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Unreviewed, UniProtKB/TrEMBL Q8CE74 (Q8CE74_MOUSE)

Last modified January 19, 2010. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information

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Names and origin

Protein namesSubmitted name:
    Putative uncharacterized protein EMBL BAC26162.1
Gene names
Name: Akt2 MGI 104874
OrganismMus musculus (Mouse) EMBL BAC26162.1
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length353 AA.
Sequence statusFragment.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Spearmint SPM000961

Sequence similarities

Belongs to the protein kinase superfamily.

Contains 1 AGC-kinase C-terminal domain.

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Ontologies

Keywords
   LigandATP-binding RuleBase RU000304V2 Spearmint SPM000961
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase RuleBase RU000305V3 Spearmint SPM000961
Transferase
Gene Ontology (GO)
   Biological processinsulin receptor signaling pathway

Inferred from electronic annotation. Source: Compara

negative regulation of plasma membrane long-chain fatty acid transport

Inferred from electronic annotation. Source: Compara

positive regulation of fatty acid beta-oxidation

Inferred from electronic annotation. Source: Compara

positive regulation of glucose import

Inferred from electronic annotation. Source: Compara

positive regulation of glucose metabolic process

Inferred from electronic annotation. Source: Compara

positive regulation of glycogen biosynthetic process

Inferred from electronic annotation. Source: Compara

positive regulation of sodium ion transport

Inferred from electronic annotation. Source: Compara

protein amino acid phosphorylation

Inferred from electronic annotation. Source: InterPro

regulation of JNK cascade

Inferred from direct assay. Source: MGI

   Cellular componentcytosol

Inferred from electronic annotation. Source: Compara

insulin-responsive compartment

Inferred from electronic annotation. Source: Compara

lamellipodium

Inferred from direct assay. Source: MGI

microsome

Inferred from electronic annotation. Source: Compara

plasma membrane

Inferred from electronic annotation. Source: Compara

soluble fraction

Inferred from electronic annotation. Source: Compara

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from electronic annotation. Source: Compara

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Experimental info

Non-terminal residue11 EMBL BAC26162.1

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Sequences

Sequence LengthMass (Da)Tools
Q8CE74-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 325D23F43975FFD7

FASTA35340,766
        10         20         30         40         50         60 
DSSTSEMMEV AVNKARAKVT MNDFDYLKLL GKGTFGKVIL VREKATGRYY AMKILRKEVI 

        70         80         90        100        110        120 
IAKDEVAHTV TESRVLQNTR HPFLTALKYA FQTHDRLCFV MEYANGGELF FHLSRERVFT 

       130        140        150        160        170        180 
EDRARFYGAE IVSALEYLHS RDVVYRDIKL ENLMLDKDGH IKITDFGLCK EGISDGATMK 

       190        200        210        220        230        240 
TFCGTPEYLA PEVLEDNDYG RAVDWWGLGV VMYEMMCGRL PFYNQDHERL FELILMEEIR 

       250        260        270        280        290        300 
FPRTLGPEAK SLLAGLLKKD PKQRLGGGPS DAKEVMEHRF FLSINWQDVV QKKLLPPFKP 

       310        320        330        340        350 
QVTSEVDTRY FDDEFTAQSI TITPPDRYDS LDPLELDQRT HFPQFSYSAS IRE

« Hide

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References

[1]"High-efficiency full-length cDNA cloning."
Carninci P., Hayashizaki Y.
Methods Enzymol. 303:19-44(1999) [PubMed: 10349636] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6J EMBL BAC26162.1.
Tissue: Skin EMBL BAC26162.1.
[2]"The Transcriptional Landscape of the Mammalian Genome."
The FANTOM Consortium, Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group)
Science 309:1559-1563(2005)
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6J EMBL BAC26162.1.
Tissue: Skin EMBL BAC26162.1.
[3]"Antisense Transcription in the Mammalian Transcriptome."
RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium
Science 309:1564-1566(2005) [PubMed: 16141073] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6J EMBL BAC26162.1.
Tissue: Skin EMBL BAC26162.1.
[4]"Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs."
The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team
Nature 420:563-573(2002)
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6J EMBL BAC26162.1.
Tissue: Skin EMBL BAC26162.1.
[5]"Functional annotation of a full-length mouse cDNA collection."
The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium
Nature 409:685-690(2001)
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6J EMBL BAC26162.1.
Tissue: Skin EMBL BAC26162.1.
[6]"Normalization and subtraction of cap-trapper-selected cDNAs to prepare full-length cDNA libraries for rapid discovery of new genes."
Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.
Genome Res. 10:1617-1630(2000) [PubMed: 11042159] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6J EMBL BAC26162.1.
Tissue: Skin EMBL BAC26162.1.
[7]"RIKEN integrated sequence analysis (RISA) system--384-format sequencing pipeline with 384 multicapillary sequencer."
Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P., Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A. expand/collapse author list , Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.
Genome Res. 10:1757-1771(2000) [PubMed: 11076861] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6J EMBL BAC26162.1.
Tissue: Skin EMBL BAC26162.1.
[8]Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P., Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W., Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T., Hori F., Imotani K. expand/collapse author list , Ishii Y., Itoh M., Kagawa I., Kasukawa T., Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S., Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M., Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y., Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H., Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M., Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T., Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6J EMBL BAC26162.1.
Tissue: Skin EMBL BAC26162.1.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK028871 mRNA. Translation: BAC26162.1.
IPIIPI00121335.
UniGeneMm.177194

3D structure databases

HSSPHSSP built from PDB template 1MRY based on UniProtKB P31751.
SMRQ8CE74. Positions 18-351.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8CE74.

Genome annotation databases

EnsemblENSMUST00000051356; ENSMUSP00000052103; ENSMUSG00000004056; Mus musculus. [Genome view]
ENSMUST00000108343; ENSMUSP00000103980; ENSMUSG00000004056; Mus musculus. [Genome view]
ENSMUST00000108344; ENSMUSP00000103981; ENSMUSG00000004056; Mus musculus. [Genome view]

Organism-specific databases

MGIMGI:104874. Akt2.

Phylogenomic databases

HOVERGENQ8CE74.
InParanoidQ8CE74.
PhylomeDBQ8CE74.

Gene expression databases

ArrayExpressQ8CE74.
BgeeQ8CE74.
GenevestigatorQ8CE74.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
IPR015744. Serine/threonine_Kinase_Rac.
[Graphical view]
PANTHERPTHR22985:SF69. Akt. 1 hit.
PfamPF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

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Entry information

Entry nameQ8CE74_MOUSE
AccessionPrimary (citable) accession number: Q8CE74
Entry history
Integrated into UniProtKB/TrEMBL: March 1, 2003
Last sequence update: March 1, 2003
Last modified: January 19, 2010
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information