IED Industry Enzyme Database

Detail Information for IndEnz0017000030
IED ID IndEnz0017000030
Enzyme Type ID manganese peroxidase000030
Protein Name Leucine-rich repeat serine/threonine-protein kinase 2
EC 2.7.11.1
EC 3.6.5.-
Dardarin
Gene Name LRRK2 PARK8
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 MASGSCQGCEEDEETLKKLIVRLNNVQEGKQIETLVQILEDLLVFTYSERASKLFQGKNIHVPLLIVLDSYMRVASVQQVGWSLLCKLIEVCPGTMQSLMGPQDVGNDWEVLGVHQLILKMLTVHNASVNLSVIGLKTLDLLLTSGKITLLILDEESDIFMLIFDAMHSFPANDEVQKLGCKALHVLFERVSEEQLTEFVENKDYMILLSALTNFKDEEEIVLHVLHCLHSLAIPCNNVEVLMSGNVRCYNIVVEAMKAFPMSERIQEVSCCLLHRLTLGNFFNILVLNEVHEFVVKAVQQYPENAALQISALSCLALLTETIFLNQDLEEKNENQENDDEGEEDKLFWLEACYKALTWHRKNKHVQEAACWALNNLLMYQNSLHEKIGDEDGHFPAHREVMLSMLMHSSSKEVFQASANALSTLLEQNVNFRKILLSKGIHLNVLELMQKHIHSPEVAESGCKMLNHLFEGSNTSLDIMAAVVPKILTVMKRHETSLPVQLEALRAILHFIVPGMPEESREDTEFHHKLNMVKKQCFKNDIHKLVLAALNRFIGNPGIQKCGLKVISSIVHFPDALEMLSLEGAMDSVLHTLQMYPDDQEIQCLGLSLIGYLITKKNVFIGTGHLLAKILVSSLYRFKDVAEIQTKGFQTILAILKLSASFSKLLVHHSFDLVIFHQMSSNIMEQKDQQFLNLCCKCFAKVAMDDYLKNVMLERACDQNNSIMVECLLLLGADANQAKEGSSLICQVCEKESSPKLVELLLNSGSREQDVRKALTISIGKGDSQIISLLLRRLALDVANNSICLGGFCIGKVEPSWLGPLFPDKTSNLRKQTNIASTLARMVIRYQMKSAVEEGTASGSDGNFSEDVLSKFDEWTFIPDSSMDSVFAQSDDLDSEGSEGSFLVKKKSNSISVGEFYRDAVLQRCSPNLQRHSNSLGPIFDHEDLLKRKRKILSSDDSLRSSKLQSHMRHSDSISSLASEREYITSLDLSANELRDIDALSQKCCISVHLEHLEKLELHQNALTSFPQQLCETLKSLTHLDLHSNKFTSFPSYLLKMSCIANLDVSRNDIGPSVVLDPTVKCPTLKQFNLSYNQLSFVPENLTDVVEKLEQLILEGNKISGICSPLRLKELKILNLSKNHISSLSENFLEACPKVESFSARMNFLAAMPFLPPSMTILKLSQNKFSCIPEAILNLPHLRSLDMSSNDIQYLPGPAHWKSLNLRELLFSHNQISILDLSEKAYLWSRVEKLHLSHNKLKEIPPEIGCLENLTSLDVSYNLELRSFPNEMGKLSKIWDLPLDELHLNFDFKHIGCKAKDIIRFLQQRLKKAVPYNRMKLMIVGNTGSGKTTLLQQLMKTKKSDLGMQSATVGIDVKDWPIQIRDKRKRDLVLNVWDFAGREEFYSTHPHFMTQRALYLAVYDLSKGQAEVDAMKPWLFNIKARASSSPVILVGTHLDVSDEKQRKACMSKITKELLNKRGFPAIRDYHFVNATEESDALAKLRKTIINESLNFKIRDQLVVGQLIPDCYVELEKIILSERKNVPIEFPVIDRKRLLQLVRENQLQLDENELPHAVHFLNESGVLLHFQDPALQLSDLYFVEPKWLCKIMAQILTVKVEGCPKHPKGIISRRDVEKFLSKKRKFPKNYMSQYFKLLEKFQIALPIGEEYLLVPSSLSDHRPVIELPHCENSEIIIRLYEMPYFPMGFWSRLINRLLEISPYMLSGRERALRPNRMYWRQGIYLNWSPEAYCLVGSEVLDNHPESFLKITVPSCRKGCILLGQVVDHIDSLMEEWFPGLLEIDICGEGETLLKKWALYSFNDGEEHQKILLDDLMKKAEEGDLLVNPDQPRLTIPISQIAPDLILADLPRNIMLNNDELEFEQAPEFLLGDGSFGSVYRAAYEGEEVAVKIFNKHTSLRLLRQELVVLCHLHHPSLISLLAAGIRPRMLVMELASKGSLDRLLQQDKASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNAAIIAKIADYGIAQYCCRMGIKTSEGTPGFRAPEVARGNVIYNQQADVYSFGLLLYDILTTGGRIVEGLKFPNEFDELEIQGKLPDPVKEYGCAPWPMVEKLIKQCLKENPQERPTSAQVFDILNSAELVCLTRRILLPKNVIVECMVATHHNSRNASIWLGCGHTDRGQLSFLDLNTEGYTSEEVADSRILCLALVHLPVEKESWIVSGTQSGTLLVINTEDGKKRHTLEKMTDSVTCLYCNSFSKQSKQKNFLLVGTADGKLAIFEDKTVKLKGAAPLKILNIGNVSTPLMCLSESTNSTERNVMWGGCGTKIFSFSNDFTIQKLIETRTSQLFSYAAFSDSNIITVVVDTALYIAKQNSPVVEVWDKKTEKLCGLIDCVHFLREVMVKENKESKHKMSYSGRVKTLCLQKNTALWIGTGGGHILLLDLSTRRLIRVIYNFCNSVRVMMTAQLGSLKNVMLVLGYNRKNTEGTQKQKEIQSCLTVWDINLPHEVQNLEKHIEVRKELAEKMRRTSVE
Enzyme Length 2527
Uniprot Accession Number Q5S007
Absorption
Active Site ACT_SITE 1994; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027"
Activity Regulation ACTIVITY REGULATION: Kinase activity is regulated by the GTPase activity of the ROC domain (PubMed:29212815, PubMed:18230735). GTP-bound LLRK2 kinase activity is stimulated by RAB29 (PubMed:29212815). Inhibited by small molecule inhibitor MLi-2 (PubMed:26824392, PubMed:29127255). {ECO:0000269|PubMed:18230735, ECO:0000269|PubMed:26824392, ECO:0000269|PubMed:29127255, ECO:0000269|PubMed:29212815}.
Binding Site BINDING 1906; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00159
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:26824392, ECO:0000269|PubMed:28720718, ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:29127255, ECO:0000269|PubMed:29212815, ECO:0000269|PubMed:30398148, ECO:0000269|PubMed:30635421}; CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:26824392, ECO:0000269|PubMed:28720718, ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:29127255, ECO:0000269|PubMed:29212815, ECO:0000269|PubMed:30398148}; CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000269|PubMed:18230735, ECO:0000269|PubMed:26824392, ECO:0000269|PubMed:28720718, ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:29212815};
DNA Binding
EC Number 2.7.11.1; 3.6.5.-
Enzyme Function FUNCTION: Serine/threonine-protein kinase which phosphorylates a broad range of proteins involved in multiple processes such as neuronal plasticity, autophagy, and vesicle trafficking (PubMed:20949042, PubMed:22012985, PubMed:26824392, PubMed:29125462, PubMed:28720718, PubMed:29127255, PubMed:30398148, PubMed:29212815, PubMed:30635421, PubMed:21850687, PubMed:23395371, PubMed:17114044, PubMed:24687852, PubMed:26014385, PubMed:25201882). Is a key regulator of RAB GTPases by regulating the GTP/GDP exchange and interaction partners of RABs through phosphorylation (PubMed:26824392, PubMed:28720718, PubMed:29127255, PubMed:30398148, PubMed:29212815, PubMed:29125462, PubMed:30635421). Phosphorylates RAB3A, RAB3B, RAB3C, RAB3D, RAB5A, RAB5B, RAB5C, RAB8A, RAB8B, RAB10, RAB12, RAB35, and RAB43 (PubMed:26824392, PubMed:28720718, PubMed:29127255, PubMed:30398148, PubMed:29212815, PubMed:29125462, PubMed:30635421, PubMed:23395371). Regulates the RAB3IP-catalyzed GDP/GTP exchange for RAB8A through the phosphorylation of 'Thr-72' on RAB8A (PubMed:26824392). Inhibits the interaction between RAB8A and GDI1 and/or GDI2 by phosphorylating 'Thr-72' on RAB8A (PubMed:26824392). Regulates primary ciliogenesis through phosphorylation of RAB8A and RAB10, which promotes SHH signaling in the brain (PubMed:29125462, PubMed:30398148). Together with RAB29, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose-6-phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner (PubMed:23395371). Regulates neuronal process morphology in the intact central nervous system (CNS) (PubMed:17114044). Plays a role in synaptic vesicle trafficking (PubMed:24687852). Plays an important role in recruiting SEC16A to endoplasmic reticulum exit sites (ERES) and in regulating ER to Golgi vesicle-mediated transport and ERES organization (PubMed:25201882). Positively regulates autophagy through a calcium-dependent activation of the CaMKK/AMPK signaling pathway (PubMed:22012985). The process involves activation of nicotinic acid adenine dinucleotide phosphate (NAADP) receptors, increase in lysosomal pH, and calcium release from lysosomes (PubMed:22012985). Phosphorylates PRDX3 (PubMed:21850687). By phosphorylating APP on 'Thr-743', which promotes the production and the nuclear translocation of the APP intracellular domain (AICD), regulates dopaminergic neuron apoptosis (PubMed:28720718). Independent of its kinase activity, inhibits the proteosomal degradation of MAPT, thus promoting MAPT oligomerization and secretion (PubMed:26014385). In addition, has GTPase activity via its Roc domain which regulates LRRK2 kinase activity (PubMed:18230735, PubMed:26824392, PubMed:29125462, PubMed:28720718, PubMed:29212815). {ECO:0000269|PubMed:17114044, ECO:0000269|PubMed:18230735, ECO:0000269|PubMed:20949042, ECO:0000269|PubMed:21850687, ECO:0000269|PubMed:22012985, ECO:0000269|PubMed:23395371, ECO:0000269|PubMed:24687852, ECO:0000269|PubMed:25201882, ECO:0000269|PubMed:26014385, ECO:0000269|PubMed:26824392, ECO:0000269|PubMed:28720718, ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:29127255, ECO:0000269|PubMed:29212815, ECO:0000269|PubMed:30398148, ECO:0000269|PubMed:30635421}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 1341..1348; /note="GTP"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00758, ECO:0000269|PubMed:18230735"; NP_BIND 1885..1893; /note="ATP"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; NP_BIND 2098..2121; /note="GTP"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"; NP_BIND 2295..2298; /note="GTP"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
Features Active site (1); Beta strand (81); Binding site (1); Chain (1); Coiled coil (1); Domain (2); Helix (71); Modified residue (6); Mutagenesis (29); Natural variant (58); Nucleotide binding (4); Region (1); Repeat (19); Sequence conflict (1); Turn (28)
Keywords 3D-structure;ATP-binding;Autophagy;Cell junction;Cell projection;Coiled coil;Cytoplasmic vesicle;Differentiation;Disease variant;Endoplasmic reticulum;Endosome;GTP-binding;GTPase activation;Golgi apparatus;Hydrolase;Kinase;Leucine-rich repeat;Lysosome;Membrane;Mitochondrion;Mitochondrion outer membrane;Neurodegeneration;Nucleotide-binding;Parkinson disease;Parkinsonism;Phosphoprotein;Reference proteome;Repeat;Serine/threonine-protein kinase;Synapse;Transferase;WD repeat
Interact With Q9UKV8; O43865; P31749; Q8N8V4; O00203; Q8N6T3-2; Q14155; O95816; O95817; Q9UL15; P10415-1; Q13191; Q16543; P60953; Q9UKI2; Q9Y6A4; P05060; P48729-1; P48730-2; Q9NWM3; P53355; Q05193; O00429; O00429-3; O14640-2; O14641; Q92997; P30084; Q05639; Q13158; O14976; P49841; P11142; Q71RC2; Q4G0J3; P07195; O75581; Q38SD2; Itself; P46821; P46734; P52564; O14733; P10636-2; P10636-8; P42679; O95140; P49406; P26038; Q7L592; Q96PY6; Q13469; Q8WUM0; O60313; Q9NQU5; P62136; Q12972; P63151; P30048; P17612; O60260; P61026; Q6IQ22; Q9H0U4; O14966; Q13637; P57729; P61020; P61006; P63000; P41220; P62906; P26373; P50914; P62750; P62888; P49207; Q9BUL9; P62280; P62277; P62841; P62249; P62269; P15880; P60866; P62266; P42677; P23396; O15027; P60896; P31947; Q99961; Q99962; P12235; P05141; P12236; O95295; P37840; Q8NHS9; Q13501; Q9UNE7; Q9UNE7-1; Q9BQ70; Q6P3X3; P07437; Q13885; P04350; P68371; Q9BUF5; Q53GS9; P21796; Q9Y6I7; P31946; P62258; P61981; Q04917; P27348; P63104; O95218; Q62848; O55143; P30275; P39053; P02687; Q811U4; P00634; P12369; Q63481; P61021; Q58A65; Q9WUD1; P61983
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000269|PubMed:16321986, ECO:0000269|PubMed:16352719, ECO:0000269|PubMed:26014385}. Perikaryon {ECO:0000269|PubMed:17120249}. Golgi apparatus membrane {ECO:0000269|PubMed:16321986, ECO:0000269|PubMed:23395371}; Peripheral membrane protein {ECO:0000269|PubMed:16321986}. Cell projection, axon {ECO:0000269|PubMed:17120249}. Cell projection, dendrite {ECO:0000269|PubMed:17120249, ECO:0000269|PubMed:21850687}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16321986, ECO:0000269|PubMed:25201882}; Peripheral membrane protein {ECO:0000269|PubMed:16321986}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:24687852}. Endosome {ECO:0000250|UniProtKB:Q5S006}. Lysosome {ECO:0000269|PubMed:17120249}. Mitochondrion outer membrane {ECO:0000269|PubMed:16269541, ECO:0000269|PubMed:16321986, ECO:0000269|PubMed:17120249, ECO:0000269|PubMed:29212815}; Peripheral membrane protein {ECO:0000269|PubMed:16269541, ECO:0000269|PubMed:16321986, ECO:0000269|PubMed:17120249, ECO:0000269|PubMed:29212815}. Note=Colocalized with RAB29 along tubular structures emerging from Golgi apparatus (PubMed:23395371). Localizes to endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER) (PubMed:25201882). {ECO:0000269|PubMed:23395371, ECO:0000269|PubMed:25201882}.
Modified Residue MOD_RES 910; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:28202711, ECO:0000269|PubMed:28720718, ECO:0000269|PubMed:29212815"; MOD_RES 935; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:28202711, ECO:0000269|PubMed:28720718, ECO:0000269|PubMed:29127255, ECO:0000269|PubMed:29212815, ECO:0000269|PubMed:30635421"; MOD_RES 955; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:28202711, ECO:0000269|PubMed:29212815"; MOD_RES 973; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:28202711, ECO:0000269|PubMed:29212815"; MOD_RES 1292; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:29212815, ECO:0000269|PubMed:30635421"; MOD_RES 1444; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:28202711"
Post Translational Modification PTM: Autophosphorylated (PubMed:28202711, PubMed:28720718, PubMed:29127255, PubMed:29212815, PubMed:30635421). Phosphorylation of Ser-910 and either Ser-935 or Ser-1444 facilitates interaction with YWHAG (PubMed:28202711). Phosphorylation of Ser-910 and/or Ser-935 facilitates interaction with SFN (PubMed:28202711). {ECO:0000269|PubMed:28202711, ECO:0000269|PubMed:28720718, ECO:0000269|PubMed:29127255, ECO:0000269|PubMed:29212815, ECO:0000269|PubMed:30635421}.
Signal Peptide
Structure 3D Electron microscopy (8); X-ray crystallography (9)
Cross Reference PDB 2ZEJ; 3D6T; 5MY9; 5MYC; 6DLO; 6DLP; 6OJE; 6OJF; 6VNO; 6VP6; 6VP7; 6XAF; 6XR4; 7LHT; 7LHW; 7LI3; 7LI4;
Mapped Pubmed ID 11891824; 14691730; 15884041; 15955578; 15955629; 16102903; 16115731; 16145815; 16149095; 16254973; 16269443; 16275903; 16436781; 16436782; 16437559; 16467219; 16511860; 16602113; 16614029; 16616379; 16622854; 16622859; 16632201; 16633828; 16643318; 16671078; 16728648; 16750377; 16750929; 16758483; 16781064; 16817197; 16822348; 16865326; 16928343; 16939701; 16966498; 16966501; 16966502; 16991141; 17017533; 17017534; 17020475; 17044089; 17050822; 17052850; 17060595; 17078063; 17080443; 17083102; 17097110; 17115391; 17116211; 17149721; 17151837; 17160203; 17179858; 17187665; 17215492; 17216639; 17222106; 17222580; 17225181; 17230458; 17235449; 17253937; 17260967; 17314670; 17324517; 17335904; 17341485; 17352347; 17353388; 17377919; 17385669; 17388990; 17394548; 17395370; 17400507; 17409193; 17419834; 17427941; 17433753; 17440812; 17447891; 17469194; 17470139; 17482357; 17512502; 17523199; 17540608; 17584768; 17596714; 17611037; 17614198; 17622782; 17625107; 17639429; 17659642; 17706965; 17720280; 17803032; 17803033; 17804834; 17846883; 17868389; 17880562; 17914064; 17938369; 17960808; 17971075; 17978862; 17999435; 18045479; 18097165; 18097693; 18098275; 18182054; 18197194; 18201193; 18201824; 18211709; 18214993; 18265005; 18272292; 18316234; 18322385; 18322396; 18337586; 18338801; 18353371; 18367605; 18378882; 18379513; 18397888; 18412265; 18434642; 18435766; 18445495; 18450497; 18464276; 18484993; 18486522; 18523722; 18523869; 18539534; 18539535; 18541113; 18544747; 18556235; 18587394; 18602856; 18617409; 18621566; 18634852; 18644660; 18665323; 18666856; 18675914; 18704525; 18716801; 18718805; 18752982; 18781329; 18804399; 18805725; 18809839; 18848304; 18923807; 18927607; 18936941; 18952485; 18973254; 18973807; 18980856; 18981379; 18986508; 19006185; 19020907; 19021752; 19025767; 19029519; 19041274; 19065525; 19076219; 19172321; 19176810; 19196961; 19204172; 19205068; 19224617; 19283415; 19302196; 19308469; 19330201; 19343804; 19353692; 19357115; 19397894; 19412725; 19458969; 19472409; 19473361; 19489756; 19513331; 19527940; 19535993; 19536328; 19538213; 19545277; 19559761; 19570025; 19576176; 19625296; 19625511; 19640773; 19640926; 19672984; 19680143; 19692353; 19699188; 19712061; 19714762; 19726410; 19733152; 19735093; 19741132; 19756366; 19760754; 19769964; 19770575; 19800393; 19804413; 19822953; 19824698; 19826009; 19833102; 19847307; 19854095; 19878656; 19879329; 19890007; 19912990; 19915575; 19915576; 19945904; 20004703; 20008657; 20018409; 20018961; 20067578; 20074637; 20090955; 20096956; 20108944; 20144646; 20173330; 20182943; 20186690; 20197411; 20197701; 20232069; 20379614; 20382224; 20386743; 20413974; 20443975; 20473834; 20483373; 20506312; 20515039; 20544233; 20571044; 20595391; 20626563; 20629711; 20642453; 20659021; 20659558; 20669299; 20669305; 20671708; 20673920; 20697102; 20711177; 20720502; 20721910; 20721913; 20721916; 20722494; 20727385; 20729864; 20818610; 20818658; 20850369; 20881132; 20921534; 20933457; 20939082; 20969957; 21048939; 21060682; 21072187; 21073465; 21088684; 21115957; 21159540; 21167764; 21168496; 21220347; 21221623; 21234781; 21238487; 21280089; 21307259; 21312285; 21353620; 21362567; 21370995; 21406209; 21449009; 21454543; 21483109; 21494637; 21538529; 21552986; 21611978; 21611983; 21632271; 21641848; 21658387; 21661047; 21676337; 21679126; 21696411; 21698001; 21699405; 21720016; 21738687; 21749573; 21753159; 21753163; 21796139; 21799870; 21806997; 21816655; 21842440; 21857923; 21858031; 21885347; 21898123; 21922152; 21924942; 21954089; 21961647; 21972245; 21983832; 21989859; 22004453; 22038903; 22047502; 22077787; 22080837; 22162019; 22166428; 22204929; 22228096; 22243833; 22251894; 22253261; 22302802; 22303461; 22315971; 22323743; 22342962; 22357653; 22363216; 22393539; 22418733; 22423108; 22433811; 22436655; 22441981; 22445250; 22488887; 22503729; 22525366; 22528366; 22534020; 22567899; 22575062; 22575234; 22594666; 22607035; 22612223; 22639965; 22652643; 22658533; 22669510; 22684232; 22689969; 22703868; 22723946; 22736029; 22773119; 22807999; 22842796; 22899650; 22914834; 22952710; 22981185; 22988861; 22988862; 22988863; 22988865; 22988866; 22988867; 22988868; 22988870; 22988872; 22988873; 22988874; 22988875; 22988877; 22988878; 22988879; 22988880; 22988882; 22998870; 23055502; 23074843; 23075850; 23082216; 23115130; 23125283; 23182315; 23183827; 23220480; 23227859; 23241358; 23241745; 23250886; 23268655; 23300640; 23318930; 23325906; 23357204; 23379419; 23389884; 23421816; 23455607; 23507417; 23531835; 23588498; 23624603; 23628791; 23664753; 23726462; 23764467; 23771111; 23813973; 23820587; 23824357; 23842774; 23886663; 23895867; 23913756; 23916833; 23924436; 23932063; 23937259; 23937295; 23938341; 23938344; 23949442; 23963289; 23967090; 24015287; 24018986; 24040382; 24046064; 24080176; 24095219; 24113872; 24123150; 24148854; 24165324; 24167564; 24211199; 24243757; 24251413; 24262189; 24275654; 24282027; 24326068; 24339985; 24351927; 24357540; 24360742; 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Motif
Gene Encoded By
Mass 286,103
Kinetics
Metal Binding
Rhea ID RHEA:46608; RHEA:17989; RHEA:19669
Cross Reference Brenda