Unreviewed, UniProtKB/TrEMBL Q8BS26 (Q8BS26_MOUSE)

Names and origin

Protein names

Submitted name:
    Putative uncharacterized protein EMBL BAC30695.1

Gene names

Name:

Akt1 MGI 87986

Organism

Mus musculus (Mouse) EMBL BAC30695.1

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	452 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

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. Contains 1 PH domain.

Ontologies

Keywords
Ligand	ATP-binding RuleBase RU000304V2 Spearmint SPM000961 Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase RuleBase RU000305V3 Spearmint SPM000961 Transferase
Gene Ontology (GO)
Biological process	activation-induced cell death of T cells Inferred from electronic annotation. Source: Compara cell projection organization Inferred from electronic annotation. Source: Compara glycogen biosynthetic process Inferred from electronic annotation. Source: Compara insulin receptor signaling pathway Inferred from electronic annotation. Source: Compara insulin-like growth factor receptor signaling pathway Inferred from electronic annotation. Source: Compara intracellular signaling cascade Inferred from electronic annotation. Source: Compara negative regulation of JNK cascade Inferred from electronic annotation. Source: Compara negative regulation of cell size Inferred from electronic annotation. Source: Compara negative regulation of fatty acid beta-oxidation Inferred from electronic annotation. Source: Compara negative regulation of plasma membrane long-chain fatty acid transport Inferred from electronic annotation. Source: Compara negative regulation of protein kinase activity Inferred from electronic annotation. Source: Compara peptidyl-serine phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of cell growth Inferred from electronic annotation. Source: Compara positive regulation of cellular protein metabolic process Inferred from electronic annotation. Source: Compara positive regulation of cyclin-dependent protein kinase activity during G1/S Inferred from electronic annotation. Source: Compara positive regulation of fat cell differentiation 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 lipid biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of nitric oxide biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of nitric-oxide synthase activity Inferred from electronic annotation. Source: Compara protein import into nucleus, translocation Inferred from electronic annotation. Source: Compara regulation of cell migration Inferred from electronic annotation. Source: Compara regulation of establishment of protein localization Inferred from electronic annotation. Source: Compara response to UV-A Inferred from electronic annotation. Source: Compara response to fluid shear stress Inferred from electronic annotation. Source: Compara
Cellular component	cytoskeleton Inferred from electronic annotation. Source: Compara soluble fraction Inferred from electronic annotation. Source: Compara
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW enzyme binding Inferred from electronic annotation. Source: Compara identical protein binding Inferred from electronic annotation. Source: Compara nitric-oxide synthase regulator activity Inferred from electronic annotation. Source: Compara phosphatidylinositol-3,4,5-trisphosphate binding Inferred from electronic annotation. Source: Compara phosphatidylinositol-3,4-bisphosphate binding Inferred from electronic annotation. Source: Compara protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q8BS26-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: E203C8F46A18EE5E	FASTA	452	52,619
	10 20 30 40 50 60 MNDVAIVKEG WLHKRGEYIK TWRPRYFLLK NDGTFIGYKE RPQDVDQRES PLNNFSVAQC 70 80 90 100 110 120 QLMKTERPRP NTFIIRCLQW TTVIERTFHV ETPEEREEWA TAIQTVADGL KRQEEETMDF 130 140 150 160 170 180 RSGSPSDNSG AEEMEVSLAK PKHRVTMNEF EYLKLLGKGT FGKVILVKEK ATGRYYAMKI 190 200 210 220 230 240 LKKEVIVAKD EVAHTLTENR VLQNSRHPFL TALKYSFQTH DRLCFVMEYA NGGELFFHLS 250 260 270 280 290 300 RERVFSEDRA RFYGAEIVSA LDYLHSEKNV VYRDLKLENL MLDKDGHIKI TDFGLCKEGI 310 320 330 340 350 360 KDGATMKTFC GTPEYLAPEV LEDNDYGRAV DWWGLGVVMY EMMCGRLPFY NQDHEKLFEL 370 380 390 400 410 420 ILMEEIRFPR TLGPEAKSLL SGLLKKDPTQ RLGGGSEDSK EIMQHRFFAN IVWQDVYEKK 430 440 450 LSPPFKPQVT SETDTRYFDE EFHSSDDHHH AA

References

[1]

"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J EMBL BAC30695.1. Tissue: Aorta and vein EMBL BAC30695.1.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK040758 mRNA. Translation: BAC30695.1.
IPI	IPI00556735.
UniGene	Mm.6645
3D structure databases
HSSP	HSSP built from PDB template 1H10 based on UniProtKB P31749.
SMR	Q8BS26. Positions 3-121, 144-442.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8BS26.
Genome annotation databases
Ensembl	ENSMUST00000001780; ENSMUSP00000001780; ENSMUSG00000001729; Mus musculus. [Genome view] ENSMUST00000109749; ENSMUSP00000105371; ENSMUSG00000001729; Mus musculus. [Genome view] ENSMUST00000121171; ENSMUSP00000113658; ENSMUSG00000001729; Mus musculus. [Genome view]
Organism-specific databases
MGI	MGI:87986. Akt1.
Phylogenomic databases
HOVERGEN	Q8BS26.
InParanoid	Q8BS26.
Gene expression databases
ArrayExpress	Q8BS26.
Bgee	Q8BS26.
Genevestigator	Q8BS26.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR011009. Kinase-like_dom. IPR011993. PH_type. IPR001849. Pleckstrin_homology. 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]
Gene3D	G3DSA:2.30.29.30. PH_type. 1 hit.
PANTHER	PTHR22985:SF69. Akt. 1 hit.
Pfam	PF00169. PH. 1 hit. PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00233. PH. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
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. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

Q8BS26_MOUSE

Accession

Primary (citable) accession number: Q8BS26

Entry history

Integrated into UniProtKB/TrEMBL:	March 1, 2003
Last sequence update:	March 1, 2003
Last modified:	January 19, 2010
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)