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Q96B36

- AKTS1_HUMAN

UniProt

Q96B36 - AKTS1_HUMAN

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Protein

Proline-rich AKT1 substrate 1

Gene

AKT1S1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequences (3)
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

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 proteins. 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.3 Publications

GO - Biological processi

  1. epidermal growth factor receptor signaling pathway Source: Reactome
  2. Fc-epsilon receptor signaling pathway Source: Reactome
  3. fibroblast growth factor receptor signaling pathway Source: Reactome
  4. innate immune response Source: Reactome
  5. negative regulation of cell size Source: UniProtKB
  6. negative regulation of protein kinase activity Source: UniProtKB
  7. negative regulation of TOR signaling Source: UniProtKB
  8. neurotrophin TRK receptor signaling pathway Source: Reactome
  9. phosphatidylinositol-mediated signaling Source: Reactome
  10. regulation of neuron apoptotic process Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_12564. AKT phosphorylates targets in the cytosol.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_200775. HSF1-dependent transactivation.
SignaLinkiQ96B36.

Names & Taxonomyi

Protein namesi
Recommended name:
Proline-rich AKT1 substrate 1
Alternative name(s):
40 kDa proline-rich AKT substrate
Gene namesi
Name:AKT1S1Imported
Synonyms:PRAS402 Publications
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:28426. AKT1S1.

Subcellular locationi

Cytoplasm › cytosol By similarity
Note: Found in the cytosolic fraction of the brain.By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi246 – 2461T → A: Suppresses S6K1 phosphorylation by mTORC1. 1 Publication

Organism-specific databases

PharmGKBiPA134943587.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 256256Proline-rich AKT1 substrate 1PRO_0000253446Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei88 – 881Phosphoserine3 Publications
Modified residuei92 – 921Phosphoserine3 Publications
Modified residuei183 – 1831Phosphoserine5 Publications
Modified residuei202 – 2021Phosphoserine3 Publications
Modified residuei203 – 2031Phosphoserine2 Publications
Modified residuei211 – 2111Phosphoserine3 Publications
Modified residuei212 – 2121Phosphoserine3 Publications
Modified residuei246 – 2461Phosphothreonine; by PKB/AKT15 Publications

Post-translational modificationi

Phosphorylated by AKT1. Phosphorylation relieves inhibitory function on mTORC1.6 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ96B36.
PaxDbiQ96B36.
PRIDEiQ96B36.

PTM databases

PhosphoSiteiQ96B36.

Expressioni

Tissue specificityi

Widely expressed with highest levels of expression in liver and heart. Expressed at higher levels in cancer cell lines (e.g. A-549 and HeLa) than in normal cell lines (e.g. HEK293).2 Publications

Gene expression databases

BgeeiQ96B36.
CleanExiHS_AKT1S1.
ExpressionAtlasiQ96B36. baseline and differential.
GenevestigatoriQ96B36.

Organism-specific databases

HPAiCAB021903.
HPA043590.

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BMH1P293113EBI-720593,EBI-3661From a different organism.
YWHAHQ049173EBI-720593,EBI-306940

Protein-protein interaction databases

BioGridi124059. 13 interactions.
IntActiQ96B36. 11 interactions.
MINTiMINT-3317903.
STRINGi9606.ENSP00000341698.

Structurei

3D structure databases

ProteinModelPortaliQ96B36.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi35 – 439Poly-ProSequence Analysis
Compositional biasi77 – 9620Pro-richSequence AnalysisAdd
BLAST

Phylogenomic databases

eggNOGiNOG40718.
GeneTreeiENSGT00390000017397.
HOVERGENiHBG059465.
InParanoidiQ96B36.
KOiK16184.
OMAiLFMMDED.
OrthoDBiEOG7X3QRW.
PhylomeDBiQ96B36.

Family and domain databases

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

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 12 Publications (identifier: Q96B36-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASGRPEELW EAVVGAAERF RARTGTELVL LTAAPPPPPR PGPCAYAAHG 
        60         70         80         90        100
RGALAEAARR CLHDIALAHR AATAARPPAP PPAPQPPSPT PSPPRPTLAR 
       110        120        130        140        150
EDNEEDEDEP TETETSGEQL GISDNGGLFV MDEDATLQDL PPFCESDPES 
       160        170        180        190        200
TDDGSLSEET PAGPPTCSVP PASALPTQQY AKSLPVSVPV WGFKEKRTEA 
       210        220        230        240        250
RSSDEENGPP SSPDLDRIAA SMRALVLREA EDTQVFGDLP RPRLNTSDFQ 

KLKRKY
Length:256
Mass (Da):27,383
Last modified:December 1, 2001 - v1
Checksum:iF6CB195CBB54326C
GO
Isoform 21 Publication (identifier: Q96B36-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-130: Missing.

Note: No experimental confirmation available.Curated

Show »
Length:126
Mass (Da):13,807
Checksum:i2E34744BBEFEC1E9
GO
Isoform 3 (identifier: Q96B36-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSFEGGDGAGPAMLATGTARM

Note: No experimental confirmation available.

Show »
Length:276
Mass (Da):29,262
Checksum:i3866EE718A29CC48
GO

Sequence cautioni

The sequence AAH00031.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti108 – 1081D → G in BAB70937. (PubMed:14702039)Curated
Sequence conflicti196 – 1961K → M in BAB70937. (PubMed:14702039)Curated
Sequence conflicti233 – 2331T → A in BAB70937. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti47 – 471A → P.1 Publication
Corresponds to variant rs17850191 [ dbSNP | Ensembl ].		VAR_028239

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 130130Missing in isoform 2. 1 PublicationVSP_052182Add
BLAST
Alternative sequencei1 – 11M → MSFEGGDGAGPAMLATGTAR M in isoform 3. 1 PublicationVSP_047536

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK055511 mRNA. Translation: BAB70937.1.
AK092610 mRNA. Translation: BAG52583.1.
AK316603 mRNA. Translation: BAG38190.1.
AK226004 mRNA. No translation available.
AC118341 Genomic DNA. No translation available.
CH471177 Genomic DNA. Translation: EAW52570.1.
CH471177 Genomic DNA. Translation: EAW52568.1.
BC000031 mRNA. Translation: AAH00031.2. Different initiation.
BC007416 mRNA. Translation: AAH07416.1.
BC015562 mRNA. Translation: AAH15562.1.
BC016043 mRNA. Translation: AAH16043.1.
BC051844 mRNA. Translation: AAH51844.1.
CCDSiCCDS12784.1. [Q96B36-1]
CCDS59410.1. [Q96B36-3]
RefSeqiNP_001092102.1. NM_001098632.2. [Q96B36-1]
NP_001092103.1. NM_001098633.3. [Q96B36-1]
NP_001265088.1. NM_001278159.1. [Q96B36-1]
NP_001265089.1. NM_001278160.1. [Q96B36-1]
NP_115751.3. NM_032375.5. [Q96B36-3]
UniGeneiHs.515542.
Hs.610819.

Genome annotation databases

EnsembliENST00000344175; ENSP00000341698; ENSG00000204673. [Q96B36-1]
ENST00000391831; ENSP00000375707; ENSG00000204673. [Q96B36-1]
ENST00000391832; ENSP00000375708; ENSG00000204673. [Q96B36-1]
ENST00000391833; ENSP00000375709; ENSG00000204673. [Q96B36-1]
ENST00000391834; ENSP00000375710; ENSG00000204673. [Q96B36-1]
ENST00000391835; ENSP00000375711; ENSG00000204673. [Q96B36-3]
GeneIDi84335.
KEGGihsa:84335.
UCSCiuc002pql.5. human.
uc002pqm.5. human. [Q96B36-1]

Polymorphism databases

DMDMi74731194.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
 AK055511 mRNA. Translation: BAB70937.1 .
AK092610 mRNA. Translation: BAG52583.1 .
AK316603 mRNA. Translation: BAG38190.1 .
AK226004 mRNA. No translation available.
AC118341 Genomic DNA. No translation available.
CH471177 Genomic DNA. Translation: EAW52570.1 .
CH471177 Genomic DNA. Translation: EAW52568.1 .
BC000031 mRNA. Translation: AAH00031.2 . Different initiation.
BC007416 mRNA. Translation: AAH07416.1 .
BC015562 mRNA. Translation: AAH15562.1 .
BC016043 mRNA. Translation: AAH16043.1 .
BC051844 mRNA. Translation: AAH51844.1 .
CCDSi CCDS12784.1. [Q96B36-1 ]
CCDS59410.1. [Q96B36-3 ]
RefSeqi NP_001092102.1. NM_001098632.2. [Q96B36-1 ]
NP_001092103.1. NM_001098633.3. [Q96B36-1 ]
NP_001265088.1. NM_001278159.1. [Q96B36-1 ]
NP_001265089.1. NM_001278160.1. [Q96B36-1 ]
NP_115751.3. NM_032375.5. [Q96B36-3 ]
UniGenei Hs.515542.
Hs.610819.

3D structure databases

ProteinModelPortali Q96B36.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124059. 13 interactions.
IntActi Q96B36. 11 interactions.
MINTi MINT-3317903.
STRINGi 9606.ENSP00000341698.

Chemistry

BindingDBi Q96B36.
ChEMBLi CHEMBL1255161.

PTM databases

PhosphoSitei Q96B36.

Polymorphism databases

DMDMi 74731194.

Proteomic databases

MaxQBi Q96B36.
PaxDbi Q96B36.
PRIDEi Q96B36.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000344175 ; ENSP00000341698 ; ENSG00000204673 . [Q96B36-1 ]
ENST00000391831 ; ENSP00000375707 ; ENSG00000204673 . [Q96B36-1 ]
ENST00000391832 ; ENSP00000375708 ; ENSG00000204673 . [Q96B36-1 ]
ENST00000391833 ; ENSP00000375709 ; ENSG00000204673 . [Q96B36-1 ]
ENST00000391834 ; ENSP00000375710 ; ENSG00000204673 . [Q96B36-1 ]
ENST00000391835 ; ENSP00000375711 ; ENSG00000204673 . [Q96B36-3 ]
GeneIDi 84335.
KEGGi hsa:84335.
UCSCi uc002pql.5. human.
uc002pqm.5. human. [Q96B36-1 ]

Organism-specific databases

CTDi 84335.
GeneCardsi GC19M050372.
HGNCi HGNC:28426. AKT1S1.
HPAi CAB021903.
HPA043590.
MIMi 610221. gene.
neXtProti NX_Q96B36.
PharmGKBi PA134943587.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG40718.
GeneTreei ENSGT00390000017397.
HOVERGENi HBG059465.
InParanoidi Q96B36.
KOi K16184.
OMAi LFMMDED.
OrthoDBi EOG7X3QRW.
PhylomeDBi Q96B36.

Enzyme and pathway databases

Reactomei REACT_12564. AKT phosphorylates targets in the cytosol.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_200775. HSF1-dependent transactivation.
SignaLinki Q96B36.

Miscellaneous databases

ChiTaRSi AKT1S1. human.
GeneWikii AKT1S1.
GenomeRNAii 84335.
NextBioi 35535165.
PROi Q96B36.
SOURCEi Search...

Gene expression databases

Bgeei Q96B36.
CleanExi HS_AKT1S1.
ExpressionAtlasi Q96B36. baseline and differential.
Genevestigatori Q96B36.

Family and domain databases

InterProi IPR026682. AKT1S1.
[Graphical view ]
PANTHERi PTHR21844. PTHR21844. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Prostate and Synovium.
  2. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Coronary artery.
  3. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORMS 1 AND 2), VARIANT PRO-47.
    Tissue: BrainImported, EyeImported and SkinImported.
  6. "Identification of a proline-rich Akt substrate as a 14-3-3 binding partner."
    Kovacina K.S., Park G.Y., Bae S.S., Guzzetta A.W., Schaefer E., Birnbaum M.J., Roth R.A.
    J. Biol. Chem. 278:10189-10194(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH 14-3-3, TISSUE SPECIFICITY, PHOSPHORYLATION AT THR-246.
  7. "Expression of proline-rich Akt-substrate PRAS40 in cell survival pathway and carcinogenesis."
    Huang B., Porter G.
    Acta Pharmacol. Sin. 26:1253-1258(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "PRAS40 is an insulin-regulated inhibitor of the mTORC1 protein kinase."
    Sancak Y., Thoreen C.C., Peterson T.R., Lindquist R.A., Kang S.A., Spooner E., Carr S.A., Sabatini D.M.
    Mol. Cell 25:903-915(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE TORC1 COMPLEX, INTERACTION WITH RPTOR.
  10. "Insulin signalling to mTOR mediated by the Akt/PKB substrate PRAS40."
    Vander Haar E., Lee S.-I., Bandhakavi S., Griffin T.J., Kim D.-H.
    Nat. Cell Biol. 9:316-323(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE TORC1 COMPLEX, MUTAGENESIS OF THR-246.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-92; SER-183; SER-202; SER-203; SER-211; SER-212 AND THR-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-92; SER-183; SER-202; SER-211; SER-212 AND THR-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-202; SER-203; SER-211; SER-212 AND THR-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-92; SER-183 AND THR-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Entry informationi

Entry nameiAKTS1_HUMAN
AccessioniPrimary (citable) accession number: Q96B36
Secondary accession number(s): A8MTQ1
, B2RE93, J3KPM3, Q96BI4, Q96IK7, Q96NG2, Q9BWR5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: December 1, 2001
Last modified: January 7, 2015
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) 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.
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