| IED ID | IndEnz0002007108 |
| Enzyme Type ID | protease007108 |
| Protein Name |
Axin-2 Axin-like protein Axil Axis inhibition protein 2 Conductin |
| Gene Name | AXIN2 |
| 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 | MSSAMLVTCLPDPSSSFREDAPRPPVPGEEGETPPCQPGVGKGQVTKPMPVSSNTRRNEDGLGEPEGRASPDSPLTRWTKSLHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDTKTLRVAKAIYKRYIENNSIVSKQLKPATKTYIRDGIKKQQIDSIMFDQAQTEIQSVMEENAYQMFLTSDIYLEYVRSGGENTAYMSNGGLGSLKVVCGYLPTLNEEEEWTCADFKCKLSPTVVGLSSKTLRATASVRSTETVDSGYRSFKRSDPVNPYHIGSGYVFAPATSANDSEISSDALTDDSMSMTDSSVDGIPPYRVGSKKQLQREMHRSVKANGQVSLPHFPRTHRLPKEMTPVEPATFAAELISRLEKLKLELESRHSLEERLQQIREDEEREGSELTLNSREGAPTQHPLSLLPSGSYEEDPQTILDDHLSRVLKTPGCQSPGVGRYSPRSRSPDHHHHHHSQYHSLLPPGGKLPPAAASPGACPLLGGKGFVTKQTTKHVHHHYIHHHAVPKTKEEIEAEATQRVHCFCPGGSEYYCYSKCKSHSKAPETMPSEQFGGSRGSTLPKRNGKGTEPGLALPAREGGAPGGAGALQLPREEGDRSQDVWQWMLESERQSKPKPHSAQSTKKAYPLESARSSPGERASRHHLWGGNSGHPRTTPRAHLFTQDPAMPPLTPPNTLAQLEEACRRLAEVSKPPKQRCCVASQQRDRNHSATVQTGATPFSNPSLAPEDHKEPKKLAGVHALQASELVVTYFFCGEEIPYRRMLKAQSLTLGHFKEQLSKKGNYRYYFKKASDEFACGAVFEEIWEDETVLPMYEGRILGKVERID |
| Enzyme Length | 843 |
| Uniprot Accession Number | Q9Y2T1 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Inhibitor of the Wnt signaling pathway. Down-regulates beta-catenin. Probably facilitate the phosphorylation of beta-catenin and APC by GSK3B. {ECO:0000250|UniProtKB:O15169}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (4); Domain (2); Motif (1); Natural variant (1); Region (7); Sequence conflict (5) |
| Keywords | ADP-ribosylation;Cytoplasm;Developmental protein;Phosphoprotein;Reference proteome;Ubl conjugation;Wnt signaling pathway |
| Interact With | Q8N944; A2BDD9; Q9BXS5; Q99728; Q9Y297; Q13895; Q2NKX9; Q9Y6W3; Q8NEF3-2; Q9UKJ5; O75638-2; P35222; Q2TBE0; Q14241; Q3B820; P09067; Q9BVG8-5; P60014; P60410; Q9BYR2; Q9BYQ4; Q8TBB1; Q96EZ8; P53350; P62714; Q15172; P49721; Q9BWG6; O75558; Q15560; Q8N8B7-2; Q15583; O95985; Q9BZW7; P40222; Q8N3L3; Q15973; Q8TAU3; Q96SQ5; Q5T619 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21383061}. |
| Modified Residue | |
| Post Translational Modification | PTM: Probably phosphorylated by GSK3B and dephosphorylated by PP2A. {ECO:0000250|UniProtKB:O15169}.; PTM: ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination and subsequent activation of the Wnt signaling pathway. {ECO:0000269|PubMed:21383061}.; PTM: Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its degradation and subsequent activation of the Wnt signaling pathway. Deubiquitinated by USP34, deubiquitinated downstream of beta-catenin stabilization step: deubiquitination is important Wnt signaling to positively regulate beta-catenin (CTNBB1)-mediated transcription. {ECO:0000269|PubMed:21383061}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10698523; 11809808; 11809809; 11940574; 15611123; 15766563; 16247484; 16432638; 16884355; 16941501; 17072303; 17143297; 17373666; 17923689; 17927870; 18330950; 18372914; 18384130; 18676680; 18683894; 18708403; 18755497; 18790474; 19065536; 19119171; 19125156; 19170196; 19270026; 19571879; 19584075; 19623616; 19625176; 19692168; 19816326; 19888426; 20056645; 20300119; 20403997; 20453000; 20508983; 20613673; 20635389; 20844743; 20858899; 21069480; 21294210; 21304492; 21541676; 21626677; 21666490; 21706018; 21733995; 21799911; 22322943; 22370446; 22440753; 22682247; 22745173; 22887353; 23144924; 23169889; 23393221; 23455922; 23516639; 23602568; 23624843; 23702820; 23838596; 24008843; 24166197; 24251807; 24299953; 24412244; 24484320; 24554542; 24581859; 24964857; 25091576; 25380820; 25873176; 25974148; 26025668; 26191213; 26252180; 26337638; 26406231; 26438599; 26514524; 26572152; 26617789; 26648507; 26715268; 26771938; 26905812; 27188720; 27228364; 28043155; 28107521; 28378643; 28694128; 28759178; 28783177; 28939076; 29114927; 29211286; 29307822; 30088857; 30671715; 30760879; 30825095; 31038806; 31063404; 31268379; 31534175; 31781599; 32184411; 32553184; 32575385; 33096676; 33523480; 33794810; 33811251; 34281460; 34309414; 34452579; |
| Motif | MOTIF 21..30; /note=Tankyrase-binding motif |
| Gene Encoded By | |
| Mass | 93,568 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |