Pimecrolimus 1% cream
Prescription only
Requires a prescription from a doctor or prescriber
Pimecrolimus is an immunomodulating agent that was first marketed by Novartis under the trade name Elidel.
Active ingredients:
Pimecrolimus
No active safety alerts
Official documents, adverse reaction reporting, and safety monitoring
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Official medicine documents
Source: MHRA Products DatabaseOGL 3.0
Updated 3 months ago(16 Jan 2026)Safety monitoring data
Yellow Card reports
MHRA
The MHRA Yellow Card scheme collects reports of suspected side effects from healthcare professionals and patients. View the Drug Analysis Profile (iDAP) for real-world adverse reaction data.
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Suspected adverse reactions reported for Pimecrolimus
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Submit a Yellow Card report to the MHRA
Data from the MHRA Yellow Card scheme. A reported reaction does not necessarily mean the medicine caused it. Contains public sector information licensed under the Open Government Licence v3.0.
EudraVigilance
EMA
The European Medicines Agency (EMA) collects suspected adverse reaction reports from across the EU/EEA through the EudraVigilance system. Search for safety data on this medicine.
View EudraVigilance report
Suspected adverse reactions reported for Pimecrolimus
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Learn about EU pharmacovigilance and safety monitoring
EudraVigilance data is published by the European Medicines Agency (EMA). A suspected adverse reaction is not necessarily caused by the medicine.
2 branded products available
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2 products
MHRA licensed products
View all licensed products for Pimecrolimus on the MHRA register
Elidel 1% cream
Show details
£19.69indicative price
This is the NHS Drug Tariff indicative price used for reimbursement purposes. It may not reflect the price paid by patients or pharmacies.
View full Drug TariffSource: NHS Drug Tariff via NHSBSA. Derived from dm+d VMPP (Virtual Medicinal Product Pack) pricing data. Contains public sector information licensed under the Open Government Licence v3.0.
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Similarity based on WHO Anatomical Therapeutic Chemical (ATC) classification and NHS BNF section grouping. Source data: NHS dm+d via TRUD (OGL v3.0), WHO ATC/DDD Index.
NHS prescribing volume and spending trends
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Clinical guidelines and formulary information
British National Formulary
Pimecrolimus
BNF
Drug monograph — bnf.nice.org.ukSource: British National Formulary, NICE. Joint Formulary Committee. Contains public sector information licensed under the Open Government Licence v3.0.
NICE clinical guidance(3)
Tacrolimus and pimecrolimus for atopic eczema (TA82)
TA82
Technology appraisal
Updated Aug 2004Atopic eczema in under 12s: diagnosis and management (CG57)
CG57
Clinical guideline
Updated Sept 2025Secondary bacterial infection of eczema and other common skin conditions: antimicrobial prescribing (NG190)
NG190
Guidance
Updated Mar 2021Source: National Institute for Health and Care Excellence (NICE). Contains public sector information licensed under the Open Government Licence v3.0.
Check stock at pharmacies and supply information
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Supply & product information
Official product databases and supply status monitoring
Pharmacy links redirect to the retailer's own search and do not represent real-time stock levels. emc (electronic medicines compendium) is operated by Datapharm Ltd. Shortage information sourced from NHS Specialist Pharmacy Service (SPS), sps.nhs.uk.
Codes for healthcare professionals and prescribing systems
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These codes are used by healthcare IT systems and prescribers to identify this medicine.
NHS UK identifiers
Browse tools
SNOMED CT and dm+d codes from NHS TRUD (Technology Reference data Update Distribution), licensed under the Open Government Licence v3.0. BNF codes from NHS Business Services Authority (NHSBSA). ATC codes from the WHO Collaborating Centre for Drug Statistics Methodology (whocc.no).
Active and completed clinical studies from ClinicalTrials.gov
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Searching UK clinical trials...
Source: ClinicalTrials.gov, a database of the U.S. National Library of Medicine (NLM), National Institutes of Health (NIH). Data accessed via ClinicalTrials.gov API v2. Trial information is provided for research purposes and does not constitute medical advice.
Pharmacology and chemical data from DrugBank
Key facts
Drug status
Approved
Major interactions
None known
Half-life
Not available
Mechanism
Pimecrolimus binds with high affinity to macrophilin-12 (FKBP-12) and inhibits t…
Food interactions
None known
Human targets
3 targets
Data: DrugBank · CC BY-NC 4.0
Pharmacokinetics at a glance
Absorption
Because of the low systemic absorption of pimecrolimus following topical application the calculation of standard pharmacokinetic measures such as AUC, Cmax, half-life, etc.…
Protein binding
74%
74%-87% (in vitro, bound to plasma proteins)
Metabolism
No drug metabolism was observed in human skin in vitro. Oral administration yielded metabolites produced from O-demethylation and oxygenation reactions.…
Elimination
80%
80% of the drug is excreted in the feces.
Pharmacokinetic data: DrugBank · CC BY-NC 4.0
Status:
Approved
Investigational
Small molecule
About this compound
Pimecrolimus is an immunomodulating agent that was first marketed by Novartis under the trade name Elidel. It is now promoted in Canada by Galderma since early 2007. It is currently available as a topic cream used in the treatment of atopic dermatitis (eczema).
Properties:
View FDA drug labelsolid
Avg. mass: 810.46 Da
DrugBank indication
For treatment of mild to moderate atopic dermatitis.
Also known as(52)
33-Epi-chloro-33-desoxyascomycin
Pimecrolimus
Pimecrolimusum
2.7.11.1
FK506-binding protein 12-rapamycin complex-associated protein 1
FKBP12-rapamycin complex-associated protein
FRAP
FRAP1
Dosage forms(12)
Cream (Cutaneous) — 1.000 g
Cream (Cutaneous) — 1 mg/g
Cream (Topical) — 1 % w/w
Cream (Topical) — 1 %
Cream (Topical) — 1.000 g
Cream (Topical) — 10 mg/1g
Cream (Cutaneous)
Cream (Cutaneous) — 1 %w/w
Molecular properties(19)
Drug interactions(312)
Known interactions with other medications. Always consult a healthcare professional.
Etanercept
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Etanercept.
Peginterferon alfa-2a
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Peginterferon alfa-2a.
Interferon alfa-n1
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Interferon alfa-n1.
Interferon alfa-n3
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Interferon alfa-n3.
Peginterferon alfa-2b
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Peginterferon alfa-2b.
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Anakinra.
Interferon gamma-1b
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Interferon gamma-1b.
Interferon alfa-2a
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Interferon alfa-2a.
Aldesleukin
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Aldesleukin.
Adalimumab
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Adalimumab.
Gemtuzumab ozogamicin
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Gemtuzumab ozogamicin.
Pegaspargase
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Pegaspargase.
Infliximab
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Infliximab.
Interferon beta-1b
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Interferon beta-1b.
Interferon alfacon-1
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Interferon alfacon-1.
Trastuzumab
Unknown severity
The risk or severity of neutropenia can be increased when Trastuzumab is combined with Pimecrolimus.
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Rituximab.
Basiliximab
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Basiliximab.
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Muromonab.
Ibritumomab tiuxetan
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Ibritumomab tiuxetan.
Tositumomab
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Tositumomab.
Alemtuzumab
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Alemtuzumab.
Cyclosporine
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Cyclosporine.
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Alefacept.
Efalizumab
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Efalizumab.
Antithymocyte immunoglobulin (rabbit)
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Antithymocyte immunoglobulin (rabbit).
Interferon alfa-2b
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Interferon alfa-2b.
Natalizumab
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Natalizumab.
Daclizumab
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Daclizumab.
Phenylalanine
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Phenylalanine.
Flunisolide
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Flunisolide.
Bortezomib
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Bortezomib.
Cladribine
Moderate
Pimecrolimus may increase the immunosuppressive activities of Cladribine.
Carmustine
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Carmustine.
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Amsacrine.
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Bleomycin.
Chlorambucil
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Chlorambucil.
Raltitrexed
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Raltitrexed.
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Mitomycin.
Bexarotene
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Bexarotene.
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Vindesine.
Floxuridine
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Floxuridine.
Indomethacin
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Indomethacin.
Tioguanine
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Tioguanine.
Vinorelbine
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Vinorelbine.
Dexrazoxane
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Dexrazoxane.
Beclomethasone dipropionate
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Beclomethasone dipropionate.
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Sorafenib.
Streptozocin
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Streptozocin.
Trifluridine
Unknown severity
The risk or severity of adverse effects can be increased when Pimecrolimus is combined with Trifluridine.
Showing 50 of 312 interactions
Toxicity & overdose
Side effects include burning sensation, irritation, pruritus, erythema, and skin infections, at the application site.
How it works
Mechanism of action
Pimecrolimus binds with high affinity to macrophilin-12 (FKBP-12) and inhibits the calcium-dependent phosphatase, calcineurin. As a consequence, it inhibits T cell activation by blocking the transcription of early cytokines. In particular, pimecrolimus inhibits at nanomolar concentrations Interleukin-2 and interferon gamma (Th1-type) and Interleukin-4 and Interleukin-10 (Th2-type) cytokine synthesis in human T cells. Also, pimecrolimus prevents the release of inflammatory cytokines and mediators from mast cells in vitro after stimulation by antigen/lgE.
Pharmacodynamics
Pimecrolimus is a chemical that is used to treat atopic dermatitis (eczema). Atopic dermatitis is a skin condition characterized by redness, itching, scaling and inflammation of the skin. The cause of atopic dermatitis is not known; however, scientists believe that it may be due to activation of the immune system by various environmental or emotional triggers. Scientists do not know exactly how pimecrolimus reduces the manifestations of atopic dermatitis, but pimecrolimus reduces the action of T-cells and mast cells which are part of the immune system and contribute to responses of the immune system. Pimecrolimus prevents the activation of T-cells by blocking the effects of chemicals (cytokines) released by the body that stimulate T-cells. Pimecrolimus also reduces the ability of mast cells to release chemicals that promote inflammation.
Pharmacokinetics
How the body processes this drug — absorption, distribution, metabolism, and elimination
Absorption
Because of the low systemic absorption of pimecrolimus following topical application the calculation of standard pharmacokinetic measures such as AUC, Cmax, half-life, etc. cannot be reliably done.
Protein binding
74%-87% (in vitro, bound to plasma proteins)
Metabolism
No drug metabolism was observed in human skin in vitro. Oral administration yielded metabolites produced from O-demethylation and oxygenation reactions.
Route of elimination
80% of the drug is excreted in the feces.
Drug targets(3)
Proteins and enzymes this drug interacts with in the body
Serine/threonine-protein kinase mTOR
MTOR
potentiator
Specific functionATP binding
Cellular location
Lysosome membrane
General function & pharmacology
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 .
PMID:12087098 PMID:12150925 PMID:12150926 PMID:12231510 PMID:12718876 PMID:14651849 PMID:15268862 PMID:15467718 PMID:15545625 PMID:15718470 PMID:18497260 PMID:18762023 PMID:18925875 PMID:20516213 PMID:20537536 PMID:21659604 PMID:23429703 PMID:23429704 PMID:25799227 PMID:26018084 PMID:29150432 PMID:29236692 PMID:31112131 PMID:31601708 PMID:32561715 PMID:34519269 PMID:37751742
MTOR directly or indirectly regulates the phosphorylation of at least 800 proteins .
PMID:15268862 PMID:15467718 PMID:17517883 PMID:18372248 PMID:18497260 PMID:18925875 PMID:20516213 PMID:21576368 PMID:21659604 PMID:23429704 PMID:30171069 PMID:29236692 PMID:37751742
Functions as part of 2 structurally and functionally distinct signaling complexes mTORC1 and mTORC2 (mTOR complex 1 and 2) .
PMID:15268862 PMID:15467718 PMID:18497260 PMID:18925875 PMID:20516213 PMID:21576368 PMID:21659604 PMID:23429704 PMID:29424687 PMID:29567957 PMID:35926713
In response to nutrients, growth factors or amino acids, mTORC1 is recruited to the lysosome membrane and promotes protein, lipid and nucleotide synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis .
PMID:12087098 PMID:12150925 PMID:12150926 PMID:12231510 PMID:12718876 PMID:14651849 PMID:15268862 PMID:15467718 PMID:15545625 PMID:15718470 PMID:18497260 PMID:18762023 PMID:18925875 PMID:20516213 PMID:20537536 PMID:21659604 PMID:23429703 PMID:23429704 PMID:25799227 PMID:26018084 PMID:29150432 PMID:29236692 PMID:31112131 PMID:34519269
This includes phosphorylation of EIF4EBP1 and release of its inhibition toward the elongation initiation factor 4E (eiF4E) .
PMID:24403073 PMID:29236692
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 .
PMID:12087098 PMID:12150925 PMID:18925875 PMID:29150432 PMID:29236692
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 .
PMID:23429703 PMID:23429704
Regulates ribosome synthesis by activating RNA polymerase III-dependent transcription through phosphorylation and inhibition of MAF1 an RNA polymerase III-repressor .
PMID:20516213
Activates dormant ribosomes by mediating phosphorylation of SERBP1, leading to SERBP1 inactivation and reactivation of translation .
PMID:36691768
In parallel to protein synthesis, also regulates lipid synthesis through SREBF1/SREBP1 and LPIN1 .
PMID:23426360
To maintain energy homeostasis mTORC1 may also regulate mitochondrial biogenesis through regulation of PPARGC1A (By similarity). In the same time, mTORC1 inhibits catabolic pathways: negatively regulates autophagy through phosphorylation of ULK1 .
PMID:32561715
Under nutrient sufficiency, phosphorylates ULK1 at 'Ser-758', disrupting the interaction with AMPK and preventing activation of ULK1 .
PMID:32561715
Also prevents autophagy through phosphorylation of the autophagy inhibitor DAP .
PMID:20537536
Also prevents autophagy by phosphorylating RUBCNL/Pacer under nutrient-rich conditions .
PMID:30704899
Prevents autophagy by mediating phosphorylation of AMBRA1, thereby inhibiting AMBRA1 ability to mediate ubiquitination of ULK1 and interaction between AMBRA1 and PPP2CA .
PMID:23524951 PMID:25438055
mTORC1 exerts a feedback control on upstream growth factor signaling that includes phosphorylation and activation of GRB10 a INSR-dependent signaling suppressor .
PMID:21659604
Among other potential targets mTORC1 may phosphorylate CLIP1 and regulate microtubules .
PMID:12231510
The mTORC1 complex is inhibited in response to starvation and amino acid depletion .
PMID:12150925 PMID:12150926 PMID:24403073 PMID:31695197
The non-canonical mTORC1 complex, which acts independently of RHEB, specifically mediates phosphorylation of MiT/TFE factors MITF, TFEB and TFE3 in the presence of nutrients, promoting their cytosolic retention and inactivation .
PMID:22343943 PMID:22576015 PMID:22692423 PMID:24448649 PMID:32612235 PMID:36608670 PMID:36697823
Upon starvation or lysosomal stress, inhibition of mTORC1 induces dephosphorylation and nuclear translocation of TFEB and TFE3, promoting their transcription factor activity .
PMID:22343943 PMID:22576015 PMID:22692423 PMID:24448649 PMID:32612235 PMID:36608670
The mTORC1 complex regulates pyroptosis in macrophages by promoting GSDMD oligomerization .
PMID:34289345
MTOR phosphorylates RPTOR which in turn inhibits mTORC1 (By similarity). As part of the mTORC2 complex, MTOR transduces signals from growth factors to pathways involved in proliferation, cytoskeletal organization, lipogenesis and anabolic output .
PMID:15268862 PMID:15467718 PMID:24670654 PMID:29424687 PMID:29567957 PMID:35926713
In response to growth factors, mTORC2 phosphorylates and activates AGC protein kinase family members, including AKT (AKT1, AKT2 and AKT3), PKC (PRKCA, PRKCB and PRKCE) and SGK1 .
PMID:15268862 PMID:15467718 PMID:21376236 PMID:24670654 PMID:29424687 PMID:29567957 PMID:35926713
In contrast to mTORC1, mTORC2 is nutrient-insensitive .
PMID:15467718
mTORC2 plays a critical role in AKT1 activation by mediating phosphorylation of different sites depending on the context, such as 'Thr-450', 'Ser-473', 'Ser-477' or 'Thr-479', facilitating the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDPK1/PDK1 which is a prerequisite for full activation .
PMID:15718470 PMID:21376236 PMID:24670654 PMID:29424687 PMID:29567957
mTORC2 also regulates the phosphorylation of SGK1 at 'Ser-422' .
PMID:18925875
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 .
PMID:15268862
The mTORC2 complex also phosphorylates various proteins involved in insulin signaling, such as FBXW8 and IGF2BP1 (By similarity).
May also regulate insulin signaling by acting as a tyrosine protein kinase that catalyzes phosphorylation of IGF1R and INSR; additional evidence are however required to confirm this result in vivo .
PMID:26584640
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)
PMID:12087098 PMID:12150925 PMID:12150926 PMID:12231510 PMID:12718876 PMID:14651849 PMID:15268862 PMID:15467718 PMID:15545625 PMID:15718470 PMID:18497260 PMID:18762023 PMID:18925875 PMID:20516213 PMID:20537536 PMID:21659604 PMID:23429703 PMID:23429704 PMID:25799227 PMID:26018084 PMID:29150432 PMID:29236692 PMID:31112131 PMID:31601708 PMID:32561715 PMID:34519269 PMID:37751742
MTOR directly or indirectly regulates the phosphorylation of at least 800 proteins .
PMID:15268862 PMID:15467718 PMID:17517883 PMID:18372248 PMID:18497260 PMID:18925875 PMID:20516213 PMID:21576368 PMID:21659604 PMID:23429704 PMID:30171069 PMID:29236692 PMID:37751742
Functions as part of 2 structurally and functionally distinct signaling complexes mTORC1 and mTORC2 (mTOR complex 1 and 2) .
PMID:15268862 PMID:15467718 PMID:18497260 PMID:18925875 PMID:20516213 PMID:21576368 PMID:21659604 PMID:23429704 PMID:29424687 PMID:29567957 PMID:35926713
In response to nutrients, growth factors or amino acids, mTORC1 is recruited to the lysosome membrane and promotes protein, lipid and nucleotide synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis .
PMID:12087098 PMID:12150925 PMID:12150926 PMID:12231510 PMID:12718876 PMID:14651849 PMID:15268862 PMID:15467718 PMID:15545625 PMID:15718470 PMID:18497260 PMID:18762023 PMID:18925875 PMID:20516213 PMID:20537536 PMID:21659604 PMID:23429703 PMID:23429704 PMID:25799227 PMID:26018084 PMID:29150432 PMID:29236692 PMID:31112131 PMID:34519269
This includes phosphorylation of EIF4EBP1 and release of its inhibition toward the elongation initiation factor 4E (eiF4E) .
PMID:24403073 PMID:29236692
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 .
PMID:12087098 PMID:12150925 PMID:18925875 PMID:29150432 PMID:29236692
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 .
PMID:23429703 PMID:23429704
Regulates ribosome synthesis by activating RNA polymerase III-dependent transcription through phosphorylation and inhibition of MAF1 an RNA polymerase III-repressor .
PMID:20516213
Activates dormant ribosomes by mediating phosphorylation of SERBP1, leading to SERBP1 inactivation and reactivation of translation .
PMID:36691768
In parallel to protein synthesis, also regulates lipid synthesis through SREBF1/SREBP1 and LPIN1 .
PMID:23426360
To maintain energy homeostasis mTORC1 may also regulate mitochondrial biogenesis through regulation of PPARGC1A (By similarity). In the same time, mTORC1 inhibits catabolic pathways: negatively regulates autophagy through phosphorylation of ULK1 .
PMID:32561715
Under nutrient sufficiency, phosphorylates ULK1 at 'Ser-758', disrupting the interaction with AMPK and preventing activation of ULK1 .
PMID:32561715
Also prevents autophagy through phosphorylation of the autophagy inhibitor DAP .
PMID:20537536
Also prevents autophagy by phosphorylating RUBCNL/Pacer under nutrient-rich conditions .
PMID:30704899
Prevents autophagy by mediating phosphorylation of AMBRA1, thereby inhibiting AMBRA1 ability to mediate ubiquitination of ULK1 and interaction between AMBRA1 and PPP2CA .
PMID:23524951 PMID:25438055
mTORC1 exerts a feedback control on upstream growth factor signaling that includes phosphorylation and activation of GRB10 a INSR-dependent signaling suppressor .
PMID:21659604
Among other potential targets mTORC1 may phosphorylate CLIP1 and regulate microtubules .
PMID:12231510
The mTORC1 complex is inhibited in response to starvation and amino acid depletion .
PMID:12150925 PMID:12150926 PMID:24403073 PMID:31695197
The non-canonical mTORC1 complex, which acts independently of RHEB, specifically mediates phosphorylation of MiT/TFE factors MITF, TFEB and TFE3 in the presence of nutrients, promoting their cytosolic retention and inactivation .
PMID:22343943 PMID:22576015 PMID:22692423 PMID:24448649 PMID:32612235 PMID:36608670 PMID:36697823
Upon starvation or lysosomal stress, inhibition of mTORC1 induces dephosphorylation and nuclear translocation of TFEB and TFE3, promoting their transcription factor activity .
PMID:22343943 PMID:22576015 PMID:22692423 PMID:24448649 PMID:32612235 PMID:36608670
The mTORC1 complex regulates pyroptosis in macrophages by promoting GSDMD oligomerization .
PMID:34289345
MTOR phosphorylates RPTOR which in turn inhibits mTORC1 (By similarity). As part of the mTORC2 complex, MTOR transduces signals from growth factors to pathways involved in proliferation, cytoskeletal organization, lipogenesis and anabolic output .
PMID:15268862 PMID:15467718 PMID:24670654 PMID:29424687 PMID:29567957 PMID:35926713
In response to growth factors, mTORC2 phosphorylates and activates AGC protein kinase family members, including AKT (AKT1, AKT2 and AKT3), PKC (PRKCA, PRKCB and PRKCE) and SGK1 .
PMID:15268862 PMID:15467718 PMID:21376236 PMID:24670654 PMID:29424687 PMID:29567957 PMID:35926713
In contrast to mTORC1, mTORC2 is nutrient-insensitive .
PMID:15467718
mTORC2 plays a critical role in AKT1 activation by mediating phosphorylation of different sites depending on the context, such as 'Thr-450', 'Ser-473', 'Ser-477' or 'Thr-479', facilitating the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDPK1/PDK1 which is a prerequisite for full activation .
PMID:15718470 PMID:21376236 PMID:24670654 PMID:29424687 PMID:29567957
mTORC2 also regulates the phosphorylation of SGK1 at 'Ser-422' .
PMID:18925875
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 .
PMID:15268862
The mTORC2 complex also phosphorylates various proteins involved in insulin signaling, such as FBXW8 and IGF2BP1 (By similarity).
May also regulate insulin signaling by acting as a tyrosine protein kinase that catalyzes phosphorylation of IGF1R and INSR; additional evidence are however required to confirm this result in vivo .
PMID:26584640
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)
Protein phosphatase 3 catalytic subunit alpha
PPP3CA
inhibitor
Specific functionATPase binding
Cellular location
Cytoplasm
General function & pharmacology
Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals .
PMID:15671020 PMID:18838687 PMID:19154138 PMID:23468591 PMID:30254215
Many of the substrates contain a PxIxIT motif and/or a LxVP motif .
PMID:17498738 PMID:17502104 PMID:22343722 PMID:23468591 PMID:27974827
In response to increased Ca(2+) levels, dephosphorylates and activates phosphatase SSH1 which results in cofilin dephosphorylation .
PMID:15671020
In response to increased Ca(2+) levels following mitochondrial depolarization, dephosphorylates DNM1L inducing DNM1L translocation to the mitochondrion .
PMID:18838687
Positively regulates the CACNA1B/CAV2.2-mediated Ca(2+) release probability at hippocampal neuronal soma and synaptic terminals (By similarity). Dephosphorylates heat shock protein HSPB1 (By similarity). Dephosphorylates and activates transcription factor NFATC1 .
PMID:19154138
In response to increased Ca(2+) levels, regulates NFAT-mediated transcription probably by dephosphorylating NFAT and promoting its nuclear translocation .
PMID:26248042
Dephosphorylates and inactivates transcription factor ELK1 .
PMID:19154138
Dephosphorylates DARPP32 .
PMID:19154138
May dephosphorylate CRTC2 at 'Ser-171' resulting in CRTC2 dissociation from 14-3-3 proteins .
PMID:30611118
Dephosphorylates transcription factor TFEB at 'Ser-211' following Coxsackievirus B3 infection, promoting nuclear translocation .
PMID:33691586
Required for postnatal development of the nephrogenic zone and superficial glomeruli in the kidneys, cell cycle homeostasis in the nephrogenic zone, and ultimately normal kidney function (By similarity).
Plays a role in intracellular AQP2 processing and localization to the apical membrane in the kidney, may thereby be required for efficient kidney filtration (By similarity). Required for secretion of salivary enzymes amylase, peroxidase, lysozyme and sialic acid via formation of secretory vesicles in the submandibular glands (By similarity). Required for calcineurin activity and homosynaptic depotentiation in the hippocampus (By similarity).
Required for normal differentiation and survival of keratinocytes and therefore required for epidermis superstructure formation (By similarity). Positively regulates osteoblastic bone formation, via promotion of osteoblast differentiation (By similarity). Positively regulates osteoclast differentiation, potentially via NFATC1 signaling (By similarity).
May play a role in skeletal muscle fiber type specification, potentially via NFATC1 signaling (By similarity). Negatively regulates MAP3K14/NIK signaling via inhibition of nuclear translocation of the transcription factors RELA and RELB (By similarity). Required for antigen-specific T-cell proliferation response (By similarity).
Dephosphorylates KLHL3, promoting the interaction between KLHL3 and WNK4 and subsequent degradation of WNK4 .
PMID:30718414
Negatively regulates SLC9A1 activity PMID:31375679
PMID:15671020 PMID:18838687 PMID:19154138 PMID:23468591 PMID:30254215
Many of the substrates contain a PxIxIT motif and/or a LxVP motif .
PMID:17498738 PMID:17502104 PMID:22343722 PMID:23468591 PMID:27974827
In response to increased Ca(2+) levels, dephosphorylates and activates phosphatase SSH1 which results in cofilin dephosphorylation .
PMID:15671020
In response to increased Ca(2+) levels following mitochondrial depolarization, dephosphorylates DNM1L inducing DNM1L translocation to the mitochondrion .
PMID:18838687
Positively regulates the CACNA1B/CAV2.2-mediated Ca(2+) release probability at hippocampal neuronal soma and synaptic terminals (By similarity). Dephosphorylates heat shock protein HSPB1 (By similarity). Dephosphorylates and activates transcription factor NFATC1 .
PMID:19154138
In response to increased Ca(2+) levels, regulates NFAT-mediated transcription probably by dephosphorylating NFAT and promoting its nuclear translocation .
PMID:26248042
Dephosphorylates and inactivates transcription factor ELK1 .
PMID:19154138
Dephosphorylates DARPP32 .
PMID:19154138
May dephosphorylate CRTC2 at 'Ser-171' resulting in CRTC2 dissociation from 14-3-3 proteins .
PMID:30611118
Dephosphorylates transcription factor TFEB at 'Ser-211' following Coxsackievirus B3 infection, promoting nuclear translocation .
PMID:33691586
Required for postnatal development of the nephrogenic zone and superficial glomeruli in the kidneys, cell cycle homeostasis in the nephrogenic zone, and ultimately normal kidney function (By similarity).
Plays a role in intracellular AQP2 processing and localization to the apical membrane in the kidney, may thereby be required for efficient kidney filtration (By similarity). Required for secretion of salivary enzymes amylase, peroxidase, lysozyme and sialic acid via formation of secretory vesicles in the submandibular glands (By similarity). Required for calcineurin activity and homosynaptic depotentiation in the hippocampus (By similarity).
Required for normal differentiation and survival of keratinocytes and therefore required for epidermis superstructure formation (By similarity). Positively regulates osteoblastic bone formation, via promotion of osteoblast differentiation (By similarity). Positively regulates osteoclast differentiation, potentially via NFATC1 signaling (By similarity).
May play a role in skeletal muscle fiber type specification, potentially via NFATC1 signaling (By similarity). Negatively regulates MAP3K14/NIK signaling via inhibition of nuclear translocation of the transcription factors RELA and RELB (By similarity). Required for antigen-specific T-cell proliferation response (By similarity).
Dephosphorylates KLHL3, promoting the interaction between KLHL3 and WNK4 and subsequent degradation of WNK4 .
PMID:30718414
Negatively regulates SLC9A1 activity PMID:31375679
Peptidyl-prolyl cis-trans isomerase FKBP1A
FKBP1A
potentiator
Specific functionactivin receptor binding
Cellular location
Cytoplasm, cytosol
General function & pharmacology
Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides
Metabolizing enzymes(1)
Enzymes involved in drug metabolism — important for understanding drug interactions
Enzyme activity key
substrate
inhibitor
inducer
CYP3A4Cytochrome P450 3A4
substrate
Scientific references(1)
Grassberger M., Baumruker T., Enz A., Hiestand P., Hultsch T., Kalthoff F., Schuler W., Schulz M., Werner F.J., Winiski A., Wolff B., Zenke G.
A novel anti-inflammatory drug, SDZ ASM 981, for the treatment of skin diseases: in vitro pharmacology.
British Journal of Dermatology
1999141(2):264-273. doi: 10.1046/j.1365-2133.1999.02974.x
ATC classification(1 code)
ATC D11AH02
Affected organisms(1)
Humans and other mammals
International brands(2)
Experimental properties(1)
Commercial products(18)
Chemical identifiers
CAS, UNII, InChI Key and database cross-references
Show
Chemical identifiers
CAS, UNII, InChI Key and database cross-references
Linked compound data from DrugBank Open Data (CC BY-NC 4.0)
Pimecrolimus
Additional database identifiers
Drugs Product Database (DPD)
12077
ChemSpider
21111755
BindingDB
50248356
ZINC
ZINC000085536990
HUGO Gene Nomenclature Committee (HGNC)
HGNC:3942
GenAtlas
FRAP1
GeneCards
MTOR
GenBank Gene Database
L34075
Guide to Pharmacology
2109
UniProt Accession
MTOR_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:9314
GeneCards
PPP3CA
GenBank Gene Database
L14778
GenBank Protein Database
306477
UniProt Accession
PP2BA_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:3711
GenAtlas
FKBP1A
GeneCards
FKBP1A
GenBank Gene Database
M34539
GenBank Protein Database
182628
Guide to Pharmacology
2609
UniProt Accession
FKB1A_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:2637
GenAtlas
CYP3A4
GeneCards
CYP3A4
GenBank Gene Database
M18907
Guide to Pharmacology
1337
UniProt Accession
CP3A4_HUMAN
International reference pricing
4 formulations
Reference pricing from DrugBank. Prices are indicative and may not reflect current UK costs.
From $3.21/g
To $315.76/tube
Elidel 1% cream
$3.21/g
Elidel 30 Gram Tube 1% 30 gm Tube
$101.44/tube
Elidel 60 Gram Tube 1% 60 gm Tube
$200.05/tube
Elidel 100 Gram Tube 1% 100 gm Tube
$315.76/tube
Source: DrugBank. Used under CC BY-NC 4.0 academic licence for non-commercial purposes.
Patent information
All patents expired, 4 expired
Approved 23 Jul 2002 · Expires 26 Dec 2018
Expired
Approved 15 Jun 1999 · Expires 15 Dec 2016
Expired
Approved 5 Mar 2002 · Expires 26 Apr 2016
Expired
2200966
Canada
Approved 19 Dec 2006 · Expires 26 Oct 2015
Expired
Patent protection has expired — generic versions may be available.
Source: DrugBank · CC BY-NC 4.0. Patent data sourced from national patent offices. Expiry dates may not reflect extensions, regulatory exclusivity periods, or legal challenges.
DrugBank citations
If you use DrugBank data in your research, please cite the following publications:
Knox C., Wilson M., Klinger C.M., et al
DrugBank 6.
0: the DrugBank Knowledgebase for 2024
Nucleic Acids Res. 2024 Jan 552(D1):D1265-D1275
Wishart D.S., Feunang Y.D., Guo A.C., et al
DrugBank 5.
0: a major update to the DrugBank database for 2018
Nucleic Acids Res. 2017 Nov 846(D1):D1074-D1082
Show earlier publications
Law V., Knox C., Djoumbou Y., et al
DrugBank 4.
0: shedding new light on drug metabolism
Nucleic Acids Res. 2014 Jan 142(1):D1091-7
Knox C., Law V., Jewison T., et al
DrugBank 3.
0: a comprehensive resource for 'omics' research on drugs
Nucleic Acids Res. 2011 Jan39(Database issue):D1035-41
Wishart D.S., Knox C., Guo A.C., et al
DrugBank: a knowledgebase for drugs, drug actions and drug targets.
Nucleic Acids Research
2008 Jan36(Database issue):D901-6
Wishart D.S., Knox C., Guo A.C., et al
DrugBank: a comprehensive resource for in silico drug discovery and exploration.
Nucleic Acids Research
2006 Jan 134(Database issue):D668-72
Source: go.drugbank.comCC BY-NC 4.0
Updated 26 days ago(8 Mar 2026)