ID   BMP2K_MOUSE             Reviewed;        1138 AA.
AC   Q91Z96; Q8C8L7;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=BMP-2-inducible protein kinase {ECO:0000303|PubMed:11500515};
DE            Short=BIKe {ECO:0000303|PubMed:11500515};
DE            EC=2.7.11.1 {ECO:0000269|PubMed:11500515};
GN   Name=Bmp2k; Synonyms=Bike;
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J;
RX   PubMed=11500515; DOI=10.1074/jbc.m106163200;
RA   Kearns A.E., Donohue M.M., Sanyal B., Demay M.B.;
RT   "Cloning and characterization of a novel protein kinase that impairs
RT   osteoblast differentiation in vitro.";
RL   J. Biol. Chem. 276:42213-42218(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1010 AND SER-1013, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-908; SER-1010; SER-1012 AND
RP   SER-1013, AND IDENTIFICATION BY 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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-908 AND SER-1010, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Lung, Pancreas, Spleen, and Testis;
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).
CC   -!- FUNCTION: May be involved in osteoblast differentiation.
CC       {ECO:0000269|PubMed:11500515}.
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:11500515};
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:11500515};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:11500515}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q91Z96-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q91Z96-2; Sequence=VSP_008094, VSP_008095;
CC   -!- TISSUE SPECIFICITY: Expressed in osteocytes and osteoblasts.
CC       {ECO:0000269|PubMed:11500515}.
CC   -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:11500515}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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; AY050249; AAK91585.1; -; mRNA.
DR   EMBL; AK046752; BAC32854.1; -; mRNA.
DR   CCDS; CCDS39175.1; -. [Q91Z96-1]
DR   RefSeq; NP_542439.1; NM_080708.1. [Q91Z96-1]
DR   AlphaFoldDB; Q91Z96; -.
DR   SMR; Q91Z96; -.
DR   BioGRID; 228314; 6.
DR   STRING; 10090.ENSMUSP00000037970; -.
DR   GlyGen; Q91Z96; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q91Z96; -.
DR   PhosphoSitePlus; Q91Z96; -.
DR   EPD; Q91Z96; -.
DR   jPOST; Q91Z96; -.
DR   MaxQB; Q91Z96; -.
DR   PaxDb; 10090-ENSMUSP00000037970; -.
DR   PeptideAtlas; Q91Z96; -.
DR   ProteomicsDB; 265218; -. [Q91Z96-1]
DR   ProteomicsDB; 265219; -. [Q91Z96-2]
DR   Pumba; Q91Z96; -.
DR   Antibodypedia; 24948; 207 antibodies from 27 providers.
DR   DNASU; 140780; -.
DR   Ensembl; ENSMUST00000035635.10; ENSMUSP00000037970.8; ENSMUSG00000034663.14. [Q91Z96-1]
DR   Ensembl; ENSMUST00000112974.6; ENSMUSP00000108598.2; ENSMUSG00000034663.14. [Q91Z96-2]
DR   GeneID; 140780; -.
DR   KEGG; mmu:140780; -.
DR   UCSC; uc008yfo.1; mouse. [Q91Z96-2]
DR   UCSC; uc008yfp.1; mouse. [Q91Z96-1]
DR   AGR; MGI:2155456; -.
DR   CTD; 55589; -.
DR   MGI; MGI:2155456; Bmp2k.
DR   VEuPathDB; HostDB:ENSMUSG00000034663; -.
DR   eggNOG; KOG1989; Eukaryota.
DR   GeneTree; ENSGT00940000157548; -.
DR   HOGENOM; CLU_000288_109_5_1; -.
DR   InParanoid; Q91Z96; -.
DR   OMA; YPTVMQQ; -.
DR   OrthoDB; 168953at2759; -.
DR   PhylomeDB; Q91Z96; -.
DR   TreeFam; TF317300; -.
DR   BioGRID-ORCS; 140780; 2 hits in 81 CRISPR screens.
DR   ChiTaRS; Bmp2k; mouse.
DR   PRO; PR:Q91Z96; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q91Z96; Protein.
DR   Bgee; ENSMUSG00000034663; Expressed in secondary oocyte and 236 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
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; IDA:MGI.
DR   GO; GO:0004672; F:protein kinase activity; IDA:MGI.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0045747; P:positive regulation of Notch signaling pathway; IBA:GO_Central.
DR   GO; GO:0030500; P:regulation of bone mineralization; IDA:MGI.
DR   GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; IBA:GO_Central.
DR   CDD; cd14037; STKc_NAK_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; PTHR47907:SF3; AP2-ASSOCIATED PROTEIN KINASE 1; 1.
DR   PANTHER; PTHR47907; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF15282; BMP2K_C; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   Genevisible; Q91Z96; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Kinase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..1138
FT                   /note="BMP-2-inducible protein kinase"
FT                   /id="PRO_0000085664"
FT   DOMAIN          48..313
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          355..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          638..831
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          906..1018
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1117..1138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        355..391
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..435
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..703
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        723..744
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        745..764
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        765..779
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        791..811
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        914..928
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        941..956
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        962..976
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        177
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         54..62
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         76
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         676
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NSY1"
FT   MOD_RES         733
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NSY1"
FT   MOD_RES         806
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NSY1"
FT   MOD_RES         807
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NSY1"
FT   MOD_RES         819
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NSY1"
FT   MOD_RES         908
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         1010
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT   MOD_RES         1012
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         1013
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19144319"
FT   MOD_RES         1020
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NSY1"
FT   MOD_RES         1022
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NSY1"
FT   MOD_RES         1087
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NSY1"
FT   MOD_RES         1091
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NSY1"
FT   VAR_SEQ         638..649
FT                   /note="NRLGASTPSDKT -> SKGHLKAYFASQ (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_008094"
FT   VAR_SEQ         650..1138
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_008095"
SQ   SEQUENCE   1138 AA;  126185 MW;  8EDDE02F1333840D CRC64;
     MKKFSRMPKS EGSGGGAAAG GAAGGGLGGG FASSSMGVRV FAVGRYQVTL EESLAEGGFS
     TVFLVRTHSG IRCALKRMYV NNTPDLNICK REITIMKELS GHKNIVGYLD CAVNSISDNV
     WEVLILMEYC RAGQVVNQMN KKLQTGFTES EVLQIFCDTC EAVARLHQCK TPIIHRDLKV
     ENILLNDAGN YVLCDFGSAT NKFLNPQKDG VNVVEEEIKK YTTLSYRAPE MINLYGGKPI
     TTKADIWALG CLLYKLCFFT LPFGESQVAI CDGSFTIPDN SRYSHNVHCL IRFMLEPDPE
     CRPDIFQVSY FAFKFAKKDC PVSNINNSFL PSTLPEPMTA TEAAARKSQM KARITDTIGP
     TETSIAPRQR PKANSTAATS SVLTIQSSAT PVKVPAPGEF SNHKPKGALR PGNGSEVLMV
     QGPPQQPPQQ HRVLQQLQQG DWRLQQLHLH RHPHHHHQQQ QQQQQQQQQQ QLQQQQQQQQ
     QLLQNAYLQQ YQHAMHQQHI LQQQFLMHSV YQPQPPASQY PAMMQQYQQA FLQQQMLARH
     QQPAQQVSPE YLTSPQEFSP ALVSYASSLP AQVGTIVDSS YGANRSVAEK EAVANFTNQK
     TISHPPDMSG WNPFGEDNFS KLTEEELLDR EFDLLRSNRL GASTPSDKTV DLPPAPHSRP
     PEEPFASVPF ISHSGSPEKK TTEHSPNQKS ITANLTKNGG SSPLCKDQRA GKKTSENPVI
     RGQVQKGHDD SESDFESDPP SPKSSEEEQE DEDAQGEHGD FNDDDTEPEN LGHRPLLMDS
     EDEEEDDKHS SDSECEQAKT KRGDTSSLRR DKPGVAPDTA LLTPARSPAD ALTPSQEFDV
     FGAVPFFAAP APQSLQHRGD GKNLSQHAFP EQEDFDVFTK APFNKKVSVQ DWPAVGPDAR
     PLPARPRSVD IFGSTPFQPF SVSASKSESK EDVFGLVPFE EITGSQQQQK VKQRSLQKLS
     SRQRRTKQDV SKSNGKRHHG TPTSAKKTLK PPYRTPERAR RHKKVGRRDS QSSNEFLTIS
     DSKENISVAL TDGKDRASVL PSDESLLDPF GAKPFHPPDL WHQPHQGLSD ICVDHTTILP
     GRPRQNSVHG SFHSAETLRM DDFGAVPFTE LVVQSVTPQQ SQPVELDPFG AAPFPSKQ
//