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Protein
Submitted name:

Phosphatase and tensin homolog, isoform CRA_a

Gene

Pten

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: 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 APC-Cdc20 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 sequence-specific DNA binding transcription factor activity Source: Ensembl
  47. postsynaptic density assembly Source: Ensembl
  48. prepulse inhibition Source: Ensembl
  49. presynaptic membrane assembly Source: Ensembl
  50. prostate gland growth Source: Ensembl
  51. protein kinase B signaling Source: Ensembl
  52. protein stabilization Source: Ensembl
  53. regulation of B cell apoptotic process Source: Ensembl
  54. regulation of myeloid cell apoptotic process Source: Ensembl
  55. response to arsenic-containing substance Source: RGD
  56. response to ATP Source: RGD
  57. response to drug Source: RGD
  58. response to estradiol Source: RGD
  59. response to ethanol Source: RGD
  60. response to glucose Source: RGD
  61. response to inorganic substance Source: RGD
  62. response to nutrient Source: RGD
  63. response to organic cyclic compound Source: RGD
  64. response to organic substance Source: RGD
  65. response to zinc ion Source: RGD
  66. rhythmic synaptic transmission Source: Ensembl
  67. social behavior Source: Ensembl
  68. synapse maturation Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

BRENDAi3.1.3.67. 5301.
ReactomeiREACT_272957. Synthesis of PIPs at the plasma membrane.
REACT_292491. Constitutive PI3K/AKT Signaling in Cancer.
REACT_321604. Negative regulation of the PI3K/AKT network.
REACT_337837. Synthesis of IP3 and IP4 in the cytosol.
REACT_342970. 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 Componenti: 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...

Family & Domainsi

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000119113.
HOGENOMiHOG000008008.
HOVERGENiHBG000239.
KOiK01110.
OMAiRSINENK.
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.
RefSeqiNP_113794.1. NM_031606.1.
UniGeneiRn.22158.

3D structure databases

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

Protein-protein interaction databases

MINTiMINT-4583512.
STRINGi10116.ENSRNOP00000028143.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5728.
RGDi61995. Pten.

Phylogenomic databases

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

Enzyme and pathway databases

BRENDAi3.1.3.67. 5301.
ReactomeiREACT_272957. Synthesis of PIPs at the plasma membrane.
REACT_292491. Constitutive PI3K/AKT Signaling in Cancer.
REACT_321604. Negative regulation of the PI3K/AKT network.
REACT_337837. Synthesis of IP3 and IP4 in the cytosol.
REACT_342970. Downstream TCR signaling.

Miscellaneous databases

NextBioi610364.
PROiO54857.

Gene expression databases

GenevestigatoriO54857.

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]
ProtoNetiSearch...

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: April 29, 2015
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

External Data

Dasty 3

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 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.