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Protein
Submitted name:

AKT1 substrate 1 (Proline-rich) (Predicted), isoform CRA_d

Gene

Akt1s1

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-RNO-165159. mTOR signalling.
R-RNO-166208. mTORC1-mediated signalling.
R-RNO-198323. AKT phosphorylates targets in the cytosol.
R-RNO-3371571. HSF1-dependent transactivation.

Names & Taxonomyi

Protein namesi
Submitted name:
AKT1 substrate 1 (Proline-rich) (Predicted), isoform CRA_dImported
Submitted name:
Protein Akt1s1Imported
Gene namesi
Name:Akt1s1Imported
Synonyms:Akt1s1_predictedImported
ORF Names:rCG_53542Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi1312049. Akt1s1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • nucleus Source: RGD
  • protein complex Source: RGD
  • TORC1 complex Source: Ensembl
Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027478.

Family & Domainsi

Phylogenomic databases

eggNOGiENOG410IXEE. Eukaryota.
ENOG41121RI. LUCA.
GeneTreeiENSGT00390000017397.
KOiK16184.
OMAiLFMMDED.
OrthoDBiEOG7X3QRW.

Family and domain databases

InterProiIPR026682. AKT1S1.
[Graphical view]
PANTHERiPTHR21844. PTHR21844. 1 hit.
PfamiPF15798. PRAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

D3ZH75-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGRPEELW EAVVGAAERF RARTGTELVL LTAAPPPPPR PGPCAYAAHG
60 70 80 90 100
RGALAEAARR CLHDIAQAHR AATATRPPGP PPAPQPPSPA PSSPPRPALA
110 120 130 140 150
REEDEEDEDE PTETETSGER LGGSDNGGLF MMDEDATLQD LPPFCESDPE
160 170 180 190 200
STDDGSLSEE TPAGPPAYPK LPATALPTQQ YAKSLPVSVP VWAFKEKRTE
210 220 230 240 250
ARSSDEENGP PSSPDLDRIA ASMRALVLRE AEDNQVFGDL PRPRLNTSDF

QKLKRKY
Length:257
Mass (Da):27,587
Last modified:April 20, 2010 - v1
Checksum:i76CD6BF22679FD7A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC094894 Genomic DNA. No translation available.
CH473979 Genomic DNA. Translation: EDM07453.1.
RefSeqiNP_001099729.2. NM_001106259.3.
UniGeneiRn.102669.
Rn.234559.

Genome annotation databases

EnsembliENSRNOT00000027478; ENSRNOP00000027478; ENSRNOG00000020289.
GeneIDi292887.
KEGGirno:292887.
UCSCiRGD:1312049. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC094894 Genomic DNA. No translation available.
CH473979 Genomic DNA. Translation: EDM07453.1.
RefSeqiNP_001099729.2. NM_001106259.3.
UniGeneiRn.102669.
Rn.234559.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027478.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000027478; ENSRNOP00000027478; ENSRNOG00000020289.
GeneIDi292887.
KEGGirno:292887.
UCSCiRGD:1312049. rat.

Organism-specific databases

CTDi84335.
RGDi1312049. Akt1s1.

Phylogenomic databases

eggNOGiENOG410IXEE. Eukaryota.
ENOG41121RI. LUCA.
GeneTreeiENSGT00390000017397.
KOiK16184.
OMAiLFMMDED.
OrthoDBiEOG7X3QRW.

Enzyme and pathway databases

ReactomeiR-RNO-165159. mTOR signalling.
R-RNO-166208. mTORC1-mediated signalling.
R-RNO-198323. AKT phosphorylates targets in the cytosol.
R-RNO-3371571. HSF1-dependent transactivation.

Miscellaneous databases

NextBioi634996.

Family and domain databases

InterProiIPR026682. AKT1S1.
[Graphical view]
PANTHERiPTHR21844. PTHR21844. 1 hit.
PfamiPF15798. PRAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  4. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiD3ZH75_RAT
AccessioniPrimary (citable) accession number: D3ZH75
Entry historyi
Integrated into UniProtKB/TrEMBL: April 20, 2010
Last sequence update: April 20, 2010
Last modified: January 20, 2016
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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 one 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.