IED Industry Enzyme Database

Detail Information for IndEnz0002012734
IED ID IndEnz0002012734
Enzyme Type ID protease012734
Protein Name Transcription factor p65
Nuclear factor NF-kappa-B p65 subunit
Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3
Gene Name RELA NFKB3
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MDELFPLIFPAEPAQASGPYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINGYTGPGTVRISLVTKDPPHRPHPHELVGKDCRDGFYEAELCPDRCIHSFQNLGIQCVKKRDLEQAISQRIQTNNNPFQVPIEEQRGDYDLNAVRLCFQVTVRDPSGRPLRLPPVLSHPIFDNRAPNTAELKICRVNRNSGSCLGGDEIFLLCDKVQKEDIEVYFTGPGWEARGSFSQADVHRQVAIVFRTPPYADPSLQAPVRVSMQLRRPSDRELSEPMEFQYLPDTDDRHRIEEKRKRTYETFKSIMKKSPFSGPTDPRPPPRRIAVPSRSSASVPKPAPQPYPFTSSLSTINYDEFPTMVFPSGQISQASALAPAPPQVLPQAPAPAPAPAMVSALAQAPAPVPVLAPGPPQAVAPPAPKPTQAGEGTLSEALLQLQFDDEDLGALLGNSTDPAVFTDLASVDNSEFQQLLNQGIPVAPHTTEPMLMEYPEAITRLVTGAQRPPDPAPAPLGAPGLPNGLLSGDEDFSSIADMDFSALLSQISS
Enzyme Length 551
Uniprot Accession Number Q04206
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The heterodimeric RELA-NFKB1 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. The NF-kappa-B heterodimeric RELA-NFKB1 and RELA-REL complexes, for instance, function as transcriptional activators. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. The inhibitory effect of I-kappa-B on NF-kappa-B through retention in the cytoplasm is exerted primarily through the interaction with RELA. RELA shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex. Beside its activity as a direct transcriptional activator, it is also able to modulate promoters accessibility to transcription factors and thereby indirectly regulate gene expression. Associates with chromatin at the NF-kappa-B promoter region via association with DDX1. Essential for cytokine gene expression in T-cells (PubMed:15790681). The NF-kappa-B homodimeric RELA-RELA complex appears to be involved in invasin-mediated activation of IL-8 expression. Key transcription factor regulating the IFN response during SARS-CoV-2 infection (PubMed:33440148). {ECO:0000269|PubMed:10928981, ECO:0000269|PubMed:12748188, ECO:0000269|PubMed:15790681, ECO:0000269|PubMed:17000776, ECO:0000269|PubMed:17620405, ECO:0000269|PubMed:19058135, ECO:0000269|PubMed:19103749, ECO:0000269|PubMed:20547752, ECO:0000269|PubMed:33440148}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (4); Beta strand (23); Chain (1); Cross-link (3); Domain (1); Helix (6); Modified residue (18); Motif (2); Mutagenesis (2); Natural variant (1); Region (5); Sequence conflict (3); Turn (5)
Keywords 3D-structure;Acetylation;Activator;Alternative splicing;Chromosomal rearrangement;Cytoplasm;DNA-binding;Disease variant;Host-virus interaction;Isopeptide bond;Methylation;Nucleus;Phosphoprotein;Reference proteome;S-nitrosylation;Transcription;Transcription regulation;Ubl conjugation
Interact With Q9NY61; P18847-3; O60885; P55212; P06307; Q96JB5; P28329-3; O15111; Q8N668; Q92793; P52943; P35222; Q9UER7; Q08211; Q9H9B1; P03372; P22607; Q99684; P06396; Q13547; P46695; O14920; Q13568; Q9Y2K7; Q14145; Q99612; P13473-2; P25791; Q9BQ69; P53779; O00255-2; Q16236; P19838; P19838; P25963; Q15653; P22736-1; Q96L73; O15294; Q53EL6; Q8N2W9; P67775; P30153; O75400-2; P62826; Itself; P23396; Q8WTS6; Q96EB6; Q8IXJ6; Q8N6T7; O95863; O15524; P40763; Q13148; P21980; Q13625; Q13625-2; P0CG48; Q9UMX0; Q9UBK9; Q9Y649; Q9ESU6; O41974; Q8VIM5-1; Q8X834; B3CRR2; B3CTB0; P0C774; P69976; P10226; P31491; A0A384KL23; A0A380PFV1; Q9NPC8; Q8VIM5-1; P25963; Q04864; Q01201; P35637; Q04864; P15884
Induction
Subcellular Location SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1493333, ECO:0000269|PubMed:15799966, ECO:0000269|PubMed:19058135, ECO:0000269|PubMed:20547752}. Cytoplasm {ECO:0000269|PubMed:1493333, ECO:0000269|PubMed:19058135, ECO:0000269|PubMed:20547752, ECO:0000269|PubMed:27736973}. Note=Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B) (PubMed:1493333). Colocalized with DDX1 in the nucleus upon TNF-alpha induction (PubMed:19058135). Colocalizes with GFI1 in the nucleus after LPS stimulation (PubMed:20547752). Translocation to the nucleus is impaired in L.monocytogenes infection (PubMed:20855622). {ECO:0000269|PubMed:1493333, ECO:0000269|PubMed:19058135, ECO:0000269|PubMed:20547752, ECO:0000269|PubMed:20855622}.
Modified Residue MOD_RES 1; /note="N-acetylmethionine"; /evidence="ECO:0007744|PubMed:22814378"; MOD_RES 38; /note="Cysteine persulfide; alternate"; /evidence="ECO:0000250"; MOD_RES 38; /note="S-nitrosocysteine; alternate"; /evidence="ECO:0000250|UniProtKB:Q04207"; MOD_RES 122; /note="N6-acetyllysine; by PCAF and EP300; alternate"; /evidence="ECO:0000269|PubMed:12419806"; MOD_RES 123; /note="N6-acetyllysine; by PCAF and EP300; alternate"; /evidence="ECO:0000269|PubMed:12419806"; MOD_RES 218; /note="N6-acetyllysine"; /evidence="ECO:0000269|PubMed:12456660"; MOD_RES 221; /note="N6-acetyllysine"; /evidence="ECO:0000269|PubMed:12456660"; MOD_RES 254; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:14690596"; MOD_RES 276; /note="Phosphoserine; by RPS6KA4 and RPS6KA5"; /evidence="ECO:0000269|PubMed:12628924"; MOD_RES 281; /note="Phosphoserine"; /evidence="ECO:0000305|PubMed:15516339"; MOD_RES 310; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000269|PubMed:12456660, ECO:0000269|PubMed:16135789, ECO:0000269|PubMed:17000776, ECO:0000269|PubMed:19103749, ECO:0007744|PubMed:19608861"; MOD_RES 310; /note="N6-methyllysine; by SETD6; alternate"; /evidence="ECO:0000250|UniProtKB:Q04207"; MOD_RES 311; /note="Phosphoserine; by PKC/PRKCZ"; /evidence="ECO:0000250|UniProtKB:Q04207"; MOD_RES 435; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:15073167"; MOD_RES 468; /note="Phosphoserine; by IKKB and IKKE"; /evidence="ECO:0000269|PubMed:16046471, ECO:0000269|PubMed:16407239"; MOD_RES 505; /note="Phosphothreonine; by CHEK1"; /evidence="ECO:0000269|PubMed:15775976"; MOD_RES 529; /note="Phosphoserine; by CK2"; /evidence="ECO:0000269|PubMed:10938077"; MOD_RES 536; /note="Phosphoserine; by IKKB"; /evidence="ECO:0000269|PubMed:10521409, ECO:0000269|PubMed:17785205"
Post Translational Modification PTM: Ubiquitinated by RNF182, leading to its proteasomal degradation. Degradation is required for termination of NF-kappa-B response. {ECO:0000269|PubMed:15226358, ECO:0000269|PubMed:31432514}.; PTM: Monomethylated at Lys-310 by SETD6 (PubMed:21515635). Monomethylation at Lys-310 is recognized by the ANK repeats of EHMT1 and promotes the formation of repressed chromatin at target genes, leading to down-regulation of NF-kappa-B transcription factor activity. Phosphorylation at Ser-311 disrupts the interaction with EHMT1 without preventing monomethylation at Lys-310 and relieves the repression of target genes (By similarity). {ECO:0000250|UniProtKB:Q04207, ECO:0000269|PubMed:21515635}.; PTM: Phosphorylation at Ser-311 disrupts the interaction with EHMT1 and promotes transcription factor activity (By similarity). Phosphorylation on Ser-536 stimulates acetylation on Lys-310 and interaction with CBP; the phosphorylated and acetylated forms show enhanced transcriptional activity. Phosphorylation at Ser-276 by RPS6KA4 and RPS6KA5 promotes its transactivation and transcriptional activities. {ECO:0000250, ECO:0000269|PubMed:10521409, ECO:0000269|PubMed:10938077, ECO:0000269|PubMed:11931769, ECO:0000269|PubMed:12456660, ECO:0000269|PubMed:12628924, ECO:0000269|PubMed:14690596, ECO:0000269|PubMed:15073167, ECO:0000269|PubMed:15516339, ECO:0000269|PubMed:15775976, ECO:0000269|PubMed:16046471, ECO:0000269|PubMed:16135789, ECO:0000269|PubMed:16407239, ECO:0000269|PubMed:17000776, ECO:0000269|PubMed:19103749}.; PTM: Reversibly acetylated; the acetylation seems to be mediated by CBP, the deacetylation by HDAC3 and SIRT2. Acetylation at Lys-122 enhances DNA binding and impairs association with NFKBIA. Acetylation at Lys-310 is required for full transcriptional activity in the absence of effects on DNA binding and NFKBIA association. Acetylation at Lys-310 promotes interaction with BRD4. Acetylation can also lower DNA-binding and results in nuclear export. Interaction with BRMS1 promotes deacetylation of Lys-310. Lys-310 is deacetylated by SIRT2. {ECO:0000269|PubMed:12419806, ECO:0000269|PubMed:12456660, ECO:0000269|PubMed:16135789, ECO:0000269|PubMed:17000776, ECO:0000269|PubMed:19103749}.; PTM: S-nitrosylation of Cys-38 inactivates the enzyme activity. {ECO:0000250}.; PTM: Sulfhydration at Cys-38 mediates the anti-apoptotic activity by promoting the interaction with RPS3 and activating the transcription factor activity. {ECO:0000250}.; PTM: Sumoylation by PIAS3 negatively regulates DNA-bound activated NF-kappa-B. {ECO:0000269|PubMed:22649547}.; PTM: Proteolytically cleaved within a conserved N-terminus region required for base-specific contact with DNA in a CPEN1-mediated manner, and hence inhibits NF-kappa-B transcriptional activity (PubMed:18212740). {ECO:0000269|PubMed:18212740}.
Signal Peptide
Structure 3D NMR spectroscopy (3); X-ray crystallography (82)
Cross Reference PDB 1NFI; 2LSP; 2O61; 3GUT; 3QXY; 3RC0; 4KV1; 4KV4; 5U4K; 5URN; 6NV2; 6QHL; 6QHM; 6YOW; 6YOX; 6YOY; 6YP2; 6YP3; 6YP8; 6YPL; 6YPY; 6YQ2; 7BI3; 7BIQ; 7BIW; 7BIY; 7BJB; 7BJF; 7BJL; 7BJW; 7BKH; 7NJ9; 7NJB; 7NK3; 7NK5; 7NLA; 7NLE; 7NM1; 7NM3; 7NM9; 7NMH; 7NQP; 7NR7; 7NSV; 7NV4; 7NVI; 7NWS; 7NXS; 7NXT; 7NXW; 7NXY; 7NY4; 7NYE; 7NYF; 7NYG; 7NZ6; 7NZG; 7NZK; 7NZV; 7O34; 7O3A; 7O3F; 7O3P; 7O3Q; 7O3R; 7O3S; 7O57; 7O59; 7O5A; 7O5C; 7O5D; 7O5F; 7O5G; 7O5O; 7O5P; 7O5S; 7O5U; 7O5X; 7O6F; 7O6G; 7O6I; 7O6J; 7O6K; 7O6M; 7O6O;
Mapped Pubmed ID 10066435; 10075690; 10230406; 10321728; 10514424; 10514433; 10593898; 10723127; 10918611; 11114305; 11279134; 11359840; 11591705; 11813986; 11872672; 11922866; 11953203; 11964305; 11980335; 12027803; 12067985; 12080470; 12213807; 12350227; 12377934; 12419817; 12429528; 12493764; 12509469; 12517770; 12559944; 12589049; 12606945; 12606947; 12618429; 12618762; 12651903; 12673201; 12690099; 12700228; 12736262; 12759443; 12767057; 12767944; 12820969; 12829026; 12842894; 12843241; 12881425; 12972607; 14514672; 14523047; 14576841; 14587029; 14593105; 14600158; 14623898; 14624448; 14685242; 14688382; 14711835; 14713228; 14716817; 14966904; 14970236; 15013781; 15016307; 15073170; 15079071; 15113757; 15128824; 15130920; 15140884; 15145317; 15152190; 15155458; 15167972; 15192014; 15200413; 15208311; 15210811; 15246972; 15256061; 15277525; 15337789; 15371334; 15465828; 15484295; 15489227; 15496460; 15498932; 15499023; 15531529; 15543947; 15556937; 15599399; 15611068; 15611276; 15657351; 15671037; 15682491; 15718492; 1574116; 15746428; 15845545; 15849198; 15885892; 15905616; 15913553; 15917220; 15935276; 15970704; 15975999; 15980040; 15988014; 16000401; 16007163; 16034126; 16054042; 16056267; 16081638; 16105840; 16163708; 16186799; 16243805; 16261446; 16280327; 16285952; 16291753; 16322332; 16329838; 16382138; 16407283; 16407467; 16408727; 16410078; 16424027; 16456540; 16497702; 16498455; 16513650; 16524505; 16573520; 16584809; 16608838; 16683270; 16723503; 16728495; 16735506; 16785565; 16806820; 16829531; 16840782; 16875840; 16928747; 16931600; 16940169; 16951195; 16982623; 16998237; 17003035; 17008051; 17011499; 17012367; 17041012; 17047224; 17054067; 17056544; 17070014; 17072321; 17079333; 17085785; 17136479; 17157788; 17158457; 17167080; 17183367; 17196614; 17207971; 17242904; 17255956; 17258784; 17301240; 17317104; 17362989; 17363905; 17374495; 17397830; 17403902; 17452529; 17462920; 17468103; 17478731; 17493236; 17521736; 17525529; 17530443; 17537731; 17548605; 1756723; 17574024; 17576778; 17586618; 17590503; 17595324; 17611696; 17612295; 17617622; 17622249; 17626072; 17631635; 17660862; 17675239; 17692505; 17707233; 17708800; 17709515; 17715045; 17720813; 17882263; 17889033; 17889859; 17904523; 17911635; 17932028; 17932106; 17947640; 17953764; 17956668; 17959673; 17962362; 17962807; 17969521; 17975552; 17982102; 17982104; 17991436; 18021261; 18024283; 18025803; 18034190; 18035048; 18036607; 18037904; 18040287; 18045535; 18056447; 18059344; 18061975; 18062909; 18070609; 18095109; 18163488; 18163503; 18172215; 18174252; 18188593; 18191107; 18191642; 18201972; 18215660; 18227347; 18241676; 18258304; 18276112; 18294642; 18310089; 18314621; 18316612; 18362147; 18362169; 18363837; 18385332; 18411265; 18412279; 18422166; 18424071; 18424438; 18434448; 18439422; 18448430; 18453612; 18461473; 18462924; 18466468; 18477470; 18501560; 18541671; 18550535; 18555777; 18555778; 18598236; 18600306; 18607537; 18621420; 18627520; 18652316; 18657320; 18660489; 18701591; 18701687; 18703796; 18714023; 18720410; 18771813; 18798274; 18823280; 18947494; 18952281; 18981184; 18983609; 18990707; 18991026; 18996613; 19019440; 19038492; 19043589; 19046417; 19060926; 19064727; 19064995; 19066035; 19067848; 19073147; 19087517; 19122653; 19124506; 19124804; 19135383; 19135889; 19140318; 19157506; 19185596; 19197368; 19201871; 19201908; 19262565; 19265173; 19270718; 19285061; 19288477; 19289499; 19296848; 19300393; 19303015; 19309400; 19322197; 19327355; 19339690; 19345327; 19350539; 19351910; 19407977; 19411070; 19422389; 19428110; 19433587; 19448676; 19453840; 19458474; 19483084; 19502777; 19507243; 19520742; 19570822; 19573080; 19587216; 19590578; 19591173; 19591457; 19619938; 19654331; 19662361; 19664333; 19668231; 19683540; 19706715; 19706766; 19734210; 19734226; 19746155; 19751727; 19758175; 19764566; 19773279; 19779021; 19789307; 19800042; 19805069; 19819989; 19860880; 19910110; 19911008; 19912635; 19913121; 19933278; 19940030; 19955102; 19957349; 20001970; 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22261743; 22267217; 22292036; 22302993; 22312446; 22325559; 22330808; 22334708; 22337883; 22348975; 22384180; 22390170; 22397926; 22406367; 22422610; 22485186; 22493284; 22496479; 22525504; 22527100; 22545750; 22558476; 22591684; 22592405; 22593190; 22619232; 22634383; 22645123; 22666431; 22670315; 22688014; 22708120; 22709495; 22715377; 22733812; 22740410; 22748181; 22750558; 22763042; 22768286; 22778400; 22781898; 22797919; 22804476; 22808155; 22809882; 22815798; 22836752; 22842493; 22847000; 22859938; 22892758; 22927901; 22931618; 22948157; 22952718; 22955280; 22964303; 22996371; 23016877; 23027940; 23038213; 23053371; 23054188; 23056468; 23056624; 23064013; 23069812; 23071666; 23077289; 23083102; 23088768; 23100252; 23115242; 23118497; 23134958; 23141142; 23144749; 23150684; 23164673; 23166834; 23174781; 23195252; 23209664; 23219896; 23221171; 23238643; 23239344; 23269273; 23273993; 23281696; 23296075; 23300567; 23318455; 23343403; 23349803; 23383209; 23408313; 23408599; 23408724; 23454417; 23454654; 23455325; 23456480; 23463347; 23467542; 23468625; 23474754; 23482348; 23504993; 23507189; 23510472; 23528368; 23536830; 23541563; 23543150; 23563178; 23563313; 23576453; 23576567; 23583404; 23588592; 23592772; 23593410; 23603903; 23604637; 23618358; 23619300; 23624912; 23628799; 23636254; 23666959; 23686307; 23696745; 23708311; 23708964; 23712703; 23715780; 23716661; 23734002; 23776612; 23784084; 23797602; 23812431; 23824799; 23839035; 23850221; 23860225; 23874387; 23904479; 23936501; 23940701; 23963448; 23975427; 24012639; 24019758; 24023820; 24036988; 24039253; 24042437; 24042463; 2405250; 24056880; 24059932; 24063540; 24067962; 24096876; 24118362; 24127926; 24140080; 24152492; 24155403; 24175631; 24216290; 24237301; 24248603; 24276753; 24286317; 24302727; 24308961; 24321067; 24337575; 24338024; 24340014; 24343129; 24349042; 24371075; 24386331; 24413684; 24418562; 24442433; 24454965; 24457201; 24469051; 24512908; 24518172; 24550391; 24562983; 24572994; 24574500; 24582884; 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27329558; 27349797; 27420986; 27427981; 27431814; 27434861; 27435858; 27466442; 27491820; 27492973; 27521929; 27524613; 27543462; 27574108; 27616356; 27619660; 27630163; 27633352; 27666165; 27667468; 27667548; 27673408; 27679575; 27686451; 27701768; 27706678; 27711077; 27721021; 27752889; 27754829; 27793942; 27798157; 27811358; 27837435; 27846267; 27864353; 27878697; 27902962; 27907201; 27973541; 27976481; 27994064; 28007956; 28039454; 28039461; 28077651; 28089769; 28099441; 28100608; 28105499; 28107185; 28122293; 28129604; 28153721; 28159925; 28219695; 28249778; 28283022; 28295567; 28298643; 28317833; 28334776; 28347237; 28358376; 28362429; 28364380; 28378844; 28381553; 28407300; 28416608; 28418896; 28423685; 28423737; 28440494; 28465487; 28466782; 28537665; 28545028; 28548219; 28569771; 28590547; 28600541; 28629334; 28629477; 28646109; 28653238; 28653898; 28675108; 28681591; 28687276; 28696292; 28762199; 28766683; 28772241; 28817833; 28825294; 28831588; 28844984; 28849713; 28859166; 28923839; 28990087; 29017500; 29024797; 29038521; 29039556; 29041983; 29059172; 29074539; 29088737; 29088783; 29115381; 29115409; 29181822; 29189925; 29207489; 29212169; 29251177; 29285221; 29311624; 29331583; 29336610; 29352261; 29363879; 29378189; 29388696; 29428966; 29463681; 29467405; 29525603; 29532994; 29567473; 29592948; 29601651; 29616186; 29622796; 29644893; 29666362; 29673591; 29708732; 29748061; 29748238; 29748881; 29749134; 29750422; 29767266; 29770869; 29784872; 29785588; 29786670; 29867198; 29891820; 29911313; 29916542; 29959281; 29968158; 29980758; 30029010; 30049795; 30057418; 30076618; 30079603; 30104883; 30119172; 30135182; 30140708; 30166344; 30211233; 30219682; 30221732; 30248551; 30293016; 30300821; 30304001; 30320402; 30325077; 30338926; 30362505; 30375448; 30387173; 30496749; 30527665; 30553016; 30562971; 30619335; 30622239; 30628021; 30646812; 30653501; 30659266; 30670829; 30704857; 30717343; 30717434; 30766526; 30798416; 30808715; 30814284; 30825051; 30828266; 30937967; 30946927; 30978403; 30980866; 30983127; 30989475; 30992075; 30995931; 31001962; 31005254; 31026442; 31054328; 31092435; 31128029; 31130368; 31197122; 31222140; 31229617; 31242600; 31262971; 31265453; 31266502; 31281309; 3129195; 31299491; 31308481; 31322430; 31337264; 31351496; 31363150; 31364735; 31391462; 31393268; 31415393; 31425554; 31427673; 31484794; 31510045; 31527064; 31545447; 31561304; 31564074; 31572379; 31580526; 31582729; 31606566; 31626638; 31626775; 31626956; 31636124; 31636182; 31652441; 31676369; 31698141; 31709256; 31723122; 31724445; 31730277; 31759055; 31819048; 31885575; 31906441; 31918570; 31964911; 31992226; 31999475; 32003539; 32015337; 32038638; 32060423; 32124932; 32183905; 32187412; 32199621; 32207045; 32209106; 32217689; 32240617; 32251485; 32277133; 32319559; 32325032; 32364285; 32386462; 32450513; 32455851; 32477319; 32501683; 32502356; 32512041; 32514758; 32546717; 32575582; 32657001; 32737283; 32753387; 32754266; 32816380; 32894380; 32908186; 32945499; 33038311; 33060567; 33067267; 33126183; 33143574; 33166679; 33279869; 33309857; 33323971; 33414434; 33417952; 33420370; 33438746; 33446690; 33459422; 33486415; 33502650; 33512636; 33515544; 33536546; 33579825; 33617838; 33685520; 33710605; 33754052; 33760140; 33791306; 33805981; 33857149; 33859619; 33895704; 34047554; 34076416; 34155144; 34216805; 34405442; 34419501; 34807912; 7479848; 7479976; 7531665; 7557387; 7575604; 7628694; 7651415; 7809113; 7831327; 7862124; 7957109; 8021507; 8234276; 8246997; 8413215; 8413306; 8550590; 8601309; 8617720; 8754811; 8999548; 9065481; 9120310; 9121587; 9135156; 9150141; 9252186; 9362451; 9660950; 9721103; 9792644; 9831247; 9859996; 9914500; 9990852; 9990853;
Motif MOTIF 301..304; /note=Nuclear localization signal; /evidence=ECO:0000255; MOTIF 536..544; /note=9aaTAD; /evidence=ECO:0000255
Gene Encoded By
Mass 60,219
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda