ID NLRP3_MACMU Reviewed; 1035 AA.
AC B0FPE9;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=NACHT, LRR and PYD domains-containing protein 3;
DE EC=3.6.4.- {ECO:0000250|UniProtKB:Q96P20};
GN Name=NLRP3;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Oocyte;
RX PubMed=18509866; DOI=10.1002/mrd.20937;
RA McDaniel P., Wu X.;
RT "Identification of oocyte-selective NLRP genes in rhesus macaque monkeys
RT (Macaca mulatta).";
RL Mol. Reprod. Dev. 76:151-159(2009).
CC -!- FUNCTION: Sensor component of the NLRP3 inflammasome, which mediates
CC inflammasome activation in response to defects in membrane integrity,
CC leading to secretion of inflammatory cytokines IL1B and IL18 and
CC pyroptosis. In response to pathogens and other damage-associated
CC signals that affect the integrity of membranes, initiates the formation
CC of the inflammasome polymeric complex composed of NLRP3, CASP1 and
CC PYCARD/ASC. Recruitment of pro-caspase-1 (proCASP1) to the NLRP3
CC inflammasome promotes caspase-1 (CASP1) activation, which subsequently
CC cleaves and activates inflammatory cytokines IL1B and IL18 and
CC gasdermin-D (GSDMD), promoting cytokine secretion and pyroptosis.
CC Activation of NLRP3 inflammasome is also required for HMGB1 secretion;
CC stimulating inflammatory responses (By similarity). Under resting
CC conditions, ADP-bound NLRP3 is autoinhibited (By similarity). NLRP3
CC activation stimuli include extracellular ATP, nigericin, reactive
CC oxygen species, crystals of monosodium urate or cholesterol, amyloid-
CC beta fibers, environmental or industrial particles and nanoparticles,
CC such as asbestos, silica, aluminum salts, cytosolic dsRNA, etc. Almost
CC all stimuli trigger intracellular K(+) efflux (By similarity). These
CC stimuli lead to membrane perturbation and activation of NLRP3 (By
CC similarity). Upon activation, NLRP3 is transported to microtubule
CC organizing center (MTOC), where it is unlocked by NEK7, leading to its
CC relocalization to dispersed trans-Golgi network (dTGN) vesicle
CC membranes and formation of an active inflammasome complex. Associates
CC with dTGN vesicle membranes by binding to phosphatidylinositol 4-
CC phosphate (PtdIns4P). Shows ATPase activity (By similarity).
CC {ECO:0000250|UniProtKB:Q8R4B8, ECO:0000250|UniProtKB:Q96P20}.
CC -!- FUNCTION: Independently of inflammasome activation, regulates the
CC differentiation of T helper 2 (Th2) cells and has a role in Th2 cell-
CC dependent asthma and tumor growth. During Th2 differentiation, required
CC for optimal IRF4 binding to IL4 promoter and for IRF4-dependent IL4
CC transcription. Binds to the consensus DNA sequence 5'-GRRGGNRGAG-3'.
CC May also participate in the transcription of IL5, IL13, GATA3, CCR3,
CC CCR4 and MAF. {ECO:0000250|UniProtKB:Q8R4B8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q8R4B8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q8R4B8};
CC -!- ACTIVITY REGULATION: Under resting conditions, NLRP3 binds ADP and is
CC autoinhibited (By similarity). Inactive NLRP3 forms homodecameric
CC double-ring cages that hide pyrin domains within NACHT-LRR rings to
CC avoid premature activation. NLRP3 activation stimuli include
CC extracellular ATP, nigericin, reactive oxygen species, crystals of
CC monosodium urate or cholesterol, amyloid-beta fibers, environmental or
CC industrial particles and nanoparticles, such as asbestos, silica,
CC aluminum salts, cytosolic dsRNA, etc. Almost all stimuli trigger
CC intracellular K(+) efflux. These stimuli lead to membrane perturbations
CC that induce activation of NLRP3. Upon activation, NLRP3 is transported
CC to microtubule organizing center (MTOC), where it is unlocked by NEK7,
CC leading to its relocalization to dispersed trans-Golgi network (dTGN)
CC vesicle membranes and recruitment of PYCARD/ASC for the formation of an
CC active inflammasome complex. NEK7-activated NLRP3 forms a disk-shaped
CC inflammasome. NLRP3 and PYCARD/ASC interact via their respective pyrin
CC domains; interaction initiates speck formation (nucleation) which
CC greatly enhances further addition of soluble PYCARD/ASC molecules to
CC the speck in a prion-like polymerization process (By similarity).
CC Clustered PYCARD/ASC nucleates the formation of CASP1 filaments through
CC the interaction of their respective CARD domains, acting as a platform
CC for CASP1 polymerization and activation. Active CASP1 then processes
CC IL1B and IL18 precursors, leading to the release of mature cytokines in
CC the extracellular milieu and inflammatory response (By similarity).
CC NLRP3 inflammasome assembly is inhibited by IRGM, which impedes NLRP3
CC oligomerization (By similarity). Specifically inhibited by sulfonylurea
CC MCC950 (also named CP-456,773, CRID3), a potent and specific small-
CC molecule inhibitor of the NLRP3 inflammasome that acts by preventing
CC ATP hydrolysis (By similarity). {ECO:0000250|UniProtKB:Q8R4B8,
CC ECO:0000250|UniProtKB:Q96P20}.
CC -!- SUBUNIT: Sensor component of NLRP3 inflammasomes; inflammasomes are
CC supramolecular complexes that assemble in the cytosol in response to
CC pathogens and other damage-associated signals and play critical roles
CC in innate immunity and inflammation. The core of NLRP3 inflammasomes
CC consists of a signal sensor component (NLRP3), an adapter (PYCARD/ASC),
CC which recruits an effector pro-inflammatory caspase (CASP1 and,
CC possibly, CASP4 and CASP5). Homodecamer; inactive NLRP3 forms
CC homodecameric double-ring cages that hide pyrin domains within NACHT-
CC LRR rings to avoid premature activation. Interacts (via pyrin domain)
CC with PYCARD/ASC (via pyrin domain); interaction is direct. Interacts
CC (via LRR repeat domain) with NEK7 (via N-terminus); the interaction is
CC required for the formation of the complex NLRP3:PYCARD, oligomerization
CC of PYCARD/ASC and activation of CASP1 (By similarity). Interacts (via
CC LRR repeat domain) with NR4A1/Nur77 (via N-terminus); the interaction
CC is direct, requires activation of NR4A1 by its ligands NBRE-containing
CC dsDNA and lipopolysaccharide, and stimulates the association of NLRP3
CC with NEK7 for non-canonical NLRP3 inflammasome activation (By
CC similarity). Interacts with CARD8; leading to inhibit formation of the
CC NLRP3 inflammasome. Interacts with MEFV; this interaction targets NLRP3
CC to degradation by autophagy, hence preventing excessive IL1B- and IL18-
CC mediated inflammation (By similarity). Interacts with EIF2AK2/PKR; this
CC interaction requires EIF2AK2 activity, is accompanied by EIF2AK2
CC autophosphorylation and promotes inflammasome assembly in response to
CC specific stimuli (By similarity). Interacts with GBP5 (via DAPIN
CC domain); this interaction promotes inflammasome assembly in response to
CC microbial and soluble, but not crystalline, agents. Interacts with PML
CC (isoform PML-1) (via the leucine-rich repeat (LRR) domain); PML-
CC mediated increase in NLRP3 inflammasome activation does not depend upon
CC this interaction. Interacts (via NACHT domain) with DHX33 (via DEAH
CC box); NLRP3 activation in presence of cytosolic dsRNA is mediated by
CC DHX33. Interacts (via NACHT and LRR domains) with ARRB2; this
CC interaction is direct and inducible by polyunsaturated fatty acids
CC (PUFAs). Interacts (via NACHT domain) with DDX3X under both LPS-primed
CC and inflammasome-activating conditions. Interacts with IRF4 (via the
CC LRR domain); this interaction is direct and is required for optimal
CC IRF4 binding to IL4 promoter and efficient IL4 transactivation during
CC differentiation of Th2 helper T-cells. Interacts with MAVS; promoting
CC localization to mitochondria and activation of the NLRP3 inflammasome.
CC Interacts with MARK4; promoting localization of NLRP3 to the
CC microtubule organizing center (MTOC) (By similarity). Interacts with
CC TRIM50; this interaction promotes also NLRP3 oligomerization and
CC subsequent inflammasome activation (By similarity). Interacts with
CC IRGM; preventing NLRP3 inflammasome assembly and promoting NLRP3
CC degradation (By similarity). Interacts (via KFERQ-like motifs) with
CC HSPA8/HSC70; promoting NLRP3 degradation by the chaperone-mediated
CC autophagy pathway (By similarity). {ECO:0000250|UniProtKB:Q8R4B8,
CC ECO:0000250|UniProtKB:Q96P20}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q8R4B8}. Inflammasome
CC {ECO:0000250|UniProtKB:Q8R4B8}. Cytoplasm, cytoskeleton, microtubule
CC organizing center {ECO:0000250|UniProtKB:Q8R4B8}. Golgi apparatus
CC membrane {ECO:0000250|UniProtKB:Q8R4B8}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q8R4B8}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q8R4B8}. Secreted
CC {ECO:0000250|UniProtKB:Q8R4B8}. Nucleus {ECO:0000250|UniProtKB:Q8R4B8}.
CC Note=In macrophages, under resting conditions, mainly located in the
CC cytosol and on membranes of various organelles, such as endoplasmic
CC reticulum, mitochondria and Golgi: forms an inactive double-ring cage
CC that is primarily localized on membranes. Upon activation, NLRP3 is
CC transported to microtubule organizing center (MTOC), where it is
CC unlocked by NEK7, leading to its relocalization to dispersed trans-
CC Golgi network (dTGN) vesicle membranes for the formation of an active
CC inflammasome complex. Recruited to dTGN vesicle membranes by binding to
CC phosphatidylinositol 4-phosphate (PtdIns4P). After the induction of
CC pyroptosis, inflammasome specks are released into the extracellular
CC space where they can further promote IL1B processing and where they can
CC be engulfed by macrophages. Phagocytosis induces lysosomal damage and
CC inflammasome activation in the recipient cells. In the Th2 subset of
CC CD4(+) helper T-cells, mainly located in the nucleus. Nuclear
CC localization depends upon KPNA2. In the Th1 subset of CD4(+) helper T-
CC cells, mainly cytoplasmic. {ECO:0000250|UniProtKB:Q8R4B8}.
CC -!- TISSUE SPECIFICITY: Highly expressed in oocyte, testis, spleen, thymus
CC and kidney. {ECO:0000269|PubMed:18509866}.
CC -!- DOMAIN: The pyrin domain (also called DAPIN domain or PYD) is involved
CC in PYCARD/ASC-binding. {ECO:0000250|UniProtKB:Q96P20}.
CC -!- DOMAIN: The FISNA domain is a critical mediator of NLRP3 conformational
CC during NLRP3 activation. It becomes ordered in its key regions during
CC activation to stabilize the active NACHT conformation and mediate most
CC interactions in the NLRP3 disk. {ECO:0000250|UniProtKB:Q96P20}.
CC -!- DOMAIN: The LRR domain mediates the interaction with IRF4, PML, NEK7
CC and NR4A1/Nur77. {ECO:0000250|UniProtKB:Q8R4B8}.
CC -!- DOMAIN: The KFERQ-like motifs mediate binding to HSPA8/HSC70 following
CC NLRP3 paylmitoylation by ZDHHC12. {ECO:0000250|UniProtKB:Q96P20}.
CC -!- PTM: The disulfide bond in the pyrin domain might play a role in
CC reactive oxygen species-mediated activation.
CC {ECO:0000250|UniProtKB:Q96P20}.
CC -!- PTM: Phosphorylation at Ser-198 by MAPK8/JNK1 increases inflammasome
CC activation by promoting deubiquitination by BRCC3 and NLRP3
CC homooligomerization. Phosphorylation at Ser-805 by CSNK1A1 prevents
CC inflammasome activation by preventing NEK7 recruitment. Phosphorylation
CC at Ser-5 in the pyrin domain inhibits homomultimerization of NLRP3 and
CC activation of the NLRP3 inflammasome: dephosphorylation by protein
CC phosphatase 2A (PP2A) promotes assembly of the NLRP3 inflammasome (By
CC similarity). Phosphorylation at Ser-295 by PKD/PRKD1 promotes NLRP3
CC inflammasome assembly (By similarity). Phosphorylation by ERK1/MAPK3
CC promotes NLRP3 inflammasome assembly. Phosphorylation by BTK (at Tyr-
CC 136, Tyr-140, Tyr-143 and Tyr-168) in the region that mediates binding
CC to phosphatidylinositol phosphate, promotes relocalization of NLRP3 and
CC assembly of the NLRP3 inflammasome. Phosphorylation at Tyr-860 inhibits
CC NLRP3 inflammasome assembly: dephosphorylation by PTPN22 promotes
CC inflammasome activation (By similarity). {ECO:0000250|UniProtKB:Q8R4B8,
CC ECO:0000250|UniProtKB:Q96P20}.
CC -!- PTM: Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked
CC polyubiquitination (By similarity). Ubiquitination does not lead to
CC degradation, but inhibits inflammasome activation. Deubiquitination is
CC catalyzed by BRCC3 and associated with NLRP3 activation and
CC inflammasome assembly. This process can be induced by the activation of
CC Toll-like receptors (by LPS), through a non-transcriptional pathway
CC dependent on the mitochondrial production of reactive oxygen species,
CC and by ATP (By similarity). Ubiquitinated by TRIM31 via 'Lys-48'-linked
CC ubiquitination, leading to its degradation by the proteasome.
CC Ubiquitinated at Lys-689 by the SCF(FBXL2) complex, leading to its
CC degradation by the proteasome (By similarity). Ubiquitinated by TRIM35
CC via 'lys-48' and 'Lys-63'-linked ubiquitination leading to inhibition
CC of NLRP3 inflammasome activation (By similarity).
CC {ECO:0000250|UniProtKB:Q8R4B8, ECO:0000250|UniProtKB:Q96P20}.
CC -!- PTM: Palmitoylation by ZDHHC12 inhibits the NLRP3 inflammasome by
CC promoting NLRP3 degradation by the chaperone-mediated autophagy
CC pathway. Following palmitoylation, HSPA8/HSC70 recognizes and binds the
CC KFERQ-like motifs on NLRP3 and promotes NLRP3 recruitment to lysosomes,
CC where it is degraded via the chaperone-mediated autophagy pathway in a
CC LAMP2-dependent process. {ECO:0000250|UniProtKB:Q96P20}.
CC -!- PTM: Degraded via selective autophagy following interaction with IRGM.
CC IRGM promotes NLRP3 recruitment to autophagosome membranes, promoting
CC its SQSTM1/p62-dependent autophagy-dependent degradation.
CC {ECO:0000250|UniProtKB:Q96P20}.
CC -!- SIMILARITY: Belongs to the NLRP family. {ECO:0000305}.
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DR EMBL; EU344966; ABY58962.1; -; mRNA.
DR RefSeq; NP_001107823.1; NM_001114351.1.
DR RefSeq; XP_014983267.1; XM_015127781.1.
DR AlphaFoldDB; B0FPE9; -.
DR SMR; B0FPE9; -.
DR STRING; 9544.ENSMMUP00000053959; -.
DR PaxDb; 9544-ENSMMUP00000007829; -.
DR GeneID; 701278; -.
DR KEGG; mcc:701278; -.
DR CTD; 114548; -.
DR eggNOG; ENOG502SBIG; Eukaryota.
DR HOGENOM; CLU_002274_2_3_1; -.
DR InParanoid; B0FPE9; -.
DR Proteomes; UP000006718; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031021; C:interphase microtubule organizing center; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0072559; C:NLRP3 inflammasome complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043531; F:ADP binding; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; ISS:UniProtKB.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISS:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0035591; F:signaling adaptor activity; ISS:UniProtKB.
DR GO; GO:0140299; F:small molecule sensor activity; ISS:UniProtKB.
DR GO; GO:0009595; P:detection of biotic stimulus; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0002674; P:negative regulation of acute inflammatory response; IBA:GO_Central.
DR GO; GO:1901223; P:negative regulation of non-canonical NF-kappaB signal transduction; IBA:GO_Central.
DR GO; GO:0044546; P:NLRP3 inflammasome complex assembly; ISS:UniProtKB.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISS:UniProtKB.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; ISS:UniProtKB.
DR GO; GO:2000553; P:positive regulation of T-helper 2 cell cytokine production; ISS:UniProtKB.
DR GO; GO:0045630; P:positive regulation of T-helper 2 cell differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0002830; P:positive regulation of type 2 immune response; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR CDD; cd00116; LRR_RI; 1.
DR CDD; cd08320; Pyrin_NALPs; 1.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR004020; DAPIN.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR029495; NACHT-assoc.
DR InterPro; IPR007111; NACHT_NTPase.
DR InterPro; IPR041267; NLRP_HD2.
DR InterPro; IPR041075; NOD2_WH.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45690; NACHT, LRR AND PYD DOMAINS-CONTAINING PROTEIN 12; 1.
DR PANTHER; PTHR45690:SF19; NACHT, LRR AND PYD DOMAINS-CONTAINING PROTEIN 3; 1.
DR Pfam; PF14484; FISNA; 1.
DR Pfam; PF13516; LRR_6; 5.
DR Pfam; PF05729; NACHT; 1.
DR Pfam; PF17776; NLRC4_HD2; 1.
DR Pfam; PF17779; NOD2_WH; 1.
DR Pfam; PF02758; PYRIN; 1.
DR SMART; SM01288; FISNA; 1.
DR SMART; SM00368; LRR_RI; 9.
DR SMART; SM01289; PYRIN; 1.
DR SUPFAM; SSF47986; DEATH domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS50824; DAPIN; 1.
DR PROSITE; PS50837; NACHT; 1.
PE 2: Evidence at transcript level;
KW Activator; Amyloidosis; ATP-binding; Cytoplasm; Cytoskeleton;
KW Disulfide bond; Endoplasmic reticulum; Golgi apparatus; Hydrolase;
KW Immunity; Inflammasome; Inflammatory response; Innate immunity;
KW Isopeptide bond; Leucine-rich repeat; Lipoprotein; Membrane; Mitochondrion;
KW Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein; Reference proteome;
KW Repeat; Secreted; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1035
FT /note="NACHT, LRR and PYD domains-containing protein 3"
FT /id="PRO_0000387569"
FT DOMAIN 1..93
FT /note="Pyrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00061"
FT DOMAIN 140..210
FT /note="FISNA"
FT /evidence="ECO:0000255"
FT DOMAIN 220..536
FT /note="NACHT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT REPEAT 741..761
FT /note="LRR 1"
FT REPEAT 770..791
FT /note="LRR 2"
FT REPEAT 798..818
FT /note="LRR 3"
FT REPEAT 827..848
FT /note="LRR 4"
FT REPEAT 855..875
FT /note="LRR 5"
FT REPEAT 884..905
FT /note="LRR 6"
FT REPEAT 912..932
FT /note="LRR 7"
FT REPEAT 941..962
FT /note="LRR 8"
FT REPEAT 969..990
FT /note="LRR 9"
FT REGION 131..134
FT /note="Required for binding to phosphatidylinositol 4-
FT phosphate (PtdIns4P)"
FT /evidence="ECO:0000250|UniProtKB:Q8R4B8"
FT MOTIF 355..359
FT /note="KFERQ-like motif 1"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT MOTIF 603..607
FT /note="KFERQ-like motif 2"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT MOTIF 797..801
FT /note="KFERQ-like motif 3"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT MOTIF 990..994
FT /note="KFERQ-like motif 4"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT BINDING 169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT BINDING 226..233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT BINDING 522
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R4B8"
FT MOD_RES 13
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT MOD_RES 136
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT MOD_RES 140
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT MOD_RES 143
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R4B8"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT MOD_RES 168
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R4B8"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT MOD_RES 727
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT MOD_RES 734
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT MOD_RES 805
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT MOD_RES 860
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT MOD_RES 974
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT MOD_RES 1034
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT LIPID 843
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT DISULFID 8..108
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT CROSSLNK 689
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT CROSSLNK 877
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT CROSSLNK 926
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
FT CROSSLNK 972
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q96P20"
SQ SEQUENCE 1035 AA; 118192 MW; 7EE691EEC6BFCF7C CRC64;
MKMASTRCKL ARYLEDLEDV DLKKFKMHLE DYPPQKGCIS LPRGQTEKAD HVDLATLMID
FNGEEKAWAM AVWIFAAINR RDLYEKAKRD EPKWGSDNAR VSNPTVICQE DSIEEEWMGL
LEYLSRISIC KKKKDYCKKY RKYVRSRFQC IEDRNARLGE SVSLNKRYTR LRLIKEHRSQ
QEREHELLAI GKTKTWESPV SPIKMELLFD PDDEHSEPVH TVVFQGAAGI GKTILARKIM
LDWASGTLYQ DRFDYLFYIH CREVSLVTQR SLGDLIMSCC PDPNPPIRKI VSKPSRILFL
MDGFDELQGA FDEHIGPLCT DWQKAERGDI LLSSLIRKKL LPEASLLITT RPVALEKLQH
LLDHPRHVEI LGFSEAKRKE YFFKYFSDEA QARAAFSLIQ ENEVLFTMCF IPLVCWIVCT
GLKQQMESGK SLAQTSKTTT AVYTFFLSSL LQPRGGSQEH RLCAHLWGLC SLAADGIWNQ
KILFEESDLR NHGLQKADVS AFLRMNLFQK EVDCEKFYSF IHMTFQEFFA AMYYLLEEEK
EGRTNVPGSC LKLPSRDVTV LLENYGKFEK GYLIFVVRFL FGLVNQERTC YLEKKLSCKI
SQQIRLELLK WIEVKAKAKK LQIQPSQLEL FYCLYEMQEE DFVQRAMDYF PKIEINLSTR
MDHVVSSFCI ENCHRVESLS LGFLHNMPKE EEEEEKEGRH LDMVQCVLPG SHAACSHRLV
NSHLTSSFCR GLFSVLSTSQ SLTELDLSDN SLGDPGMRVL CETLQHPDCN IRRLWLGRCG
LSHECCFDIS LVLSSNQKLV ELDLSDNALG DFGIRLLCVG LKHLLCNLKK LWLVSCCLTS
ACCQDLASVL STSRSLTRLY VGENALGDAG VAILCEKAKN PQCNLQKLGL VNSGLTSACC
SALSSVLSTN QNLTHLYLRG NTLGDKGIKL LCEGLLHPDC KLQVLELDNC NLTSHCCWDL
STLLTSSQSL RKLSLGNNDL GDLGVMMFCE VLKQQSCLLQ NLGLSEMYFN YETKSALETL
QEEKPELTIV FEPSW
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