NEK3_HUMAN
ID NEK3_HUMAN Reviewed; 506 AA.
AC P51956; A8K2J4; Q5TAP2; Q8J023; Q8WUN5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Serine/threonine-protein kinase Nek3;
DE EC=2.7.11.1;
DE AltName: Full=HSPK 36;
DE AltName: Full=Never in mitosis A-related kinase 3;
DE Short=NimA-related protein kinase 3;
GN Name=NEK3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=12063396; DOI=10.1159/000059342;
RA Kimura M., Okano Y.;
RT "Molecular cloning and characterization of the human NIMA-related protein
RT kinase 3 gene (NEK3).";
RL Cytogenet. Cell Genet. 95:177-182(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 48-506 (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=7522034;
RA Schultz S.J., Fry A.M., Suetterlin C., Ried T., Nigg E.A.;
RT "Cell cycle-dependent expression of Nek2, a novel human protein kinase
RT related to the NIMA mitotic regulator of Aspergillus nidulans.";
RL Cell Growth Differ. 5:625-635(1994).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 76-189.
RX PubMed=8274451;
RA Schultz S.J., Nigg E.A.;
RT "Identification of 21 novel human protein kinases, including 3 members of a
RT family related to the cell cycle regulator nimA of Aspergillus nidulans.";
RL Cell Growth Differ. 4:821-830(1993).
RN [8]
RP FUNCTION, INTERACTION WITH PRLR; VAV1 AND VAV2, AND ACTIVITY REGULATION.
RX PubMed=15618286; DOI=10.1210/me.2004-0443;
RA Miller S.L., DeMaria J.E., Freier D.O., Riegel A.M., Clevenger C.V.;
RT "Novel association of Vav2 and Nek3 modulates signaling through the human
RT prolactin receptor.";
RL Mol. Endocrinol. 19:939-949(2005).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH PXN.
RX PubMed=17297458; DOI=10.1038/sj.onc.1210264;
RA Miller S.L., Antico G., Raghunath P.N., Tomaszewski J.E., Clevenger C.V.;
RT "Nek3 kinase regulates prolactin-mediated cytoskeletal reorganization and
RT motility of breast cancer cells.";
RL Oncogene 26:4668-4678(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-479, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP VARIANTS [LARGE SCALE ANALYSIS] LEU-23; ARG-60; HIS-122; LEU-170; GLY-259;
RP ASP-305; ASN-461 AND LYS-477.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Protein kinase which influences neuronal morphogenesis and
CC polarity through effects on microtubules. Regulates microtubule
CC acetylation in neurons. Contributes to prolactin-mediated
CC phosphorylation of PXN and VAV2. Implicated in prolactin-mediated
CC cytoskeletal reorganization and motility of breast cancer cells through
CC mechanisms involving RAC1 activation and phosphorylation of PXN and
CC VAV2. {ECO:0000269|PubMed:15618286, ECO:0000269|PubMed:17297458}.
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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Prolactin stimulates its activity.
CC {ECO:0000269|PubMed:15618286}.
CC -!- SUBUNIT: Interacts with PXN, PRLR, VAV1 and VAV2 and this interaction
CC is prolactin-dependent. {ECO:0000269|PubMed:15618286,
CC ECO:0000269|PubMed:17297458}.
CC -!- INTERACTION:
CC P51956; P52735: VAV2; NbExp=3; IntAct=EBI-476041, EBI-297549;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection, axon
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P51956-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P51956-2; Sequence=VSP_035427;
CC -!- TISSUE SPECIFICITY: Up-regulated in malignant versus normal breast
CC tissue. Isoform 2 shows a high level of expression in testis, ovary and
CC brain. {ECO:0000269|PubMed:12063396, ECO:0000269|PubMed:17297458}.
CC -!- PTM: Phosphorylation at Thr-479 regulates its catalytic activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAX08907.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB072828; BAC15599.1; -; mRNA.
DR EMBL; AK290259; BAF82948.1; -; mRNA.
DR EMBL; AL139082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08907.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC019916; AAH19916.2; -; mRNA.
DR EMBL; Z29067; CAA82310.1; -; mRNA.
DR EMBL; Z25434; CAA80921.1; -; mRNA.
DR CCDS; CCDS73576.1; -. [P51956-1]
DR PIR; I38224; I38224.
DR RefSeq; NP_001139571.1; NM_001146099.1. [P51956-2]
DR RefSeq; NP_002489.1; NM_002498.2. [P51956-1]
DR RefSeq; NP_689933.1; NM_152720.2. [P51956-1]
DR AlphaFoldDB; P51956; -.
DR SMR; P51956; -.
DR BioGRID; 110827; 10.
DR IntAct; P51956; 16.
DR STRING; 9606.ENSP00000484443; -.
DR BindingDB; P51956; -.
DR ChEMBL; CHEMBL5679; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; P51956; -.
DR GuidetoPHARMACOLOGY; 2118; -.
DR iPTMnet; P51956; -.
DR PhosphoSitePlus; P51956; -.
DR BioMuta; NEK3; -.
DR DMDM; 20178297; -.
DR EPD; P51956; -.
DR jPOST; P51956; -.
DR MassIVE; P51956; -.
DR MaxQB; P51956; -.
DR PaxDb; P51956; -.
DR PeptideAtlas; P51956; -.
DR PRIDE; P51956; -.
DR ProteomicsDB; 56457; -. [P51956-1]
DR ProteomicsDB; 56458; -. [P51956-2]
DR Antibodypedia; 24171; 244 antibodies from 29 providers.
DR DNASU; 4752; -.
DR Ensembl; ENST00000610828.5; ENSP00000480328.1; ENSG00000136098.17. [P51956-1]
DR Ensembl; ENST00000611833.4; ENSP00000484086.1; ENSG00000136098.17. [P51956-2]
DR Ensembl; ENST00000618534.4; ENSP00000484443.1; ENSG00000136098.17. [P51956-1]
DR GeneID; 4752; -.
DR KEGG; hsa:4752; -.
DR MANE-Select; ENST00000610828.5; ENSP00000480328.1; NM_002498.3; NP_002489.1.
DR UCSC; uc032agd.2; human. [P51956-1]
DR CTD; 4752; -.
DR DisGeNET; 4752; -.
DR GeneCards; NEK3; -.
DR HGNC; HGNC:7746; NEK3.
DR HPA; ENSG00000136098; Low tissue specificity.
DR MIM; 604044; gene.
DR neXtProt; NX_P51956; -.
DR OpenTargets; ENSG00000136098; -.
DR PharmGKB; PA31547; -.
DR VEuPathDB; HostDB:ENSG00000136098; -.
DR eggNOG; KOG0589; Eukaryota.
DR GeneTree; ENSGT00940000159738; -.
DR HOGENOM; CLU_000288_63_39_1; -.
DR InParanoid; P51956; -.
DR OMA; YSYELQY; -.
DR OrthoDB; 70360at2759; -.
DR PhylomeDB; P51956; -.
DR TreeFam; TF106472; -.
DR BRENDA; 2.7.11.1; 2681.
DR PathwayCommons; P51956; -.
DR SignaLink; P51956; -.
DR SIGNOR; P51956; -.
DR BioGRID-ORCS; 4752; 11 hits in 741 CRISPR screens.
DR ChiTaRS; NEK3; human.
DR GeneWiki; NEK3; -.
DR GenomeRNAi; 4752; -.
DR Pharos; P51956; Tchem.
DR PRO; PR:P51956; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; P51956; protein.
DR Bgee; ENSG00000136098; Expressed in sural nerve and 167 other tissues.
DR ExpressionAtlas; P51956; baseline and differential.
DR Genevisible; P51956; HS.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; NAS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030010; P:establishment of cell polarity; IEA:Ensembl.
DR GO; GO:0000278; P:mitotic cell cycle; NAS:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; IEA:Ensembl.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cell cycle; Cell division;
KW Cell projection; Cytoplasm; Kinase; Magnesium; Metal-binding; Mitosis;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..506
FT /note="Serine/threonine-protein kinase Nek3"
FT /id="PRO_0000086423"
FT DOMAIN 4..257
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..285
FT /note="Interaction with VAV2"
FT /evidence="ECO:0000269|PubMed:15618286"
FT REGION 302..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..488
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 127
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 161
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 479
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT VAR_SEQ 293..309
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12063396"
FT /id="VSP_035427"
FT VARIANT 23
FT /note="H -> L (in dbSNP:rs17482764)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_033906"
FT VARIANT 60
FT /note="P -> R (in dbSNP:rs55946204)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040908"
FT VARIANT 122
FT /note="R -> H (in dbSNP:rs56190615)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040909"
FT VARIANT 170
FT /note="P -> L (in dbSNP:rs56021040)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040910"
FT VARIANT 259
FT /note="R -> G (in dbSNP:rs34077016)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040911"
FT VARIANT 305
FT /note="E -> D (in dbSNP:rs55969405)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040912"
FT VARIANT 461
FT /note="D -> N (in dbSNP:rs34076988)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040913"
FT VARIANT 477
FT /note="E -> K (in dbSNP:rs34488913)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040914"
FT CONFLICT 14
FT /note="S -> F (in Ref. 1; BAC15599)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="L -> S (in Ref. 6; CAA82310)"
FT /evidence="ECO:0000305"
FT CONFLICT 77..78
FT /note="IV -> LY (in Ref. 7; CAA80921)"
FT /evidence="ECO:0000305"
FT CONFLICT 187..189
FT /note="SLG -> PSV (in Ref. 7; CAA80921)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 506 AA; 57705 MW; 4437EB4A41A44777 CRC64;
MDDYMVLRMI GEGSFGRALL VQHESSNQMF AMKEIRLPKS FSNTQNSRKE AVLLAKMKHP
NIVAFKESFE AEGHLYIVME YCDGGDLMQK IKQQKGKLFP EDMILNWFTQ MCLGVNHIHK
KRVLHRDIKS KNIFLTQNGK VKLGDFGSAR LLSNPMAFAC TYVGTPYYVP PEIWENLPYN
NKSDIWSLGC ILYELCTLKH PFQANSWKNL ILKVCQGCIS PLPSHYSYEL QFLVKQMFKR
NPSHRPSATT LLSRGIVARL VQKCLPPEII MEYGEEVLEE IKNSKHNTPR KKTNPSRIRI
ALGNEASTVQ EEEQDRKGSH TDLESINENL VESALRRVNR EEKGNKSVHL RKASSPNLHR
RQWEKNVPNT ALTALENASI LTSSLTAEDD RGGSVIKYSK NTTRKQWLKE TPDTLLNILK
NADLSLAFQT YTIYRPGSEG FLKGPLSEET EASDSVDGGH DSVILDPERL EPGLDEEDTD
FEEEDDNPDW VSELKKRAGW QGLCDR
