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P42345

- MTOR_HUMAN

UniProt

P42345 - MTOR_HUMAN

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Protein

Serine/threonine-protein kinase mTOR

Gene

MTOR

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

Functioni

Serine/threonine protein kinase which is a central regulator of cellular metabolism, growth and survival in response to hormones, growth factors, nutrients, energy and stress signals. MTOR directly or indirectly regulates the phosphorylation of at least 800 proteins. Functions as part of 2 structurally and functionally distinct signaling complexes mTORC1 and mTORC2 (mTOR complex 1 and 2). Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. This includes phosphorylation of EIF4EBP1 and release of its inhibition toward the elongation initiation factor 4E (eiF4E). Moreover, phosphorylates and activates RPS6KB1 and RPS6KB2 that promote protein synthesis by modulating the activity of their downstream targets including ribosomal protein S6, eukaryotic translation initiation factor EIF4B, and the inhibitor of translation initiation PDCD4. Stimulates the pyrimidine biosynthesis pathway, both by acute regulation through RPS6KB1-mediated phosphorylation of the biosynthetic enzyme CAD, and delayed regulation, through transcriptional enhancement of the pentose phosphate pathway which produces 5-phosphoribosyl-1-pyrophosphate (PRPP), an allosteric activator of CAD at a later step in synthesis, this function is dependent on the mTORC1 complex. Regulates ribosome synthesis by activating RNA polymerase III-dependent transcription through phosphorylation and inhibition of MAF1 an RNA polymerase III-repressor. In parallel to protein synthesis, also regulates lipid synthesis through SREBF1/SREBP1 and LPIN1. To maintain energy homeostasis mTORC1 may also regulate mitochondrial biogenesis through regulation of PPARGC1A. mTORC1 also negatively regulates autophagy through phosphorylation of ULK1. Under nutrient sufficiency, phosphorylates ULK1 at 'Ser-758', disrupting the interaction with AMPK and preventing activation of ULK1. Also prevents autophagy through phosphorylation of the autophagy inhibitor DAP. mTORC1 exerts a feedback control on upstream growth factor signaling that includes phosphorylation and activation of GRB10 a INSR-dependent signaling suppressor. Among other potential targets mTORC1 may phosphorylate CLIP1 and regulate microtubules. As part of the mTORC2 complex MTOR may regulate other cellular processes including survival and organization of the cytoskeleton. Plays a critical role in the phosphorylation at 'Ser-473' of AKT1, a pro-survival effector of phosphoinositide 3-kinase, facilitating its activation by PDK1. mTORC2 may regulate the actin cytoskeleton, through phosphorylation of PRKCA, PXN and activation of the Rho-type guanine nucleotide exchange factors RHOA and RAC1A or RAC1B. mTORC2 also regulates the phosphorylation of SGK1 at 'Ser-422'.18 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activation of mTORC1 by growth factors such as insulin involves AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase a potent activator of the protein kinase activity of mTORC1. Insulin-stimulated and amino acid-dependent phosphorylation at Ser-1261 promotes autophosphorylation and the activation of mTORC1. Activation by amino acids requires relocalization of the mTORC1 complex to lysosomes that is mediated by the Ragulator complex and the Rag GTPases RRAGA, RRAGB, RRAGC and RRAGD. On the other hand, low cellular energy levels can inhibit mTORC1 through activation of PRKAA1 while hypoxia inhibits mTORC1 through a REDD1-dependent mechanism which may also require PRKAA1. The kinase activity of MTOR within the mTORC1 complex is positively regulated by MLST8 and negatively regulated by DEPTOR and AKT1S1. MTOR phosphorylates RPTOR which in turn inhibits mTORC1. MTOR is the target of the immunosuppressive and anti-cancer drug rapamycin which acts in complex with FKBP1A/FKBP12, and specifically inhibits its kinase activity. mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive. It may be regulated by RHEB but in an indirect manner through the PI3K signaling pathway.5 Publications

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. drug binding Source: InterPro
  3. kinase activity Source: UniProtKB
  4. phosphoprotein binding Source: UniProtKB
  5. protein serine/threonine kinase activity Source: UniProtKB
  6. ribosome binding Source: Ensembl
  7. RNA polymerase III type 1 promoter DNA binding Source: UniProtKB
  8. RNA polymerase III type 2 promoter DNA binding Source: UniProtKB
  9. RNA polymerase III type 3 promoter DNA binding Source: UniProtKB
  10. TFIIIC-class transcription factor binding Source: UniProtKB

GO - Biological processi

  1. cell growth Source: UniProtKB
  2. cellular response to hypoxia Source: UniProtKB
  3. cellular response to nutrient levels Source: UniProtKB
  4. epidermal growth factor receptor signaling pathway Source: Reactome
  5. Fc-epsilon receptor signaling pathway Source: Reactome
  6. fibroblast growth factor receptor signaling pathway Source: Reactome
  7. germ cell development Source: Ensembl
  8. growth Source: UniProtKB
  9. innate immune response Source: Reactome
  10. insulin receptor signaling pathway Source: Reactome
  11. negative regulation of autophagy Source: UniProtKB
  12. negative regulation of cell size Source: Ensembl
  13. negative regulation of macroautophagy Source: Ensembl
  14. negative regulation of NFAT protein import into nucleus Source: Ensembl
  15. neurotrophin TRK receptor signaling pathway Source: Reactome
  16. peptidyl-serine phosphorylation Source: UniProtKB
  17. peptidyl-threonine phosphorylation Source: Ensembl
  18. phosphatidylinositol-mediated signaling Source: Reactome
  19. phosphorylation Source: UniProtKB
  20. positive regulation of actin filament polymerization Source: Ensembl
  21. positive regulation of endothelial cell proliferation Source: Ensembl
  22. positive regulation of gene expression Source: UniProtKB
  23. positive regulation of lamellipodium assembly Source: Ensembl
  24. positive regulation of lipid biosynthetic process Source: UniProtKB
  25. positive regulation of myotube differentiation Source: Ensembl
  26. positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
  27. positive regulation of protein kinase B signaling Source: Ensembl
  28. positive regulation of protein phosphorylation Source: UniProtKB
  29. positive regulation of stress fiber assembly Source: Ensembl
  30. positive regulation of transcription from RNA polymerase III promoter Source: UniProtKB
  31. positive regulation of translation Source: UniProtKB
  32. protein autophosphorylation Source: MGI
  33. protein catabolic process Source: UniProtKB
  34. protein phosphorylation Source: UniProtKB
  35. regulation of actin cytoskeleton organization Source: UniProtKB
  36. regulation of carbohydrate utilization Source: Ensembl
  37. regulation of fatty acid beta-oxidation Source: Ensembl
  38. regulation of glycogen biosynthetic process Source: Ensembl
  39. regulation of protein kinase activity Source: Ensembl
  40. regulation of Rac GTPase activity Source: Ensembl
  41. regulation of response to food Source: Ensembl
  42. response to amino acid Source: UniProtKB
  43. response to nutrient Source: UniProtKB
  44. response to stress Source: UniProtKB
  45. ruffle organization Source: Ensembl
  46. signal transduction Source: UniProtKB
  47. T cell costimulation Source: Reactome
  48. TOR signaling Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_19358. CD28 dependent PI3K/Akt signaling.
REACT_200775. HSF1-dependent transactivation.
REACT_228016. VEGFR2 mediated vascular permeability.
REACT_6754. S6K1-mediated signalling.
REACT_6836. Release of eIF4E.
REACT_6838. mTOR signalling.
REACT_75829. PIP3 activates AKT signaling.
SignaLinkiP42345.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase mTOR (EC:2.7.11.1)
Alternative name(s):
FK506-binding protein 12-rapamycin complex-associated protein 1
FKBP12-rapamycin complex-associated protein
Mammalian target of rapamycin
Short name:
mTOR
Mechanistic target of rapamycin
Rapamycin and FKBP12 target 1
Rapamycin target protein 1
Gene namesi
Name:MTOR
Synonyms:FRAP, FRAP1, FRAP2, RAFT1, RAPT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3942. MTOR.

Subcellular locationi

Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side. Lysosome. Cytoplasm By similarity. NucleusPML body By similarity
Note: Shuttles between cytoplasm and nucleus. Accumulates in the nucleus in response to hypoxia (By similarity). Targeting to lysosomes depends on amino acid availability and RRAGA and RRAGB.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. endomembrane system Source: UniProtKB
  4. endoplasmic reticulum Source: UniProtKB-KW
  5. Golgi apparatus Source: UniProtKB-KW
  6. lysosomal membrane Source: UniProtKB
  7. lysosome Source: UniProtKB
  8. membrane Source: UniProtKB
  9. mitochondrial outer membrane Source: UniProtKB-KW
  10. phosphatidylinositol 3-kinase complex Source: UniProtKB
  11. PML body Source: Ensembl
  12. TORC1 complex Source: UniProtKB
  13. TORC2 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Lysosome, Membrane, Mitochondrion, Mitochondrion outer membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2159 – 21591S → A: Reduces mTORC1-associated S-2481 autophosphorylation; when associated with A-2164. 1 Publication
Mutagenesisi2159 – 21591S → D: Stronger phosphorylation of RPS6KB1; when associated with E-2164. 1 Publication
Mutagenesisi2164 – 21641T → A: Reduces mTORC1-associated S-2481 autophosphorylation; when associated with A-2159. 1 Publication
Mutagenesisi2164 – 21641T → E: Stronger phosphorylation of RPS6KB1; when associated with D-2159. 1 Publication
Mutagenesisi2173 – 21731T → A: Increased mTOR kinase activity. 1 Publication
Mutagenesisi2340 – 23401H → A: Barely detectable kinase activity. 1 Publication

Organism-specific databases

PharmGKBiPA28360.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 25492549Serine/threonine-protein kinase mTORPRO_0000088808Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei567 – 5671Phosphoserine3 Publications
Modified residuei1162 – 11621Phosphothreonine1 Publication
Modified residuei1218 – 12181N6-acetyllysine1 Publication
Modified residuei1261 – 12611Phosphoserine1 Publication
Modified residuei2159 – 21591Phosphoserine1 Publication
Modified residuei2164 – 21641Phosphothreonine1 Publication
Modified residuei2173 – 21731Phosphothreonine; by PKB/AKT11 Publication
Modified residuei2446 – 24461Phosphothreonine; by RPS6KB11 Publication
Modified residuei2448 – 24481Phosphoserine; by RPS6KB12 Publications
Modified residuei2478 – 24781Phosphoserine1 Publication
Modified residuei2481 – 24811Phosphoserine; by autocatalysis2 Publications

Post-translational modificationi

Autophosphorylates when part of mTORC1 or mTORC2. Phosphorylation at Ser-1261, Ser-2159 and Thr-2164 promotes autophosphorylation. Phosphorylation in the kinase domain modulates the interactions of MTOR with RPTOR and PRAS40 and leads to increased intrinsic mTORC1 kinase activity. Phosphorylation at Thr-2173 in the ATP-binding region by AKT1 strongly reduces kinase activity.11 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP42345.
PaxDbiP42345.
PRIDEiP42345.

PTM databases

PhosphoSiteiP42345.

Expressioni

Tissue specificityi

Expressed in numerous tissues, with highest levels in testis.2 Publications

Gene expression databases

BgeeiP42345.
CleanExiHS_FRAP1.
ExpressionAtlasiP42345. baseline and differential.
GenevestigatoriP42345.

Organism-specific databases

HPAiCAB005057.

Interactioni

Subunit structurei

Part of the mammalian target of rapamycin complex 1 (mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR. The mTORC1 complex is a 1 Md obligate dimer of two stoichiometric heterotetramers with overall dimensions of 290 A x 210 A x 135 A. It has a rhomboid shape and a central cavity, the dimeric interfaces are formed by interlocking interactions between the two MTOR and the two RPTOR subunits. the MLST8 subunits forms distal foot-like protuberances, and contacts only one MTOR within the complex, while the small PRAS40 localizes to the midsection of the central core, in close proximity to RPTOR. Part of the mammalian target of rapamycin COmplex 2 (mTORC2) which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR. Interacts with PPAPDC3 and PML. Interacts with PRR5 and RICTOR; the interaction is direct within the mTORC2 complex. Interacts with UBQLN1. Interacts with TTI1 and TELO2. Interacts with CLIP1; phosphorylates and regulates CLIP1. Interacts with NBN.20 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AKT1P317492EBI-359260,EBI-296087
DEPTORQ8TB455EBI-359260,EBI-2359040
EIF4EBP1Q135412EBI-359260,EBI-74090
FKBP1AP629422EBI-359260,EBI-1027571
MLST8Q9BVC44EBI-359260,EBI-1387471
PREX1Q8TCU611EBI-359260,EBI-1046542
RICTORQ6R32728EBI-359260,EBI-1387196
RPTORQ8N12230EBI-359260,EBI-1567928
SIRT1Q96EB62EBI-359260,EBI-1802965
TPCN2Q8NHX92EBI-359260,EBI-5239949

Protein-protein interaction databases

BioGridi108757. 110 interactions.
DIPiDIP-790N.
IntActiP42345. 49 interactions.
MINTiMINT-121301.
STRINGi9606.ENSP00000354558.

Structurei

Secondary structure

1
2549
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1387 – 140620Combined sources
Helixi1410 – 142213Combined sources
Helixi1426 – 143914Combined sources
Helixi1446 – 14527Combined sources
Helixi1456 – 146914Combined sources
Helixi1474 – 148613Combined sources
Helixi1490 – 14989Combined sources
Beta strandi1501 – 15033Combined sources
Helixi1506 – 152116Combined sources
Turni1522 – 15243Combined sources
Helixi1526 – 15338Combined sources
Helixi1541 – 155313Combined sources
Helixi1557 – 157216Combined sources
Turni1573 – 15775Combined sources
Turni1584 – 15863Combined sources
Helixi1587 – 160519Combined sources
Beta strandi1606 – 16083Combined sources
Helixi1609 – 16113Combined sources
Helixi1612 – 162413Combined sources
Helixi1630 – 164011Combined sources
Turni1641 – 16433Combined sources
Turni1646 – 16483Combined sources
Helixi1650 – 166314Combined sources
Helixi1666 – 167712Combined sources
Beta strandi1681 – 16844Combined sources
Helixi1694 – 170613Combined sources
Helixi1710 – 172920Combined sources
Helixi1737 – 176226Combined sources
Turni1766 – 17683Combined sources
Helixi1769 – 178214Combined sources
Turni1783 – 17853Combined sources
Helixi1787 – 181327Combined sources
Helixi1868 – 189326Combined sources
Beta strandi1896 – 18983Combined sources
Helixi1900 – 191314Combined sources
Helixi1917 – 192913Combined sources
Helixi1933 – 19386Combined sources
Helixi1939 – 19435Combined sources
Turni1944 – 19474Combined sources
Helixi1951 – 196616Combined sources
Helixi1970 – 198011Combined sources
Helixi1985 – 202036Combined sources
Helixi2025 – 203915Combined sources
Helixi2044 – 205815Combined sources
Helixi2065 – 209127Combined sources
Helixi2094 – 211118Combined sources
Helixi2115 – 21173Combined sources
Beta strandi2119 – 21224Combined sources
Helixi2123 – 21264Combined sources
Helixi2128 – 21325Combined sources
Beta strandi2137 – 21393Combined sources
Beta strandi2152 – 21565Combined sources
Beta strandi2158 – 21625Combined sources
Beta strandi2165 – 21673Combined sources
Beta strandi2170 – 21767Combined sources
Beta strandi2181 – 21899Combined sources
Helixi2193 – 221119Combined sources
Helixi2213 – 22175Combined sources
Beta strandi2227 – 22293Combined sources
Beta strandi2231 – 22333Combined sources
Beta strandi2235 – 22384Combined sources
Beta strandi2243 – 22453Combined sources
Helixi2246 – 225611Combined sources
Helixi2263 – 22719Combined sources
Helixi2275 – 22773Combined sources
Helixi2280 – 229112Combined sources
Helixi2298 – 23069Combined sources
Helixi2310 – 233425Combined sources
Turni2341 – 23433Combined sources
Beta strandi2344 – 23474Combined sources
Turni2348 – 23503Combined sources
Beta strandi2353 – 23553Combined sources
Helixi2364 – 23674Combined sources
Beta strandi2369 – 23713Combined sources
Helixi2381 – 23866Combined sources
Turni2389 – 23946Combined sources
Helixi2395 – 240915Combined sources
Helixi2411 – 242212Combined sources
Turni2425 – 24273Combined sources
Helixi2428 – 24358Combined sources
Helixi2493 – 250715Combined sources
Turni2508 – 25103Combined sources
Beta strandi2512 – 25165Combined sources
Helixi2521 – 253313Combined sources
Helixi2535 – 25384Combined sources
Helixi2543 – 25453Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AUEX-ray2.33A/B2015-2114[»]
1FAPX-ray2.70B2018-2112[»]
1NSGX-ray2.20B2019-2112[»]
2FAPX-ray2.20B2019-2112[»]
2GAQNMR-A2015-2114[»]
2NPUNMR-A2015-2114[»]
2RSENMR-B2019-2112[»]
3FAPX-ray1.85B2019-2112[»]
4DRHX-ray2.30B/E2025-2114[»]
4DRIX-ray1.45B2025-2114[»]
4DRJX-ray1.80B2025-2114[»]
4FAPX-ray2.80B2019-2112[»]
4JSNX-ray3.20A/B1376-2549[»]
4JSPX-ray3.30A/B1376-2549[»]
4JSVX-ray3.50A/B1376-2549[»]
4JSXX-ray3.50A/B1376-2549[»]
4JT5X-ray3.45A/B1376-2549[»]
4JT6X-ray3.60A/B1376-2549[»]
ProteinModelPortaliP42345.
SMRiP42345. Positions 164-213, 430-463, 580-631, 696-895, 991-1082, 2025-2422, 2517-2549.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42345.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati16 – 5338HEAT 1Add
BLAST
Repeati55 – 9945HEAT 2Add
BLAST
Repeati100 – 13738HEAT 3Add
BLAST
Repeati138 – 17942HEAT 4Add
BLAST
Repeati180 – 22041HEAT 5Add
BLAST
Repeati222 – 27655HEAT 6Add
BLAST
Repeati277 – 31337HEAT 7Add
BLAST
Repeati314 – 36451HEAT 8Add
BLAST
Repeati365 – 40945HEAT 9Add
BLAST
Repeati410 – 44536HEAT 10Add
BLAST
Repeati446 – 49449HEAT 11Add
BLAST
Repeati495 – 52935HEAT 12Add
BLAST
Repeati530 – 56334HEAT 13Add
BLAST
Repeati564 – 59633HEAT 14Add
BLAST
Repeati597 – 63640HEAT 15Add
BLAST
Repeati637 – 68347HEAT 16Add
BLAST
Repeati686 – 72439HEAT 17Add
BLAST
Repeati727 – 76640HEAT 18Add
BLAST
Repeati769 – 81143HEAT 19Add
BLAST
Repeati814 – 85340HEAT 20Add
BLAST
Repeati857 – 89337HEAT 21Add
BLAST
Repeati894 – 94249HEAT 22Add
BLAST
Repeati943 – 98846HEAT 23Add
BLAST
Repeati989 – 102739HEAT 24Add
BLAST
Repeati1029 – 106840HEAT 25Add
BLAST
Repeati1069 – 110537HEAT 26Add
BLAST
Repeati1106 – 114439HEAT 27Add
BLAST
Repeati1145 – 118844HEAT 28Add
BLAST
Repeati1189 – 122537HEAT 29Add
BLAST
Repeati1226 – 127348HEAT 30Add
BLAST
Repeati1274 – 131138HEAT 31Add
BLAST
Repeati1312 – 134534HEAT 32Add
BLAST
Repeati1346 – 138237TPR 1Add
BLAST
Domaini1382 – 1982601FATPROSITE-ProRule annotationAdd
BLAST
Repeati1383 – 140826TPR 2Add
BLAST
Repeati1409 – 144234TPR 3Add
BLAST
Repeati1443 – 147331TPR 4Add
BLAST
Repeati1474 – 150734TPR 5Add
BLAST
Repeati1508 – 154134TPR 6Add
BLAST
Repeati1542 – 157433TPR 7Add
BLAST
Repeati1575 – 161440TPR 8Add
BLAST
Repeati1615 – 164935TPR 9Add
BLAST
Repeati1650 – 169344TPR 10Add
BLAST
Repeati1694 – 173138TPR 11Add
BLAST
Repeati1732 – 178655TPR 12Add
BLAST
Repeati1787 – 184660TPR 13Add
BLAST
Repeati1898 – 193033TPR 14Add
BLAST
Repeati1931 – 197040TPR 15Add
BLAST
Repeati1971 – 200535TPR 16Add
BLAST
Domaini2182 – 2516335PI3K/PI4KPROSITE-ProRule annotationAdd
BLAST
Domaini2517 – 254933FATCPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 651651Interaction with NBNAdd
BLAST
Regioni2012 – 2144133Sufficient for interaction with the FKBP1A/rapamycin complexBy similarityAdd
BLAST
Regioni2258 – 229639Interaction with MLST8Add
BLAST

Domaini

The kinase domain (PI3K/PI4K) is intrinsically active but has a highly restricted catalytic center.1 Publication
The FAT domain forms three discontinuous subdomains of alpha-helical TPR repeats plus a single subdomain of HEAT repeats. The four domains pack sequentially to form a C-shaped a-solenoid that clamps onto the kinase domain (PubMed:23636326).1 Publication

Sequence similaritiesi

Belongs to the PI3/PI4-kinase family.Curated
Contains 1 FAT domain.PROSITE-ProRule annotation
Contains 1 FATC domain.PROSITE-ProRule annotation
Contains 32 HEAT repeats.Curated
Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation
Contains 16 TPR repeats.Curated

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiCOG5032.
GeneTreeiENSGT00760000119382.
HOGENOMiHOG000163215.
HOVERGENiHBG005744.
InParanoidiP42345.
KOiK07203.
OMAiTYKQNIG.
PhylomeDBiP42345.
TreeFamiTF105134.

Family and domain databases

Gene3Di1.10.1070.11. 3 hits.
1.20.120.150. 1 hit.
1.25.10.10. 4 hits.
1.25.40.10. 2 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024585. DUF3385_TOR.
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.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PfamiPF11865. DUF3385. 1 hit.
PF02259. 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.
SSF48371. SSF48371. 5 hits.
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.

P42345-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLGTGPAAAT TAATTSSNVS VLQQFASGLK SRNEETRAKA AKELQHYVTM
60 70 80 90 100
ELREMSQEES TRFYDQLNHH IFELVSSSDA NERKGGILAI ASLIGVEGGN
110 120 130 140 150
ATRIGRFANY LRNLLPSNDP VVMEMASKAI GRLAMAGDTF TAEYVEFEVK
160 170 180 190 200
RALEWLGADR NEGRRHAAVL VLRELAISVP TFFFQQVQPF FDNIFVAVWD
210 220 230 240 250
PKQAIREGAV AALRACLILT TQREPKEMQK PQWYRHTFEE AEKGFDETLA
260 270 280 290 300
KEKGMNRDDR IHGALLILNE LVRISSMEGE RLREEMEEIT QQQLVHDKYC
310 320 330 340 350
KDLMGFGTKP RHITPFTSFQ AVQPQQSNAL VGLLGYSSHQ GLMGFGTSPS
360 370 380 390 400
PAKSTLVESR CCRDLMEEKF DQVCQWVLKC RNSKNSLIQM TILNLLPRLA
410 420 430 440 450
AFRPSAFTDT QYLQDTMNHV LSCVKKEKER TAAFQALGLL SVAVRSEFKV
460 470 480 490 500
YLPRVLDIIR AALPPKDFAH KRQKAMQVDA TVFTCISMLA RAMGPGIQQD
510 520 530 540 550
IKELLEPMLA VGLSPALTAV LYDLSRQIPQ LKKDIQDGLL KMLSLVLMHK
560 570 580 590 600
PLRHPGMPKG LAHQLASPGL TTLPEASDVG SITLALRTLG SFEFEGHSLT
610 620 630 640 650
QFVRHCADHF LNSEHKEIRM EAARTCSRLL TPSIHLISGH AHVVSQTAVQ
660 670 680 690 700
VVADVLSKLL VVGITDPDPD IRYCVLASLD ERFDAHLAQA ENLQALFVAL
710 720 730 740 750
NDQVFEIREL AICTVGRLSS MNPAFVMPFL RKMLIQILTE LEHSGIGRIK
760 770 780 790 800
EQSARMLGHL VSNAPRLIRP YMEPILKALI LKLKDPDPDP NPGVINNVLA
810 820 830 840 850
TIGELAQVSG LEMRKWVDEL FIIIMDMLQD SSLLAKRQVA LWTLGQLVAS
860 870 880 890 900
TGYVVEPYRK YPTLLEVLLN FLKTEQNQGT RREAIRVLGL LGALDPYKHK
910 920 930 940 950
VNIGMIDQSR DASAVSLSES KSSQDSSDYS TSEMLVNMGN LPLDEFYPAV
960 970 980 990 1000
SMVALMRIFR DQSLSHHHTM VVQAITFIFK SLGLKCVQFL PQVMPTFLNV
1010 1020 1030 1040 1050
IRVCDGAIRE FLFQQLGMLV SFVKSHIRPY MDEIVTLMRE FWVMNTSIQS
1060 1070 1080 1090 1100
TIILLIEQIV VALGGEFKLY LPQLIPHMLR VFMHDNSPGR IVSIKLLAAI
1110 1120 1130 1140 1150
QLFGANLDDY LHLLLPPIVK LFDAPEAPLP SRKAALETVD RLTESLDFTD
1160 1170 1180 1190 1200
YASRIIHPIV RTLDQSPELR STAMDTLSSL VFQLGKKYQI FIPMVNKVLV
1210 1220 1230 1240 1250
RHRINHQRYD VLICRIVKGY TLADEEEDPL IYQHRMLRSG QGDALASGPV
1260 1270 1280 1290 1300
ETGPMKKLHV STINLQKAWG AARRVSKDDW LEWLRRLSLE LLKDSSSPSL
1310 1320 1330 1340 1350
RSCWALAQAY NPMARDLFNA AFVSCWSELN EDQQDELIRS IELALTSQDI
1360 1370 1380 1390 1400
AEVTQTLLNL AEFMEHSDKG PLPLRDDNGI VLLGERAAKC RAYAKALHYK
1410 1420 1430 1440 1450
ELEFQKGPTP AILESLISIN NKLQQPEAAA GVLEYAMKHF GELEIQATWY
1460 1470 1480 1490 1500
EKLHEWEDAL VAYDKKMDTN KDDPELMLGR MRCLEALGEW GQLHQQCCEK
1510 1520 1530 1540 1550
WTLVNDETQA KMARMAAAAA WGLGQWDSME EYTCMIPRDT HDGAFYRAVL
1560 1570 1580 1590 1600
ALHQDLFSLA QQCIDKARDL LDAELTAMAG ESYSRAYGAM VSCHMLSELE
1610 1620 1630 1640 1650
EVIQYKLVPE RREIIRQIWW ERLQGCQRIV EDWQKILMVR SLVVSPHEDM
1660 1670 1680 1690 1700
RTWLKYASLC GKSGRLALAH KTLVLLLGVD PSRQLDHPLP TVHPQVTYAY
1710 1720 1730 1740 1750
MKNMWKSARK IDAFQHMQHF VQTMQQQAQH AIATEDQQHK QELHKLMARC
1760 1770 1780 1790 1800
FLKLGEWQLN LQGINESTIP KVLQYYSAAT EHDRSWYKAW HAWAVMNFEA
1810 1820 1830 1840 1850
VLHYKHQNQA RDEKKKLRHA SGANITNATT AATTAATATT TASTEGSNSE
1860 1870 1880 1890 1900
SEAESTENSP TPSPLQKKVT EDLSKTLLMY TVPAVQGFFR SISLSRGNNL
1910 1920 1930 1940 1950
QDTLRVLTLW FDYGHWPDVN EALVEGVKAI QIDTWLQVIP QLIARIDTPR
1960 1970 1980 1990 2000
PLVGRLIHQL LTDIGRYHPQ ALIYPLTVAS KSTTTARHNA ANKILKNMCE
2010 2020 2030 2040 2050
HSNTLVQQAM MVSEELIRVA ILWHEMWHEG LEEASRLYFG ERNVKGMFEV
2060 2070 2080 2090 2100
LEPLHAMMER GPQTLKETSF NQAYGRDLME AQEWCRKYMK SGNVKDLTQA
2110 2120 2130 2140 2150
WDLYYHVFRR ISKQLPQLTS LELQYVSPKL LMCRDLELAV PGTYDPNQPI
2160 2170 2180 2190 2200
IRIQSIAPSL QVITSKQRPR KLTLMGSNGH EFVFLLKGHE DLRQDERVMQ
2210 2220 2230 2240 2250
LFGLVNTLLA NDPTSLRKNL SIQRYAVIPL STNSGLIGWV PHCDTLHALI
2260 2270 2280 2290 2300
RDYREKKKIL LNIEHRIMLR MAPDYDHLTL MQKVEVFEHA VNNTAGDDLA
2310 2320 2330 2340 2350
KLLWLKSPSS EVWFDRRTNY TRSLAVMSMV GYILGLGDRH PSNLMLDRLS
2360 2370 2380 2390 2400
GKILHIDFGD CFEVAMTREK FPEKIPFRLT RMLTNAMEVT GLDGNYRITC
2410 2420 2430 2440 2450
HTVMEVLREH KDSVMAVLEA FVYDPLLNWR LMDTNTKGNK RSRTRTDSYS
2460 2470 2480 2490 2500
AGQSVEILDG VELGEPAHKK TGTTVPESIH SFIGDGLVKP EALNKKAIQI
2510 2520 2530 2540
INRVRDKLTG RDFSHDDTLD VPTQVELLIK QATSHENLCQ CYIGWCPFW
Length:2,549
Mass (Da):288,892
Last modified:November 1, 1995 - v1
Checksum:i7D9AD6E784882AB4
GO

Sequence cautioni

The sequence AAC39933.1 differs from that shown. Reason: Frameshift at positions 956 and 999. Curated
The sequence BAE06077.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti353 – 3531K → N in AAC39933. (PubMed:9653645)Curated
Sequence conflicti359 – 3591S → N in AAC39933. (PubMed:9653645)Curated
Sequence conflicti364 – 3641D → N in AAC39933. (PubMed:9653645)Curated
Sequence conflicti390 – 3901M → L in AAC39933. (PubMed:9653645)Curated
Sequence conflicti430 – 4301R → L in AAC39933. (PubMed:9653645)Curated
Sequence conflicti455 – 4573VLD → GVE in AAC39933. (PubMed:9653645)Curated
Sequence conflicti461 – 4611A → G in AAC39933. (PubMed:9653645)Curated
Sequence conflicti482 – 4843VFT → FFN in AAC39933. (PubMed:9653645)Curated
Sequence conflicti489 – 4891L → V in AAC39933. (PubMed:9653645)Curated
Sequence conflicti513 – 5131L → I in AAC39933. (PubMed:9653645)Curated
Sequence conflicti539 – 5391L → V in AAC39933. (PubMed:9653645)Curated
Sequence conflicti553 – 5531R → C in AAC39933. (PubMed:9653645)Curated
Sequence conflicti857 – 8571P → L in BAE06077. 1 PublicationCurated
Sequence conflicti1075 – 10751I → S in AAC39933. (PubMed:9653645)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti8 – 81A → S in a lung large cell carcinoma sample; somatic mutation. 1 Publication
VAR_041537
Natural varianti135 – 1351M → T in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_041538
Natural varianti1083 – 10831M → V.1 Publication
Corresponds to variant rs56164650 [ dbSNP | Ensembl ].
VAR_041539
Natural varianti1134 – 11341A → V.1 Publication
Corresponds to variant rs28730685 [ dbSNP | Ensembl ].
VAR_041540
Natural varianti1178 – 11781S → F.1 Publication
Corresponds to variant rs55975118 [ dbSNP | Ensembl ].
VAR_041541
Natural varianti2011 – 20111M → V in an ovarian mucinous carcinoma sample; somatic mutation. 1 Publication
VAR_041542
Natural varianti2215 – 22151S → Y in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041543
Natural varianti2220 – 22201L → F Found in a renal cell carcinoma sample; somatic mutation. 1 Publication
VAR_064733
Natural varianti2406 – 24061V → A Found in a renal cell carcinoma sample; somatic mutation. 1 Publication
VAR_064734
Natural varianti2476 – 24761P → L in a glioblastoma multiforme sample; somatic mutation. 1 Publication
VAR_041544

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34075 mRNA. Translation: AAA58486.1.
U88966 mRNA. Translation: AAC39933.1. Frameshift.
AB209995 mRNA. Translation: BAE06077.1. Different initiation.
AL109811, AL049653, AL391561 Genomic DNA. Translation: CAI22105.1.
AL391561, AL049653, AL109811 Genomic DNA. Translation: CAI17228.1.
AL049653, AL109811, AL391561 Genomic DNA. Translation: CAI22145.1.
BC117166 mRNA. Translation: AAI17167.1.
AJ300188 Genomic DNA. Translation: CAC15570.1.
L35478 mRNA. Translation: AAC41713.1.
CCDSiCCDS127.1.
PIRiS45340.
RefSeqiNP_004949.1. NM_004958.3.
XP_005263495.1. XM_005263438.1.
UniGeneiHs.338207.

Genome annotation databases

EnsembliENST00000361445; ENSP00000354558; ENSG00000198793.
GeneIDi2475.
KEGGihsa:2475.
UCSCiuc001asd.3. human.

Polymorphism databases

DMDMi1169735.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Wikipedia

Mammalian target of rapamycin entry

Target mTOR

mTOR signaling pathway and mTOR inhibition resource

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34075 mRNA. Translation: AAA58486.1 .
U88966 mRNA. Translation: AAC39933.1 . Frameshift.
AB209995 mRNA. Translation: BAE06077.1 . Different initiation.
AL109811 , AL049653 , AL391561 Genomic DNA. Translation: CAI22105.1 .
AL391561 , AL049653 , AL109811 Genomic DNA. Translation: CAI17228.1 .
AL049653 , AL109811 , AL391561 Genomic DNA. Translation: CAI22145.1 .
BC117166 mRNA. Translation: AAI17167.1 .
AJ300188 Genomic DNA. Translation: CAC15570.1 .
L35478 mRNA. Translation: AAC41713.1 .
CCDSi CCDS127.1.
PIRi S45340.
RefSeqi NP_004949.1. NM_004958.3.
XP_005263495.1. XM_005263438.1.
UniGenei Hs.338207.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AUE X-ray 2.33 A/B 2015-2114 [» ]
1FAP X-ray 2.70 B 2018-2112 [» ]
1NSG X-ray 2.20 B 2019-2112 [» ]
2FAP X-ray 2.20 B 2019-2112 [» ]
2GAQ NMR - A 2015-2114 [» ]
2NPU NMR - A 2015-2114 [» ]
2RSE NMR - B 2019-2112 [» ]
3FAP X-ray 1.85 B 2019-2112 [» ]
4DRH X-ray 2.30 B/E 2025-2114 [» ]
4DRI X-ray 1.45 B 2025-2114 [» ]
4DRJ X-ray 1.80 B 2025-2114 [» ]
4FAP X-ray 2.80 B 2019-2112 [» ]
4JSN X-ray 3.20 A/B 1376-2549 [» ]
4JSP X-ray 3.30 A/B 1376-2549 [» ]
4JSV X-ray 3.50 A/B 1376-2549 [» ]
4JSX X-ray 3.50 A/B 1376-2549 [» ]
4JT5 X-ray 3.45 A/B 1376-2549 [» ]
4JT6 X-ray 3.60 A/B 1376-2549 [» ]
ProteinModelPortali P42345.
SMRi P42345. Positions 164-213, 430-463, 580-631, 696-895, 991-1082, 2025-2422, 2517-2549.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108757. 110 interactions.
DIPi DIP-790N.
IntActi P42345. 49 interactions.
MINTi MINT-121301.
STRINGi 9606.ENSP00000354558.

Chemistry

BindingDBi P42345.
ChEMBLi CHEMBL2221341.
DrugBanki DB01590. Everolimus.
DB00337. Pimecrolimus.
DB00877. Sirolimus.
DB06287. Temsirolimus.
GuidetoPHARMACOLOGYi 2109.

PTM databases

PhosphoSitei P42345.

Polymorphism databases

DMDMi 1169735.

Proteomic databases

MaxQBi P42345.
PaxDbi P42345.
PRIDEi P42345.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000361445 ; ENSP00000354558 ; ENSG00000198793 .
GeneIDi 2475.
KEGGi hsa:2475.
UCSCi uc001asd.3. human.

Organism-specific databases

CTDi 2475.
GeneCardsi GC01M011166.
HGNCi HGNC:3942. MTOR.
HPAi CAB005057.
MIMi 601231. gene.
neXtProti NX_P42345.
PharmGKBi PA28360.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5032.
GeneTreei ENSGT00760000119382.
HOGENOMi HOG000163215.
HOVERGENi HBG005744.
InParanoidi P42345.
KOi K07203.
OMAi TYKQNIG.
PhylomeDBi P42345.
TreeFami TF105134.

Enzyme and pathway databases

Reactomei REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_19358. CD28 dependent PI3K/Akt signaling.
REACT_200775. HSF1-dependent transactivation.
REACT_228016. VEGFR2 mediated vascular permeability.
REACT_6754. S6K1-mediated signalling.
REACT_6836. Release of eIF4E.
REACT_6838. mTOR signalling.
REACT_75829. PIP3 activates AKT signaling.
SignaLinki P42345.

Miscellaneous databases

ChiTaRSi MTOR. human.
EvolutionaryTracei P42345.
GeneWikii Mammalian_target_of_rapamycin.
GenomeRNAii 2475.
NextBioi 9805.
PROi P42345.
SOURCEi Search...

Gene expression databases

Bgeei P42345.
CleanExi HS_FRAP1.
ExpressionAtlasi P42345. baseline and differential.
Genevestigatori P42345.

Family and domain databases

Gene3Di 1.10.1070.11. 3 hits.
1.20.120.150. 1 hit.
1.25.10.10. 4 hits.
1.25.40.10. 2 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024585. DUF3385_TOR.
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.
IPR011990. TPR-like_helical_dom.
[Graphical view ]
Pfami PF11865. DUF3385. 1 hit.
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.
SSF48371. SSF48371. 5 hits.
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. "A mammalian protein targeted by G1-arresting rapamycin-receptor complex."
    Brown E.J., Albers M.W., Shin T.B., Ichikawa K., Keith C.T., Lane W.S., Schreiber S.L.
    Nature 369:756-758(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Molecular cloning and expression analysis of five novel genes in chromosome 1p36."
    Onyango P., Lubyova B., Gardellin P., Kurzbauer R., Weith A.
    Genomics 50:187-198(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
    Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cerebellum.
  6. "The human gene for mannan-binding lectin-associated serine protease-2 (MASP-2), the effector component of the lectin route of complement activation, is part of a tightly linked gene cluster on chromosome 1p36.2-3."
    Stover C., Endo Y., Takahashi M., Lynch N., Constantinescu C., Vorup-Jensen T., Thiel S., Friedl H., Hankeln T., Hall R., Gregory S., Fujita T., Schwaeble W.
    Genes Immun. 2:119-127(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1362-2549.
  7. "RAPT1, a mammalian homolog of yeast Tor, interacts with the FKBP12/rapamycin complex."
    Chiu M.I., Katz H., Berlin V.
    Proc. Natl. Acad. Sci. U.S.A. 91:12574-12578(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1987-2146, TISSUE SPECIFICITY.
    Tissue: B-cell.
  8. "Expression, enzyme activity, and subcellular localization of mammalian target of rapamycin in insulin-responsive cells."
    Withers D.J., Ouwens D.M., Nave B.T., van der Zon G.C.M., Alarcon C.M., Cardenas M.E., Heitman J., Maassen J.A., Shepherd P.R.
    Biochem. Biophys. Res. Commun. 241:704-709(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION.
  9. "Characterization of ubiquilin 1, an mTOR-interacting protein."
    Wu S., Mikhailov A., Kallo-Hosein H., Hara K., Yonezawa K., Avruch J.
    Biochim. Biophys. Acta 1542:41-56(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBQLN1.
  10. "mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the growth machinery."
    Kim D.-H., Sarbassov D.D., Ali S.M., King J.E., Latek R.R., Erdjument-Bromage H., Tempst P., Sabatini D.M.
    Cell 110:163-175(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NUTRIENT-DEPENDENT CELL GROWTH, FUNCTION IN PHOSPHORYLATION OF RPS6KB1, INTERACTION WITH RPTOR.
  11. "Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action."
    Hara K., Maruki Y., Long X., Yoshino K., Oshiro N., Hidayat S., Tokunaga C., Avruch J., Yonezawa K.
    Cell 110:177-189(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RPTOR.
  12. "The FKBP12-rapamycin-associated protein (FRAP) is a CLIP-170 kinase."
    Choi J.H., Bertram P.G., Drenan R., Carvalho J., Zhou H.H., Zheng X.F.
    EMBO Rep. 3:988-994(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CLIP1, FUNCTION IN PHOSPHORYLATION OF CLIP1.
  13. "Regulation of ribosomal S6 kinase 2 by mammalian target of rapamycin."
    Park I.H., Bachmann R., Shirazi H., Chen J.
    J. Biol. Chem. 277:31423-31429(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF RPS6KB2.
  14. "Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control."
    Loewith R., Jacinto E., Wullschleger S., Lorberg A., Crespo J.L., Bonenfant D., Oppliger W., Jenoe P., Hall M.N.
    Mol. Cell 10:457-468(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MLST8 AND RPTOR, IDENTIFICATION IN THE MTORC1 COMPLEX, TISSUE SPECIFICITY.
  15. "FKBP12-rapamycin-associated protein associates with mitochondria and senses osmotic stress via mitochondrial dysfunction."
    Desai B.N., Myers B.R., Schreiber S.L.
    Proc. Natl. Acad. Sci. U.S.A. 99:4319-4324(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  16. "TSC2 mediates cellular energy response to control cell growth and survival."
    Inoki K., Zhu T., Guan K.L.
    Cell 115:577-590(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, FUNCTION IN RESPONSE TO LOW CELLULAR ENERGY.
  17. "GbetaL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR."
    Kim D.-H., Sarbassov D.D., Ali S.M., Latek R.R., Guntur K.V.P., Erdjument-Bromage H., Tempst P., Sabatini D.M.
    Mol. Cell 11:895-904(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MLST8.
  18. "Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton."
    Sarbassov D.D., Ali S.M., Kim D.-H., Guertin D.A., Latek R.R., Erdjument-Bromage H., Tempst P., Sabatini D.M.
    Curr. Biol. 14:1296-1302(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF PRKCA, FUNCTION IN REGULATION OF THE ACTIN CYTOSKELETON, IDENTIFICATION IN THE MTORC2 COMPLEX, INTERACTION WITH RICTOR.
  19. "Regulation of mTOR function in response to hypoxia by REDD1 and the TSC1/TSC2 tumor suppressor complex."
    Brugarolas J., Lei K., Hurley R.L., Manning B.D., Reiling J.H., Hafen E., Witters L.A., Ellisen L.W., Kaelin W.G. Jr.
    Genes Dev. 18:2893-2904(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, FUNCTION IN RESPONSE TO HYPOXIA.
  20. "FKBP12-rapamycin-associated protein or mammalian target of rapamycin (FRAP/mTOR) localization in the endoplasmic reticulum and the Golgi apparatus."
    Drenan R.M., Liu X., Bertram P.G., Zheng X.F.S.
    J. Biol. Chem. 279:772-778(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  21. "Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive."
    Jacinto E., Loewith R., Schmidt A., Lin S., Ruegg M.A., Hall A., Hall M.N.
    Nat. Cell Biol. 6:1122-1128(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF THE ACTIN CYTOSKELETON, FUNCTION IN PHOSPHORYLATION OF PXN, IDENTIFICATION IN THE MTORC2 COMPLEX, INTERACTION WITH RICTOR, AUTOPHOSPHORYLATION.
  22. "Identification of S6 kinase 1 as a novel mammalian target of rapamycin (mTOR)-phosphorylating kinase."
    Holz M.K., Blenis J.
    J. Biol. Chem. 280:26089-26093(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-2446 AND SER-2448.
  23. "Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex."
    Sarbassov D.D., Guertin D.A., Ali S.M., Sabatini D.M.
    Science 307:1098-1101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF AKT1.
  24. "PRR5, a novel component of mTOR complex 2, regulates platelet-derived growth factor receptor beta expression and signaling."
    Woo S.-Y., Kim D.-H., Jun C.-B., Kim Y.-M., Haar E.V., Lee S.-I., Hegg J.W., Bandhakavi S., Griffin T.J., Kim D.-H.
    J. Biol. Chem. 282:25604-25612(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MTORC2 COMPLEX, INTERACTION WITH PRR5.
  25. "PRAS40 is an insulin-regulated inhibitor of the mTORC1 protein kinase."
    Sancak Y., Thoreen C.C., Peterson T.R., Lindquist R.A., Kang S.A., Spooner E., Carr S.A., Sabatini D.M.
    Mol. Cell 25:903-915(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AKT1S1, ENZYME REGULATION.
  26. "mTOR complex 2 (mTORC2) controls hydrophobic motif phosphorylation and activation of serum- and glucocorticoid-induced protein kinase 1 (SGK1)."
    Garcia-Martinez J.M., Alessi D.R.
    Biochem. J. 416:375-385(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MTORC1 AND MTORC2 COMPLEXES, FUNCTION IN PHOSPHORYLATION OF RPS6KB1 AND SGK1.
  27. "SREBP activity is regulated by mTORC1 and contributes to Akt-dependent cell growth."
    Porstmann T., Santos C.R., Griffiths B., Cully M., Wu M., Leevers S., Griffiths J.R., Chung Y.L., Schulze A.
    Cell Metab. 8:224-236(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LIPID SYNTHESIS AND CELL GROWTH.
  28. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  29. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2478 AND SER-2481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  30. "The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1."
    Sancak Y., Peterson T.R., Shaul Y.D., Lindquist R.A., Thoreen C.C., Bar-Peled L., Sabatini D.M.
    Science 320:1496-1501(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION.
  31. "DEPTOR is an mTOR inhibitor frequently overexpressed in multiple myeloma cells and required for their survival."
    Peterson T.R., Laplante M., Thoreen C.C., Sancak Y., Kang S.A., Kuehl W.M., Gray N.S., Sabatini D.M.
    Cell 137:873-886(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DEPTOR, ENZYME REGULATION.
  32. "Site-specific mTOR phosphorylation promotes mTORC1-mediated signaling and cell growth."
    Acosta-Jaquez H.A., Keller J.A., Foster K.G., Ekim B., Soliman G.A., Feener E.P., Ballif B.A., Fingar D.C.
    Mol. Cell. Biol. 29:4308-4324(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-1261.
  33. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. "mTOR phosphorylated at S2448 binds to raptor and rictor."
    Rosner M., Siegel N., Valli A., Fuchs C., Hengstschlager M.
    Amino Acids 38:223-228(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-2448.
  36. "Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids."
    Sancak Y., Bar-Peled L., Zoncu R., Markhard A.L., Nada S., Sabatini D.M.
    Cell 141:290-303(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  37. "DAP1, a novel substrate of mTOR, negatively regulates autophagy."
    Koren I., Reem E., Kimchi A.
    Curr. Biol. 20:1093-1098(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF DAP, FUNCTION IN AUTOPHAGY.
  38. "A genetic screen identifies the Triple T complex required for DNA damage signaling and ATM and ATR stability."
    Hurov K.E., Cotta-Ramusino C., Elledge S.J.
    Genes Dev. 24:1939-1950(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TTI1.
  39. "Tel2 structure and function in the Hsp90-dependent maturation of mTOR and ATR complexes."
    Takai H., Xie Y., de Lange T., Pavletich N.P.
    Genes Dev. 24:2019-2030(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TELO2.
  40. "Tti1 and Tel2 are critical factors in mammalian target of rapamycin complex assembly."
    Kaizuka T., Hara T., Oshiro N., Kikkawa U., Yonezawa K., Takehana K., Iemura S., Natsume T., Mizushima N.
    J. Biol. Chem. 285:20109-20116(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TELO2 AND TTI1.
  41. Cited for: FUNCTION IN REGULATION OF RNA POLYMERASE III TRANSCRIPTION, FUNCTION IN PHOSPHORYLATION OF MAF1.
  42. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567 AND THR-1162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  43. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  44. "mTOR kinase domain phosphorylation promotes mTORC1 signaling, cell growth, and cell cycle progression."
    Ekim B., Magnuson B., Acosta-Jaquez H.A., Keller J.A., Feener E.P., Fingar D.C.
    Mol. Cell. Biol. 31:2787-2801(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-2159; THR-2164 AND SER-2481, MUTAGENESIS OF SER-2159 AND THR-2164.
  45. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  46. "The mTOR-regulated phosphoproteome reveals a mechanism of mTORC1-mediated inhibition of growth factor signaling."
    Hsu P.P., Kang S.A., Rameseder J., Zhang Y., Ottina K.A., Lim D., Peterson T.R., Choi Y., Gray N.S., Yaffe M.B., Marto J.A., Sabatini D.M.
    Science 332:1317-1322(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF GRB10, FUNCTION IN INSR-DEPENDENT SIGNALING.
  47. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  48. "Phosphorylation of the TOR ATP binding domain by AGC kinase constitutes a novel mode of TOR inhibition."
    Halova L., Du W., Kirkham S., Smith D.L., Petersen J.
    J. Cell Biol. 203:595-604(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-2173, MUTAGENESIS OF THR-2173.
  49. "Interaction between NBS1 and the mTOR/Rictor/SIN1 complex through specific domains."
    Wang J.Q., Chen J.H., Chen Y.C., Chen M.Y., Hsieh C.Y., Teng S.C., Wu K.J.
    PLoS ONE 8:E65586-E65586(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NBN.
  50. "Quantitative phosphoproteomics reveal mTORC1 activates de novo pyrimidine synthesis."
    Robitaille A.M., Christen S., Shimobayashi M., Cornu M., Fava L.L., Moes S., Prescianotto-Baschong C., Sauer U., Jenoe P., Hall M.N.
    Science 339:1320-1323(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION OF RPS6KB1, REGULATION OF PYRIMIDINE SYNTHESIS.
  51. "Stimulation of de novo pyrimidine synthesis by growth signaling through mTOR and S6K1."
    Ben-Sahra I., Howell J.J., Asara J.M., Manning B.D.
    Science 339:1323-1328(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION OF RPS6KB1, REGULATION OF PYRIMIDINE SYNTHESIS.
  52. "Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP."
    Choi J., Chen J., Schreiber S.L., Clardy J.
    Science 273:239-242(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2018-2112 IN COMPLEX WITH FKBP1A AND INHIBITOR RAPAMYCIN.
  53. "Refined structure of the FKBP12-rapamycin-FRB ternary complex at 2.2 A resolution."
    Liang J., Choi J., Clardy J.
    Acta Crystallogr. D 55:736-744(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2018-2112 IN COMPLEX WITH FKBP1A AND INHIBITOR RAPAMYCIN.
  54. "Insights into the domain and repeat architecture of target of rapamycin."
    Knutson B.A.
    J. Struct. Biol. 170:354-363(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING, HEAT-REPEATS, TPR-REPEATS.
  55. "Structure of the human mTOR complex I and its implications for rapamycin inhibition."
    Yip C.K., Murata K., Walz T., Sabatini D.M., Kang S.A.
    Mol. Cell 38:768-774(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYO-ELECTRON MICROSCOPY (26 ANGSTROMS) OF MTORC1 COMPLEX, SUBUNIT.
  56. Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1376-2549 IN COMPLEX WITH MLST8, SUBUNIT, TPR-REPEATS, DOMAINS, MUTAGENESIS OF HIS-2340.
  57. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-8; THR-135; VAL-1083; VAL-1134; PHE-1178; VAL-2011; TYR-2215 AND LEU-2476.
  58. Cited for: VARIANTS PHE-2220 AND ALA-2406.

Entry informationi

Entry nameiMTOR_HUMAN
AccessioniPrimary (citable) accession number: P42345
Secondary accession number(s): Q4LE76
, Q5TER1, Q6LE87, Q96QG3, Q9Y4I3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 26, 2014
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3