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B1AKP8 (B1AKP8_HUMAN) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein attributes

Sequence length754 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Contains FAT domain. SAAS SAAS018936

Contains FATC domain. SAAS SAAS018936

Contains PI3K/PI4K domain. SAAS SAAS018936

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data. Ensembl ENSP00000366034

Ontologies

Keywords
   LigandATP-binding SAAS SAAS018936
Nucleotide-binding
   Molecular functionKinase SAAS SAAS018936
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to hypoxia

Inferred from electronic annotation. Source: Ensembl

cellular response to nutrient levels

Inferred from electronic annotation. Source: Ensembl

germ cell development

Inferred from electronic annotation. Source: Ensembl

negative regulation of NFAT protein import into nucleus

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell size

Inferred from electronic annotation. Source: Ensembl

negative regulation of macroautophagy

Inferred from electronic annotation. Source: Ensembl

peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

peptidyl-threonine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of actin filament polymerization

Inferred from electronic annotation. Source: Ensembl

positive regulation of endothelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of lamellipodium assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of myotube differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of stress fiber assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of translation

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

regulation of Rac GTPase activity

Inferred from electronic annotation. Source: Ensembl

regulation of carbohydrate utilization

Inferred from electronic annotation. Source: Ensembl

regulation of fatty acid beta-oxidation

Inferred from electronic annotation. Source: Ensembl

regulation of glycogen biosynthetic process

Inferred from electronic annotation. Source: Ensembl

regulation of protein kinase activity

Inferred from electronic annotation. Source: Ensembl

regulation of response to food

Inferred from electronic annotation. Source: Ensembl

response to amino acid

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from electronic annotation. Source: Ensembl

ruffle organization

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentPML body

Inferred from electronic annotation. Source: Ensembl

TORC1 complex

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from electronic annotation. Source: Ensembl

mTOR-FKBP12-rapamycin complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

drug binding

Inferred from electronic annotation. Source: InterPro

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: Ensembl

ribosome binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
B1AKP8 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 0AC837B2544A1CEA

FASTA75485,901
        10         20         30         40         50         60 
MNFEAVLHYK HQNQARDEKK KLRHASGANI TNATTAATTA ATATTTASTE GSNSESEAES 

        70         80         90        100        110        120 
TENSPTPSPL QKKVTEDLSK TLLMYTVPAV QGFFRSISLS RGNNLQDTLR VLTLWFDYGH 

       130        140        150        160        170        180 
WPDVNEALVE GVKAIQIDTW LQVIPQLIAR IDTPRPLVGR LIHQLLTDIG RYHPQALIYP 

       190        200        210        220        230        240 
LTVASKSTTT ARHNAANKIL KNMCEHSNTL VQQAMMVSEE LIRVAILWHE MWHEGLEEAS 

       250        260        270        280        290        300 
RLYFGERNVK GMFEVLEPLH AMMERGPQTL KETSFNQAYG RDLMEAQEWC RKYMKSGNVK 

       310        320        330        340        350        360 
DLTQAWDLYY HVFRRISKQL PQLTSLELQY VSPKLLMCRD LELAVPGTYD PNQPIIRIQS 

       370        380        390        400        410        420 
IAPSLQVITS KQRPRKLTLM GSNGHEFVFL LKGHEDLRQD ERVMQLFGLV NTLLANDPTS 

       430        440        450        460        470        480 
LRKNLSIQRY AVIPLSTNSG LIGWVPHCDT LHALIRDYRE KKKILLNIEH RIMLRMAPDY 

       490        500        510        520        530        540 
DHLTLMQKVE VFEHAVNNTA GDDLAKLLWL KSPSSEVWFD RRTNYTRSLA VMSMVGYILG 

       550        560        570        580        590        600 
LGDRHPSNLM LDRLSGKILH IDFGDCFEVA MTREKFPEKI PFRLTRMLTN AMEVTGLDGN 

       610        620        630        640        650        660 
YRITCHTVME VLREHKDSVM AVLEAFVYDP LLNWRLMDTN TKGNKRSRTR TDSYSAGQSV 

       670        680        690        700        710        720 
EILDGVELGE PAHKKTGTTV PESIHSFIGD GLVKPEALNK KAIQIINRVR DKLTGRDFSH 

       730        740        750 
DDTLDVPTQV ELLIKQATSH ENLCQCYIGW CPFW 

« Hide

References

« Hide 'large scale' references
[1]"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., 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., 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., 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., 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., McLaren S., Milne S., Mistry S., Moore M.J., 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., 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., Banerjee R., Bryant S.P., Burford D.C., Burrill W.D., Clegg S.M., Dhami P., Dovey O., Faulkner L.M., Gribble S.M., Langford C.F., Pandian R.D., Porter K.M., Prigmore E.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[3]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[4]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[5]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]Ensembl
Submitted (FEB-2012) to UniProtKB
Cited for: IDENTIFICATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL049653 Genomic DNA. No translation available.
AL109811 Genomic DNA. No translation available.
AL391561 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortalB1AKP8.
SMRB1AKP8. Positions 230-319, 722-754.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEB1AKP8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376838; ENSP00000366034; ENSG00000198793.
UCSCuc001asc.3. human.

Organism-specific databases

HGNCHGNC:3942. MTOR.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000049044.
HOVERGENHBG102007.
OrthoDBEOG7CCBQ4.

Gene expression databases

ArrayExpressB1AKP8.

Family and domain databases

Gene3D1.10.1070.11. 3 hits.
1.20.120.150. 1 hit.
InterProIPR003152. FATC.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
IPR009076. Rapamycin-bd_dom.
[Graphical view]
PfamPF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF08771. Rapamycin_bind. 1 hit.
[Graphical view]
SMARTSM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMSSF47212. SSF47212. 1 hit.
SSF56112. SSF56112. 2 hits.
PROSITEPS51189. FAT. 1 hit.
PS51190. FATC. 1 hit.
PS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMTOR. human.
NextBio35466581.

Entry information

Entry nameB1AKP8_HUMAN
AccessionPrimary (citable) accession number: B1AKP8
Entry history
Integrated into UniProtKB/TrEMBL: April 8, 2008
Last sequence update: April 8, 2008
Last modified: June 11, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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.