BMP2K_HUMAN
ID BMP2K_HUMAN Reviewed; 1161 AA.
AC Q9NSY1; O94791; Q4W5H2; Q8IYF2; Q8N2G7; Q8NHG9; Q9NTG8;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=BMP-2-inducible protein kinase {ECO:0000250|UniProtKB:Q91Z96};
DE Short=BIKe {ECO:0000250|UniProtKB:Q91Z96};
DE EC=2.7.11.1 {ECO:0000269|PubMed:26853940};
GN Name=BMP2K; Synonyms=BIKE; ORFNames=HRIHFB2017;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Synovium, and Thyroid;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT SER-405.
RC TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 537-1161 (ISOFORM 2).
RC TISSUE=Ovary;
RA Guo J.H., Yu L.;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 946-1161 (ISOFORM 1), AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=9853615; DOI=10.1038/4315;
RA Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.;
RT "Selection system for genes encoding nuclear-targeted proteins.";
RL Nat. Biotechnol. 16:1338-1342(1998).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-834 AND SER-1076, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-1107, AND
RP IDENTIFICATION BY 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029 AND SER-1032, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029; SER-1107 AND SER-1111,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-689; SER-742; SER-817;
RP SER-818; SER-1029; SER-1032; SER-1041; SER-1107 AND SER-1111, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-1039, AND
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 [16] {ECO:0007744|PDB:4W9W, ECO:0007744|PDB:4W9X}
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 39-344 IN COMPLEX WITH
RP INHIBITORS, AND CATALYTIC ACTIVITY.
RX PubMed=26853940; DOI=10.1016/j.str.2015.12.015;
RA Sorrell F.J., Szklarz M., Abdul Azeez K.R., Elkins J.M., Knapp S.;
RT "Family-wide Structural Analysis of Human Numb-Associated Protein
RT Kinases.";
RL Structure 24:401-411(2016).
RN [17] {ECO:0007744|PDB:5I3O, ECO:0007744|PDB:5I3R}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 42-343.
RA Counago R.M., Sorrell F.J., Krojer T., Elkins J.M., Gileadi O.,
RA Willson T.M., Arrowsmith C.H., Edwards A.M., Bountra C., Arruda P.;
RT "Crystal Structure of BMP-2-inducible kinase in complex with an Indazole
RT inhibitor.";
RL Submitted (FEB-2016) to the PDB data bank.
RN [18] {ECO:0007744|PDB:5IKW}
RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 38-345.
RA Counago R.M., Sorrell F.J., Krojer T., Savitsky P., Elkins J.M., Axtman A.,
RA Drewry D., Wells C., Zhang C., Zuercher W., Willson T.M., Arrowsmith C.H.,
RA Edwards A.M., Bountra C., Arruda P., Gileadi O.;
RT "Crystal Structure of BMP-2-inducible kinase in complex with a 3-
RT acylaminoindazole inhibitor GSK3236425A.";
RL Submitted (MAR-2016) to the PDB data bank.
RN [19]
RP VARIANTS [LARGE SCALE ANALYSIS] MET-68; VAL-212 AND HIS-288.
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: May be involved in osteoblast differentiation.
CC {ECO:0000250|UniProtKB:Q91Z96}.
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 Evidence={ECO:0000269|PubMed:26853940};
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; Evidence={ECO:0000269|PubMed:26853940};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9853615}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NSY1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NSY1-2; Sequence=VSP_008091, VSP_008092;
CC Name=3;
CC IsoId=Q9NSY1-3; Sequence=VSP_008093, VSP_008091, VSP_008092;
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q91Z96}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AK075278; BAC11515.1; -; mRNA.
DR EMBL; AK292147; BAF84836.1; -; mRNA.
DR EMBL; AL137275; CAB70673.1; -; mRNA.
DR EMBL; AL137661; CAB70863.1; -; mRNA.
DR EMBL; AC098818; AAY40926.1; -; Genomic_DNA.
DR EMBL; BC036021; AAH36021.1; -; mRNA.
DR EMBL; AF527532; AAM88867.1; -; mRNA.
DR EMBL; AB015331; BAA34790.1; -; mRNA.
DR CCDS; CCDS34019.1; -. [Q9NSY1-2]
DR CCDS; CCDS47083.1; -. [Q9NSY1-1]
DR PIR; T46347; T46347.
DR PIR; T46364; T46364.
DR RefSeq; NP_060063.2; NM_017593.3. [Q9NSY1-2]
DR RefSeq; NP_942595.1; NM_198892.1. [Q9NSY1-1]
DR PDB; 4W9W; X-ray; 1.72 A; A=39-344.
DR PDB; 4W9X; X-ray; 2.14 A; A=38-345.
DR PDB; 5I3O; X-ray; 2.40 A; A/B=42-343.
DR PDB; 5I3R; X-ray; 2.40 A; A/B=42-343.
DR PDB; 5IKW; X-ray; 2.41 A; A=38-345.
DR PDBsum; 4W9W; -.
DR PDBsum; 4W9X; -.
DR PDBsum; 5I3O; -.
DR PDBsum; 5I3R; -.
DR PDBsum; 5IKW; -.
DR AlphaFoldDB; Q9NSY1; -.
DR SMR; Q9NSY1; -.
DR BioGRID; 120735; 93.
DR IntAct; Q9NSY1; 61.
DR MINT; Q9NSY1; -.
DR STRING; 9606.ENSP00000334836; -.
DR BindingDB; Q9NSY1; -.
DR ChEMBL; CHEMBL4522; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q9NSY1; -.
DR GuidetoPHARMACOLOGY; 1941; -.
DR GlyGen; Q9NSY1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NSY1; -.
DR PhosphoSitePlus; Q9NSY1; -.
DR BioMuta; BMP2K; -.
DR DMDM; 34222653; -.
DR EPD; Q9NSY1; -.
DR jPOST; Q9NSY1; -.
DR MassIVE; Q9NSY1; -.
DR MaxQB; Q9NSY1; -.
DR PaxDb; Q9NSY1; -.
DR PeptideAtlas; Q9NSY1; -.
DR PRIDE; Q9NSY1; -.
DR ProteomicsDB; 82594; -. [Q9NSY1-1]
DR ProteomicsDB; 82595; -. [Q9NSY1-2]
DR ProteomicsDB; 82596; -. [Q9NSY1-3]
DR Antibodypedia; 24948; 194 antibodies from 27 providers.
DR DNASU; 55589; -.
DR Ensembl; ENST00000502613.3; ENSP00000424668.2; ENSG00000138756.19. [Q9NSY1-1]
DR Ensembl; ENST00000502871.5; ENSP00000421768.1; ENSG00000138756.19. [Q9NSY1-2]
DR GeneID; 55589; -.
DR KEGG; hsa:55589; -.
DR MANE-Select; ENST00000502613.3; ENSP00000424668.2; NM_198892.2; NP_942595.1.
DR UCSC; uc003hlj.4; human. [Q9NSY1-1]
DR CTD; 55589; -.
DR DisGeNET; 55589; -.
DR GeneCards; BMP2K; -.
DR HGNC; HGNC:18041; BMP2K.
DR HPA; ENSG00000138756; Low tissue specificity.
DR MIM; 617648; gene.
DR neXtProt; NX_Q9NSY1; -.
DR OpenTargets; ENSG00000138756; -.
DR PharmGKB; PA134992822; -.
DR VEuPathDB; HostDB:ENSG00000138756; -.
DR eggNOG; KOG1989; Eukaryota.
DR GeneTree; ENSGT00940000157548; -.
DR HOGENOM; CLU_000288_109_5_1; -.
DR InParanoid; Q9NSY1; -.
DR OMA; PWHPSHQ; -.
DR OrthoDB; 826336at2759; -.
DR PhylomeDB; Q9NSY1; -.
DR TreeFam; TF335936; -.
DR PathwayCommons; Q9NSY1; -.
DR SignaLink; Q9NSY1; -.
DR BioGRID-ORCS; 55589; 19 hits in 1108 CRISPR screens.
DR ChiTaRS; BMP2K; human.
DR GeneWiki; BMP2K; -.
DR GenomeRNAi; 55589; -.
DR Pharos; Q9NSY1; Tchem.
DR PRO; PR:Q9NSY1; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9NSY1; protein.
DR Bgee; ENSG00000138756; Expressed in adrenal tissue and 195 other tissues.
DR ExpressionAtlas; Q9NSY1; baseline and differential.
DR Genevisible; Q9NSY1; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0035612; F:AP-2 adaptor complex binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019208; F:phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0030500; P:regulation of bone mineralization; IBA:GO_Central.
DR GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; IBA:GO_Central.
DR InterPro; IPR026105; BMP-2-ind_kinase.
DR InterPro; IPR028182; BMP2K_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22967:SF10; PTHR22967:SF10; 1.
DR Pfam; PF15282; BMP2K_C; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1161
FT /note="BMP-2-inducible protein kinase"
FT /id="PRO_0000085663"
FT DOMAIN 51..316
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..776
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..995
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 180
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 57..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 818
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 834
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 928
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91Z96"
FT MOD_RES 1029
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1031
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91Z96"
FT MOD_RES 1032
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1039
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1076
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 1107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 330..340
FT /note="NSSIPSALPEP -> KCCKQLLRHGALLTEILLFLQLFLNR (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_008093"
FT VAR_SEQ 651..662
FT /note="NRLEERASSDKN -> SKGHLKAYFASQ (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT ECO:0000303|Ref.5"
FT /id="VSP_008091"
FT VAR_SEQ 663..1161
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT ECO:0000303|Ref.5"
FT /id="VSP_008092"
FT VARIANT 68
FT /note="V -> M (in a lung squamous cell carcinoma sample;
FT somatic mutation; dbSNP:rs770167074)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040388"
FT VARIANT 212
FT /note="D -> V (in dbSNP:rs56143363)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040389"
FT VARIANT 288
FT /note="R -> H (in dbSNP:rs55782848)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040390"
FT VARIANT 405
FT /note="G -> S (in dbSNP:rs2288255)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_051618"
FT VARIANT 486
FT /note="Q -> H (in dbSNP:rs2114202)"
FT /id="VAR_059765"
FT VARIANT 1002
FT /note="T -> S (in dbSNP:rs12507099)"
FT /id="VAR_051619"
FT CONFLICT 342
FT /note="T -> A (in Ref. 4; AAH36021)"
FT /evidence="ECO:0000305"
FT CONFLICT 471..486
FT /note="Missing (in Ref. 2; CAB70863)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="Q -> R (in Ref. 4; AAH36021)"
FT /evidence="ECO:0000305"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:4W9W"
FT STRAND 49..59
FT /evidence="ECO:0007829|PDB:4W9W"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:4W9W"
FT STRAND 75..85
FT /evidence="ECO:0007829|PDB:4W9W"
FT HELIX 86..102
FT /evidence="ECO:0007829|PDB:4W9W"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:4W9W"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:4W9W"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:4W9W"
FT HELIX 138..144
FT /evidence="ECO:0007829|PDB:4W9W"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:4W9W"
FT HELIX 152..170
FT /evidence="ECO:0007829|PDB:4W9W"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:4W9W"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:4W9W"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:4W9W"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:4W9W"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:4W9W"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:4W9W"
FT HELIX 214..224
FT /evidence="ECO:0007829|PDB:4W9W"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:4W9W"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:4W9W"
FT HELIX 245..261
FT /evidence="ECO:0007829|PDB:4W9W"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:4W9W"
FT HELIX 270..275
FT /evidence="ECO:0007829|PDB:4W9W"
FT HELIX 288..297
FT /evidence="ECO:0007829|PDB:4W9W"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:4W9W"
FT HELIX 308..318
FT /evidence="ECO:0007829|PDB:4W9W"
SQ SEQUENCE 1161 AA; 129172 MW; 5C38A86E95935EC2 CRC64;
MKKFSRMPKS EGGSGGGAAG GGAGGAGAGA GCGSGGSSVG VRVFAVGRHQ VTLEESLAEG
GFSTVFLVRT HGGIRCALKR MYVNNMPDLN VCKREITIMK ELSGHKNIVG YLDCAVNSIS
DNVWEVLILM EYCRAGQVVN QMNKKLQTGF TEPEVLQIFC DTCEAVARLH QCKTPIIHRD
LKVENILLND GGNYVLCDFG SATNKFLNPQ KDGVNVVEEE IKKYTTLSYR APEMINLYGG
KPITTKADIW ALGCLLYKLC FFTLPFGESQ VAICDGNFTI PDNSRYSRNI HCLIRFMLEP
DPEHRPDIFQ VSYFAFKFAK KDCPVSNINN SSIPSALPEP MTASEAAARK SQIKARITDT
IGPTETSIAP RQRPKANSAT TATPSVLTIQ SSATPVKVLA PGEFGNHRPK GALRPGNGPE
ILLGQGPPQQ PPQQHRVLQQ LQQGDWRLQQ LHLQHRHPHQ QQQQQQQQQQ QQQQQQQQQQ
QQQQQQHHHH HHHHLLQDAY MQQYQHATQQ QQMLQQQFLM HSVYQPQPSA SQYPTMMPQY
QQAFFQQQML AQHQPSQQQA SPEYLTSPQE FSPALVSYTS SLPAQVGTIM DSSYSANRSV
ADKEAIANFT NQKNISNPPD MSGWNPFGED NFSKLTEEEL LDREFDLLRS NRLEERASSD
KNVDSLSAPH NHPPEDPFGS VPFISHSGSP EKKAEHSSIN QENGTANPIK NGKTSPASKD
QRTGKKTSVQ GQVQKGNDES ESDFESDPPS PKSSEEEEQD DEEVLQGEQG DFNDDDTEPE
NLGHRPLLMD SEDEEEEEKH SSDSDYEQAK AKYSDMSSVY RDRSGSGPTQ DLNTILLTSA
QLSSDVAVET PKQEFDVFGA VPFFAVRAQQ PQQEKNEKNL PQHRFPAAGL EQEEFDVFTK
APFSKKVNVQ ECHAVGPEAH TIPGYPKSVD VFGSTPFQPF LTSTSKSESN EDLFGLVPFD
EITGSQQQKV KQRSLQKLSS RQRRTKQDMS KSNGKRHHGT PTSTKKTLKP TYRTPERARR
HKKVGRRDSQ SSNEFLTISD SKENISVALT DGKDRGNVLQ PEESLLDPFG AKPFHSPDLS
WHPPHQGLSD IRADHNTVLP GRPRQNSLHG SFHSADVLKM DDFGAVPFTE LVVQSITPHQ
SQQSQPVELD PFGAAPFPSK Q
