TRPM7_MOUSE
ID TRPM7_MOUSE Reviewed; 1863 AA.
AC Q923J1; A2AI58; Q8C7S7; Q8CE54; Q921Y5; Q925B2; Q9CUT2; Q9JLQ1;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Transient receptor potential cation channel subfamily M member 7;
DE EC=2.7.11.1;
DE AltName: Full=Channel-kinase 1;
DE AltName: Full=Long transient receptor potential channel 7;
DE Short=LTrpC-7;
DE Short=LTrpC7;
DE AltName: Full=Transient receptor potential-phospholipase C-interacting kinase;
DE Short=TRP-PLIK;
GN Name=Trpm7; Synonyms=Chak, Ltrpc7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND FUNCTION.
RX PubMed=11385574; DOI=10.1038/35079092;
RA Nadler M.J.S., Hermosura M.C., Inabe K., Perraud A.-L., Zhu Q.,
RA Stokes A.J., Kurosaki T., Kinet J.-P., Penner R., Scharenberg A.M.,
RA Fleig A.;
RT "LTRPC7 is a Mg.ATP-regulated divalent cation channel required for cell
RT viability.";
RL Nature 411:590-595(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, PHOSPHORYLATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF GLY-1797; CYS-1810 AND CYS-1813.
RC STRAIN=BALB/cJ;
RX PubMed=11161216; DOI=10.1126/science.1058519;
RA Runnels L.W., Yue L., Clapham D.E.;
RT "TRP-PLIK, a bifunctional protein with kinase and ion channel activities.";
RL Science 291:1043-1047(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Matsushita M.;
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-372; 632-1146 AND 1243-1863.
RC STRAIN=C57BL/6J; TISSUE=Head, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1687-1863.
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1502, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1255 AND SER-1445, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP PHOSPHORYLATION AT SER-1224; SER-1300; SER-1385; SER-1386; THR-1404;
RP THR-1466; SER-1498; SER-1567; SER-1846 AND SER-1849.
RX PubMed=22222377; DOI=10.1016/j.bbrc.2011.12.085;
RA Kim T.Y., Shin S.K., Song M.Y., Lee J.E., Park K.S.;
RT "Identification of the phosphorylation sites on intact TRPM7 channels from
RT mammalian cells.";
RL Biochem. Biophys. Res. Commun. 417:1030-1034(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1551-1828, COFACTOR, AND SUBUNIT.
RX PubMed=11389851; DOI=10.1016/s1097-2765(01)00256-8;
RA Yamaguchi H., Matsushita M., Nairn A.C., Kuriyan J.;
RT "Crystal structure of the atypical protein kinase domain of a TRP channel
RT with phosphotransferase activity.";
RL Mol. Cell 7:1047-1057(2001).
CC -!- FUNCTION: Essential ion channel and serine/threonine-protein kinase.
CC Divalent cation channel permeable to calcium and magnesium. Has a
CC central role in magnesium ion homeostasis and in the regulation of
CC anoxic neuronal cell death. Involved in TNF-induced necroptosis
CC downstream of MLKL by mediating calcium influx. The kinase activity is
CC essential for the channel function. May be involved in a fundamental
CC process that adjusts plasma membrane divalent cation fluxes according
CC to the metabolic state of the cell. Phosphorylates annexin A1 (ANXA1).
CC {ECO:0000269|PubMed:11385574}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:11389851};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:11389851};
CC -!- SUBUNIT: Forms heterodimers with TRPM6. Interacts with PLCB1 (By
CC similarity). Homodimer. {ECO:0000250, ECO:0000269|PubMed:11389851}.
CC -!- INTERACTION:
CC Q923J1; P60710: Actb; NbExp=2; IntAct=EBI-8010314, EBI-353957;
CC Q923J1; Q3U1J4: Ddb1; NbExp=2; IntAct=EBI-8010314, EBI-2552275;
CC Q923J1; Q8VDD5: Myh9; NbExp=4; IntAct=EBI-8010314, EBI-400906;
CC Q923J1; O00571: DDX3X; Xeno; NbExp=2; IntAct=EBI-8010314, EBI-353779;
CC Q923J1; Q8N488: RYBP; Xeno; NbExp=3; IntAct=EBI-8010314, EBI-752324;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Found to be expressed in brain and skeletal muscle,
CC with stronger signals in kidney, heart, liver and spleen.
CC {ECO:0000269|PubMed:11161216}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:11161216,
CC ECO:0000269|PubMed:22222377}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC superfamily. Alpha-type protein kinase family. ALPK subfamily.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the transient
CC receptor (TC 1.A.4) family. LTrpC subfamily. TRPM7 sub-subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY032951; AAK50377.1; -; mRNA.
DR EMBL; AF376052; AAK57433.1; -; mRNA.
DR EMBL; AF149013; AAF73131.1; -; mRNA.
DR EMBL; AL732330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK049329; BAC33685.1; -; mRNA.
DR EMBL; AK029000; BAC26234.1; -; mRNA.
DR EMBL; AK014698; BAB29509.1; -; mRNA.
DR EMBL; BC009137; AAH09137.1; -; mRNA.
DR CCDS; CCDS16689.1; -.
DR RefSeq; NP_001157797.1; NM_001164325.1.
DR RefSeq; NP_067425.2; NM_021450.2.
DR PDB; 1IA9; X-ray; 2.00 A; A/B=1549-1828.
DR PDB; 1IAH; X-ray; 2.40 A; A/B=1549-1828.
DR PDB; 1IAJ; X-ray; 2.80 A; A/B=1549-1828.
DR PDB; 5ZX5; EM; 3.28 A; A/B/C/D=2-1230.
DR PDB; 6BWD; EM; 3.70 A; A/B/C/D=467-1300.
DR PDB; 6BWF; EM; 4.10 A; A/B/C/D=467-1300.
DR PDBsum; 1IA9; -.
DR PDBsum; 1IAH; -.
DR PDBsum; 1IAJ; -.
DR PDBsum; 5ZX5; -.
DR PDBsum; 6BWD; -.
DR PDBsum; 6BWF; -.
DR AlphaFoldDB; Q923J1; -.
DR SMR; Q923J1; -.
DR BioGRID; 208438; 5.
DR IntAct; Q923J1; 105.
DR MINT; Q923J1; -.
DR STRING; 10090.ENSMUSP00000099513; -.
DR BindingDB; Q923J1; -.
DR ChEMBL; CHEMBL3714706; -.
DR DrugCentral; Q923J1; -.
DR GuidetoPHARMACOLOGY; 499; -.
DR iPTMnet; Q923J1; -.
DR PhosphoSitePlus; Q923J1; -.
DR SwissPalm; Q923J1; -.
DR CPTAC; non-CPTAC-4068; -.
DR jPOST; Q923J1; -.
DR MaxQB; Q923J1; -.
DR PaxDb; Q923J1; -.
DR PRIDE; Q923J1; -.
DR ProteomicsDB; 300026; -.
DR ABCD; Q923J1; 1 sequenced antibody.
DR Antibodypedia; 24755; 470 antibodies from 40 providers.
DR DNASU; 58800; -.
DR Ensembl; ENSMUST00000103224; ENSMUSP00000099513; ENSMUSG00000027365.
DR GeneID; 58800; -.
DR KEGG; mmu:58800; -.
DR UCSC; uc008mef.2; mouse.
DR CTD; 54822; -.
DR MGI; MGI:1929996; Trpm7.
DR VEuPathDB; HostDB:ENSMUSG00000027365; -.
DR eggNOG; KOG3614; Eukaryota.
DR GeneTree; ENSGT00940000157091; -.
DR InParanoid; Q923J1; -.
DR OMA; ENNFQTA; -.
DR OrthoDB; 738147at2759; -.
DR PhylomeDB; Q923J1; -.
DR TreeFam; TF314204; -.
DR Reactome; R-MMU-3295583; TRP channels.
DR BioGRID-ORCS; 58800; 25 hits in 75 CRISPR screens.
DR ChiTaRS; Trpm7; mouse.
DR EvolutionaryTrace; Q923J1; -.
DR PRO; PR:Q923J1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q923J1; protein.
DR Bgee; ENSMUSG00000027365; Expressed in molar tooth and 249 other tissues.
DR ExpressionAtlas; Q923J1; baseline and differential.
DR Genevisible; Q923J1; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0001726; C:ruffle; IDA:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0043196; C:varicosity; ISO:MGI.
DR GO; GO:0003779; F:actin binding; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005262; F:calcium channel activity; IDA:MGI.
DR GO; GO:0005261; F:cation channel activity; ISO:MGI.
DR GO; GO:0016301; F:kinase activity; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017022; F:myosin binding; IPI:MGI.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0031032; P:actomyosin structure organization; IDA:MGI.
DR GO; GO:0006816; P:calcium ion transport; IDA:MGI.
DR GO; GO:0016340; P:calcium-dependent cell-matrix adhesion; IDA:MGI.
DR GO; GO:0098655; P:cation transmembrane transport; IBA:GO_Central.
DR GO; GO:0010961; P:cellular magnesium ion homeostasis; ISO:MGI.
DR GO; GO:0072507; P:divalent inorganic cation homeostasis; IBA:GO_Central.
DR GO; GO:0007613; P:memory; ISO:MGI.
DR GO; GO:0070266; P:necroptotic process; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR Gene3D; 1.20.5.1010; -; 1.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR004166; MHCK_EF2_kinase.
DR InterPro; IPR029601; TRPM7.
DR InterPro; IPR041491; TRPM_SLOG.
DR InterPro; IPR032415; TRPM_tetra.
DR InterPro; IPR037162; TRPM_tetra_sf.
DR PANTHER; PTHR13800:SF8; PTHR13800:SF8; 1.
DR Pfam; PF02816; Alpha_kinase; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF18139; LSDAT_euk; 1.
DR Pfam; PF16519; TRPM_tetra; 1.
DR SMART; SM00811; Alpha_kinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51158; ALPHA_KINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Calcium; Calcium channel;
KW Calcium transport; Coiled coil; Ion channel; Ion transport; Kinase;
KW Membrane; Metal-binding; Necrosis; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Transmembrane; Transmembrane helix; Transport; Zinc.
FT CHAIN 1..1863
FT /note="Transient receptor potential cation channel
FT subfamily M member 7"
FT /id="PRO_0000215332"
FT TOPO_DOM 1..755
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 756..776
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 777..855
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 856..876
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 877..918
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 919..939
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 940..962
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 963..983
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 984..995
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 996..1016
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1017..1035
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 1036..1056
FT /note="Pore-forming"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1057..1074
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1075..1095
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1096..1863
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1592..1822
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00501"
FT REGION 544..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1380..1418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1498..1539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1838..1863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1198..1250
FT /evidence="ECO:0000250"
FT COMPBIAS 544..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1765
FT /note="Proton acceptor"
FT BINDING 1622
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 1646
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 1718
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 1751
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 1767
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 1775
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 1792..1798
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 1808
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 1810
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 1814
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96QT4"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QT4"
FT MOD_RES 1224
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22222377"
FT MOD_RES 1255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1300
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22222377"
FT MOD_RES 1385
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22222377"
FT MOD_RES 1386
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22222377"
FT MOD_RES 1389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QT4"
FT MOD_RES 1394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QT4"
FT MOD_RES 1403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QT4"
FT MOD_RES 1404
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22222377"
FT MOD_RES 1445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1466
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22222377"
FT MOD_RES 1498
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22222377"
FT MOD_RES 1502
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 1525
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QT4"
FT MOD_RES 1567
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22222377"
FT MOD_RES 1846
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22222377"
FT MOD_RES 1849
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22222377"
FT MUTAGEN 1797
FT /note="G->D: Severe reduction of kinase activity."
FT /evidence="ECO:0000269|PubMed:11161216"
FT MUTAGEN 1810
FT /note="C->A: Loss of kinase activity; when associated with
FT A-1813."
FT /evidence="ECO:0000269|PubMed:11161216"
FT MUTAGEN 1813
FT /note="C->A: Loss of kinase activity; when associated with
FT A-1820."
FT /evidence="ECO:0000269|PubMed:11161216"
FT CONFLICT 66
FT /note="K -> R (in Ref. 3; AAF73131)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="L -> F (in Ref. 5; BAB29509)"
FT /evidence="ECO:0000305"
FT CONFLICT 723
FT /note="K -> E (in Ref. 5; BAC33685)"
FT /evidence="ECO:0000305"
FT CONFLICT 810
FT /note="I -> T (in Ref. 5; BAC33685)"
FT /evidence="ECO:0000305"
FT CONFLICT 1494
FT /note="Missing (in Ref. 2; AAK57433 and 5; BAC26234)"
FT /evidence="ECO:0000305"
FT HELIX 7..16
FT /evidence="ECO:0007829|PDB:5ZX5"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:5ZX5"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 152..164
FT /evidence="ECO:0007829|PDB:5ZX5"
FT TURN 165..168
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 262..271
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:5ZX5"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 311..314
FT /evidence="ECO:0007829|PDB:5ZX5"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 362..365
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 392..398
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 399..402
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 407..416
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 420..427
FT /evidence="ECO:0007829|PDB:5ZX5"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 439..448
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 452..461
FT /evidence="ECO:0007829|PDB:5ZX5"
FT TURN 466..468
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 472..475
FT /evidence="ECO:0007829|PDB:5ZX5"
FT TURN 476..478
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 489..493
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 509..519
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 527..529
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 531..536
FT /evidence="ECO:0007829|PDB:5ZX5"
FT STRAND 619..621
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 622..631
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 635..642
FT /evidence="ECO:0007829|PDB:5ZX5"
FT STRAND 643..647
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 648..667
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 676..679
FT /evidence="ECO:0007829|PDB:5ZX5"
FT TURN 680..682
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 683..700
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 702..708
FT /evidence="ECO:0007829|PDB:5ZX5"
FT STRAND 714..716
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 721..727
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 731..734
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 737..748
FT /evidence="ECO:0007829|PDB:5ZX5"
FT TURN 753..755
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 759..766
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 768..770
FT /evidence="ECO:0007829|PDB:5ZX5"
FT TURN 779..781
FT /evidence="ECO:0007829|PDB:5ZX5"
FT STRAND 782..785
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 843..849
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 852..875
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 884..905
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 916..919
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 923..943
FT /evidence="ECO:0007829|PDB:5ZX5"
FT STRAND 950..952
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 956..966
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 969..980
FT /evidence="ECO:0007829|PDB:5ZX5"
FT TURN 984..986
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 987..997
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 1001..1022
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 1031..1041
FT /evidence="ECO:0007829|PDB:5ZX5"
FT TURN 1042..1046
FT /evidence="ECO:0007829|PDB:5ZX5"
FT TURN 1050..1052
FT /evidence="ECO:0007829|PDB:5ZX5"
FT STRAND 1057..1059
FT /evidence="ECO:0007829|PDB:5ZX5"
FT TURN 1068..1071
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 1073..1086
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 1088..1122
FT /evidence="ECO:0007829|PDB:5ZX5"
FT TURN 1130..1134
FT /evidence="ECO:0007829|PDB:5ZX5"
FT TURN 1136..1138
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 1164..1184
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 1185..1187
FT /evidence="ECO:0007829|PDB:5ZX5"
FT STRAND 1189..1192
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 1193..1227
FT /evidence="ECO:0007829|PDB:5ZX5"
FT HELIX 1555..1562
FT /evidence="ECO:0007829|PDB:1IA9"
FT HELIX 1563..1565
FT /evidence="ECO:0007829|PDB:1IA9"
FT STRAND 1576..1583
FT /evidence="ECO:0007829|PDB:1IA9"
FT STRAND 1585..1588
FT /evidence="ECO:0007829|PDB:1IA9"
FT HELIX 1590..1595
FT /evidence="ECO:0007829|PDB:1IA9"
FT STRAND 1598..1600
FT /evidence="ECO:0007829|PDB:1IA9"
FT STRAND 1605..1613
FT /evidence="ECO:0007829|PDB:1IA9"
FT STRAND 1620..1632
FT /evidence="ECO:0007829|PDB:1IA9"
FT HELIX 1633..1635
FT /evidence="ECO:0007829|PDB:1IA9"
FT STRAND 1641..1648
FT /evidence="ECO:0007829|PDB:1IA9"
FT HELIX 1650..1655
FT /evidence="ECO:0007829|PDB:1IA9"
FT TURN 1657..1659
FT /evidence="ECO:0007829|PDB:1IA9"
FT HELIX 1664..1689
FT /evidence="ECO:0007829|PDB:1IA9"
FT STRAND 1704..1708
FT /evidence="ECO:0007829|PDB:1IA9"
FT TURN 1709..1712
FT /evidence="ECO:0007829|PDB:1IA9"
FT STRAND 1713..1719
FT /evidence="ECO:0007829|PDB:1IA9"
FT STRAND 1726..1729
FT /evidence="ECO:0007829|PDB:1IA9"
FT HELIX 1741..1756
FT /evidence="ECO:0007829|PDB:1IA9"
FT TURN 1757..1759
FT /evidence="ECO:0007829|PDB:1IA9"
FT STRAND 1760..1764
FT /evidence="ECO:0007829|PDB:1IA9"
FT STRAND 1767..1769
FT /evidence="ECO:0007829|PDB:1IA9"
FT STRAND 1772..1775
FT /evidence="ECO:0007829|PDB:1IAJ"
FT STRAND 1777..1780
FT /evidence="ECO:0007829|PDB:1IA9"
FT HELIX 1786..1788
FT /evidence="ECO:0007829|PDB:1IA9"
FT STRAND 1790..1793
FT /evidence="ECO:0007829|PDB:1IA9"
FT HELIX 1800..1807
FT /evidence="ECO:0007829|PDB:1IA9"
FT HELIX 1812..1816
FT /evidence="ECO:0007829|PDB:1IA9"
FT STRAND 1822..1824
FT /evidence="ECO:0007829|PDB:1IAJ"
SQ SEQUENCE 1863 AA; 212399 MW; 87551B4431CAD773 CRC64;
MSQKSWIEST LTKRECVYII PSSKDPHRCL PGCQICQQLV RCFCGRLVKQ HACFTASLAM
KYSDVKLGEH FNQAIEEWSV EKHTEQSPTD AYGVINFQGG SHSYRAKYVR LSYDTKPEII
LQLLLKEWQM ELPKLVISVH GGMQKFELHP RIKQLLGKGL IKAAVTTGAW ILTGGVNTGV
AKHVGDALKE HASRSSRKIC TIGIAPWGVI ENRNDLVGRD VVAPYQTLLN PLSKLNVLNN
LHSHFILVDD GTVGKYGAEV RLRRELEKTI NQQRIHARIG QGVPVVALIF EGGPNVILTV
LEYLQESPPV PVVVCEGTGR AADLLAYIHK QTEEGGNLPD AAEPDIISTI KKTFNFGQSE
AVHLFQTMME CMKKKELITV FHIGSEDHQD IDVAILTALL KGTNASAFDQ LILTLAWDRV
DIAKNHVFVY GQQWLVGSLE QAMLDALVMD RVSFVKLLIE NGVSMHKFLT IPRLEELYNT
KQGPTNPMLF HLIRDVKQGN LPPGYKITLI DIGLVIEYLM GGTYRCTYTR KRFRLIYNSL
GGNNRRSGRN TSSSTPQLRK SHETFGNRAD KKEKMRHNHF IKTAQPYRPK MDASMEEGKK
KRTKDEIVDI DDPETKRFPY PLNELLIWAC LMKRQVMARF LWQHGEESMA KALVACKIYR
SMAYEAKQSD LVDDTSEELK QYSNDFGQLA VELLEQSFRQ DETMAMKLLT YELKNWSNST
CLKLAVSSRL RPFVAHTCTQ MLLSDMWMGR LNMRKNSWYK VILSILVPPA ILMLEYKTKA
EMSHIPQSQD AHQMTMEDSE NNFHNITEEI PMEVFKEVKI LDSSDGKNEM EIHIKSKKLP
ITRKFYAFYH APIVKFWFNT LAYLGFLMLY TFVVLVKMEQ LPSVQEWIVI AYIFTYAIEK
VREVFMSEAG KISQKIKVWF SDYFNVSDTI AIISFFVGFG LRFGAKWNYI NAYDNHVFVA
GRLIYCLNII FWYVRLLDFL AVNQQAGPYV MMIGKMVANM FYIVVIMALV LLSFGVPRKA
ILYPHEEPSW SLAKDIVFHP YWMIFGEVYA YEIDVCANDS TLPTICGPGT WLTPFLQAVY
LFVQYIIMVN LLIAFFNNVY LQVKAISNIV WKYQRYHFIM AYHEKPVLPP PLIILSHIVS
LFCCVCKRRK KDKTSDGPKL FLTEEDQKKL HDFEEQCVEM YFDEKDDKFN SGSEERIRVT
FERVEQMSIQ IKEVGDRVNY IKRSLQSLDS QIGHLQDLSA LTVDTLKTLT AQKASEASKV
HNEITRELSI SKHLAQNLID DVPVRPLWKK PSAVNTLSSS LPQGDRESNN PFLCNIFMKD
EKDPQYNLFG QDLPVIPQRK EFNIPEAGSS CGALFPSAVS PPELRQRRHG VEMLKIFNKN
QKLGSSPNSS PHMSSPPTKF SVSTPSQPSC KSHLESTTKD QEPIFYKAAE GDNIEFGAFV
GHRDSMDLQR FKETSNKIRE LLSNDTPENT LKHVGAAGYS ECCKTSTSLH SVQAESCSRR
ASTEDSPEVD SKAALLPDWL RDRPSNREMP SEGGTLNGLA SPFKPVLDTN YYYSAVERNN
LMRLSQSIPF VPVPPRGEPV TVYRLEESSP SILNNSMSSW SQLGLCAKIE FLSKEEMGGG
LRRAVKVLCT WSEHDILKSG HLYIIKSFLP EVINTWSSIY KEDTVLHLCL REIQQQRAAQ
KLTFAFNQMK PKSIPYSPRF LEVFLLYCHS AGQWFAVEEC MTGEFRKYNN NNGDEIIPTN
TLEEIMLAFS HWTYEYTRGE LLVLDLQGVG ENLTDPSVIK AEEKRSCDMV FGPANLGEDA
IKNFRAKHHC NSCCRKLKLP DLKRNDYTPD KIIFPQDESS DLNLQSGNST KESEATNSVR
LML
