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O54857 (O54857_RAT) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein names

Protein Pten Ensembl ENSRNOP00000028143

Protein tyrosine phosphatase and tensin homolog/mutated in multiple advanced cancers protein EMBL AAB96620.1

Protein tyrosine phosphatase and tensin-like protein EMBL AAO31948.1
Gene names
Name:Pten RGD 61995 EMBL AAO31948.1 Ensembl ENSRNOP00000028143
Synonyms:PTEN/MMAC1 EMBL AAB96620.1
ORF Names:rCG_47874 EMBL EDM13141.1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length403 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

Ontologies

Keywords
   Technical term3D-structure PDB 2K20
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of mitotic anaphase-promoting complex activity

Inferred from electronic annotation. Source: Compara

angiogenesis

Inferred from electronic annotation. Source: Compara

canonical Wnt receptor signaling pathway

Inferred from electronic annotation. Source: Compara

cardiac muscle tissue development

Inferred from electronic annotation. Source: Compara

central nervous system myelin maintenance

Inferred from electronic annotation. Source: Compara

central nervous system neuron axonogenesis

Inferred from electronic annotation. Source: Compara

dendritic spine morphogenesis

Inferred from electronic annotation. Source: Compara

dentate gyrus development

Inferred from electronic annotation. Source: Compara

endothelial cell migration

Inferred from electronic annotation. Source: Compara

forebrain morphogenesis

Inferred from electronic annotation. Source: Compara

induction of apoptosis

Inferred from electronic annotation. Source: Compara

inositol phosphate dephosphorylation

Inferred from electronic annotation. Source: Compara

learning or memory

Inferred from electronic annotation. Source: Compara

locomotor rhythm

Inferred from electronic annotation. Source: Compara

long-term synaptic potentiation

Inferred from electronic annotation. Source: Compara

male mating behavior

Inferred from electronic annotation. Source: Compara

maternal behavior

Inferred from electronic annotation. Source: Compara

multicellular organismal response to stress

Inferred from electronic annotation. Source: Compara

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Compara

negative regulation of axonogenesis

Inferred from electronic annotation. Source: Compara

negative regulation of cell aging

Inferred from electronic annotation. Source: Compara

negative regulation of cell migration

Inferred from electronic annotation. Source: Compara

negative regulation of cell size

Inferred from electronic annotation. Source: Compara

negative regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S

Inferred from electronic annotation. Source: Compara

negative regulation of dendritic spine morphogenesis

Inferred from electronic annotation. Source: Compara

negative regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Compara

negative regulation of excitatory postsynaptic membrane potential

Inferred from electronic annotation. Source: Compara

negative regulation of focal adhesion assembly

Inferred from electronic annotation. Source: Compara

negative regulation of myelination

Inferred from electronic annotation. Source: Compara

negative regulation of organ growth

Inferred from electronic annotation. Source: Compara

negative regulation of protein kinase B signaling cascade

Inferred from electronic annotation. Source: Compara

negative regulation of ribosome biogenesis

Inferred from electronic annotation. Source: Compara

negative regulation of synaptic vesicle clustering

Inferred from electronic annotation. Source: Compara

neuron-neuron synaptic transmission

Inferred from electronic annotation. Source: Compara

phosphatidylinositol dephosphorylation

Inferred from electronic annotation. Source: Compara

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Compara

positive regulation of excitatory postsynaptic membrane potential

Inferred from electronic annotation. Source: Compara

positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Compara

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Compara

postsynaptic density assembly

Inferred from electronic annotation. Source: Compara

prepulse inhibition

Inferred from electronic annotation. Source: Compara

presynaptic membrane assembly

Inferred from electronic annotation. Source: Compara

prostate gland growth

Inferred from electronic annotation. Source: Compara

protein kinase B signaling cascade

Inferred from electronic annotation. Source: Compara

protein stabilization

Inferred from electronic annotation. Source: Compara

regulation of B cell apoptotic process

Inferred from electronic annotation. Source: Compara

regulation of myeloid cell apoptotic process

Inferred from electronic annotation. Source: Compara

rhythmic synaptic transmission

Inferred from electronic annotation. Source: Compara

social behavior

Inferred from electronic annotation. Source: Compara

synapse maturation

Inferred from electronic annotation. Source: Compara

   Cellular_componentSchmidt-Lanterman incisure

Inferred from electronic annotation. Source: Compara

cytoplasm

Inferred from electronic annotation. Source: Compara

internal side of plasma membrane

Inferred from electronic annotation. Source: Compara

myelin sheath adaxonal region

Inferred from electronic annotation. Source: Compara

neuron projection

Inferred from electronic annotation. Source: Compara

nucleus

Inferred from electronic annotation. Source: Compara

   Molecular_functioninositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity

Inferred from electronic annotation. Source: Compara

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity

Inferred from electronic annotation. Source: Compara

phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity

Inferred from electronic annotation. Source: Compara

phosphatidylinositol-3-phosphatase activity

Inferred from electronic annotation. Source: Compara

protein serine/threonine phosphatase activity

Inferred from electronic annotation. Source: Compara

protein tyrosine phosphatase activity

Inferred from electronic annotation. Source: Compara

protein tyrosine/serine/threonine phosphatase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
O54857 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 243BFE35FE209FE5

FASTA40347,118
        10         20         30         40         50         60 
MTAIIKEIVS RNKRRYQEDG FDLDLTYIYP NIIAMGFPAE RLEGVYRNNI DDVVRFLDSK 

        70         80         90        100        110        120 
HKNHYKIYNL CAERHYDTAK FNCRVAQYPF EDHNPPQLEL IKPFCEDLDQ WLSEDDNHVA 

       130        140        150        160        170        180 
AIHCKAGKGR TGVMICAYLL HRGKFLKAQE ALDFYGEVRT RDKKGVTIPS QRRYVYYYSY 

       190        200        210        220        230        240 
LLKNHLDYRP VALLFHKMMF ETIPMFSGGT CNPQFVVCQL KVKIYSSNSG PTRREDKLMY 

       250        260        270        280        290        300 
FEFPQPLPVC GDIKVEFFHK QNKMLKKDKM FHFWVNTFFI PGPEETSEKV ENGSLCDQEI 

       310        320        330        340        350        360 
DSICSIERAD NDKEYLVLTL TKNDLDKANK DKANRYFSPN FKVKLYFTKT VEEPSNPEAS 

       370        380        390        400 
SSTSVTPDVS DNEPDHYRYS DTTDSDPENE PFDEDQHSQI TKV 

« Hide

References

« Hide 'large scale' references
[1]Roz L., Finocchiaro G.
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: Sprague-Dawley EMBL AAB96620.1.
Tissue: Brain EMBL AAB96620.1.
[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: BN EMBL AAO31948.1.
[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. expand/collapse author list , 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 Norway Ensembl ENSRNOP00000028143.
[4]"Gene and alternative splicing annotation with AIR."
Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M., Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z., Istrail S., Li P., Sutton G.
Genome Res. 15:54-66(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: BN EMBL EDM13141.1.
[5]Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M., Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F. expand/collapse author list , Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: BN EMBL EDM13141.1.
[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 Norway Ensembl ENSRNOP00000028143.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
IPIIPI00199035.
RefSeqNP_113794.1. NM_031606.1.
UniGeneRn.22158.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2K20NMR-B393-403[»]
SMRO54857. Positions 14-351.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000028143.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000028143; ENSRNOP00000028143; ENSRNOG00000020723.
GeneID50557.
KEGGrno:50557.

Organism-specific databases

CTD5728.
RGD61995. Pten.

Phylogenomic databases

eggNOGCOG2453.
GeneTreeENSGT00620000087779.
HOGENOMHOG000008008.
HOVERGENHBG000239.
InParanoidO54857.
KOK01110.
OMATRREDKH.
OrthoDBEOG434W64.

Gene expression databases

GenevestigatorO54857.

Family and domain databases

InterProIPR017361. Bifunc_PIno_P3_Pase/Pase_PTEN.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR014019. Phosphatase_tensin-typ.
IPR014020. Tensin_phosphatase_C2-dom.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PfamPF00782. DSPc. 1 hit.
PF10409. PTEN_C2. 1 hit.
[Graphical view]
PIRSFPIRSF038025. PTEN. 1 hit.
SUPFAMSSF49562. C2_CaLB. 1 hit.
PROSITEPS51182. C2_TENSIN. 1 hit.
PS51181. PPASE_TENSIN. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO54857.
NextBio610364.

Entry information

Entry nameO54857_RAT
AccessionPrimary (citable) accession number: O54857
Entry history
Integrated into UniProtKB/TrEMBL: June 1, 1998
Last sequence update: June 1, 1998
Last modified: May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)