembl
  21. negative regulation of axonogenesis Source: Ensembl
  22. negative regulation of cell aging Source: Ensembl
  23. negative regulation of cell migration Source: InterPro
  24. negative regulation of cell proliferation Source: RGD
  25. negative regulation of cell size Source: Ensembl
  26. negative regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle Source: Ensembl
  27. negative regulation of dendritic spine morphogenesis Source: Ensembl
  28. negative regulation of epithelial cell proliferation Source: Ensembl
  29. negative regulation of excitatory postsynaptic membrane potential Source: Ensembl
  30. negative regulation of focal adhesion assembly Source: InterPro
  31. negative regulation of G1/S transition of mitotic cell cycle Source: Ensembl
  32. negative regulation of myelination Source: Ensembl
  33. negative regulation of organ growth Source: Ensembl
  34. negative regulation of phagocytosis Source: RGD
  35. negative regulation of protein kinase B signaling Source: Ensembl
  36. negative regulation of ribosome biogenesis Source: Ensembl
  37. negative regulation of synaptic vesicle clustering Source: Ensembl
  38. neuron-neuron synaptic transmission Source: Ensembl
  39. neuron projection development Source: RGD
  40. phosphatidylinositol dephosphorylation Source: RGD
  41. platelet-derived growth factor receptor signaling pathway Source: RGD
  42. positive regulation of apoptotic process Source: RGD
  43. positive regulation of apoptotic signaling pathway Source: Ensembl
  44. positive regulation of cell proliferation Source: Ensembl
  45. positive regulation of excitatory postsynaptic membrane potential Source: Ensembl
  46. positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: Ensembl
  47. positive regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
  48. postsynaptic density assembly Source: Ensembl
  49. prepulse inhibition Source: Ensembl
  50. presynaptic membrane assembly Source: Ensembl
  51. prostate gland growth Source: Ensembl
  52. protein kinase B signaling Source: Ensembl
  53. protein stabilization Source: Ensembl
  54. regulation of B cell apoptotic process Source: Ensembl
  55. regulation of myeloid cell apoptotic process Source: Ensembl
  56. response to arsenic-containing substance Source: RGD
  57. response to ATP Source: RGD
  58. response to drug Source: RGD
  59. response to estradiol Source: RGD
  60. response to ethanol Source: RGD
  61. response to glucose Source: RGD
  62. response to inorganic substance Source: RGD
  63. response to nutrient Source: RGD
  64. response to organic cyclic compound Source: RGD
  65. response to organic substance Source: RGD
  66. response to zinc ion Source: RGD
  67. rhythmic synaptic transmission Source: Ensembl
  68. social behavior Source: Ensembl
  69. synapse maturation Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_198600. Synthesis of PIPs at the plasma membrane.
REACT_198661. Synthesis of IP3 and IP4 in the cytosol.
REACT_198729. Constitutive PI3K/AKT Signaling in Cancer.
REACT_251465. Negative regulation of the PI3K/AKT network.
REACT_254949. Downstream TCR signaling.

Names & Taxonomyi

Protein namesi
Submitted name:
Phosphatase and tensin homolog, isoform CRA_aImported
Submitted name:
Protein PtenImported
Submitted name:
Protein tyrosine phosphatase and tensin homolog/mutated in multiple advanced cancers proteinImported
Submitted name:
Protein tyrosine phosphatase and tensin-like proteinImported
Gene namesi
Name:PtenImported
Synonyms:PTEN/MMAC1Imported
ORF Names:rCG_47874Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 1

Organism-specific databases

RGDi61995. Pten.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: RGD
  2. cytoplasmic side of plasma membrane Source: Ensembl
  3. dendritic spine Source: RGD
  4. mitochondrion Source: RGD
  5. myelin sheath adaxonal region Source: Ensembl
  6. neuron projection Source: RGD
  7. nucleus Source: RGD
  8. postsynaptic membrane Source: RGD
  9. Schmidt-Lanterman incisure Source: Ensembl
Complete GO annotation...

Expressioni

Gene expression databases

GenevestigatoriO54857.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Dbn1Q072663EBI-8074312,EBI-918187
Dlg4P310165EBI-8074312,EBI-375655

Protein-protein interaction databases

MINTiMINT-4583512.
STRINGi10116.ENSRNOP00000028143.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K20NMR-B393-403[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO54857.

Family & Domainsi

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000119113.
HOGENOMiHOG000008008.
HOVERGENiHBG000239.
KOiK01110.
OMAiKEYLILT.
OrthoDBiEOG7R2BJ5.
TreeFamiTF324513.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR017361. Bifunc_PIno_P3_Pase/Pase_PTEN.
IPR000008. C2_dom.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR014020. Tensin_C2-dom.
IPR029023. Tensin_lipid_phosphatase_dom.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PfamiPF00782. DSPc. 1 hit.
PF10409. PTEN_C2. 1 hit.
[Graphical view]
PIRSFiPIRSF038025. PTEN. 1 hit.
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF52799. SSF52799. 1 hit.
PROSITEiPS51182. C2_TENSIN. 1 hit.
PS51181. PPASE_TENSIN. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O54857-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTAIIKEIVS RNKRRYQEDG FDLDLTYIYP NIIAMGFPAE RLEGVYRNNI
60 70 80 90 100
DDVVRFLDSK HKNHYKIYNL CAERHYDTAK FNCRVAQYPF EDHNPPQLEL
110 120 130 140 150
IKPFCEDLDQ WLSEDDNHVA AIHCKAGKGR TGVMICAYLL HRGKFLKAQE
160 170 180 190 200
ALDFYGEVRT RDKKGVTIPS QRRYVYYYSY LLKNHLDYRP VALLFHKMMF
210 220 230 240 250
ETIPMFSGGT CNPQFVVCQL KVKIYSSNSG PTRREDKLMY FEFPQPLPVC
260 270 280 290 300
GDIKVEFFHK QNKMLKKDKM FHFWVNTFFI PGPEETSEKV ENGSLCDQEI
310 320 330 340 350
DSICSIERAD NDKEYLVLTL TKNDLDKANK DKANRYFSPN FKVKLYFTKT
360 370 380 390 400
VEEPSNPEAS SSTSVTPDVS DNEPDHYRYS DTTDSDPENE PFDEDQHSQI

TKV
Length:403
Mass (Da):47,118
Last modified:June 1, 1998 - v1
Checksum:i243BFE35FE209FE5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06010605 Genomic DNA. No translation available.
AABR06010606 Genomic DNA. No translation available.
AABR06010607 Genomic DNA. No translation available.
AF017185 mRNA. Translation: AAB96620.1.
AF455569 mRNA. Translation: AAO31948.1.
CH473953 Genomic DNA. Translation: EDM13141.1.
RefSeqiNP_113794.1. NM_031606.1.
UniGeneiRn.22158.

Genome annotation databases

EnsembliENSRNOT00000028143; ENSRNOP00000028143; ENSRNOG00000020723.
GeneIDi50557.
KEGGirno:50557.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06010605 Genomic DNA. No translation available.
AABR06010606 Genomic DNA. No translation available.
AABR06010607 Genomic DNA. No translation available.
AF017185 mRNA. Translation: AAB96620.1 .
AF455569 mRNA. Translation: AAO31948.1 .
CH473953 Genomic DNA. Translation: EDM13141.1 .
RefSeqi NP_113794.1. NM_031606.1.
UniGenei Rn.22158.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2K20 NMR - B 393-403 [» ]
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-4583512.
STRINGi 10116.ENSRNOP00000028143.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000028143 ; ENSRNOP00000028143 ; ENSRNOG00000020723 .
GeneIDi 50557.
KEGGi rno:50557.

Organism-specific databases

CTDi 5728.
RGDi 61995. Pten.

Phylogenomic databases

eggNOGi COG2453.
GeneTreei ENSGT00760000119113.
HOGENOMi HOG000008008.
HOVERGENi HBG000239.
KOi K01110.
OMAi KEYLILT.
OrthoDBi EOG7R2BJ5.
TreeFami TF324513.

Enzyme and pathway databases

Reactomei REACT_198600. Synthesis of PIPs at the plasma membrane.
REACT_198661. Synthesis of IP3 and IP4 in the cytosol.
REACT_198729. Constitutive PI3K/AKT Signaling in Cancer.
REACT_251465. Negative regulation of the PI3K/AKT network.
REACT_254949. Downstream TCR signaling.

Miscellaneous databases

EvolutionaryTracei O54857.
NextBioi 610364.
PROi O54857.

Gene expression databases

Genevestigatori O54857.

Family and domain databases

Gene3Di 3.90.190.10. 1 hit.
InterProi IPR017361. Bifunc_PIno_P3_Pase/Pase_PTEN.
IPR000008. C2_dom.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR014020. Tensin_C2-dom.
IPR029023. Tensin_lipid_phosphatase_dom.
IPR016130. Tyr_Pase_AS.
[Graphical view ]
Pfami PF00782. DSPc. 1 hit.
PF10409. PTEN_C2. 1 hit.
[Graphical view ]
PIRSFi PIRSF038025. PTEN. 1 hit.
SUPFAMi SSF49562. SSF49562. 1 hit.
SSF52799. SSF52799. 1 hit.
PROSITEi PS51182. C2_TENSIN. 1 hit.
PS51181. PPASE_TENSIN. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Roz L., Finocchiaro G.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Sprague-DawleyImported.
    Tissue: BrainImported.
  2. "Recurrent allelic imbalance at the rat Pten locus in DMBA-induced fibrosarcomas."
    Sjoling A., Samuelson E., Adamovic T., Behboudi A., Rohme D., Levan G.
    Genes Chromosomes Cancer 36:70-79(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  3. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  4. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  5. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  6. "Solution structure of Par-3 PDZ3 in complex with PTEN peptide."
    Feng W., Wu H., Chan L., Zhang M.
    Submitted (MAR-2008) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 393-403.
  7. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiO54857_RAT
AccessioniPrimary (citable) accession number: O54857
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 1998
Last sequence update: June 1, 1998
Last modified: November 26, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported, Complete proteome, Reference proteomeImported

External Data

Dasty 3