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Q9D1F4 (AKTS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proline-rich AKT1 substrate 1

Short name=Proline-rich AKT substrate
Gene names
Name:Akt1s1
Synonyms:Pras
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length257 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.5

Subunit structure

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. Ref.3

Subcellular location

Cytoplasmcytosol. Note: Found in the cytosolic fraction of the brain. Colocalizes with cortical neurons following ischemic/reperfusion injury. Ref.3

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 257257Proline-rich AKT1 substrate 1
PRO_0000253447

Regions

Compositional bias35 – 439Poly-Pro
Compositional bias77 – 9721Pro-rich

Amino acid modifications

Modified residue881Phosphoserine By similarity
Modified residue921Phosphoserine By similarity
Modified residue1841Phosphoserine By similarity
Modified residue2031Phosphoserine Ref.6
Modified residue2041Phosphoserine Ref.6
Modified residue2121Phosphoserine Ref.6
Modified residue2131Phosphoserine Ref.6
Modified residue2471Phosphothreonine; by PKB/AKT1 By similarity UniProtKB Q96B36

Sequences

Sequence LengthMass (Da)Tools
Q9D1F4 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 4BFFC8630DBBA5EC

FASTA25727,483
        10         20         30         40         50         60 
MASGRPEELW EAVVGAAERF QARTGTELVL LTAAPPPPPR PGPCAYAAHG RGALAEAARR 

        70         80         90        100        110        120 
CLHDIAQAHR AATATRPPGP PPAPQPPSPA PSPPPRPALA REDEEEDEDE PTETETSGER 

       130        140        150        160        170        180 
LGGSDNGGLF MMDEDATLQD LPPFCESDPE STDDGSLSEE TPAGPTACPQ PPATALPTQQ 

       190        200        210        220        230        240 
YAKSLPVSVP VWAFKEKRTE ARSSDEENGP PSSPDLDRIA ASMRALVLRE AEDTQVFGDL 

       250 
PRPRLNTSDF QKLKRKY 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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/6J and NOD.
Tissue: Embryo.
[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]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS21218.1.
RefSeqNP_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.
UniGeneMm.148007.
Mm.491121.

3D structure databases

ProteinModelPortalQ9D1F4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9D1F4. 1 interaction.

PTM databases

PhosphoSiteQ9D1F4.

Proteomic databases

MaxQBQ9D1F4.
PaxDbQ9D1F4.
PRIDEQ9D1F4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000054343; ENSMUSP00000049764; ENSMUSG00000011096.
ENSMUST00000107880; ENSMUSP00000103512; ENSMUSG00000011096.
GeneID67605.
KEGGmmu:67605.
UCSCuc009grd.2. mouse.

Organism-specific databases

CTD84335.
MGIMGI:1914855. Akt1s1.

Phylogenomic databases

eggNOGNOG40718.
GeneTreeENSGT00390000017397.
HOGENOMHOG000236322.
HOVERGENHBG059465.
InParanoidA2RT52.
KOK16184.
PhylomeDBQ9D1F4.

Gene expression databases

ArrayExpressQ9D1F4.
BgeeQ9D1F4.
CleanExMM_AKT1S1.
GenevestigatorQ9D1F4.

Family and domain databases

InterProIPR026682. AKT1S1.
[Graphical view]
PANTHERPTHR21844. PTHR21844. 1 hit.
ProtoNetSearch...

Other

ChiTaRSAKT1S1. mouse.
NextBio325025.
PROQ9D1F4.
SOURCESearch...

Entry information

Entry nameAKTS1_MOUSE
AccessionPrimary (citable) accession number: Q9D1F4
Secondary accession number(s): A2RT52
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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