BMP2K_MOUSE
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 03-AUG-2022, entry version 154.
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}.
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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 iPTMnet; Q91Z96; -.
DR PhosphoSitePlus; Q91Z96; -.
DR EPD; Q91Z96; -.
DR jPOST; Q91Z96; -.
DR MaxQB; Q91Z96; -.
DR PaxDb; Q91Z96; -.
DR PeptideAtlas; Q91Z96; -.
DR PRIDE; Q91Z96; -.
DR ProteomicsDB; 265218; -. [Q91Z96-1]
DR ProteomicsDB; 265219; -. [Q91Z96-2]
DR Antibodypedia; 24948; 194 antibodies from 27 providers.
DR DNASU; 140780; -.
DR Ensembl; ENSMUST00000035635; ENSMUSP00000037970; ENSMUSG00000034663. [Q91Z96-1]
DR Ensembl; ENSMUST00000112974; ENSMUSP00000108598; ENSMUSG00000034663. [Q91Z96-2]
DR GeneID; 140780; -.
DR KEGG; mmu:140780; -.
DR UCSC; uc008yfo.1; mouse. [Q91Z96-2]
DR UCSC; uc008yfp.1; mouse. [Q91Z96-1]
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; PWHPSHQ; -.
DR OrthoDB; 826336at2759; -.
DR PhylomeDB; Q91Z96; -.
DR TreeFam; TF317300; -.
DR BioGRID-ORCS; 140780; 2 hits in 76 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 234 other tissues.
DR Genevisible; Q91Z96; MM.
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: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; IDA:MGI.
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 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
