Detail Information for IndEnz0002002504
IED ID IndEnz0002002504
Enzyme Type ID protease002504
Protein Name Serine/threonine-protein kinase LMTK2
EC 2.7.11.1
Apoptosis-associated tyrosine kinase 2
Brain-enriched kinase
hBREK
CDK5/p35-regulated kinase
CPRK
Kinase/phosphatase/inhibitor 2
Lemur tyrosine kinase 2
Serine/threonine-protein kinase KPI-2
Gene Name LMTK2 AATYK2 BREK KIAA1079 KPI2 LMR2
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 MPGPPALRRRLLLLLLVLLIAGSAGAAPLPQTGAGEAPPAAEVSSSFVILCVCSLIILIVLIANCVSCCKDPEIDFKEFEDNFDDEIDFTPPAEDTPSVQSPAEVFTLSVPNISLPAPSQFQPSVEGLKSQVARHSLNYIQEIGNGWFGKVLLGEIYTGTSVARVIVKELKASANPKEQDTFLKNGEPYYILQHPNILQCVGQCVEAIPYLLVFEFCDLGDLKAYLRSEQEHMRGDSQTMLLQRMACEVAAGLAAMHKLHFLHSDLALRNCFLTSDLNVKVGDYGIGFSRYKEDYIETDDKKVFPLRWTAPELVTSFQDRLLTADQTKYSNIWSLGVTLWELFDNAAQPYSNLSNLDVLNQVIRERDTKLPKPQLEQPYSDRWYEVLQFCWLSPEKRPAAEDVHRLLTYLRLQSQRDSEVDFEQQWNALKPNTNSRDSSNNAAFPILDHFARDRLGREMEEVLTVTETSQGLSFEYVWEAAKHDHFDERSRGHLDEGLSYTSIFYPVEVFESSLSDPGPGKQDDSGQDVPLRVPGVVPVFDAHNLSVGSDYYIQLEEKSGSNLELDYPPALLTTDMDNPERTGPELSQLTALRSVELEESSTDEDFFQSSTDPKDSSLPGDLHVTSGPESPFNNIFNDVDKSEDLPSHQKIFDLMELNGVQADFKPATLSSSLDNPKESVITGHFEKEKPRKIFDSEPLCLSDNLMHQDNFDPLNVQELSENFLFLQEKNLLKGSLSSKEHINDLQTELKNAGFTEAMLETSCRNSLDTELQFAENKPGLSLLQENVSTKGDDTDVMLTGDTLSTSLQSSPEVQVPPTSFETEETPRRVPPDSLPTQGETQPTCLDVIVPEDCLHQDISPDAVTVPVEILSTDARTHSLDNRSQDSPGESEETLRLTESDSVLADDILASRVSVGSSLPELGQELHNKPFSEDHHSHRRLEKNLEAVETLNQLNSKDAAKEAGLVSALSSDSTSQDSLLEDSLSAPFPASEPSLETPDSLESVDVHEALLDSLGSHTPQKLVPPDKPADSGYETENLESPEWTLHPAPEGTADSEPATTGDGGHSGLPPNPVIVISDAGDGHRGTEVTPETFTAGSQGSYRDSAYFSDNDSEPEKRSEEVPGTSPSALVLVQEQPLPEPVLPEQSPAAQDSCLEARKSQPDESCLSALHNSSDLELRATPEPAQTGVPQQVHPTEDEASSPWSVLNAELSSGDDFETQDDRPCTLASTGTNTNELLAYTNSALDKSLSSHSEGPKLKEPDIEGKYLGKLGVSGMLDLSEDGMDADEEDENSDDSDEDLRAFNLHSLSSESEDETEHPVPIILSNEDGRHLRSLLKPTAANAPDPLPEDWKKEKKAVTFFDDVTVYLFDQETPTKELGPCGGEACGPDLSGPAPASGSPYLSRCINSESSTDEEGGGFEWDDDFSPDPFMSKTTSNLLSSKPSLQTSKYFSPPPPARSTEQSWPHSAPYSRFSISPANIASFSLTHLTDSDIEQGGSSEDGEKD
Enzyme Length 1503
Uniprot Accession Number Q8IWU2
Absorption
Active Site ACT_SITE 265; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028"
Activity Regulation
Binding Site BINDING 168; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00159
Calcium Binding
catalytic Activity 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; 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;
DNA Binding
EC Number 2.7.11.1
Enzyme Function FUNCTION: Phosphorylates PPP1C, phosphorylase b and CFTR.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 143..151; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00159
Features Active site (1); Binding site (1); Chain (1); Compositional bias (7); Domain (1); Erroneous initiation (1); Modified residue (11); Natural variant (13); Nucleotide binding (1); Region (7); Sequence conflict (3); Topological domain (3); Transmembrane (2)
Keywords ATP-binding;Kinase;Membrane;Nucleotide-binding;Phosphoprotein;Reference proteome;Serine/threonine-protein kinase;Transferase;Transmembrane;Transmembrane helix
Interact With P36873; P41236
Induction
Subcellular Location SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:23114966}; Multi-pass membrane protein {ECO:0000269|PubMed:23114966}.
Modified Residue MOD_RES 805; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q3TYD6; MOD_RES 806; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q3TYD6; MOD_RES 886; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:23186163; MOD_RES 1107; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:23186163; MOD_RES 1305; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q3TYD6; MOD_RES 1307; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q3TYD6; MOD_RES 1308; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q3TYD6; MOD_RES 1310; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q3TYD6; MOD_RES 1450; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:23186163; MOD_RES 1496; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q3TYD6; MOD_RES 1497; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q3TYD6
Post Translational Modification PTM: Autophosphorylated. Phosphorylated (By similarity). {ECO:0000250}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12832520; 16428298; 18029400; 18264097; 18429820; 18794092; 19318432; 19366831; 19423541; 19549807; 19855435; 19866473; 19900942; 19902474; 20450899; 20460480; 20564319; 20569440; 20878950; 21071540; 21382349; 22220831; 24366813; 24727471; 26008968; 26496610; 26559041; 28040547; 31395338; 31722712; 31748522;
Motif
Gene Encoded By
Mass 164,900
Kinetics
Metal Binding
Rhea ID RHEA:17989; RHEA:46608
Cross Reference Brenda