P42345 (MTOR_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 138.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | 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 names |
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| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 2549 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | 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. 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. Regulates ribosome synthesis by activating RNA polymerase III-dependent transcription through phosphorylation and inhibition of MAF1 a 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'. Ref.10 Ref.11 Ref.12 Ref.13 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.23 Ref.26 Ref.27 Ref.30 Ref.36 Ref.40 Ref.45 |
| Catalytic activity | ATP + a protein = ADP + a phosphoprotein. |
| Enzyme regulation | 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. mTORC1 binds and is inhibited by the FKBP1A-rapamycin complex. 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. Ref.16 Ref.19 Ref.25 Ref.30 Ref.31 |
| Subunit structure | Part of the mammalian target of rapamycin complex 1 (mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR. Part of the mammalian target of rapamycin complex 2 (mTORC2) which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR. Interacts with PPAPDC3 and PML By similarity. Interacts with PRR5 and RICTOR; the interaction is direct within the mTORC2 complex By similarity. Interacts with UBQLN1 By similarity. Interacts with TTI1 and TELO2 By similarity. Interacts with CLIP1; phosphorylates and regulates CLIP1 By similarity. Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.17 Ref.18 Ref.21 Ref.24 Ref.25 Ref.26 Ref.31 Ref.37 Ref.38 Ref.39 |
| Subcellular location | 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. Nucleus › PML 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. Ref.8 Ref.15 Ref.20 Ref.30 Ref.35 |
| Tissue specificity | Expressed in numerous tissues, with highest levels in testis. Ref.7 Ref.14 |
| Post-translational modification | Phosphorylated. Autophosphorylates when part of mTORC1 or mTORC2. Phosphorylation at Ser-1261 promotes autophosphorylation. Ref.8 Ref.21 Ref.22 Ref.32 Ref.43 |
| Sequence similarities | Belongs to the PI3/PI4-kinase family. Contains 1 FAT domain. Contains 1 FATC domain. Contains 7 HEAT repeats. Contains 1 PI3K/PI4K domain. |
| Sequence caution | The sequence AAC39933.1 differs from that shown. Reason: Frameshift at positions 956 and 999. The sequence BAE06077.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| DEPTOR | Q8TB45 | 5 | EBI-359260,EBI-2359040 | |
| EIF4EBP1 | Q13541 | 2 | EBI-359260,EBI-74090 | |
| MLST8 | Q9BVC4 | 4 | EBI-359260,EBI-1387471 | |
| PREX1 | Q8TCU6 | 11 | EBI-359260,EBI-1046542 | |
| RICTOR | Q6R327 | 16 | EBI-359260,EBI-1387196 | |
| RPTOR | Q8N122 | 12 | EBI-359260,EBI-1567928 | |
| SIRT1 | Q96EB6 | 2 | EBI-359260,EBI-1802965 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||
Molecule processing | ||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 2549 | 2549 | Serine/threonine-protein kinase mTOR | PRO_0000088808 | ||||||||||||||||
Regions | ||||||||||||||||||||
| Repeat | 16 – 53 | 38 | HEAT 1 | |||||||||||||||||
| Repeat | 650 – 688 | 39 | HEAT 2 | |||||||||||||||||
| Repeat | 859 – 897 | 39 | HEAT 3 | |||||||||||||||||
| Repeat | 988 – 1025 | 38 | HEAT 4 | |||||||||||||||||
| Repeat | 1069 – 1106 | 38 | HEAT 5 | |||||||||||||||||
| Repeat | 1109 – 1148 | 40 | HEAT 6 | |||||||||||||||||
| Repeat | 1150 – 1186 | 37 | HEAT 7 | |||||||||||||||||
| Domain | 1382 – 1982 | 601 | FAT | |||||||||||||||||
| Domain | 2182 – 2516 | 335 | PI3K/PI4K | |||||||||||||||||
| Domain | 2517 – 2549 | 33 | FATC | |||||||||||||||||
| Region | 2012 – 2144 | 133 | Sufficient for interaction with the FKBP1A/rapamycin complex By similarity | |||||||||||||||||
Amino acid modifications | ||||||||||||||||||||
| Modified residue | 567 | 1 | Phosphoserine Ref.28 Ref.33 Ref.41 | |||||||||||||||||
| Modified residue | 1162 | 1 | Phosphothreonine Ref.41 | |||||||||||||||||
| Modified residue | 1218 | 1 | N6-acetyllysine Ref.34 | |||||||||||||||||
| Modified residue | 1261 | 1 | Phosphoserine Ref.32 | |||||||||||||||||
| Modified residue | 2159 | 1 | Phosphoserine; by autocatalysis Ref.43 | |||||||||||||||||
| Modified residue | 2164 | 1 | Phosphothreonine; by autocatalysis By similarity | |||||||||||||||||
| Modified residue | 2446 | 1 | Phosphothreonine; by autocatalysis Ref.22 | |||||||||||||||||
| Modified residue | 2478 | 1 | Phosphoserine Ref.29 | |||||||||||||||||
| Modified residue | 2481 | 1 | Phosphoserine Ref.29 | |||||||||||||||||
Natural variations | ||||||||||||||||||||
| Natural variant | 8 | 1 | A → S in a lung large cell carcinoma sample; somatic mutation. Ref.48 | VAR_041537 | ||||||||||||||||
| Natural variant | 135 | 1 | M → T in a metastatic melanoma sample; somatic mutation. Ref.48 | VAR_041538 | ||||||||||||||||
| Natural variant | 1083 | 1 | M → V. Ref.48 Corresponds to variant rs56164650 [ dbSNP | Ensembl ]. | VAR_041539 | ||||||||||||||||
| Natural variant | 1134 | 1 | A → V. Ref.48 Corresponds to variant rs28730685 [ dbSNP | Ensembl ]. | VAR_041540 | ||||||||||||||||
| Natural variant | 1178 | 1 | S → F. Ref.48 Corresponds to variant rs55975118 [ dbSNP | Ensembl ]. | VAR_041541 | ||||||||||||||||
| Natural variant | 2011 | 1 | M → V in an ovarian mucinous carcinoma sample; somatic mutation. Ref.48 | VAR_041542 | ||||||||||||||||
| Natural variant | 2215 | 1 | S → Y in a colorectal adenocarcinoma sample; somatic mutation. Ref.48 | VAR_041543 | ||||||||||||||||
| Natural variant | 2220 | 1 | L → F Found in a renal cell carcinoma sample; somatic mutation. Ref.49 | VAR_064733 | ||||||||||||||||
| Natural variant | 2406 | 1 | V → A Found in a renal cell carcinoma sample; somatic mutation. Ref.49 | VAR_064734 | ||||||||||||||||
| Natural variant | 2476 | 1 | P → L in a glioblastoma multiforme sample; somatic mutation. Ref.48 | VAR_041544 | ||||||||||||||||
Experimental info | ||||||||||||||||||||
| Sequence conflict | 353 | 1 | K → N in AAC39933. Ref.2 | |||||||||||||||||
| Sequence conflict | 359 | 1 | S → N in AAC39933. Ref.2 | |||||||||||||||||
| Sequence conflict | 364 | 1 | D → N in AAC39933. Ref.2 | |||||||||||||||||
| Sequence conflict | 390 | 1 | M → L in AAC39933. Ref.2 | |||||||||||||||||
| Sequence conflict | 430 | 1 | R → L in AAC39933. Ref.2 | |||||||||||||||||
| Sequence conflict | 455 – 457 | 3 | VLD → GVE in AAC39933. Ref.2 | |||||||||||||||||
| Sequence conflict | 461 | 1 | A → G in AAC39933. Ref.2 | |||||||||||||||||
| Sequence conflict | 482 – 484 | 3 | VFT → FFN in AAC39933. Ref.2 | |||||||||||||||||
| Sequence conflict | 489 | 1 | L → V in AAC39933. Ref.2 | |||||||||||||||||
| Sequence conflict | 513 | 1 | L → I in AAC39933. Ref.2 | |||||||||||||||||
| Sequence conflict | 539 | 1 | L → V in AAC39933. Ref.2 | |||||||||||||||||
| Sequence conflict | 553 | 1 | R → C in AAC39933. Ref.2 | |||||||||||||||||
| Sequence conflict | 857 | 1 | P → L in BAE06077. Ref.3 | |||||||||||||||||
| Sequence conflict | 1075 | 1 | I → S in AAC39933. Ref.2 | |||||||||||||||||
Secondary structure | ||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||
| Beta strand | 2017 – 2019 | 3 | ||||||||||||||||||
| Beta strand | 2020 – 2022 | 3 | ||||||||||||||||||
| Helix | 2025 – 2039 | 15 | ||||||||||||||||||
| Helix | 2044 – 2058 | 15 | ||||||||||||||||||
| Helix | 2065 – 2091 | 27 | ||||||||||||||||||
| Helix | 2094 – 2111 | 18 | ||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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. 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: AUTOPHOSPHORYLATION AT THR-2446. |
| [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, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [29] | "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2478 AND SER-2481, MASS SPECTROMETRY. 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] | "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567, MASS SPECTROMETRY. |
| [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, MASS SPECTROMETRY. |
| [35] | "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. |
| [36] | "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. |
| [37] | "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. |
| [38] | "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. |
| [39] | "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. |
| [40] | "mTORC1 directly phosphorylates and regulates human MAF1." Michels A.A., Robitaille A.M., Buczynski-Ruchonnet D., Hodroj W., Reina J.H., Hall M.N., Hernandez N. Mol. Cell. Biol. 30:3749-3757(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF RNA POLYMERASE III TRANSCRIPTION, FUNCTION IN PHOSPHORYLATION OF MAF1. |
| [41] | "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, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [42] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer 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]. |
| [43] | "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: AUTOPHOSPHORYLATION AT SER-2159. |
| [44] | "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]. |
| [45] | "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. |
| [46] | "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. |
| [47] | "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. |
| [48] | "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. 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. |
| [49] | "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma." Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M. Futreal P.A.Nature 469:539-542(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PHE-2220 AND ALA-2406. |
| + | Additional computationally mapped references. |
Web resources
| Atlas of Genetics and Cytogenetics in Oncology and Haematology |
| Wikipedia Mammalian target of rapamycin entry |
| Target mTOR mTOR signaling pathway and mTOR inhibition resource |
Cross-references
Sequence databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| EMBL GenBank DDBJ | 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. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| IPI | IPI00031410. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PIR | S45340. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| RefSeq | NP_004949.1. NM_004958.3. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| UniGene | Hs.338207. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| ProteinModelPortal | P42345. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| DIP | DIP-790N. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| IntAct | P42345. 31 interactions. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| MINT | MINT-121301. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| STRING | 9606.ENSP00000354558. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PTM databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PhosphoSite | P42345. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Polymorphism databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| DMDM | 1169735. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PaxDb | P42345. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PRIDE | P42345. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Ensembl | ENST00000361445; ENSP00000354558; ENSG00000198793. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| GeneID | 2475. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| KEGG | hsa:2475. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| UCSC | uc001asd.3. human. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| CTD | 2475. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| GeneCards | GC01M011166. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| HGNC | HGNC:3942. MTOR. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| HPA | CAB005057. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| MIM | 601231. gene. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| neXtProt | NX_P42345. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PharmGKB | PA28360. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| eggNOG | COG5032. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| HOGENOM | HOG000163215. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| HOVERGEN | HBG005744. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| InParanoid | P42345. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| KO | K07203. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| OMA | DPYKHKM. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| OrthoDB | EOG41RPT0. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Pathway_Interaction_DB | pi3kciaktpathway. Class I PI3K signaling events mediated by Akt. endothelinpathway. Endothelins. ifngpathway. IFN-gamma pathway. il12_2pathway. IL12-mediated signaling events. il2_pi3kpathway. IL2 signaling events mediated by PI3K. il4_2pathway. IL4-mediated signaling events. mtor_4pathway. mTOR signaling pathway. telomerasepathway. Regulation of Telomerase. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Reactome | REACT_111102. Signal Transduction. REACT_116125. Disease. REACT_6900. Immune System. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| ArrayExpress | P42345. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Bgee | P42345. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| CleanEx | HS_FRAP1. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Genevestigator | P42345. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| GermOnline | ENSG00000198793. Homo sapiens. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Gene3D | 1.10.1070.11. 3 hits. 1.25.10.10. 4 hits. 1.25.40.10. 2 hits. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| InterPro | 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. IPR026683. TOR/Smg1. IPR011990. TPR-like_helical. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PANTHER | PTHR11139:SF9. PTHR11139:SF9. 1 hit. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Pfam | 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] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| SMART | SM00146. PI3Kc. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| SUPFAM | SSF48371. ARM-type_fold. 2 hits. SSF47212. FRAP_FKBP12_bind. 1 hit. SSF56112. Kinase_like. 1 hit. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PROSITE | PS51189. FAT. 1 hit. PS51190. FATC. 1 hit. PS50077. HEAT_REPEAT. False negative. PS00915. PI3_4_KINASE_1. 1 hit. PS00916. PI3_4_KINASE_2. 1 hit. PS50290. PI3_4_KINASE_3. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Other | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| BindingDB | P42345. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| ChEMBL | CHEMBL2842. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| ChiTaRS | MTOR. human. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| EvolutionaryTrace | P42345. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| GenomeRNAi | 2475. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| NextBio | 9805. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Entry information
| Entry name | MTOR_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P42345 Secondary accession number(s): Q4LE76 Q9Y4I3 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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. | ||||||||
Relevant documents
| Human and mouse protein kinases Human and mouse protein kinases: classification and index |
| Human chromosome 1 Human chromosome 1: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
