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B1AKP8

- B1AKP8_HUMAN

UniProt

B1AKP8 - B1AKP8_HUMAN

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Protein
Submitted name:

Serine/threonine-protein kinase mTOR

Gene

MTOR

Organism
Homo sapiens (Human)
Status
Unreviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. drug binding Source: InterPro
  3. protein serine/threonine kinase activity Source: Ensembl
  4. ribosome binding Source: Ensembl

GO - Biological processi

  1. cellular response to hypoxia Source: Ensembl
  2. cellular response to nutrient levels Source: Ensembl
  3. germ cell development Source: Ensembl
  4. negative regulation of cell size Source: Ensembl
  5. negative regulation of macroautophagy Source: Ensembl
  6. negative regulation of NFAT protein import into nucleus Source: Ensembl
  7. peptidyl-serine phosphorylation Source: Ensembl
  8. peptidyl-threonine phosphorylation Source: Ensembl
  9. positive regulation of actin filament polymerization Source: Ensembl
  10. positive regulation of endothelial cell proliferation Source: Ensembl
  11. positive regulation of lamellipodium assembly Source: Ensembl
  12. positive regulation of myotube differentiation Source: Ensembl
  13. positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
  14. positive regulation of protein kinase B signaling Source: Ensembl
  15. positive regulation of stress fiber assembly Source: Ensembl
  16. positive regulation of translation Source: Ensembl
  17. protein autophosphorylation Source: Ensembl
  18. regulation of carbohydrate utilization Source: Ensembl
  19. regulation of fatty acid beta-oxidation Source: Ensembl
  20. regulation of glycogen biosynthetic process Source: Ensembl
  21. regulation of protein kinase activity Source: Ensembl
  22. regulation of Rac GTPase activity Source: Ensembl
  23. regulation of response to food Source: Ensembl
  24. response to amino acid Source: Ensembl
  25. response to insulin Source: Ensembl
  26. ruffle organization Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

KinaseSAAS annotation, Transferase

Keywords - Ligandi

ATP-bindingSAAS annotation, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Submitted name:
Serine/threonine-protein kinase mTORImported
Gene namesi
Name:MTORImported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3942. MTOR.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. dendrite Source: Ensembl
  3. neuronal cell body Source: Ensembl
  4. PML body Source: Ensembl
  5. TORC1 complex Source: Ensembl
Complete GO annotation...

PTM / Processingi

Proteomic databases

PRIDEiB1AKP8.

Expressioni

Gene expression databases

ExpressionAtlasiB1AKP8. baseline and differential.

Interactioni

Structurei

3D structure databases

ProteinModelPortaliB1AKP8.
SMRiB1AKP8. Positions 230-319, 722-754.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Contains FAT domain.SAAS annotation
Contains FATC domain.SAAS annotation
Contains PI3K/PI4K domain.SAAS annotation

Phylogenomic databases

GeneTreeiENSGT00760000119382.
HOGENOMiHOG000049044.
HOVERGENiHBG102007.
OrthoDBiEOG7CCBQ4.

Family and domain databases

Gene3Di1.10.1070.11. 3 hits.
1.20.120.150. 1 hit.
InterProiIPR003152. 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]
PfamiPF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF08771. Rapamycin_bind. 1 hit.
[Graphical view]
SMARTiSM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMiSSF47212. SSF47212. 1 hit.
SSF56112. SSF56112. 2 hits.
PROSITEiPS51189. 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]

Sequencei

Sequence statusi: Complete.

B1AKP8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNFEAVLHYK HQNQARDEKK KLRHASGANI TNATTAATTA ATATTTASTE
60 70 80 90 100
GSNSESEAES TENSPTPSPL QKKVTEDLSK TLLMYTVPAV QGFFRSISLS
110 120 130 140 150
RGNNLQDTLR VLTLWFDYGH WPDVNEALVE GVKAIQIDTW LQVIPQLIAR
160 170 180 190 200
IDTPRPLVGR LIHQLLTDIG RYHPQALIYP LTVASKSTTT ARHNAANKIL
210 220 230 240 250
KNMCEHSNTL VQQAMMVSEE LIRVAILWHE MWHEGLEEAS RLYFGERNVK
260 270 280 290 300
GMFEVLEPLH AMMERGPQTL KETSFNQAYG RDLMEAQEWC RKYMKSGNVK
310 320 330 340 350
DLTQAWDLYY HVFRRISKQL PQLTSLELQY VSPKLLMCRD LELAVPGTYD
360 370 380 390 400
PNQPIIRIQS IAPSLQVITS KQRPRKLTLM GSNGHEFVFL LKGHEDLRQD
410 420 430 440 450
ERVMQLFGLV NTLLANDPTS LRKNLSIQRY AVIPLSTNSG LIGWVPHCDT
460 470 480 490 500
LHALIRDYRE KKKILLNIEH RIMLRMAPDY DHLTLMQKVE VFEHAVNNTA
510 520 530 540 550
GDDLAKLLWL KSPSSEVWFD RRTNYTRSLA VMSMVGYILG LGDRHPSNLM
560 570 580 590 600
LDRLSGKILH IDFGDCFEVA MTREKFPEKI PFRLTRMLTN AMEVTGLDGN
610 620 630 640 650
YRITCHTVME VLREHKDSVM AVLEAFVYDP LLNWRLMDTN TKGNKRSRTR
660 670 680 690 700
TDSYSAGQSV EILDGVELGE PAHKKTGTTV PESIHSFIGD GLVKPEALNK
710 720 730 740 750
KAIQIINRVR DKLTGRDFSH DDTLDVPTQV ELLIKQATSH ENLCQCYIGW

CPFW
Length:754
Mass (Da):85,901
Last modified:April 8, 2008 - v1
Checksum:i0AC837B2544A1CEA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL049653 Genomic DNA. No translation available.
AL109811 Genomic DNA. No translation available.
AL391561 Genomic DNA. No translation available.
KF495866 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENST00000376838; ENSP00000366034; ENSG00000198793.
UCSCiuc001asc.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL049653 Genomic DNA. No translation available.
AL109811 Genomic DNA. No translation available.
AL391561 Genomic DNA. No translation available.
KF495866 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortali B1AKP8.
SMRi B1AKP8. Positions 230-319, 722-754.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi B1AKP8.

Proteomic databases

PRIDEi B1AKP8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000376838 ; ENSP00000366034 ; ENSG00000198793 .
UCSCi uc001asc.3. human.

Organism-specific databases

HGNCi HGNC:3942. MTOR.
GenAtlasi Search...

Phylogenomic databases

GeneTreei ENSGT00760000119382.
HOGENOMi HOG000049044.
HOVERGENi HBG102007.
OrthoDBi EOG7CCBQ4.

Miscellaneous databases

ChiTaRSi MTOR. human.
NextBioi 35466581.

Gene expression databases

ExpressionAtlasi B1AKP8. baseline and differential.

Family and domain databases

Gene3Di 1.10.1070.11. 3 hits.
1.20.120.150. 1 hit.
InterProi IPR003152. 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 ]
Pfami PF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF08771. Rapamycin_bind. 1 hit.
[Graphical view ]
SMARTi SM00146. PI3Kc. 1 hit.
[Graphical view ]
SUPFAMi SSF47212. SSF47212. 1 hit.
SSF56112. SSF56112. 2 hits.
PROSITEi PS51189. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiB1AKP8_HUMAN
AccessioniPrimary (citable) accession number: B1AKP8
Entry historyi
Integrated into UniProtKB/TrEMBL: April 8, 2008
Last sequence update: April 8, 2008
Last modified: November 26, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (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.

Miscellaneousi

Caution

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

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3