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Protein

Proline-rich AKT1 substrate 1

Gene

Akt1s1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Subunit of mTORC1, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino acids. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Within mTORC1, AKT1S1 negatively regulates mTOR activity in a manner that is dependent on its phosphorylation state and binding to 14-3-3. Inhibits RHEB-GTP-dependent mTORC1 activation. Substrate for AKT1 phosphorylation, but can also be activated by AKT1-independent mechanisms. May also play a role in nerve growth factor-mediated neuroprotection.2 Publications

GO - Biological processi

  1. negative regulation of cell size Source: MGI
  2. negative regulation of protein kinase activity Source: MGI
  3. negative regulation of TOR signaling Source: MGI
  4. neurotrophin TRK receptor signaling pathway Source: InterPro
  5. Notch signaling pathway Source: MGI
  6. regulation of neuron apoptotic process Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
REACT_213550. HSF1-dependent transactivation.
REACT_220918. AKT phosphorylates targets in the cytosol.

Names & Taxonomyi

Protein namesi
Recommended name:
Proline-rich AKT1 substrate 1
Short name:
Proline-rich AKT substrate
Gene namesi
Name:Akt1s1Imported
Synonyms:Pras1 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1914855. Akt1s1.

Subcellular locationi

Cytoplasmcytosol 1 Publication
Note: Found in the cytosolic fraction of the brain. Colocalizes with cortical neurons following ischemic/reperfusion injury.

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: UniProtKB
  3. nucleus Source: Ensembl
  4. TORC1 complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 257257Proline-rich AKT1 substrate 1PRO_0000253447Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei88 – 881PhosphoserineBy similarity
Modified residuei92 – 921PhosphoserineBy similarity
Modified residuei184 – 1841PhosphoserineBy similarity
Modified residuei203 – 2031Phosphoserine1 Publication
Modified residuei204 – 2041Phosphoserine1 Publication
Modified residuei212 – 2121Phosphoserine1 Publication
Modified residuei213 – 2131Phosphoserine1 Publication
Modified residuei247 – 2471Phosphothreonine; by PKB/AKT1By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9D1F4.
PaxDbiQ9D1F4.
PRIDEiQ9D1F4.

PTM databases

PhosphoSiteiQ9D1F4.

Expressioni

Gene expression databases

BgeeiQ9D1F4.
CleanExiMM_AKT1S1.
ExpressionAtlasiQ9D1F4. baseline and differential.
GenevestigatoriQ9D1F4.

Interactioni

Subunit structurei

Part of the mammalian target of rapamycin complex 1 (mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR. mTORC1 binds to and is inhibited by FKBP12-rapamycin. Interacts directly with RPTOR. The phosphorylated form interacts with 14-3-3 proteins and with phosphorylated AKT1 following transient focal cerebral ischemia in vivo.1 Publication

Protein-protein interaction databases

IntActiQ9D1F4. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9D1F4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi35 – 439Poly-ProSequence Analysis
Compositional biasi77 – 9721Pro-richSequence AnalysisAdd
BLAST

Phylogenomic databases

eggNOGiNOG40718.
GeneTreeiENSGT00390000017397.
HOGENOMiHOG000236322.
HOVERGENiHBG059465.
InParanoidiQ9D1F4.
KOiK16184.
PhylomeDBiQ9D1F4.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q9D1F4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASGRPEELW EAVVGAAERF QARTGTELVL LTAAPPPPPR PGPCAYAAHG
60 70 80 90 100
RGALAEAARR CLHDIAQAHR AATATRPPGP PPAPQPPSPA PSPPPRPALA
110 120 130 140 150
REDEEEDEDE PTETETSGER LGGSDNGGLF MMDEDATLQD LPPFCESDPE
160 170 180 190 200
STDDGSLSEE TPAGPTACPQ PPATALPTQQ YAKSLPVSVP VWAFKEKRTE
210 220 230 240 250
ARSSDEENGP PSSPDLDRIA ASMRALVLRE AEDTQVFGDL PRPRLNTSDF

QKLKRKY
Length:257
Mass (Da):27,483
Last modified:June 1, 2001 - v1
Checksum:i4BFFC8630DBBA5EC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003638 mRNA. Translation: BAB22905.1.
AK141771 mRNA. Translation: BAE24829.1.
AK154110 mRNA. Translation: BAE32383.1.
BC132372 mRNA. Translation: AAI32373.1.
BC132374 mRNA. Translation: AAI32375.1.
CCDSiCCDS21218.1.
RefSeqiNP_001240849.1. NM_001253920.1.
NP_001277623.1. NM_001290694.1.
NP_001277624.1. NM_001290695.1.
NP_080546.1. NM_026270.4.
XP_006541182.1. XM_006541119.1.
XP_006541183.1. XM_006541120.1.
XP_006541184.1. XM_006541121.1.
XP_006541185.1. XM_006541122.1.
UniGeneiMm.148007.
Mm.491121.

Genome annotation databases

EnsembliENSMUST00000054343; ENSMUSP00000049764; ENSMUSG00000011096.
ENSMUST00000107880; ENSMUSP00000103512; ENSMUSG00000011096.
GeneIDi67605.
KEGGimmu:67605.
UCSCiuc009grd.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003638 mRNA. Translation: BAB22905.1.
AK141771 mRNA. Translation: BAE24829.1.
AK154110 mRNA. Translation: BAE32383.1.
BC132372 mRNA. Translation: AAI32373.1.
BC132374 mRNA. Translation: AAI32375.1.
CCDSiCCDS21218.1.
RefSeqiNP_001240849.1. NM_001253920.1.
NP_001277623.1. NM_001290694.1.
NP_001277624.1. NM_001290695.1.
NP_080546.1. NM_026270.4.
XP_006541182.1. XM_006541119.1.
XP_006541183.1. XM_006541120.1.
XP_006541184.1. XM_006541121.1.
XP_006541185.1. XM_006541122.1.
UniGeneiMm.148007.
Mm.491121.

3D structure databases

ProteinModelPortaliQ9D1F4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9D1F4. 1 interaction.

PTM databases

PhosphoSiteiQ9D1F4.

Proteomic databases

MaxQBiQ9D1F4.
PaxDbiQ9D1F4.
PRIDEiQ9D1F4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000054343; ENSMUSP00000049764; ENSMUSG00000011096.
ENSMUST00000107880; ENSMUSP00000103512; ENSMUSG00000011096.
GeneIDi67605.
KEGGimmu:67605.
UCSCiuc009grd.2. mouse.

Organism-specific databases

CTDi84335.
MGIiMGI:1914855. Akt1s1.

Phylogenomic databases

eggNOGiNOG40718.
GeneTreeiENSGT00390000017397.
HOGENOMiHOG000236322.
HOVERGENiHBG059465.
InParanoidiQ9D1F4.
KOiK16184.
PhylomeDBiQ9D1F4.

Enzyme and pathway databases

ReactomeiREACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
REACT_213550. HSF1-dependent transactivation.
REACT_220918. AKT phosphorylates targets in the cytosol.

Miscellaneous databases

ChiTaRSiAkt1s1. mouse.
NextBioi325025.
PROiQ9D1F4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D1F4.
CleanExiMM_AKT1S1.
ExpressionAtlasiQ9D1F4. baseline and differential.
GenevestigatoriQ9D1F4.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6JImported and NODImported.
    Tissue: EmbryoImported.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  3. "Neuroprotective role of a proline-rich Akt substrate in apoptotic neuronal cell death after stroke: relationships with nerve growth factor."
    Saito A., Narasimhan P., Hayashi T., Okuno S., Ferrand-Drake M., Chan P.H.
    J. Neurosci. 24:1584-1593(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  5. "Modulation of proline-rich akt substrate survival signaling pathways by oxidative stress in mouse brains after transient focal cerebral ischemia."
    Saito A., Hayashi T., Okuno S., Nishi T., Chan P.H.
    Stroke 37:513-517(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-204; SER-212 AND SER-213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiAKTS1_MOUSE
AccessioniPrimary (citable) accession number: Q9D1F4
Secondary accession number(s): A2RT52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: June 1, 2001
Last modified: February 4, 2015
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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.