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Entry version 166 (18 Sep 2019)
Sequence version 3 (07 Dec 2004)
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Protein

RAC serine/threonine-protein kinase

Gene

Akt1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Serine/threonine kinase involved in various developmental processes (PubMed:9601646, PubMed:10587646, PubMed:10962553, PubMed:11740943, PubMed:12172554, PubMed:11872800, PubMed:14525946, PubMed:12893776, PubMed:15466161, PubMed:15712201). During early embryogenesis, acts as a survival protein (PubMed:9601646, PubMed:10962553). During mid-embryogenesis, phosphorylates and activates trh, a transcription factor required for tracheal cell fate determination (PubMed:11740943). Also regulates tracheal cell migration (PubMed:11740943, PubMed:14525946). Later in development, acts downstream of PI3K and Pk61C/PDK1 in the insulin receptor transduction pathway which regulates cell growth and organ size, by phosphorylating and antagonizing FOXO transcription factor (PubMed:10587646, PubMed:10962553, PubMed:11752451, PubMed:12893776, PubMed:25329475, PubMed:29025897, PubMed:24603715). Controls follicle cell size during oogenesis (PubMed:15712201). May also stimulate cell growth by phosphorylating Gig/Tsc2 and inactivating the Tsc complex (PubMed:12172554, PubMed:15466161). Dephosphorylation of 'Ser-586' by Phlpp triggers apoptosis and suppression of tumor growth (PubMed:10962553).14 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei295ATPCurated1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei389Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi272 – 280ATPPROSITE-ProRule annotation9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDevelopmental protein, Kinase, Serine/threonine-protein kinase, Transferase
Biological processApoptosis, Growth regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-DME-110478 Insulin signaling pathway
R-DME-110523 TOR signaling pathway
R-DME-1257604 PIP3 activates AKT signaling
R-DME-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation
R-DME-165158 Activation of AKT2
R-DME-165159 mTOR signalling
R-DME-165181 Inhibition of TSC complex formation by PKB
R-DME-198323 AKT phosphorylates targets in the cytosol
R-DME-198693 AKT phosphorylates targets in the nucleus
R-DME-199418 Negative regulation of the PI3K/AKT network
R-DME-203615 eNOS activation
R-DME-354192 Integrin alphaIIb beta3 signaling
R-DME-3769402 Deactivation of the beta-catenin transactivating complex
R-DME-389357 CD28 dependent PI3K/Akt signaling
R-DME-392451 G beta:gamma signalling through PI3Kgamma
R-DME-450385 Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA
R-DME-5218920 VEGFR2 mediated vascular permeability
R-DME-6804757 Regulation of TP53 Degradation
R-DME-6804758 Regulation of TP53 Activity through Acetylation
R-DME-9009391 Extra-nuclear estrogen signaling
R-DME-9634638 Estrogen-dependent nuclear events downstream of ESR-membrane signaling

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
Q8INB9

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
RAC serine/threonine-protein kinase (EC:2.7.11.1)
Short name:
DAkt
Short name:
DRAC-PK
Short name:
Dakt1
Alternative name(s):
Akt
Protein kinase B
Short name:
PKB
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Akt1Imported
ORF Names:CG4006Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiDrosophila melanogaster (Fruit fly)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri7227 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000803 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3R

Organism-specific databases

Drosophila genome database

More...
FlyBasei
FBgn0010379 Akt1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Death at the first instar larval stage (PubMed:9601646). Conditional RNAi-mediated knockdown in the female germline reduces ovary size (PubMed:24786828). RNAi-mediated knockdown in both larval salivary glands and fat body, results in small salivary glands displaying ectopic lipid storage and reduced expression of CdsA (PubMed:24603715).3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi180G → S: Fails to be recruited at the membrane upon activation. 1 Publication1
Mutagenesisi260K → A: Abolishes enzymatic activity. 1
Mutagenesisi295K → M: Abolishes enzymatic activity. 1 Publication1
Mutagenesisi408F → I: Abolishes enzymatic activity. 2 Publications1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000457841 – 611RAC serine/threonine-protein kinaseAdd BLAST611

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei30Phosphoserine1 Publication1
Modified residuei586Phosphoserine3 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated and activated by Pk61C/PDK1 (PubMed:11344272). Phosphorylated on Ser-586 by the TORC2 complex (PubMed:10962553, PubMed:15718470, PubMed:22493059).4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q8INB9

PRoteomics IDEntifications database

More...
PRIDEi
Q8INB9

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q8INB9

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitously expressed. Present in ovary, where it is concentrated at the basal side of follicle cells.1 Publication

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed both maternally and zygotically. Strongly expressed in embryo and pupa. Weakly expressed in larva. Mildly expressed in adult.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
FBgn0010379 Expressed in 48 organ(s), highest expression level in embryo

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q8INB9 DM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with trbl.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
67008, 199 interactors

Database of interacting proteins

More...
DIPi
DIP-49060N

Protein interaction database and analysis system

More...
IntActi
Q8INB9, 43 interactors

Molecular INTeraction database

More...
MINTi
Q8INB9

STRING: functional protein association networks

More...
STRINGi
7227.FBpp0082682

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q8INB9

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini106 – 211PHPROSITE-ProRule annotationAdd BLAST106
Domaini266 – 523Protein kinasePROSITE-ProRule annotationAdd BLAST258
Domaini524 – 597AGC-kinase C-terminalAdd BLAST74

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Binding of the PH domain to the phosphatidylinositol 3-kinase alpha (PI3K) results in its targeting to the plasma membrane.Curated

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0598 Eukaryota
ENOG410XNPH LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000168810

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q8INB9

KEGG Orthology (KO)

More...
KOi
K04456

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q8INB9

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01241 PH_PKB, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.30.29.30, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000961 AGC-kinase_C
IPR011009 Kinase-like_dom_sf
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
IPR039026 PH_PKB
IPR017892 Pkinase_C
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00169 PH, 1 hit
PF00069 Pkinase, 1 hit
PF00433 Pkinase_C, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00233 PH, 1 hit
SM00133 S_TK_X, 1 hit
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51285 AGC_KINASE_CTER, 1 hit
PS50003 PH_DOMAIN, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative initiation. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform C (identifier: Q8INB9-1) [UniParc]FASTAAdd to basket
Also known as: PK85

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MNYLPFVLQR RSTVVASAPA PGSASRIPES PTTTGSNIIN IIYSQSTHPN
60 70 80 90 100
SSPTSGSAEK FSWQQSWPSR TSAAPTHDSG TMSINTTFDL SSPSVTSGHA
110 120 130 140 150
LTEQTQVVKE GWLMKRGEHI KNWRQRYFVL HSDGRLMGYR SKPADSASTP
160 170 180 190 200
SDFLLNNFTV RGCQIMTVDR PKPFTFIIRG LQWTTVIERT FAVESELERQ
210 220 230 240 250
QWTEAIRNVS SRLIDVGEVA MTPSEQTDMT DVDMATIAED ELSEQFSVQG
260 270 280 290 300
TTCNSSGVKK VTLENFEFLK VLGKGTFGKV ILCREKATAK LYAIKILKKE
310 320 330 340 350
VIIQKDEVAH TLTESRVLKS TNHPFLISLK YSFQTNDRLC FVMQYVNGGE
360 370 380 390 400
LFWHLSHERI FTEDRTRFYG AEIISALGYL HSQGIIYRDL KLENLLLDKD
410 420 430 440 450
GHIKVADFGL CKEDITYGRT TKTFCGTPEY LAPEVLDDND YGQAVDWWGT
460 470 480 490 500
GVVMYEMICG RLPFYNRDHD VLFTLILVEE VKFPRNITDE AKNLLAGLLA
510 520 530 540 550
KDPKKRLGGG KDDVKEIQAH PFFASINWTD LVLKKIPPPF KPQVTSDTDT
560 570 580 590 600
RYFDKEFTGE SVELTPPDPT GPLGSIAEEP LFPQFSYQGD MASTLGTSSH
610
ISTSTSLASM Q
Length:611
Mass (Da):68,485
Last modified:December 7, 2004 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iC139380152580934
GO
Isoform A (identifier: Q8INB9-2) [UniParc]FASTAAdd to basket
Also known as: PK66

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.

Note: Major form.
Show »
Length:530
Mass (Da):59,911
Checksum:iF7508582C7F4A288
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0B4LIA3A0A0B4LIA3_DROME
Non-specific serine/threonine prote...
Akt1 AKT, Akt, akt, AKT1, akt1
530Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti73A → T in CAA58499 (PubMed:7876156).Curated1
Sequence conflicti200 – 201QQ → HE in CAA81204 (PubMed:8302573).Curated2

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0188331 – 81Missing in isoform A. 2 PublicationsAdd BLAST81

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Z26242 mRNA Translation: CAA81204.1
X83510 Genomic DNA Translation: CAA58499.2
X83510 Genomic DNA Translation: CAA58500.1
AE014297 Genomic DNA Translation: AAF55275.1
AE014297 Genomic DNA Translation: AAN13699.3
AY069856 mRNA Translation: AAL40001.1

Protein sequence database of the Protein Information Resource

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PIRi
A55888

NCBI Reference Sequences

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RefSeqi
NP_001287353.1, NM_001300424.1 [Q8INB9-2]
NP_001287354.1, NM_001300425.1 [Q8INB9-2]
NP_732113.3, NM_169705.2 [Q8INB9-1]
NP_732114.1, NM_169706.2 [Q8INB9-2]
NP_732115.1, NM_169707.2 [Q8INB9-2]

Genome annotation databases

Ensembl metazoan genome annotation project

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EnsemblMetazoai
FBtr0083226; FBpp0082680; FBgn0010379 [Q8INB9-2]
FBtr0083227; FBpp0082681; FBgn0010379 [Q8INB9-2]
FBtr0344470; FBpp0310841; FBgn0010379 [Q8INB9-2]
FBtr0344717; FBpp0311050; FBgn0010379 [Q8INB9-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
41957

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
dme:Dmel_CG4006

Keywords - Coding sequence diversityi

Alternative initiation

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z26242 mRNA Translation: CAA81204.1
X83510 Genomic DNA Translation: CAA58499.2
X83510 Genomic DNA Translation: CAA58500.1
AE014297 Genomic DNA Translation: AAF55275.1
AE014297 Genomic DNA Translation: AAN13699.3
AY069856 mRNA Translation: AAL40001.1
PIRiA55888
RefSeqiNP_001287353.1, NM_001300424.1 [Q8INB9-2]
NP_001287354.1, NM_001300425.1 [Q8INB9-2]
NP_732113.3, NM_169705.2 [Q8INB9-1]
NP_732114.1, NM_169706.2 [Q8INB9-2]
NP_732115.1, NM_169707.2 [Q8INB9-2]

3D structure databases

SMRiQ8INB9
ModBaseiSearch...

Protein-protein interaction databases

BioGridi67008, 199 interactors
DIPiDIP-49060N
IntActiQ8INB9, 43 interactors
MINTiQ8INB9
STRINGi7227.FBpp0082682

PTM databases

iPTMnetiQ8INB9

Proteomic databases

PaxDbiQ8INB9
PRIDEiQ8INB9

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0083226; FBpp0082680; FBgn0010379 [Q8INB9-2]
FBtr0083227; FBpp0082681; FBgn0010379 [Q8INB9-2]
FBtr0344470; FBpp0310841; FBgn0010379 [Q8INB9-2]
FBtr0344717; FBpp0311050; FBgn0010379 [Q8INB9-2]
GeneIDi41957
KEGGidme:Dmel_CG4006

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
207
FlyBaseiFBgn0010379 Akt1

Phylogenomic databases

eggNOGiKOG0598 Eukaryota
ENOG410XNPH LUCA
GeneTreeiENSGT00940000168810
InParanoidiQ8INB9
KOiK04456
PhylomeDBiQ8INB9

Enzyme and pathway databases

ReactomeiR-DME-110478 Insulin signaling pathway
R-DME-110523 TOR signaling pathway
R-DME-1257604 PIP3 activates AKT signaling
R-DME-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation
R-DME-165158 Activation of AKT2
R-DME-165159 mTOR signalling
R-DME-165181 Inhibition of TSC complex formation by PKB
R-DME-198323 AKT phosphorylates targets in the cytosol
R-DME-198693 AKT phosphorylates targets in the nucleus
R-DME-199418 Negative regulation of the PI3K/AKT network
R-DME-203615 eNOS activation
R-DME-354192 Integrin alphaIIb beta3 signaling
R-DME-3769402 Deactivation of the beta-catenin transactivating complex
R-DME-389357 CD28 dependent PI3K/Akt signaling
R-DME-392451 G beta:gamma signalling through PI3Kgamma
R-DME-450385 Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA
R-DME-5218920 VEGFR2 mediated vascular permeability
R-DME-6804757 Regulation of TP53 Degradation
R-DME-6804758 Regulation of TP53 Activity through Acetylation
R-DME-9009391 Extra-nuclear estrogen signaling
R-DME-9634638 Estrogen-dependent nuclear events downstream of ESR-membrane signaling
SignaLinkiQ8INB9

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Akt1 fly

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
41957

Protein Ontology

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PROi
PR:Q8INB9

Gene expression databases

BgeeiFBgn0010379 Expressed in 48 organ(s), highest expression level in embryo
GenevisibleiQ8INB9 DM

Family and domain databases

CDDicd01241 PH_PKB, 1 hit
Gene3Di2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR000961 AGC-kinase_C
IPR011009 Kinase-like_dom_sf
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
IPR039026 PH_PKB
IPR017892 Pkinase_C
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00169 PH, 1 hit
PF00069 Pkinase, 1 hit
PF00433 Pkinase_C, 1 hit
SMARTiView protein in SMART
SM00233 PH, 1 hit
SM00133 S_TK_X, 1 hit
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS51285 AGC_KINASE_CTER, 1 hit
PS50003 PH_DOMAIN, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAKT1_DROME
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q8INB9
Secondary accession number(s): Q0KI65
, Q24293, Q24469, Q24470, Q7JN11, Q8T9A5, Q9VEY7
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: December 7, 2004
Last modified: September 18, 2019
This is version 166 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
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