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Q9Y243 (AKT3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RAC-gamma serine/threonine-protein kinase
EC=2.7.11.1
Alternative name(s):
Protein kinase Akt-3
Protein kinase B gamma
Short name=PKB gamma
RAC-PK-gamma
STK-2
Gene names
Name:AKT3
Synonyms:PKBG
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

AKT3 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT3 is the least studied AKT isoform. It plays an important role in brain development and is crucial for the viability of malignant glioma cells. AKT3 isoform may also be the key molecule in up-regulation and down-regulation of MMP13 via IL13. Required for the coordination of mitochondrial biogenesis with growth factor-induced increases in cellular energy demands. Down-regulation by RNA interference reduces the expression of the phosphorylated form of BAD, resulting in the induction of caspase-dependent apoptosis. Ref.18 Ref.23

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Two specific sites, one in the kinase domain (Thr-305) and the other in the C-terminal regulatory region (Ser-472), need to be phosphorylated for its full activation By similarity. IGF-1 leads to the activation of AKT3, which may play a role in regulating cell survival.

Subunit structure

Interacts (via PH domain) with TCL1A; this enhances AKT3 phosphorylation and activation. Interacts with TRAF6. Ref.12 Ref.13 Ref.20

Subcellular location

Nucleus. Cytoplasm. Membrane; Peripheral membrane protein. Note: Membrane-associated after cell stimulation leading to its translocation. Ref.21

Tissue specificity

In adult tissues, it is highly expressed in brain, lung and kidney, but weakly in heart, testis and liver. In fetal tissues, it is highly expressed in heart, liver and brain and not at all in kidney.

Domain

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

Post-translational modification

Phosphorylation on Thr-305 and Ser-472 is required for full activity By similarity. Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.10 Ref.11 Ref.17

Ubiquitinated. When fully phosphorylated and translocated into the nucleus, undergoes 'Lys-48'-polyubiquitination catalyzed by TTC3, leading to its degradation by the proteasome. Ref.10 Ref.11 Ref.17

Involvement in disease

Note=AKT3 is a key modulator of several tumors like melanoma, glioma and ovarian cancer. Active AKT3 increases progressively during melanoma tumor progression with highest levels present in advanced-stage metastatic melanomas. Promotes melanoma tumorigenesis by decreasing apoptosis. Plays a key role in the genesis of ovarian cancers through modulation of G2/M phase transition. With AKT2, plays a pivotal role in the biology of glioblastoma.

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 PH domain.

Contains 1 protein kinase domain.

Caution

In light of strong homologies in the primary amino acid sequence, the 3 AKT kinases were long surmised to play redundant and overlapping roles. More recent studies has brought into question the redundancy within AKT kinase isoforms and instead pointed to isoform specific functions in different cellular events and diseases. AKT1 is more specifically involved in cellular survival pathways, by inhibiting apoptotic processes; whereas AKT2 is more specific for the insulin receptor signaling pathway. Moreover, while AKT1 and AKT2 are often implicated in many aspects of cellular transformation, the 2 isoforms act in a complementary opposing manner. The role of AKT3 is less clear, though it appears to be predominantly expressed in brain.

Biophysicochemical properties

Kinetic parameters:

KM=87.9 µM for ATP (for purified and in vitro activated AKT3) Ref.16

KM=12.4 µM for peptide substrate (for purified and in vitro activated AKT3)

KM=118.7 µM for ATP (for recombinant myristoylated AKT3 expressed and immunoprecipitated from Rat-1 cells)

KM=2.3 µM for peptide substrate (for recombinant myristoylated AKT3 expressed and immunoprecipitated from Rat-1 cells)

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y243-1)

Also known as: PKB gamma;

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.
Isoform 2 (identifier: Q9Y243-2)

Also known as: PKB gamma 1;

The sequence of this isoform differs from the canonical sequence as follows:
     452-479: YDEDGMDCMDNERRPHFPQFSYSASGRE → CQQSDCGMLGNWKK

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 479479RAC-gamma serine/threonine-protein kinase
PRO_0000085611

Regions

Domain5 – 107103PH
Domain148 – 405258Protein kinase
Domain406 – 47974AGC-kinase C-terminal
Nucleotide binding154 – 1629ATP By similarity

Sites

Active site2711Proton acceptor By similarity
Binding site1771ATP By similarity

Amino acid modifications

Modified residue1201Phosphoserine Ref.17
Modified residue1231Phosphoserine Ref.17
Modified residue3051Phosphothreonine; by PDPK1 Ref.10
Modified residue4721Phosphoserine; by PKC/PRKCZ Ref.11
Disulfide bond59 ↔ 76 By similarity
Disulfide bond293 ↔ 307 By similarity

Natural variations

Alternative sequence452 – 47928YDEDG…ASGRE → CQQSDCGMLGNWKK in isoform 2.
VSP_004947
Natural variant171E → K in melanoma; results in activation of AKT. Ref.27
VAR_065830
Natural variant1711G → R in a glioblastoma multiforme sample; somatic mutation. Ref.26
VAR_040358

Experimental info

Mutagenesis3051T → A: No activation after pervanadate treatment. Ref.6
Mutagenesis3051T → D: 2-fold increase of phosphorylation steady state level, no activation after pervanadate treatment. Ref.6
Mutagenesis4471T → A: No effect. Ref.6
Mutagenesis4471T → D: No effect. Ref.6
Mutagenesis4721S → A: 67% decrease of activity after pervanadate treatment.
Mutagenesis4721S → D: 1.4-fold increase of phosphorylation steady state level, 50% decrease of activity after pervanadate treatment.
Sequence conflict2791L → R in AAI21155. Ref.9

Secondary structure

1 ......................... 479
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (PKB gamma) [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: F08BDDE6502E78FB

FASTA47955,775
        10         20         30         40         50         60 
MSDVTIVKEG WVQKRGEYIK NWRPRYFLLK TDGSFIGYKE KPQDVDLPYP LNNFSVAKCQ 

        70         80         90        100        110        120 
LMKTERPKPN TFIIRCLQWT TVIERTFHVD TPEEREEWTE AIQAVADRLQ RQEEERMNCS 

       130        140        150        160        170        180 
PTSQIDNIGE EEMDASTTHH KRKTMNDFDY LKLLGKGTFG KVILVREKAS GKYYAMKILK 

       190        200        210        220        230        240 
KEVIIAKDEV AHTLTESRVL KNTRHPFLTS LKYSFQTKDR LCFVMEYVNG GELFFHLSRE 

       250        260        270        280        290        300 
RVFSEDRTRF YGAEIVSALD YLHSGKIVYR DLKLENLMLD KDGHIKITDF GLCKEGITDA 

       310        320        330        340        350        360 
ATMKTFCGTP EYLAPEVLED NDYGRAVDWW GLGVVMYEMM CGRLPFYNQD HEKLFELILM 

       370        380        390        400        410        420 
EDIKFPRTLS SDAKSLLSGL LIKDPNKRLG GGPDDAKEIM RHSFFSGVNW QDVYDKKLVP 

       430        440        450        460        470 
PFKPQVTSET DTRYFDEEFT AQTITITPPE KYDEDGMDCM DNERRPHFPQ FSYSASGRE

« Hide

Isoform 2 (PKB gamma 1) [UniParc].

Checksum: 592EF88B6937D1E0
Show »

FASTA46554,032

References

« Hide 'large scale' references
[1]"A human protein kinase B gamma with regulatory phosphorylation sites in the activation loop and in the C-terminal hydrophobic domain."
Brodbeck D., Cron P., Hemmings B.A.
J. Biol. Chem. 274:9133-9136(1999) [PubMed: 10092583] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS.
[2]"Identification of a human Akt3 (protein kinase B gamma) which contains the regulatory serine phosphorylation site."
Nakatani K., Sakaue H., Thompson D.A., Weigel R.J., Roth R.A.
Biochem. Biophys. Res. Commun. 257:906-910(1999) [PubMed: 10208883] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Molecular cloning, expression and characterization of the human serine/threonine kinase Akt-3."
Masure S., Haefner B., Wesselink J.-J., Hoefnagel E., Mortier E., Verhasselt P., Tuytelaars A., Gordon R., Richardson A.
Eur. J. Biochem. 265:353-360(1999) [PubMed: 10491192] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[4]"Cloning of a novel human cDNA, STK-2, which encodes a rat serine-threonine protein kinase (STK) homolog."
Li X., Yu L., Huang H., Zhang M., Zhao Y., Zhao S.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Testis.
[6]"Two splice variants of PKB gamma have different regulatory capacity depending on the presence or absence of the regulatory phosphorylation site Ser-472 in the C-terminal hydrophobic domain."
Brodbeck D., Hill M.M., Hemmings B.A.
J. Biol. Chem. 276:29550-29558(2001) [PubMed: 11387345] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), MUTAGENESIS OF THR-305 AND THR-447.
[7]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[10]"Activation of protein kinase B beta and gamma isoforms by insulin in vivo and by 3-phosphoinositide-dependent protein kinase-1 in vitro: comparison with protein kinase B alpha."
Walker K.S., Deak M., Paterson A., Hudson K., Cohen P., Alessi D.R.
Biochem. J. 331:299-308(1998) [PubMed: 9512493] [Abstract]
Cited for: CHARACTERIZATION, PHOSPHORYLATION AT THR-305 BY PDPK1.
[11]"Characterization of PDK2 activity against protein kinase B gamma."
Hodgkinson C.P., Sale E.M., Sale G.J.
Biochemistry 41:10351-10359(2002) [PubMed: 12162751] [Abstract]
Cited for: PHOSPHORYLATION AT SER-472.
[12]"Differential regulation of Akt kinase isoforms by the members of the TCL1 oncogene family."
Laine J., Kuenstle G., Obata T., Noguchi M.
J. Biol. Chem. 277:3743-3751(2002) [PubMed: 11707444] [Abstract]
Cited for: INTERACTION WITH TCL1A.
[13]"Identification of Akt association and oligomerization domains of the Akt kinase coactivator TCL1."
Kuenstle G., Laine J., Pierron G., Kagami S., Nakajima H., Hoh F., Roumestand C., Stern M.H., Noguchi M.
Mol. Cell. Biol. 22:1513-1525(2002) [PubMed: 11839817] [Abstract]
Cited for: INTERACTION WITH TCL1A.
[14]"Deregulated Akt3 activity promotes development of malignant melanoma."
Stahl J.M., Sharma A., Cheung M., Zimmerman M., Cheng J.Q., Bosenberg M.W., Kester M., Sandirasegarane L., Robertson G.P.
Cancer Res. 64:7002-7010(2004) [PubMed: 15466193] [Abstract]
Cited for: INVOLVEMENT IN TUMORS.
[15]"A specific role for AKT3 in the genesis of ovarian cancer through modulation of G(2)-M phase transition."
Cristiano B.E., Chan J.C., Hannan K.M., Lundie N.A., Marmy-Conus N.J., Campbell I.G., Phillips W.A., Robbie M., Hannan R.D., Pearson R.B.
Cancer Res. 66:11718-11725(2006) [PubMed: 17178867] [Abstract]
Cited for: INVOLVEMENT IN TUMORS.
[16]"Kinetic mechanism of AKT/PKB enzyme family."
Zhang X., Zhang S., Yamane H., Wahl R., Ali A., Lofgren J.A., Kendall R.L.
J. Biol. Chem. 281:13949-13956(2006) [PubMed: 16540465] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[17]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-123, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[18]"VEGF stimulation of mitochondrial biogenesis: requirement of AKT3 kinase."
Wright G.L., Maroulakou I.G., Eldridge J., Liby T.L., Sridharan V., Tsichlis P.N., Muise-Helmericks R.C.
FASEB J. 22:3264-3275(2008) [PubMed: 18524868] [Abstract]
Cited for: FUNCTION.
[19]"The E3 ligase TTC3 facilitates ubiquitination and degradation of phosphorylated Akt."
Suizu F., Hiramuki Y., Okumura F., Matsuda M., Okumura A.J., Hirata N., Narita M., Kohno T., Yokota J., Bohgaki M., Obuse C., Hatakeyama S., Obata T., Noguchi M.
Dev. Cell 17:800-810(2009) [PubMed: 20059950] [Abstract]
Cited for: UBIQUITINATION BY TTC3.
[20]"The E3 ligase TRAF6 regulates Akt ubiquitination and activation."
Yang W.-L., Wang J., Chan C.-H., Lee S.-W., Campos A.D., Lamothe B., Hur L., Grabiner B.C., Lin X., Darnay B.G., Lin H.-K.
Science 325:1134-1138(2009) [PubMed: 19713527] [Abstract]
Cited for: INTERACTION WITH TRAF6.
[21]"The Akt isoforms are present at distinct subcellular locations."
Santi S.A., Lee H.
Am. J. Physiol. 298:C580-C591(2010) [PubMed: 20018949] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[22]"Akt2 and Akt3 play a pivotal role in malignant gliomas."
Mure H., Matsuzaki K., Kitazato K.T., Mizobuchi Y., Kuwayama K., Kageji T., Nagahiro S.
Neuro-oncol. 12:221-232(2010) [PubMed: 20167810] [Abstract]
Cited for: INVOLVEMENT IN TUMORS.
[23]"Expression of matrix metalloproteinase-13 is controlled by IL-13 via PI3K/Akt3 and PKC-delta in normal human dermal fibroblasts."
Moriya C., Jinnin M., Yamane K., Maruo K., Muchemwa F.C., Igata T., Makino T., Fukushima S., Ihn H.
J. Invest. Dermatol. 131:655-661(2011) [PubMed: 21191416] [Abstract]
Cited for: FUNCTION.
[24]"Akt signalling in health and disease."
Hers I., Vincent E.E., Tavare J.M.
Cell. Signal. 23:1515-1527(2011) [PubMed: 21620960] [Abstract]
Cited for: REVIEW ON FUNCTION.
[25]"The crystal structure of the Ph domain of human Akt3 protein kinase."
Vollmar M., Wang J., Zhang Y., Elkins J.M., Burgess-Brown N., Chaikuad A., Pike A.C.W., Von Delft F., Bountra C., Arrowsmith C.H., Weigelt J., Edwards A., Knapp S.
Submitted (DEC-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 1-118.
[26]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed: 17344846] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-171.
[27]"A novel AKT3 mutation in melanoma tumours and cell lines."
Davies M.A., Stemke-Hale K., Tellez C., Calderone T.L., Deng W., Prieto V.G., Lazar A.J., Gershenwald J.E., Mills G.B.
Br. J. Cancer 99:1265-1268(2008) [PubMed: 18813315] [Abstract]
Cited for: VARIANT MELANOMA LYS-17, CHARACTERIZATION OF VARIANT MELANOMA LYS-17.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF124141 mRNA. Translation: AAD29089.1.
AF135794 mRNA. Translation: AAD24196.1.
AF085234 mRNA. Translation: AAL40392.1.
AJ245709 mRNA. Translation: CAB53537.1.
AL117525 mRNA. Translation: CAB55977.1. Different termination.
AY005799 mRNA. Translation: AAF91073.1.
AL591721 expand/collapse EMBL AC list , AC096539, AL592151, AL662889 Genomic DNA. Translation: CAH71866.1.
AL591721 expand/collapse EMBL AC list , AC096539, AL592151, AL662889 Genomic DNA. Translation: CAH71867.1.
AL592151 expand/collapse EMBL AC list , AC096539, AL591721, AL662889 Genomic DNA. Translation: CAH72891.1.
AL592151 expand/collapse EMBL AC list , AC096539, AL591721, AL662889 Genomic DNA. Translation: CAH72892.1.
AL662889 expand/collapse EMBL AC list , AC096539, AL591721, AL592151 Genomic DNA. Translation: CAH73072.1.
AL662889 expand/collapse EMBL AC list , AC096539, AL591721, AL592151 Genomic DNA. Translation: CAH73073.1.
CH471148 Genomic DNA. Translation: EAW77093.1.
CH471148 Genomic DNA. Translation: EAW77094.1.
BC121154 mRNA. Translation: AAI21155.1.
IPIIPI00031747.
IPI00219411.
PIRA59380.
T17287.
RefSeqNP_001193658.1. NM_001206729.1.
NP_005456.1. NM_005465.4.
NP_859029.1. NM_181690.2.
UniGeneHs.498292.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2X18X-ray1.46A/B/C/D/E/F/G/H1-118[»]
ProteinModelPortalQ9Y243.
SMRQ9Y243. Positions 2-476.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9Y243. 1 interaction.
MINTMINT-222821.
STRINGQ9Y243.

PTM databases

PhosphoSiteQ9Y243.

Polymorphism databases

DMDM12643943.

Proteomic databases

PRIDEQ9Y243.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263826; ENSP00000263826; ENSG00000117020.
ENST00000366539; ENSP00000355497; ENSG00000117020.
GeneID10000.
KEGGhsa:10000.
NMPDRfig|9606.3.peg.3340.
UCSCuc001hzz.1. human.
uc001iab.1. human.

Organism-specific databases

CTD10000.
GeneCardsGC01M243653.
HGNCHGNC:393. AKT3.
HPACAB013090.
HPA026441.
MIM611223. gene.
neXtProtNX_Q9Y243.
PharmGKBPA24686.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG15723.
GeneTreeENSGT00590000082790.
HOGENOMHBG755340.
HOVERGENHBG108317.
InParanoidQ9Y243.
OMAIMSDVTI.
OrthoDBEOG40GCQP.
PhylomeDBQ9Y243.

Enzyme and pathway databases

BRENDA2.7.11.1. 2681.
Pathway_Interaction_DBpi3kciaktpathway. Class I PI3K signaling events mediated by Akt.
s1p_s1p3_pathway. S1P3 pathway.
ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ9Y243.
BgeeQ9Y243.
CleanExHS_AKT3.
GenevestigatorQ9Y243.
GermOnlineENSG00000117020. Homo sapiens.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR011993. PH_type.
IPR017892. Pkinase_C.
IPR001849. Pleckstrin_homology.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_kinase-like_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR002290. Ser/Thr_kinase_dom.
[Graphical view]
Gene3DG3DSA:2.30.29.30. PH_type. 1 hit.
KOK04456.
PfamPF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. Kinase_like. 1 hit.
PROSITEPS51285. 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.
[Graphical view]
ProtoNetSearch...

Other

BindingDBQ9Y243.
NextBio37765.
SOURCESearch...

Entry information

Entry nameAKT3_HUMAN
AccessionPrimary (citable) accession number: Q9Y243
Secondary accession number(s): Q0VAA6 expand/collapse secondary AC list , Q5VTI1, Q5VTI2, Q96QV3, Q9UFP5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: January 25, 2012
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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