Protein

Serine/threonine-protein kinase mTOR

Gene

MTOR

Organism

Homo sapiens (Human)

Status

Reviewed-Annotation score: -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 (PubMed:12087098, PubMed:12150925, PubMed:12150926, PubMed:12231510, PubMed:12718876, PubMed:14651849, PubMed:15268862, PubMed:15467718, PubMed:15545625, PubMed:15718470, PubMed:18497260, PubMed:18762023, PubMed:18925875, PubMed:20516213, PubMed:20537536, PubMed:21659604, PubMed:23429703, PubMed:23429704, PubMed:25799227, PubMed:26018084). 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) (PubMed:15268862, PubMed:15467718, PubMed:18925875, PubMed:18497260, PubMed:20516213, PubMed:21576368, PubMed:21659604, PubMed:23429704). Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis (PubMed:12087098, PubMed:12150925, PubMed:12150926, PubMed:12231510, PubMed:12718876, PubMed:14651849, PubMed:15268862, PubMed:15467718, PubMed:15545625, PubMed:15718470, PubMed:18497260, PubMed:18762023, PubMed:18925875, PubMed:20516213, PubMed:20537536, PubMed:21659604, PubMed:23429703, PubMed:23429704, PubMed:25799227, PubMed:26018084). This includes phosphorylation of EIF4EBP1 and release of its inhibition toward the elongation initiation factor 4E (eiF4E) (By similarity). 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 (PubMed:12150925, PubMed:12087098, PubMed:18925875). This also includes mTORC1 signaling cascade controlling the MiT/TFE factors TFEB and TFE3: in the presence of nutrients, mediates phosphorylation of TFEB and TFE3, promoting their cytosolic retention and inactivation (PubMed:22576015, PubMed:22343943, PubMed:22692423). Upon starvation or lysosomal stress, inhibition of mTORC1 induces dephosphorylation and nuclear translocation of TFEB and TFE3, promoting their transcription factor activity (PubMed:22576015, PubMed:22343943, PubMed:22692423). 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 (PubMed:23429704, PubMed:23429703). Regulates ribosome synthesis by activating RNA polymerase III-dependent transcription through phosphorylation and inhibition of MAF1 an RNA polymerase III-repressor (PubMed:20516213). In parallel to protein synthesis, also regulates lipid synthesis through SREBF1/SREBP1 and LPIN1 (By similarity). To maintain energy homeostasis mTORC1 may also regulate mitochondrial biogenesis through regulation of PPARGC1A (By similarity). mTORC1 also negatively regulates autophagy through phosphorylation of ULK1 (By similarity). Under nutrient sufficiency, phosphorylates ULK1 at 'Ser-758', disrupting the interaction with AMPK and preventing activation of ULK1 (By similarity). Also prevents autophagy through phosphorylation of the autophagy inhibitor DAP (PubMed:20537536). Also prevents autophagy by phosphorylating RUBCNL/Pacer under nutrient-rich conditions (PubMed:30704899). mTORC1 exerts a feedback control on upstream growth factor signaling that includes phosphorylation and activation of GRB10 a INSR-dependent signaling suppressor (PubMed:21659604). Among other potential targets mTORC1 may phosphorylate CLIP1 and regulate microtubules (PubMed:12231510). As part of the mTORC2 complex MTOR may regulate other cellular processes including survival and organization of the cytoskeleton (PubMed:15268862, PubMed:15467718). 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 (PubMed:15718470). 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 (PubMed:15268862). mTORC2 also regulates the phosphorylation of SGK1 at 'Ser-422' (PubMed:18925875). Regulates osteoclastogenesis by adjusting the expression of CEBPB isoforms (By similarity). Plays an important regulatory role in the circadian clock function; regulates period length and rhythm amplitude of the suprachiasmatic nucleus (SCN) and liver clocks (By similarity). Phosphorylates SQSTM1, promoting interaction between SQSTM1 and KEAP1 and subsequent inactivation of the BCR(KEAP1) complex (By similarity).By similarity25 Publications

Catalytic activityⁱ

Activity 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, SLC38A9, and the Rag GTPases RRAGA, RRAGB, RRAGC and RRAGD (PubMed:18497260, PubMed:20381137, PubMed:25561175, PubMed:25567906). 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.8 Publications

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Kinase, Serine/threonine-protein kinase, Transferase
Biological process	Biological rhythms
Ligand	ATP-binding, Nucleotide-binding

Enzyme and pathway databases

PathwayCommonsⁱ	P42345
Reactomeⁱ	R-HSA-1257604, PIP3 activates AKT signaling R-HSA-1632852, Macroautophagy R-HSA-165159, mTOR signalling R-HSA-166208, mTORC1-mediated signalling R-HSA-3371571, HSF1-dependent transactivation R-HSA-380972, Energy dependent regulation of mTOR by LKB1-AMPK R-HSA-389357, CD28 dependent PI3K/Akt signaling R-HSA-5218920, VEGFR2 mediated vascular permeability R-HSA-5628897, TP53 Regulates Metabolic Genes R-HSA-5674400, Constitutive Signaling by AKT1 E17K in Cancer R-HSA-6804757, Regulation of TP53 Degradation R-HSA-8943724, Regulation of PTEN gene transcription R-HSA-9639288, Amino acids regulate mTORC1
SABIO-RKⁱ	P42345
SignaLinkⁱ	P42345
SIGNORⁱ	P42345

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Serine/threonine-protein kinase mTOR (EC:2.7.11.17 Publications) 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
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 1

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000198793.12
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:3942, MTOR
MIMⁱ	601231, gene
neXtProtⁱ	NX_P42345

Keywords - Cellular componentⁱ

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

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Smith-Kingsmore syndrome (SKS)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal dominant syndrome characterized by intellectual disability, macrocephaly, seizures, umbilical hernia, and facial dysmorphic features.

Related information in OMIM

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_078832	1490	W → R in SKS. 1 Publication	1
Natural variantⁱVAR_078833	1595	M → I in SKS. 1 PublicationCorresponds to variant dbSNP:rs869312671EnsemblClinVar.	1
Natural variantⁱVAR_075072	1799	E → K in SKS; results in increased mTOR signaling. 2 PublicationsCorresponds to variant dbSNP:rs863225264EnsemblClinVar.	1
Natural variantⁱVAR_078835	1832	A → T in SKS. 1 PublicationCorresponds to variant dbSNP:rs369088781EnsemblClinVar.	1
Natural variantⁱVAR_078836	1888	F → C in SKS. 1 PublicationCorresponds to variant dbSNP:rs869312666EnsemblClinVar.	1
Natural variantⁱVAR_078840	2327	M → I in SKS. 1 PublicationCorresponds to variant dbSNP:rs878855328EnsemblClinVar.	1

Focal cortical dysplasia 2 (FCORD2)4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of focal cortical dysplasia, a malformation of cortical development that results in medically refractory epilepsy in the pediatric population and in adults. FCORD2 is a severe form, with onset usually in childhood, characterized by disrupted cortical lamination and specific cytological abnormalities. It is classified in 2 subtypes: type IIA characterized by dysmorphic neurons and lack of balloon cells; type IIB with dysmorphic neurons and balloon cells.

Related information in OMIM

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_078824	624	R → H in FCORD2; somatic mutation; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs913197212Ensembl.	1
Natural variantⁱVAR_078826	1450	Y → D in FCORD2; somatic mutation. 1 Publication	1
Natural variantⁱVAR_078827	1456	W → G in FCORD2; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1085307114EnsemblClinVar.	1
Natural variantⁱVAR_078828	1459	A → D in FCORD2; somatic mutation; increased TOR signaling. 1 Publication	1
Natural variantⁱVAR_078829	1459	A → S in FCORD2; somatic mutation. 1 Publication	1
Natural variantⁱVAR_078830	1460	L → P in FCORD2; somatic mutation; increased TOR signaling. 2 PublicationsCorresponds to variant dbSNP:rs1057519779EnsemblClinVar.	1
Natural variantⁱVAR_078831	1483	C → R in FCORD2; somatic mutation; increased TOR signaling; increased kinase activity. 1 PublicationCorresponds to variant dbSNP:rs1057519914EnsemblClinVar.	1
Natural variantⁱVAR_078834	1709	R → H in FCORD2; somatic mutation; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs587777895EnsemblClinVar.	1
Natural variantⁱVAR_078837	1977	T → K in FCORD2; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs587777893EnsemblClinVar.	1
Natural variantⁱVAR_078838	2193	R → C in FCORD2; somatic mutation. 1 Publication	1
Natural variantⁱVAR_078839	2215	S → F in FCORD2; somatic mutation; increased TOR signaling. 3 PublicationsCorresponds to variant dbSNP:rs587777894EnsemblClinVar.	1
Natural variantⁱVAR_041543	2215	S → Y in FCORD2; also found in a colorectal adenocarcinoma sample; somatic mutation; increased TOR signaling. 3 PublicationsCorresponds to variant dbSNP:rs587777894EnsemblClinVar.	1
Natural variantⁱVAR_078841	2427	L → P in FCORD2; somatic mutation; increased TOR signaling; increased kinase activity. 1 PublicationCorresponds to variant dbSNP:rs1085307113EnsemblClinVar.	1
Natural variantⁱVAR_078842	2427	L → Q in FCORD2; somatic mutation; increased TOR signaling; increased kinase activity. 1 PublicationCorresponds to variant dbSNP:rs1085307113EnsemblClinVar.	1

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	2159	S → A: Reduces mTORC1-associated S-2481 autophosphorylation; when associated with A-2164. 1 Publication	1
Mutagenesisⁱ	2159	S → D: Stronger phosphorylation of RPS6KB1; when associated with E-2164. 1 Publication	1
Mutagenesisⁱ	2164	T → A: Reduces mTORC1-associated S-2481 autophosphorylation; when associated with A-2159. 1 Publication	1
Mutagenesisⁱ	2164	T → E: Stronger phosphorylation of RPS6KB1; when associated with D-2159. 1 Publication	1
Mutagenesisⁱ	2173	T → A: Increased mTOR kinase activity. 1 Publication	1
Mutagenesisⁱ	2340	H → A: Barely detectable kinase activity. 1 Publication	1
Mutagenesisⁱ	2357	D → E: Kinase-dead mutant, loss of interaction with TM4SF5 and loss of lysosome membrane localization; when associated with I-2364. 1 Publication	1
Mutagenesisⁱ	2364	V → I: Kinase-dead mutant, loss of interaction with TM4SF5 and loss of lysosome membrane localization; when associated with E-2357. 1 Publication	1

Keywords - Diseaseⁱ

Disease mutation, Epilepsy, Mental retardation

Organism-specific databases

DisGeNET More...DisGeNETⁱ	2475
MalaCards human disease database More...MalaCardsⁱ	MTOR
MIMⁱ	607341, phenotype 616638, phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000198793
Orphanetⁱ	269001, Isolated focal cortical dysplasia type IIa 269008, Isolated focal cortical dysplasia type IIb 457485, Macrocephaly-intellectual disability-neurodevelopmental disorder-small thorax syndrome
PharmGKBⁱ	PA28360

Miscellaneous databases

Pharosⁱ	P42345, Tclin

Pharosⁱ

P42345, Tclin

Chemistry databases

ChEMBLⁱ	CHEMBL2842
Drug and drug target database More...DrugBankⁱ	DB01590, Everolimus DB12010, Fostamatinib DB00337, Pimecrolimus DB06233, Ridaforolimus DB04974, Rimiducid DB05210, SF1126 DB00877, Sirolimus DB06287, Temsirolimus DB05241, XL765
DrugCentral More...DrugCentralⁱ	P42345
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	2109

Polymorphism and mutation databases

BioMutaⁱ	MTOR
DMDMⁱ	1169735

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000088808	1 – 2549	Serine/threonine-protein kinase mTORAdd BLAST		2549

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	1	N-acetylmethionineCombined sources	1
Modified residueⁱ	567	PhosphoserineCombined sources	1
Modified residueⁱ	1162	PhosphothreonineCombined sources	1
Modified residueⁱ	1218	N6-acetyllysineCombined sources	1
Modified residueⁱ	1261	PhosphoserineCombined sources1 Publication	1
Modified residueⁱ	2159	Phosphoserine1 Publication	1
Modified residueⁱ	2164	Phosphothreonine1 Publication	1
Modified residueⁱ	2173	Phosphothreonine; by PKB/AKT11 Publication	1
Modified residueⁱ	2446	Phosphothreonine; by RPS6KB11 Publication	1
Modified residueⁱ	2448	Phosphoserine; by RPS6KB1Combined sources2 Publications	1
Modified residueⁱ	2478	PhosphoserineCombined sources	1
Modified residueⁱ	2481	Phosphoserine; by autocatalysisCombined sources1 Publication	1

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.7 Publications

Keywords - PTMⁱ

Acetylation, Phosphoprotein

Proteomic databases

The CPTAC Assay portal More...CPTACⁱ	CPTAC-1360 CPTAC-1361
EPDⁱ	P42345
jPOSTⁱ	P42345
MassIVEⁱ	P42345
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P42345
PaxDbⁱ	P42345
PeptideAtlas More...PeptideAtlasⁱ	P42345
PRIDEⁱ	P42345
ProteomicsDBⁱ	55511

PTM databases

iPTMnetⁱ	P42345
MetOSiteⁱ	P42345
PhosphoSitePlusⁱ	P42345
SwissPalmⁱ	P42345

Expressionⁱ

Tissue specificityⁱ

Gene expression databases

Bgeeⁱ	ENSG00000198793, Expressed in testis and 180 other tissues
ExpressionAtlasⁱ	P42345, baseline and differential
Genevisibleⁱ	P42345, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000198793, Low tissue specificity

HPAⁱ

ENSG00000198793, Low tissue specificity

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 subunit 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 PLPP7 and PML.

Interacts with PRR5 and RICTOR; the interaction is direct within the mTORC2 complex.

Interacts with WAC; WAC positively regulates MTOR activity by promoting the assembly of the TTT complex composed of TELO2, TTI1 and TTI2 and the RUVBL complex composed of RUVBL1 and RUVBL2 into the TTT-RUVBL complex which leads to the dimerization of the mTORC1 complex and its subsequent activation (PubMed:26812014).

Interacts with UBQLN1.

Interacts with TTI1 and TELO2.

Interacts with CLIP1; phosphorylates and regulates CLIP1.

Interacts with NBN.

Interacts with HTR6 (PubMed:23027611).

Interacts with BRAT1.

Interacts with MEAK7 (via C-terminal domain); the interaction increases upon nutrient stimulation (PubMed:29750193).

Interacts with TM4SF5; the interaction is positively regulated by arginine and is negatively regulated by leucine (PubMed:30956113).

Interacts with GPR137B (PubMed:31036939).

26 Publications

Binary interactionsⁱ

Hide details

P42345

With	#Exp.	IntAct
AKT1 [P31749]	4	EBI-359260,EBI-296087
BCL2L1 - isoform Bcl-X(L) [Q07817-1]	4	EBI-359260,EBI-287195
DEPTOR [Q8TB45]	5	EBI-359260,EBI-2359040
EIF4EBP1 [Q13541]	2	EBI-359260,EBI-74090
FKBP1A [P62942]	5	EBI-359260,EBI-1027571
GTF3C2 [Q8WUA4]	3	EBI-359260,EBI-1237062
MLST8 [Q9BVC4]	5	EBI-359260,EBI-1387471
MLST8 - isoform 1 [Q9BVC4-1]	7	EBI-359260,EBI-16056342
MTMR3 [Q13615]	3	EBI-359260,EBI-371938
itself	2	EBI-359260,EBI-359260
PREX1 [Q8TCU6]	11	EBI-359260,EBI-1046542
RAB1A [P62820]	4	EBI-359260,EBI-716845
RHEB [Q15382]	2	EBI-359260,EBI-1055287
RICTOR [Q6R327]	34	EBI-359260,EBI-1387196
RPTOR [Q8N122]	47	EBI-359260,EBI-1567928
SIRT1 [Q96EB6]	2	EBI-359260,EBI-1802965
TPCN2 [Q8NHX9]	2	EBI-359260,EBI-5239949
ULK1 [O75385]	7	EBI-359260,EBI-908831

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	108757, 245 interactors
ComplexPortalⁱ	CPX-4402, mTORC2 complex CPX-503, mTORC1 complex
CORUMⁱ	P42345
Database of interacting proteins More...DIPⁱ	DIP-790N
IntActⁱ	P42345, 102 interactors
Molecular INTeraction database More...MINTⁱ	P42345
STRINGⁱ	9606.ENSP00000354558

Chemistry databases

BindingDBⁱ	P42345

BindingDBⁱ

P42345

Miscellaneous databases

RNActⁱ	P42345, protein

RNActⁱ

P42345, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	1386 – 1406	Combined sources	21
Helixⁱ	1410 – 1421	Combined sources	12
Turnⁱ	1422 – 1424	Combined sources	3
Helixⁱ	1426 – 1439	Combined sources	14
Helixⁱ	1446 – 1452	Combined sources	7
Helixⁱ	1456 – 1469	Combined sources	14
Helixⁱ	1474 – 1487	Combined sources	14
Helixⁱ	1490 – 1498	Combined sources	9
Beta strandⁱ	1501 – 1503	Combined sources	3
Helixⁱ	1506 – 1523	Combined sources	18
Helixⁱ	1526 – 1535	Combined sources	10
Beta strandⁱ	1538 – 1540	Combined sources	3
Helixⁱ	1541 – 1553	Combined sources	13
Helixⁱ	1557 – 1577	Combined sources	21
Turnⁱ	1584 – 1586	Combined sources	3
Helixⁱ	1587 – 1605	Combined sources	19
Beta strandⁱ	1606 – 1608	Combined sources	3
Helixⁱ	1609 – 1611	Combined sources	3
Helixⁱ	1613 – 1624	Combined sources	12
Helixⁱ	1630 – 1640	Combined sources	11
Turnⁱ	1641 – 1643	Combined sources	3
Turnⁱ	1646 – 1648	Combined sources	3
Helixⁱ	1650 – 1663	Combined sources	14
Helixⁱ	1666 – 1677	Combined sources	12
Beta strandⁱ	1681 – 1684	Combined sources	4
Helixⁱ	1694 – 1706	Combined sources	13
Helixⁱ	1710 – 1729	Combined sources	20
Helixⁱ	1738 – 1761	Combined sources	24
Helixⁱ	1768 – 1782	Combined sources	15
Turnⁱ	1783 – 1785	Combined sources	3
Helixⁱ	1787 – 1813	Combined sources	27
Helixⁱ	1868 – 1893	Combined sources	26
Beta strandⁱ	1896 – 1898	Combined sources	3
Helixⁱ	1900 – 1913	Combined sources	14
Helixⁱ	1917 – 1929	Combined sources	13
Helixⁱ	1932 – 1938	Combined sources	7
Helixⁱ	1939 – 1943	Combined sources	5
Turnⁱ	1944 – 1947	Combined sources	4
Helixⁱ	1951 – 1966	Combined sources	16
Helixⁱ	1969 – 1971	Combined sources	3
Helixⁱ	1973 – 1980	Combined sources	8
Helixⁱ	1985 – 2020	Combined sources	36
Helixⁱ	2025 – 2039	Combined sources	15
Helixⁱ	2044 – 2058	Combined sources	15
Helixⁱ	2065 – 2091	Combined sources	27
Helixⁱ	2094 – 2111	Combined sources	18
Turnⁱ	2115 – 2117	Combined sources	3
Beta strandⁱ	2119 – 2122	Combined sources	4
Helixⁱ	2123 – 2126	Combined sources	4
Helixⁱ	2128 – 2132	Combined sources	5
Beta strandⁱ	2137 – 2139	Combined sources	3
Turnⁱ	2141 – 2143	Combined sources	3
Beta strandⁱ	2146 – 2148	Combined sources	3
Beta strandⁱ	2152 – 2156	Combined sources	5
Beta strandⁱ	2158 – 2162	Combined sources	5
Beta strandⁱ	2165 – 2167	Combined sources	3
Beta strandⁱ	2170 – 2176	Combined sources	7
Beta strandⁱ	2181 – 2189	Combined sources	9
Helixⁱ	2193 – 2211	Combined sources	19
Helixⁱ	2213 – 2217	Combined sources	5
Beta strandⁱ	2227 – 2229	Combined sources	3
Beta strandⁱ	2231 – 2233	Combined sources	3
Beta strandⁱ	2235 – 2238	Combined sources	4
Beta strandⁱ	2243 – 2245	Combined sources	3
Helixⁱ	2246 – 2256	Combined sources	11
Helixⁱ	2263 – 2271	Combined sources	9
Helixⁱ	2275 – 2277	Combined sources	3
Helixⁱ	2280 – 2292	Combined sources	13
Helixⁱ	2298 – 2306	Combined sources	9
Helixⁱ	2310 – 2334	Combined sources	25
Turnⁱ	2341 – 2343	Combined sources	3
Beta strandⁱ	2344 – 2347	Combined sources	4
Turnⁱ	2348 – 2350	Combined sources	3
Beta strandⁱ	2353 – 2355	Combined sources	3
Helixⁱ	2364 – 2367	Combined sources	4
Beta strandⁱ	2369 – 2371	Combined sources	3
Helixⁱ	2381 – 2386	Combined sources	6
Turnⁱ	2389 – 2394	Combined sources	6
Helixⁱ	2395 – 2409	Combined sources	15
Helixⁱ	2411 – 2422	Combined sources	12
Turnⁱ	2425 – 2428	Combined sources	4
Helixⁱ	2429 – 2432	Combined sources	4
Helixⁱ	2433 – 2435	Combined sources	3
Helixⁱ	2493 – 2509	Combined sources	17
Beta strandⁱ	2512 – 2516	Combined sources	5
Helixⁱ	2521 – 2533	Combined sources	13
Helixⁱ	2535 – 2540	Combined sources	6
Helixⁱ	2543 – 2545	Combined sources	3

Show more details

3D structure databases

BMRBⁱ	P42345
SMRⁱ	P42345
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P42345

EvolutionaryTraceⁱ

P42345

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Repeatⁱ	16 – 53	HEAT 1Add BLAST	38
Repeatⁱ	55 – 99	HEAT 2Add BLAST	45
Repeatⁱ	100 – 137	HEAT 3Add BLAST	38
Repeatⁱ	138 – 179	HEAT 4Add BLAST	42
Repeatⁱ	180 – 220	HEAT 5Add BLAST	41
Repeatⁱ	222 – 276	HEAT 6Add BLAST	55
Repeatⁱ	277 – 313	HEAT 7Add BLAST	37
Repeatⁱ	314 – 364	HEAT 8Add BLAST	51
Repeatⁱ	365 – 409	HEAT 9Add BLAST	45
Repeatⁱ	410 – 445	HEAT 10Add BLAST	36
Repeatⁱ	446 – 494	HEAT 11Add BLAST	49
Repeatⁱ	495 – 529	HEAT 12Add BLAST	35
Repeatⁱ	530 – 563	HEAT 13Add BLAST	34
Repeatⁱ	564 – 596	HEAT 14Add BLAST	33
Repeatⁱ	597 – 636	HEAT 15Add BLAST	40
Repeatⁱ	637 – 683	HEAT 16Add BLAST	47
Repeatⁱ	686 – 724	HEAT 17Add BLAST	39
Repeatⁱ	727 – 766	HEAT 18Add BLAST	40
Repeatⁱ	769 – 811	HEAT 19Add BLAST	43
Repeatⁱ	814 – 853	HEAT 20Add BLAST	40
Repeatⁱ	857 – 893	HEAT 21Add BLAST	37
Repeatⁱ	894 – 942	HEAT 22Add BLAST	49
Repeatⁱ	943 – 988	HEAT 23Add BLAST	46
Repeatⁱ	989 – 1027	HEAT 24Add BLAST	39
Repeatⁱ	1029 – 1068	HEAT 25Add BLAST	40
Repeatⁱ	1069 – 1105	HEAT 26Add BLAST	37
Repeatⁱ	1106 – 1144	HEAT 27Add BLAST	39
Repeatⁱ	1145 – 1188	HEAT 28Add BLAST	44
Repeatⁱ	1189 – 1225	HEAT 29Add BLAST	37
Repeatⁱ	1226 – 1273	HEAT 30Add BLAST	48
Repeatⁱ	1274 – 1311	HEAT 31Add BLAST	38
Repeatⁱ	1312 – 1345	HEAT 32Add BLAST	34
Repeatⁱ	1346 – 1382	TPR 1Add BLAST	37
Domainⁱ	1382 – 1982	FATPROSITE-ProRule annotationAdd BLAST	601
Repeatⁱ	1383 – 1408	TPR 2Add BLAST	26
Repeatⁱ	1409 – 1442	TPR 3Add BLAST	34
Repeatⁱ	1443 – 1473	TPR 4Add BLAST	31
Repeatⁱ	1474 – 1507	TPR 5Add BLAST	34
Repeatⁱ	1508 – 1541	TPR 6Add BLAST	34
Repeatⁱ	1542 – 1574	TPR 7Add BLAST	33
Repeatⁱ	1575 – 1614	TPR 8Add BLAST	40
Repeatⁱ	1615 – 1649	TPR 9Add BLAST	35
Repeatⁱ	1650 – 1693	TPR 10Add BLAST	44
Repeatⁱ	1694 – 1731	TPR 11Add BLAST	38
Repeatⁱ	1732 – 1786	TPR 12Add BLAST	55
Repeatⁱ	1787 – 1846	TPR 13Add BLAST	60
Repeatⁱ	1898 – 1930	TPR 14Add BLAST	33
Repeatⁱ	1931 – 1970	TPR 15Add BLAST	40
Repeatⁱ	1971 – 2005	TPR 16Add BLAST	35
Domainⁱ	2182 – 2516	PI3K/PI4KPROSITE-ProRule annotationAdd BLAST	335
Domainⁱ	2517 – 2549	FATCPROSITE-ProRule annotationAdd BLAST	33

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	1 – 651	Interaction with NBN1 PublicationAdd BLAST	651
Regionⁱ	2012 – 2144	Sufficient for interaction with the FKBP1A/rapamycin complexBy similarityAdd BLAST	133
Regionⁱ	2258 – 2296	Interaction with MLST8Add BLAST	39

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

Keywords - Domainⁱ

Repeat, TPR repeat

Phylogenomic databases

eggNOGⁱ	KOG0891, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00930000151037
HOGENOMⁱ	CLU_000178_7_1_1
InParanoidⁱ	P42345
KEGG Orthology (KO) More...KOⁱ	K07203
OMAⁱ	LNIQRYP
Database of Orthologous Groups More...OrthoDBⁱ	26975at2759
PhylomeDBⁱ	P42345
TreeFamⁱ	TF105134

Family and domain databases

Gene3Dⁱ	1.10.1070.11, 1 hit 1.20.120.150, 1 hit 1.25.10.10, 4 hits 1.25.40.10, 1 hit
IDEALⁱ	IID00598
InterProⁱ	View protein in InterPro IPR011989, ARM-like IPR016024, ARM-type_fold IPR024585, DUF3385_TOR IPR003152, FATC_dom IPR009076, FRB_dom IPR036738, FRB_sf IPR011009, Kinase-like_dom_sf IPR000403, PI3/4_kinase_cat_dom IPR036940, PI3/4_kinase_cat_sf IPR018936, PI3/4_kinase_CS IPR003151, PIK-rel_kinase_FAT IPR014009, PIK_FAT IPR026683, TOR IPR011990, TPR-like_helical_dom_sf
PANTHERⁱ	PTHR11139:SF9, PTHR11139:SF9, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF11865, DUF3385, 1 hit PF02259, FAT, 1 hit PF02260, FATC, 1 hit PF08771, FRB_dom, 1 hit PF00454, PI3_PI4_kinase, 1 hit
SMARTⁱ	View protein in SMART SM01346, DUF3385, 1 hit SM01343, FATC, 1 hit SM00146, PI3Kc, 1 hit
SUPFAMⁱ	SSF47212, SSF47212, 1 hit SSF48371, SSF48371, 2 hits SSF56112, SSF56112, 1 hit
PROSITEⁱ	View protein in PROSITE 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

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show all Align All

P42345-1 [UniParc]FASTA Add to basket

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        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

Computationally mapped potential isoform sequencesⁱ

There are 2 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

B1AKP8	B1AKP8_HUMAN	Non-specific serine/threonine prote... Non-specific serine/threonine protein kinase, EC 2.7.11.1	MTOR	754	Annotation score:
B1AKQ2	B1AKQ2_HUMAN	Serine/threonine-protein kinase mTO... Serine/threonine-protein kinase mTOR	MTOR	161	Annotation score:

Sequence cautionⁱ

The sequence AAC39933 differs from that shown. Reason: Frameshift.Curated

The sequence BAE06077 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	353	K → N in AAC39933 (PubMed:9653645).Curated	1
Sequence conflictⁱ	359	S → N in AAC39933 (PubMed:9653645).Curated	1
Sequence conflictⁱ	364	D → N in AAC39933 (PubMed:9653645).Curated	1
Sequence conflictⁱ	390	M → L in AAC39933 (PubMed:9653645).Curated	1
Sequence conflictⁱ	430	R → L in AAC39933 (PubMed:9653645).Curated	1
Sequence conflictⁱ	455 – 457	VLD → GVE in AAC39933 (PubMed:9653645).Curated	3
Sequence conflictⁱ	461	A → G in AAC39933 (PubMed:9653645).Curated	1
Sequence conflictⁱ	482 – 484	VFT → FFN in AAC39933 (PubMed:9653645).Curated	3
Sequence conflictⁱ	489	L → V in AAC39933 (PubMed:9653645).Curated	1
Sequence conflictⁱ	513	L → I in AAC39933 (PubMed:9653645).Curated	1
Sequence conflictⁱ	539	L → V in AAC39933 (PubMed:9653645).Curated	1
Sequence conflictⁱ	553	R → C in AAC39933 (PubMed:9653645).Curated	1
Sequence conflictⁱ	857	P → L in BAE06077 (Ref. 3) Curated	1
Sequence conflictⁱ	1075	I → S in AAC39933 (PubMed:9653645).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_041537	8	A → S in a lung large cell carcinoma sample; somatic mutation. 1 Publication	1
Natural variantⁱVAR_041538	135	M → T in a metastatic melanoma sample; somatic mutation. 1 Publication	1
Natural variantⁱVAR_078824	624	R → H in FCORD2; somatic mutation; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs913197212Ensembl.	1
Natural variantⁱVAR_041539	1083	M → V1 PublicationCorresponds to variant dbSNP:rs56164650EnsemblClinVar.	1
Natural variantⁱVAR_041540	1134	A → V1 PublicationCorresponds to variant dbSNP:rs28730685EnsemblClinVar.	1
Natural variantⁱVAR_041541	1178	S → F1 PublicationCorresponds to variant dbSNP:rs55975118

UniProtKB

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UniProtKB - P42345 (MTOR_HUMAN)

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Serine/threonine-protein kinase mTOR

MTOR

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Endoplasmic reticulum

Nucleus

Lysosome

Mitochondrion

Golgi apparatus

Other locations

Cytosol

Endoplasmic reticulum

Golgi apparatus

Lysosome

Mitochondrion

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Keywords - Diseasei

Organism-specific databases

Miscellaneous databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

P42345

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Natural variant

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ